|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
100-1314 |
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: 741.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 100 PVDNAGLFSCMTFSWLSSLARVAHKKgELSMEDVWSLSKHESSDVNCRRLERLWQEE----------------------- 156
Cdd:TIGR00957 203 PESSASFLSRITFWWITGMAVYGYRQ-PLEESDLWSLNKEDTSEMVVPVLVENWKKEckktrkqpvsavygkkdpskpkg 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 157 ---LNEVGPDAA------------SLRRVVWIFCRTRLILSIVCLMITQLAGFSGPAfMVKHLLEYTQATESNLQYSLLL 221
Cdd:TIGR00957 282 ssqLDANEEVEAlivksphkprkpSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQ-ILSLLIRFVNDPMAPDWQGYFY 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 222 VLGLLLTEIVRSWSLALTWALNYRTGVRLRGAILTMAFKKILKLKNIKEKS--LGELINICSNDGQRMFEAAAVGSLLAG 299
Cdd:TIGR00957 361 TGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSstVGEIVNLMSVDAQRFMDLATYINMIWS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 300 GPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQ 379
Cdd:TIGR00957 441 APLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLD 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 380 SVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFD--LTAAQAFTVVTVFNSMTFALKVTPFSVKSL 457
Cdd:TIGR00957 521 KVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENniLDAEKAFVSLALFNILRFPLNILPMVISSI 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 458 SEASVAVDRFKSLFLMEEV--HMIKNKPASP--HIKIEMKNATLAWDSshssiqnspkltpkmkkdkrasrgkkekvrql 533
Cdd:TIGR00957 601 VQASVSLKRLRIFLSHEELepDSIERRTIKPgeGNSITVHNATFTWAR-------------------------------- 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 534 qrtehqavlaeqkghllldsDERPspeeeegkhihlghlrlqrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMT 613
Cdd:TIGR00957 649 --------------------DLPP-------------------TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 614 LLEGSIAISGTFAYVAQQAWILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRI 693
Cdd:TIGR00957 690 KVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRV 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 694 SLARALYSDRSIYILDDPLSALDAHVGNHIFNSAI--RKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELM 771
Cdd:TIGR00957 770 SLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 772 NLNGDYATIFNNLLLGE-----------------------------TPPVEINSKKETSGSQKKSQDKGPKTGSVKK-EK 821
Cdd:TIGR00957 850 QRDGAFAEFLRTYAPDEqqghledswtalvsgegkeakliengmlvTDVVGKQLQRQLSASSSDSGDQSRHHGSSAElQK 929
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 822 A-VKPEEGQLVQLEEKGQGSVPWSVYGVYIQAAGGPLAFLVIMaLFMLNVGSTAFSTWWLSYWIKQGSGNTTvtrGNETS 900
Cdd:TIGR00957 930 AeAKEETWKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIF-LFVCNHVSALASNYWLSLWTDDPMVNGT---QNNTS 1005
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 901 VSDSMKDNPHMQYYASIYALSMAVMLilkairgvvfvkGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMD 980
Cdd:TIGR00957 1006 LRLSVYGALGILQGFAVFGYSMAVSI------------GGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELD 1073
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 981 EVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQG 1060
Cdd:TIGR00957 1074 TVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLG 1153
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1061 LATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLT 1140
Cdd:TIGR00957 1154 VSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVT 1233
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1141 GLFQFTVRLASETEARFTSVERINHYIKTlSLEAPARIKNKAPSPDWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPK 1220
Cdd:TIGR00957 1234 FYLNWLVRMSSEMETNIVAVERLKEYSET-EKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGG 1312
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1221 EKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIW 1300
Cdd:TIGR00957 1313 EKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVW 1392
|
1290
....*....|....
gi 767925452 1301 DALERTHMKECDSS 1314
Cdd:TIGR00957 1393 WALELAHLKTFVSA 1406
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
100-1310 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 730.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 100 PVDNAGLFSCMTFSWLSSLARVAHKKgELSMEDVWSLSKHESSDVNCRRLERLWQEELNEVGP-DAASLRRVVWifcrTR 178
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKR-PLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPKPwLLRALNNSLG----GR 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 179 LILSIVCLMITQLAGFSGPAFMvKHLLEYTQATESNLQ---YSLLlvlglllteIVRSWSLALTWALNY-----RTGVRL 250
Cdd:PLN03130 303 FWLGGFFKIGNDLSQFVGPLLL-NLLLESMQNGEPAWIgyiYAFS---------IFVGVVLGVLCEAQYfqnvmRVGFRL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 251 RGAILTMAFKKILKLKNIKEKSL--GELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFIL 328
Cdd:PLN03130 373 RSTLVAAVFRKSLRLTHEGRKKFtsGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 329 FYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGYFQSITVGVAPI 408
Cdd:PLN03130 453 MFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNS 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 409 VVVIASVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRFKSLFLMEEVHMIKNKPASPHI 488
Cdd:PLN03130 533 IPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVLLPNPPLEPGL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 489 -KIEMKNATLAWDSShssiqnspkltpkmkkdkrasrgkkekvrqlqrtehqavlaeqkghllldsDERPspeeeegkhi 567
Cdd:PLN03130 613 pAISIKNGYFSWDSK---------------------------------------------------AERP---------- 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 568 hlghlrlqrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQM-TLLEGSIAISGTFAYVAQQAWILNATLRDNILFG 646
Cdd:PLN03130 632 ---------TLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELpPRSDASVVIRGTVAYVPQVSWIFNATVRDNILFG 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 647 KEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNS 726
Cdd:PLN03130 703 SPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDK 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 727 AIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNlNGdyaTIFNNLLLGETPPVEINSKK-ETSGSQK 805
Cdd:PLN03130 783 CIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN-NG---PLFQKLMENAGKMEEYVEENgEEEDDQT 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 806 KSQDKGPKTGSVKKEKAV---KPEEGQ--LVQLEEKGQGSVPWSVYGVYIQAAGGplaFLVIMALFMLNVGSTAF---ST 877
Cdd:PLN03130 859 SSKPVANGNANNLKKDSSskkKSKEGKsvLIKQEERETGVVSWKVLERYKNALGG---AWVVMILFLCYVLTEVFrvsSS 935
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 878 WWLSYWIKQGSGNTtvtrgnetsvsdsmkDNPhmQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILR 957
Cdd:PLN03130 936 TWLSEWTDQGTPKT---------------HGP--LFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILR 998
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 958 SPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNV---ILVFFCVGMIAGVFPWflvAVGPLVILFSVLHIVSRV 1034
Cdd:PLN03130 999 APMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIfqlLSTFVLIGIVSTISLW---AIMPLLVLFYGAYLYYQS 1075
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1035 LIRELKRLDNITQSPFLSHITSSIQGLATIHAYnKGQEFLHRYQELLDDNQAPFFLFT-CAMRWLAVRLDLISIALITTT 1113
Cdd:PLN03130 1076 TAREVKRLDSITRSPVYAQFGEALNGLSTIRAY-KAYDRMAEINGRSMDNNIRFTLVNmSSNRWLAIRLETLGGLMIWLT 1154
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1114 GLMIVLMHGQI--PPAYA---GLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYIKtLSLEAPARIKNKAPSPDWP 1188
Cdd:PLN03130 1155 ASFAVMQNGRAenQAAFAstmGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYID-LPSEAPLVIENNRPPPGWP 1233
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1189 QEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRS 1268
Cdd:PLN03130 1234 SSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|..
gi 767925452 1269 KLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKE 1310
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKD 1355
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
100-1310 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 687.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 100 PVDNAGLFSCMTFSWLSSLARVAHKKgELSMEDVWSLSKHESSDVNCRRLERLWQEELNEVGPdaaSLRRVVWIFCRTRL 179
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRK-PITEKDVWQLDQWDQTETLIKRFQRCWTEESRRPKP---WLLRALNNSLGGRF 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 180 ILSIVCLMITQLAGFSGPAfMVKHLLEYTQATES---NLQYSLLLVLGLLLTEIVRSWSLALTWalnyRTGVRLRGAILT 256
Cdd:PLN03232 304 WLGGIFKIGHDLSQFVGPV-ILSHLLQSMQEGDPawvGYVYAFLIFFGVTFGVLCESQYFQNVG----RVGFRLRSTLVA 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 257 MAFKKILKLKNIKEKSL--GELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMM 334
Cdd:PLN03232 379 AIFHKSLRLTHEARKNFasGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQT 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 335 FASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKA---GYFQSITVGVAPIVVv 411
Cdd:PLN03232 459 LIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAqllSAFNSFILNSIPVVV- 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 412 iaSVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRFKSLFLMEEVHMIKNKPASPHI-KI 490
Cdd:PLN03232 538 --TLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGApAI 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 491 EMKNATLAWDSShssiqnspkltpkmkkdkrasrgkkekvrqlqrtehqavlaeqkghllldsDERPspeeeegkhihlg 570
Cdd:PLN03232 616 SIKNGYFSWDSK---------------------------------------------------TSKP------------- 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 571 hlrlqrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLE-GSIAISGTFAYVAQQAWILNATLRDNILFGKEY 649
Cdd:PLN03232 632 ------TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATVRENILFGSDF 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 650 DEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIR 729
Cdd:PLN03232 706 ESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 730 KHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNlNGdyaTIFNNLLLGETppvEINSKKETSGSQKKSQD 809
Cdd:PLN03232 786 DELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSK-SG---SLFKKLMENAG---KMDATQEVNTNDENILK 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 810 KGPK-TGSVKKEKAVKPEEGQ-----LVQLEEKGQGSVPWSVYGVYIQAAGGPLAFLVIMALFMLNVGSTAFSTWWLSYW 883
Cdd:PLN03232 859 LGPTvTIDVSERNLGSTKQGKrgrsvLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVCYLTTEVLRVSSSTWLSIW 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 884 IKQgsgnttvtrgnetsvsdSMKDNPHMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFF 963
Cdd:PLN03232 939 TDQ-----------------STPKSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFF 1001
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 964 DTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQ---NVILVFFCVGMIAGVFPWflvAVGPLVILFSVLHIVSRVLIRELK 1040
Cdd:PLN03232 1002 HTNPTGRVINRFSKDIGDIDRNVANLMNMFMNqlwQLLSTFALIGTVSTISLW---AIMPLLILFYAAYLYYQSTSREVR 1078
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1041 RLDNITQSPFLSHITSSIQGLATIHAYnKGQEFLHRYQELLDDNQAPFFLF-TCAMRWLAVRLDLISIALITTTGLMIVL 1119
Cdd:PLN03232 1079 RLDSVTRSPIYAQFGEALNGLSSIRAY-KAYDRMAKINGKSMDNNIRFTLAnTSSNRWLTIRLETLGGVMIWLTATFAVL 1157
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1120 MHGQIP-----PAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYIKtLSLEAPARIKNKAPSPDWPQEGEVT 1194
Cdd:PLN03232 1158 RNGNAEnqagfASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYID-LPSEATAIIENNRPVSGWPSRGSIK 1236
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1195 FENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIP 1274
Cdd:PLN03232 1237 FEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIP 1316
|
1210 1220 1230
....*....|....*....|....*....|....*.
gi 767925452 1275 QEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKE 1310
Cdd:PLN03232 1317 QSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKD 1352
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
855-1167 |
0e+00 |
|
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: 539.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 855 GPLAFLVIMALFMLNVGSTAFSTWWLSYWIKQGSGNTTVTRGNETSVSDSMKDNPHMQYYASIYALSMAVMLILKAIRGV 934
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDNSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 935 VFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWF 1014
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1015 LVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCA 1094
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925452 1095 MRWLAVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 1167
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
164-1310 |
9.14e-174 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 559.01 E-value: 9.14e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 164 AASLRRVVWIFCRTRLILSIVCLMItqlagfsgpAFMVKHLLEYTQATESNLQYSLLLVLGLLLTEIVRSWSLALTWALN 243
Cdd:PTZ00243 239 FAALPYYVWWQIPFKLLSDVCTLTL---------PVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYIS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 244 YRTGVRLRGA----ILTMAFKKILKLKNIKEKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTG 319
Cdd:PTZ00243 310 IRCGLQYRSAlnalIFEKCFTISSKSLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 320 FLGSAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGYFQ 399
Cdd:PTZ00243 390 LMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLAR 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 400 SIT--VGVAPIVVVIASVvtFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRFkSLFL----- 472
Cdd:PTZ00243 470 VATsfVNNATPTLMIAVV--FTVYYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRI-STFLecdna 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 473 -------MEE-VHMIKNKPASPHIKIEMKNAtlawdSSHSSIQNSPKLTPKMK----------------KDKRASRGKKE 528
Cdd:PTZ00243 547 tcstvqdMEEyWREQREHSTACQLAAVLENV-----DVTAFVPVKLPRAPKVKtsllsralrmlcceqcRPTKRHPSPSV 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 529 KVRQLQRTEHQAVLAEQKGHLLLDSDERPSPEEEEGKHIHLG-----HLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTS 603
Cdd:PTZ00243 622 VVEDTDYGSPSSASRHIVEGGTGGGHEATPTSERSAKTPKMKtddffELEPKVLLRDVSVSVPRGKLTVVLGATGSGKST 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 604 LISAILGQMTLLEGSIAISGTFAYVAQQAWILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGA 683
Cdd:PTZ00243 702 LLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGV 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 684 NLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITE 763
Cdd:PTZ00243 782 NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEF 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 764 RGTHEELMNlngdyATIFNNLLLG--------------ETPPVEINSKKETSGSQKKSQDKGPKTGSVKkeKAVKPEEGQ 829
Cdd:PTZ00243 862 SGSSADFMR-----TSLYATLAAElkenkdskegdadaEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDG--AALDAAAGR 934
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 830 LVQLEEKGQGSVPWSVYGVYIQAAGGPLAFLVIMALFMLNVGSTAFSTWWLSYWikqgsgnTTvtrgNETSVSDSMkdnp 909
Cdd:PTZ00243 935 LMTREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSSGVWLSMW-------ST----RSFKLSAAT---- 999
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 910 hmqyYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPfq 989
Cdd:PTZ00243 1000 ----YLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLP-- 1073
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 990 aeMFIQNVILVFF--CVGMIAGVF--PWFLVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIH 1065
Cdd:PTZ00243 1074 --MSYLYLLQCLFsiCSSILVTSAsqPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATIT 1151
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1066 AYNKG----QEFLHRyqelLDDNQAPFFLFTCAMRWLAVRLDLIS------IALITTTGLMIVLMHGQIppAYAGLAISY 1135
Cdd:PTZ00243 1152 AYGKAhlvmQEALRR----LDVVYSCSYLENVANRWLGVRVEFLSnivvtvIALIGVIGTMLRATSQEI--GLVSLSLTM 1225
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1136 AVQLTGLFQFTVRLASETEARFTSVERINHYIKTLSLEA----------------------------PARIKNKAPSPdw 1187
Cdd:PTZ00243 1226 AMQTTATLNWLVRQVATVEADMNSVERLLYYTDEVPHEDmpeldeevdalerrtgmaadvtgtvviePASPTSAAPHP-- 1303
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1188 PQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLR 1267
Cdd:PTZ00243 1304 VQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELR 1383
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|...
gi 767925452 1268 SKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKE 1310
Cdd:PTZ00243 1384 RQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRE 1426
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
181-467 |
1.05e-136 |
|
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: 420.04 E-value: 1.05e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 181 LSIVCLMITQLAGFSGPAFMVKHLLEYTQATESNLQYSLLLVLGLLLTEIVRSWSLALTWALNYRTGVRLRGAILTMAFK 260
Cdd:cd18592 1 FSILLLLISLIFGFIGPTILIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 261 KILKLKNIKEKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFASRLT 340
Cdd:cd18592 81 KILRLRSLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 341 AYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSV 420
Cdd:cd18592 161 GKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767925452 421 HMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRF 467
Cdd:cd18592 241 HVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
100-1309 |
1.63e-129 |
|
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: 436.26 E-value: 1.63e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 100 PVDNAGLFSCMTFSWLSSLARVAHKKgELSMEDVWSLSKHESSDVNCRRLERLWQEELNEVGPDAA---SLRRV-VWIFC 175
Cdd:TIGR01271 5 PVEKANFLSKLFFWWTRPILRKGYRQ-KLELSDIYQIPSFDSADNLSERLEREWDRELASAKKNPKllnALRRCfFWRFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 176 RTRLILSIVCLMIT---QLAGFSGPAFMVKHLLEYTQATESNLQYSLLLvlglllteIVRSWSLALTWALNYRTGVRLRG 252
Cdd:TIGR01271 84 FYGILLYFGEATKAvqpLLLGRIIASYDPFNAPEREIAYYLALGLCLLF--------IVRTLLLHPAIFGLHHLGMQMRI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 253 AILTMAFKKILKLKNIK--EKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAIL--GMIYNviILGPTGFLGSAVFIL 328
Cdd:TIGR01271 156 ALFSLIYKKTLKLSSRVldKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILlmGLIWE--LLEVNGFCGLGFLIL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 329 FYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAG---YFQSITVGV 405
Cdd:TIGR01271 234 LALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAylrYFYSSAFFF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 406 APIVVVIASVVTFSVHMTLgfdlTAAQAFTvvTVFNSMTFALKVT---PFSVKSLSEASVAVDRFKSLFLMEEVHMIKNK 482
Cdd:TIGR01271 314 SGFFVVFLSVVPYALIKGI----ILRRIFT--TISYCIVLRMTVTrqfPGAIQTWYDSLGAITKIQDFLCKEEYKTLEYN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 483 PASPhiKIEMKNATLAWDSSHSSIqnspkltpkmkkdkrasrgkKEKVRQlqrtehqavlaeqkghlllDSDERPSPEEE 562
Cdd:TIGR01271 388 LTTT--EVEMVNVTASWDEGIGEL--------------------FEKIKQ-------------------NNKARKQPNGD 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 563 EGKHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNATLRDN 642
Cdd:TIGR01271 427 DGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDN 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 643 ILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 722
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 723 IFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIF-------------NNLLLGET 789
Cdd:TIGR01271 587 IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLlgleafdnfsaerRNSILTET 666
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 790 -------------------------PPVEINSKKETS------GSQKKSQ--DKGPKTGSVKKEKAVKPEEGQ----LVQ 832
Cdd:TIGR01271 667 lrrvsidgdstvfsgpetikqsfkqPPPEFAEKRKQSiilnpiASARKFSfvQMGPQKAQATTIEDAVREPSErkfsLVP 746
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 833 LEEKGQGSVP---------------------------------------------------------------------- 842
Cdd:TIGR01271 747 EDEQGEESLPrgnqyhhglqhqaqrrqsvlqlmthsnrgenrreqlqtsfrkkssitqqnelaseldiysrrlskdsvye 826
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 843 --------------------------WSVYGVYIqAAGGPLAFLVIMAL--FMLNVGSTAFSTWWLS---YWIKQGSGNT 891
Cdd:TIGR01271 827 iseeineedlkecfaderenvfetttWNTYLRYI-TTNRNLVFVLIFCLviFLAEVAASLLGLWLITdnpSAPNYVDQQH 905
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 892 TVTRGNETSVSDSMKDNPHMqYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRI 971
Cdd:TIGR01271 906 ANASSPDVQKPVIITPTSAY-YIFYIYVGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRI 984
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 972 LNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFL 1051
Cdd:TIGR01271 985 LNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIF 1064
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1052 SHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHgQIPPAYAGL 1131
Cdd:TIGR01271 1065 SHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTN-QDGEGEVGI 1143
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1132 AISYAVQLTGLFQFTVRLASETEARFTSVERINHYI-------------KTLSLEAPARIKNKAPSPDWPQEGEVTFENA 1198
Cdd:TIGR01271 1144 ILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIdlpqeeprpsgggGKYQLSTVLVIENPHAQKCWPSGGQMDVQGL 1223
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1199 EMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGcIKIDGVRISDIGLADLRSKLSIIPQEPV 1278
Cdd:TIGR01271 1224 TAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGE-IQIDGVSWNSVTLQTWRKAFGVIPQKVF 1302
|
1370 1380 1390
....*....|....*....|....*....|.
gi 767925452 1279 LFSGTVRSNLDPFNQYTEDQIWDALERTHMK 1309
Cdd:TIGR01271 1303 IFSGTFRKNLDPYEQWSDEEIWKVAEEVGLK 1333
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
577-759 |
7.05e-110 |
|
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: 344.45 E-value: 7.05e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 577 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNATLRDNILFGKEYDEERYNS 656
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGKPFDEERYEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 657 VLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKHLK-SK 735
Cdd:cd03250 100 VIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLnNK 179
|
170 180
....*....|....*....|....
gi 767925452 736 TVLFVTHQLQYLVDCDEVIFMKEG 759
Cdd:cd03250 180 TRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
859-1167 |
1.90e-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: 333.32 E-value: 1.90e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 859 FLVIMALFMLNVGSTAFSTWWLSYWIKQGSGNTTVTRGnetsvsdsmkdnphmQYYASIYALSMAVMLILKAIRGVVFVK 938
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSG---------------YYLGVYAALLVLASVLLVLLRWLLFVL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 939 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 1018
Cdd:cd18580 66 AGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1019 GPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAMRWL 1098
Cdd:cd18580 146 PPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 1099 AVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 1167
Cdd:cd18580 226 GLRLDLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
859-1166 |
3.16e-87 |
|
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: 285.91 E-value: 3.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 859 FLVIMALFMLNVGSTAFSTWWLSYWIKQGSGNTTvtrgnetsvsdsmKDNPHMQYYASIYALSMAVMLILKAIRGVVFVK 938
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGT-------------QDTEQRDYRLGVYGALGLGQAIFVFLGSLALAL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 939 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 1018
Cdd:cd18603 68 GCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1019 GPLVILFsvlHIVSRVLI---RELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAM 1095
Cdd:cd18603 148 IPLAILY---FFIQRFYVatsRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSN 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 1096 RWLAVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 1166
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 ... |
859-1166 |
2.96e-86 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 282.83 E-value: 2.96e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 859 FLVIMALFMLNVGSTAFSTWWLSYWIKQGSGNTTvtrgnetsvsdsmkdnphmQYYASIYALSMAVMLILKAIRGVVFVK 938
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTEDFFGLSQ-------------------GFYIGIYAGLGVLQAIFLFLFGLLLAY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 939 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 1018
Cdd:cd18606 62 LGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1019 GPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAMRWL 1098
Cdd:cd18606 142 PPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWL 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767925452 1099 AVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 1166
Cdd:cd18606 222 AIRLDLLGSLLVLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
859-1167 |
2.57e-83 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 274.73 E-value: 2.57e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 859 FLVIMALFMLNVGSTAFSTWWLSYWikqgsgnttvTRGNETSVSDSmKDNPHMQYYASIYALSMAVMLILKAIRGVVFVK 938
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQSWWLGIW----------ASAYETSSALP-PSEVSVLYYLGIYALISLLSVLLGTLRYLLFFF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 939 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 1018
Cdd:cd18604 70 GSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1019 GPLVILFSVlhiVSRVLI---RELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAM 1095
Cdd:cd18604 150 VVLAALYVY---IGRLYLrasRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLN 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 1096 RWLAVRLDLISIALITTTGLMIVLMHGqIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 1167
Cdd:cd18604 227 RWLSVRIDLLGALFSFATAALLVYGPG-IDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
859-1167 |
4.07e-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: 4.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 859 FLVIMALFMLNVGSTAFSTWWLSYWIkqgsgnttvtrgNETSVSDSMKDNPHMQYYASIYALSMAVMLILKAIRGVVFVK 938
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWV------------SHSNNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 939 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVilvFFCVGMIAGV---FPWFL 1015
Cdd:cd18605 69 GGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQL---FGLLGYLVVIcyqLPWLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1016 VAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAM 1095
Cdd:cd18605 146 LLLLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAAS 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 1096 RWLAVRLDLISIALITTTGLMIVLMH---GQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 1167
Cdd:cd18605 226 QWLSIRLQLLGVLIVTFVALTAVVQHffgLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
855-1166 |
3.13e-80 |
|
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: 266.88 E-value: 3.13e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 855 GPLAFLVIMALFMLNVGSTAFSTWWLSYWiKQGSGNTTVTRGNETSVSDSMKDNPHMQ--YYASIYALSMAVMLILKAIR 932
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYW-ANLEEKLNDTTDRVQGENSTNVDIEDLDrdFNLGIYAGLTAATFVFGFLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 933 GVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFP 1012
Cdd:cd18601 80 SLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1013 WFLVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFT 1092
Cdd:cd18601 160 WVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767925452 1093 CAMRWLAVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 1166
Cdd:cd18601 240 ATSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
859-1166 |
1.27e-75 |
|
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: 253.29 E-value: 1.27e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 859 FLVIMALFMLNVGSTAFSTWWLSYWIKQGSGNTTVtrgNETSVSDSMKDNPHMqYYASIYALSMAVMLILKAIRGVVFVK 938
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEANHDVASV---VFNITSSSLEDDEVS-YYISVYAGLSLGAVILSLVTNLAGEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 939 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 1018
Cdd:cd18602 77 AGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1019 GPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAMRWL 1098
Cdd:cd18602 157 IPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 1099 AVRLDLISiALITTTGLMIVL---MHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 1166
Cdd:cd18602 237 GIRLDYLG-AVIVFLAALSSLtaaLAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1191-1310 |
9.74e-69 |
|
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: 230.46 E-value: 9.74e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1191 GEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 1270
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767925452 1271 SIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKE 1310
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKE 120
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
913-1310 |
7.32e-67 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 237.37 E-value: 7.32e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 913 YYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 992
Cdd:COG1132 62 LLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 993 FIQNVILVFFCVGMIAGVFPWF-LVAVGPLVILFSVLHIVSRvLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQ 1071
Cdd:COG1132 142 LVRSVVTLIGALVVLFVIDWRLaLIVLLVLPLLLLVLRLFGR-RLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1072 EFLHRYQELLDDNQAPFFLFTCAMRWLAVRLDLI---SIALITTTGLMIVLmHGQIPPAYAGLAISYAVQLTGLFQFTVR 1148
Cdd:COG1132 221 RELERFREANEELRRANLRAARLSALFFPLMELLgnlGLALVLLVGGLLVL-SGSLTVGDLVAFILYLLRLFGPLRQLAN 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1149 LASETEARFTSVERINHYiktlsLEAPARIKNKA-PSPDWPQEGEVTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVG 1227
Cdd:COG1132 300 VLNQLQRALASAERIFEL-----LDEPPEIPDPPgAVPLPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1228 RTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALE 1304
Cdd:COG1132 374 PSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAK 451
|
....*.
gi 767925452 1305 RTHMKE 1310
Cdd:COG1132 452 AAQAHE 457
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
163-782 |
1.27e-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: 1.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 163 DAASLRRVVWIF--CRTRLILSIVCLMITQLAGFSGPAFMVKHLLEYTQATESN--LQYSLLLVLGLLLTEIVRSWSLAL 238
Cdd:COG1132 5 PRKLLRRLLRYLrpYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSalLLLLLLLLGLALLRALLSYLQRYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 239 TWALNYRTGVRLRGAI------LTMAFKKilklknikEKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNV 312
Cdd:COG1132 85 LARLAQRVVADLRRDLfehllrLPLSFFD--------RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 313 IILGPTgfLGSAVFILFyPAMMFASRLTAYFRRKCVAATDERVQKMNEVLT-YIKFIKMyawVKAFSQ---SVQKIREEE 388
Cdd:COG1132 157 FVIDWR--LALIVLLVL-PLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQeSLSGIRV---VKAFGReerELERFREAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 389 RRILEKAGYFQSITVGVAPIV-----VVIASVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVA 463
Cdd:COG1132 231 EELRRANLRAARLSALFFPLMellgnLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALAS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 464 VDRFKSLflMEEVHMIKNKPASPHIK-----IEMKNATLAWDsshssiqnspkltpkmkkdkrasrgkkekvrqlqrteh 538
Cdd:COG1132 311 AERIFEL--LDEPPEIPDPPGAVPLPpvrgeIEFENVSFSYP-------------------------------------- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 539 qavlaeqkghllldsDERPspeeeegkhihlghlrlqrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGS 618
Cdd:COG1132 351 ---------------GDRP-------------------VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 619 IAISGT-------------FAYVAQQAWILNATLRDNILFGK-EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGAN 684
Cdd:COG1132 397 ILIDGVdirdltleslrrqIGVVPQDTFLFSGTIRENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 685 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNsAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITER 764
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQE-ALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQ 555
|
650
....*....|....*...
gi 767925452 765 GTHEELMNLNGDYATIFN 782
Cdd:COG1132 556 GTHEELLARGGLYARLYR 573
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
577-759 |
6.42e-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: 204.87 E-value: 6.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 577 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAIS-----------------GTFAYVAQQAWILNATL 639
Cdd:cd03290 16 TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnknesepsfeatrsrnrYSVAYAAQKPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 640 RDNILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 719
Cdd:cd03290 96 EENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767925452 720 GNHIFNSAIRKHLK--SKTVLFVTHQLQYLVDCDEVIFMKEG 759
Cdd:cd03290 176 SDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
575-775 |
4.32e-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: 4.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRD 641
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrrqIAWVPQNPYLFAGTIRE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 642 NILFGK-EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 720
Cdd:COG4988 430 NLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 721 NHIFNsAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNG 775
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 ... |
181-466 |
9.60e-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: 195.78 E-value: 9.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 181 LSIVCLMITQLAGFSGPaFMVKHLLEYTQA-TESNLQYSLLLVLGLLLTEIVRSWSLALTWALNYRTGVRLRGAILTMAF 259
Cdd:cd18579 1 LAGLLKLLEDLLSLAQP-LLLGLLISYLSSyPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 260 kkilklknikEKSL------------GELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFI 327
Cdd:cd18579 80 ----------RKALrlsssarqetstGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 328 LFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGYFQSITVGVAP 407
Cdd:cd18579 150 LLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFF 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 408 IVVVIASVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 466
Cdd:cd18579 230 STPVLVSLATFATYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKR 288
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
912-1306 |
5.23e-55 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 205.45 E-value: 5.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 912 QYYASIYALSMAVML------ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkDMDEVDVR 985
Cdd:COG2274 190 QDLSTLWVLAIGLLLallfegLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREF 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 986 LPFQAEMFIQNVILVFFCVGMIAGVFPWF----LVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSpflsHITSSIQGL 1061
Cdd:COG2274 269 LTGSLLTALLDLLFVLIFLIVLFFYSPPLalvvLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQS----LLVETLRGI 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1062 ATIHAYNKGQEFLHRYQELLDDNQAPFFlftcAMRWLAVRLDLISIAL--ITTTGLMIV----LMHGQIPP-------AY 1128
Cdd:COG2274 345 ETIKALGAESRFRRRWENLLAKYLNARF----KLRRLSNLLSTLSGLLqqLATVALLWLgaylVIDGQLTLgqliafnIL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1129 AGLAISYAVQLTGLFQftvRLAsetEARfTSVERINHYIKTLSLEAPARIKNKAPSPdwpqEGEVTFENAEMRYRENLPL 1208
Cdd:COG2274 421 SGRFLAPVAQLIGLLQ---RFQ---DAK-IALERLDDILDLPPEREEGRSKLSLPRL----KGDIELENVSFRYPGDSPP 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL 1288
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENI 569
|
410 420
....*....|....*....|.
gi 767925452 1289 ---DPfnQYTEDQIWDALERT 1306
Cdd:COG2274 570 tlgDP--DATDEEIIEAARLA 588
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
271-783 |
5.33e-55 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 205.45 E-value: 5.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 271 KSLGELINicsndgqRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGS---AVFILFYPAMMFASRLTAYFRRKC 347
Cdd:COG2274 250 RSVGDLAS-------RFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPplaLVVLLLIPLYVLLGLLFQPRLRRL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 348 VAATDERVQKMN----EVLTYIKFIKMYA--------WVKAFSQSVqKIREEERRILEKAGYFQSITVGVAPIVVVIASV 415
Cdd:COG2274 323 SREESEASAKRQsllvETLRGIETIKALGaesrfrrrWENLLAKYL-NARFKLRRLSNLLSTLSGLLQQLATVALLWLGA 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 416 vtFSV---HMTLGfDLTAAQAFtVVTVFNSMT-FALKVTpfsvkSLSEASVAVDRFKSLFLME-EVHMIKNKPASPHIK- 489
Cdd:COG2274 402 --YLVidgQLTLG-QLIAFNIL-SGRFLAPVAqLIGLLQ-----RFQDAKIALERLDDILDLPpEREEGRSKLSLPRLKg 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 490 -IEMKNATLawdsshssiqnspkltpkmkkdkrasrgkkekvrqlqrtehqavlaeqkghllldsdeRPSPEEEEgkhih 568
Cdd:COG2274 473 dIELENVSF----------------------------------------------------------RYPGDSPP----- 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 569 lghlrlqrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWIL 635
Cdd:COG2274 490 --------VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdlrqidpaslrrqIGVVLQDVFLF 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 636 NATLRDNILFGKEY-DEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:COG2274 562 SGTIRENITLGDPDaTDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 715 LDAHvGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNN 783
Cdd:COG2274 642 LDAE-TEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1187-1304 |
9.93e-55 |
|
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: 189.55 E-value: 9.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1187 WPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADL 1266
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 767925452 1267 RSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALE 1304
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR 118
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
578-787 |
7.61e-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: 184.29 E-value: 7.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNATLRDNILFGKEYDEERYNSV 657
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 658 LNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKHLKSKTV 737
Cdd:cd03291 133 VKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTR 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767925452 738 LFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDyatiFNNLLLG 787
Cdd:cd03291 213 ILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPD----FSSKLMG 258
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
578-778 |
3.26e-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: 188.05 E-value: 3.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 644
Cdd:COG4987 351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrdldeddlrrrIAVVPQRPHLFDTTLRENLR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 FGKEY-DEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI 723
Cdd:COG4987 431 LARPDaTDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 724 FNsAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:COG4987 511 LA-DLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYR 564
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
573-759 |
3.77e-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: 157.93 E-value: 3.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 573 RLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATL 639
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldleslrknIAYVPQDPFLFSGTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 640 RDNILfgkeydeerynsvlnscclrpdlailpssdlteigerganlSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 719
Cdd:cd03228 93 RENIL-----------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767925452 720 GNHIFNsAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEG 759
Cdd:cd03228 132 EALILE-ALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
565-782 |
4.96e-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: 154.31 E-value: 4.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 565 KHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQ 631
Cdd:cd03253 4 ENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 632 AWILNATLRDNILFGKE--YDEERYNSVLnSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILD 709
Cdd:cd03253 84 TVLFNDTIGYNIRYGRPdaTDEEVIEAAK-AAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925452 710 DPLSALDAHVGNHIFNsAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFN 782
Cdd:cd03253 163 EATSALDTHTEREIQA-ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWK 234
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
577-775 |
2.19e-41 |
|
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: 151.99 E-value: 2.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 577 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNI 643
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslrsmIGVVLQDTFLFSGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 644 LFGKEY-DEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 722
Cdd:cd03254 98 RLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767925452 723 IfNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNG 775
Cdd:cd03254 178 I-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
578-778 |
4.59e-41 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 151.61 E-value: 4.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 644
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 FGK-EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVGNHI 723
Cdd:cd03251 98 YGRpGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT-ESERL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 724 FNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:cd03251 177 VQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
843-1167 |
1.90e-40 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350044 [Multi-domain] Cd Length: 324 Bit Score: 152.65 E-value: 1.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 843 WSVYGVYIQAAGGPLAFLV-IMALFMLNVGSTAFSTWWLSYWIKQGSGNTTVTRGNETSVSDSMKDNPHMQYyasIYALS 921
Cdd:cd18600 3 WNTYLRYITSHKSLIFVLIlCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSNTYAVIVTFTSSYYVFY---IYVGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 922 MAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVF 1001
Cdd:cd18600 80 ADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1002 FCVGMIAGVFPWFLVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELL 1081
Cdd:cd18600 160 GAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1082 DDNQAPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHGQiPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVE 1161
Cdd:cd18600 240 NLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGD-GEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVS 318
|
....*.
gi 767925452 1162 RINHYI 1167
Cdd:cd18600 319 RIFKFI 324
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
530-756 |
7.13e-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: 156.29 E-value: 7.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 530 VRQLQRTEH---QAVLAEQKGHLLLDSDERPSPEEEEGKHIHLGHLRLQ----------RTLHSIDLEIQEGKLVGICGS 596
Cdd:TIGR02857 277 LRQLGAQYHaraDGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSgvsvaypgrrPALRPVSFTVPPGERVALVGP 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 597 VGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNILFGK-EYDEERYNSVLNSCC 662
Cdd:TIGR02857 357 SGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAENIRLARpDASDAEIREALERAG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 663 LRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKHLKSKTVLFVTH 742
Cdd:TIGR02857 437 LDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV-LEALRALAQGRTVLLVTH 515
|
250
....*....|....
gi 767925452 743 QLQYLVDCDEVIFM 756
Cdd:TIGR02857 516 RLALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
577-761 |
3.06e-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: 3.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 577 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNI 643
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqldpadlrrnIGYVPQDVTLFYGTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 644 LFGKEY-DEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 722
Cdd:cd03245 99 TLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEER 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 767925452 723 IFnSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCI 761
Cdd:cd03245 179 LK-ERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
230-466 |
6.17e-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: 147.21 E-value: 6.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 230 IVRSWSLALTWALNYRTGVRLRGAILTMAFkkilklknikEKSL------------GELINICSNDGQRMFEAAAVGSLL 297
Cdd:cd18597 54 LLSSLLLNHFFYRSMLTGAQVRAALTKAIY----------RKSLrlsgksrhefpnGKITNLMSTDLSRIDFALGFFHFL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 298 AGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAF 377
Cdd:cd18597 124 WTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 378 SQSVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSL 457
Cdd:cd18597 204 LERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASMLSFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSL 283
|
....*....
gi 767925452 458 SEASVAVDR 466
Cdd:cd18597 284 ADALVALKR 292
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
581-783 |
1.40e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 153.46 E-value: 1.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 581 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLlEGSIAISGT-------------FAYVAQQAWILNATLRDNILFGK 647
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIelreldpeswrkhLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 648 -EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNS 726
Cdd:PRK11174 448 pDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV-MQ 526
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767925452 727 AIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNN 783
Cdd:PRK11174 527 ALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
181-466 |
1.81e-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: 143.40 E-value: 1.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 181 LSIVCLMITQLAGFSGPAFMvKHLLEY-TQATESNLQYSLLLVLGLLLTEIVRSWSLALTWALNYRTGVRLRgAILTMA- 258
Cdd:cd18596 1 LQALLAVLSSVLSFAPPFFL-NRLLRYlEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLR-AILTQLi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 259 ---------------------FKKILKLKNIKEKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGP 317
Cdd:cd18596 79 fekalrrrdksgssksseskkKDKEEDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 318 TGFLGSAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGY 397
Cdd:cd18596 159 SALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 398 FQSITVGVAPIVVVIASVVTFSVH-MTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 466
Cdd:cd18596 239 LDLLLSLLWFLIPILVTVVTFATYtLVMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDR 308
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
578-766 |
2.33e-37 |
|
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: 140.32 E-value: 2.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNIL 644
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISIIPQDPVLFSGTIRSNLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 FGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIf 724
Cdd:cd03244 100 PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALI- 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767925452 725 NSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGT 766
Cdd:cd03244 179 QKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1191-1309 |
2.33e-36 |
|
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: 138.89 E-value: 2.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1191 GEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 1270
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110
....*....|....*....|....*....|....*....
gi 767925452 1271 SIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMK 1309
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLK 136
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
577-782 |
1.58e-35 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 144.09 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 577 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNI 643
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHdladytlaslrrqVALVSQDVVLFNDTIANNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 644 LFGK--EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 721
Cdd:TIGR02203 427 AYGRteQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESER 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 722 HIfNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFN 782
Cdd:TIGR02203 507 LV-QAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHN 566
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
578-778 |
2.05e-35 |
|
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: 135.36 E-value: 2.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 644
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 FGKEY--DEERyNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVgNH 722
Cdd:cd03249 99 YGKPDatDEEV-EEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES-EK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767925452 723 IFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:cd03249 177 LVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYA 232
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
578-777 |
5.94e-35 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 142.16 E-value: 5.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI-------------AISGTFAYVAQQAWILNATLRDNIL 644
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklqldSWRSRLAVVSQTPFLFSDTVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 FGK-EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI 723
Cdd:PRK10789 411 LGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767925452 724 FNSaIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDY 777
Cdd:PRK10789 491 LHN-LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
230-466 |
7.02e-35 |
|
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: 135.29 E-value: 7.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 230 IVRSWSLALTWALNYRTGVRLRGAILTMAFkkilklknikEKSL------------GELINICSNDGQRMFEAAAVGSLL 297
Cdd:cd18595 49 IIQSLLLHQYFHRCFRLGMRIRTALTSAIY----------RKALrlsnsarkkstvGEIVNLMSVDAQRIQDLVPYLNML 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 298 AGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAF 377
Cdd:cd18595 119 WSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 378 SQSVQKIREEERRILEKAGYFQSITV---GVAPIVVviaSVVTFSVHMTLGFD--LTAAQAFTVVTVFNSMTFALKVTPF 452
Cdd:cd18595 199 EKKILKIREKELKLLKKAAYLNAVSSflwTCAPFLV---SLATFATYVLSDPDnvLDAEKAFVSLSLFNILRFPLSMLPM 275
|
250
....*....|....
gi 767925452 453 SVKSLSEASVAVDR 466
Cdd:cd18595 276 VISNLVQASVSLKR 289
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
578-778 |
7.54e-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: 133.77 E-value: 7.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNIL 644
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 FGKE-YDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDaHVGNHI 723
Cdd:cd03252 98 LADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD-YESEHA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 724 FNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:cd03252 177 IMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
859-1143 |
6.61e-33 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 129.30 E-value: 6.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 859 FLVIMALFMLNVGSTAFSTWWLSYWIKqgsgnttvtrgneTSVSDSMKDNPHMQYYASIYALSMAVMLILKAIRGVVFVK 938
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILD-------------VLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 939 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVIlVFFCVGMIAGVFPWFL--- 1015
Cdd:pfam00664 68 TGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLA-TIVGGIIVMFYYGWKLtlv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1016 -VAVGPLVILFSVlhIVSRVLiRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCA 1094
Cdd:pfam00664 147 lLAVLPLYILVSA--VFAKIL-RKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 767925452 1095 MRWLAVRLDLI---SIALITTTGlMIVLMHGQIPPAYAGLAISYAVQLTGLF 1143
Cdd:pfam00664 224 NGLSFGITQFIgylSYALALWFG-AYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
272-467 |
2.29e-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: 2.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 272 SLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFASRLTAYFRRKCVAAT 351
Cdd:cd18594 94 TTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 352 DERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFDLTAA 431
Cdd:cd18594 174 DERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTGNTLTAR 253
|
170 180 190
....*....|....*....|....*....|....*...
gi 767925452 432 QAFTVVTVFNS--MTFALKVtPFSVKSLSEASVAVDRF 467
Cdd:cd18594 254 KVFTVISLLNAlrMTITRFF-PESIQTLSESRVSLKRI 290
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1193-1288 |
7.60e-32 |
|
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: 122.49 E-value: 7.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 1272
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90
....*....|....*.
gi 767925452 1273 IPQEPVLFSGTVRSNL 1288
Cdd:cd03228 81 VPQDPFLFSGTIRENI 96
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
242-466 |
1.09e-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: 123.88 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 242 LNYRTGVRLRGAILTMAF----KKILKLKNIKEKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGP 317
Cdd:cd18591 79 IVIREGIRLKTALQAMIYekalRLSSWNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 318 TGFLGSAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGY 397
Cdd:cd18591 159 SALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAV 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 398 FQSITVGVAPIVVVIASVVTFSVHMTL-GFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 466
Cdd:cd18591 239 YWSLMTFLTQASPILVTLVTFGLYPYLeGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRR 308
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
575-778 |
4.28e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 127.25 E-value: 4.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRD 641
Cdd:PRK11160 353 QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrqaISVVSQRVHLFSATLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 642 NILFGK-EYDEERYNSVLNscclRPDLAILPSSDL---TEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:PRK11160 433 NLLLAApNASDEALIEVLQ----QVGLEKLLEDDKglnAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 718 HVGNHIFnSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:PRK11160 509 ETERQIL-ELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYY 568
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
578-778 |
6.34e-30 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 127.06 E-value: 6.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 644
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdytlaslrnqVALVSQNVHLFNDTIANNIA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 FGKE--YDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGNH 722
Cdd:PRK11176 439 YARTeqYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE-SER 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767925452 723 IFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:PRK11176 518 AIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYA 573
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
542-744 |
6.77e-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: 6.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 542 LAEQKGHLLLDSDERPSPEEEEG-----KHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLE 616
Cdd:TIGR02868 310 VLDAAGPVAEGSAPAAGAVGLGKptlelRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 617 GSIAISG-------------TFAYVAQQAWILNATLRDNILFGK-EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERG 682
Cdd:TIGR02868 390 GEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLRALPDGLDTVLGEGG 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 683 ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnSAIRKHLKSKTVLFVTHQL 744
Cdd:TIGR02868 470 ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELL-EDLLAALSGRTVVLITHHL 530
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
578-757 |
3.11e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 116.48 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------FAYVAQQA---WILNATLRDNIL-- 644
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQRRsidRDFPISVRDVVLmg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 ------FGKEYDEERYNSVLnscclrpdlAILPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:cd03235 95 lyghkgLFRRLSKADKAKVD---------EALERVGLSELADRQiGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767925452 718 HvGNHIFNSAIRK-HLKSKTVLFVTHQLQYLVD-CDEVIFMK 757
Cdd:cd03235 166 K-TQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLLN 206
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
578-778 |
3.21e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 125.99 E-value: 3.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 644
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqydhhylhrqVALVGQEPVLFSGSVRENIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 FG-KEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI 723
Cdd:TIGR00958 577 YGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 724 FNSairKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:TIGR00958 657 QES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
565-765 |
3.29e-29 |
|
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: 115.49 E-value: 3.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 565 KHIHLGHL-RLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI------------AISGTFAYVAQQ 631
Cdd:cd03247 4 NNVSFSYPeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEItldgvpvsdlekALSSLISVLNQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 632 AWILNATLRDNIlfgkeydeerynsvlnscclrpdlailpssdlteigerGANLSGGQRQRISLARALYSDRSIYILDDP 711
Cdd:cd03247 84 PYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767925452 712 LSALDAHVGNHIFnSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERG 765
Cdd:cd03247 126 TVGLDPITERQLL-SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
578-772 |
5.16e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.11 E-value: 5.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------FAYVAQQA---WILNATLRDNILFG 646
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVPQRAevdWDFPITVRDVVLMG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 647 --------KEYDEERYNSVLNScclrpdLAILpssDLTE-----IGErganLSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:COG1121 102 rygrrglfRRPSRADREAVDEA------LERV---GLEDladrpIGE----LSGGQQQRVLLARALAQDPDLLLLDEPFA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 714 ALDAHVGNHIFnsAIRKHLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCITErGTHEELMN 772
Cdd:COG1121 169 GVDAATEEALY--ELLRELRRegKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLT 227
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
578-778 |
6.26e-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: 124.85 E-value: 6.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWI---LNATLRDNILFGKEYDEery 654
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLrrqMGVVLQENVLFSRSIRD--- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 655 nsvlNSCCLRPDLAI------------------LPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD 716
Cdd:TIGR01846 550 ----NIALCNPGAPFehvihaaklagahdfiseLPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALD 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 717 AHvGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:TIGR01846 626 YE-SEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYA 686
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
575-778 |
8.62e-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: 123.27 E-value: 8.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRD 641
Cdd:TIGR02204 353 QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVdlrqldpaelrarMALVPQDPVLFAASVME 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 642 NILFGK--EYDEERYNSVLNScclRPDLAI--LPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:TIGR02204 433 NIRYGRpdATDEEVEAAARAA---HAHEFIsaLPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDA 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 718 HvGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:TIGR02204 510 E-SEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYA 569
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
549-778 |
1.26e-28 |
|
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: 123.90 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 549 LLLDSDERPSPEEEEGK---HIHL-----GHLRLQRTLHS-IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI 619
Cdd:TIGR03796 457 LLEEPEGSAATSEPPRRlsgYVELrnitfGYSPLEPPLIEnFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEI 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 620 AISG-------------TFAYVAQQAWILNATLRDNI-LFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANL 685
Cdd:TIGR03796 537 LFDGipreeiprevlanSVAMVDQDIFLFEGTVRDNLtLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANL 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 686 SGGQRQRISLARALYSDRSIYILDDPLSALDAHVgNHIFNSAIRKhlKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERG 765
Cdd:TIGR03796 617 SGGQRQRLEIARALVRNPSILILDEATSALDPET-EKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRG 693
|
250
....*....|...
gi 767925452 766 THEELMNLNGDYA 778
Cdd:TIGR03796 694 THEELWAVGGAYA 706
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
578-783 |
1.27e-28 |
|
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: 124.08 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 644
Cdd:TIGR01193 490 LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFslkdidrhtlrqfINYLPQEPYIFSGSILENLL 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 FG--KEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 722
Cdd:TIGR01193 570 LGakENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKK 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 723 IFNSAIRkhLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNN 783
Cdd:TIGR01193 650 IVNNLLN--LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
578-778 |
2.38e-28 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 122.24 E-value: 2.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLI-----------SAIL--GQ----MTL--LEGSIAIsgtfayVAQQAWILNAT 638
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLArllfrfydvtsGRILidGQdirdVTQasLRAAIGI------VPQDTVLFNDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 639 LRDNILFGK-EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:COG5265 448 IAYNIAYGRpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 718 HVGNHIfNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:COG5265 528 RTERAI-QAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYA 587
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
575-759 |
2.63e-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: 111.95 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTfayvaQQAWILNATLRDNIlfgkeydeery 654
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-----DIAKLPLEELRRRI----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 655 nsvlnscclrpdlAILPSsdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGnHIFNSAIRKHLKS 734
Cdd:cd00267 76 -------------GYVPQ------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR-ERLLELLRELAEE 129
|
170 180
....*....|....*....|....*..
gi 767925452 735 -KTVLFVTHQLQYLVD-CDEVIFMKEG 759
Cdd:cd00267 130 gRTVIIVTHDPELAELaADRVIVLKDG 156
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
563-772 |
4.61e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 114.52 E-value: 4.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 563 EGKHIHLGH---LRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FA 626
Cdd:COG1124 3 EVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrrrVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 627 YVAQQ-----------AWILNATLRdniLFGKEYDEERYNSVLNSCCLRPDLAilpssdlteiGERGANLSGGQRQRISL 695
Cdd:COG1124 83 MVFQDpyaslhprhtvDRILAEPLR---IHGLPDREERIAELLEQVGLPPSFL----------DRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 696 ARALYSDRSIYILDDPLSALDAHVGNHIFN--SAIRKHLKSkTVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEELM 771
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNllKDLREERGL-TYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVADLL 227
|
.
gi 767925452 772 N 772
Cdd:COG1124 228 A 228
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
272-466 |
2.36e-27 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350037 [Multi-domain] Cd Length: 291 Bit Score: 113.47 E-value: 2.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 272 SLGELINICSNDGQRMFEAAAVGSLLAGGPV--VAILGMIYNVIilGPTGFLGSAVFILFYPAMMFASRLTAYFRRKCVA 349
Cdd:cd18593 95 TVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLqlIAVIYILWFEI--GWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 350 ATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFDLT 429
Cdd:cd18593 173 RTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLGNILT 252
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767925452 430 AAQAFTVVTVFNS----MTFALkvtPFSVKSLSEASVAVDR 466
Cdd:cd18593 253 AERVFVTMALYNAvrltMTLFF---PFAIQFGSELSVSIRR 290
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1191-1308 |
4.81e-27 |
|
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: 110.78 E-value: 4.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1191 GEVTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 1270
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 767925452 1271 SIIPQEPVLFSGTVRSNLDPFNQY-TEDQIWDALERTHM 1308
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNaTDEEVIEAAKEAGA 118
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
578-772 |
4.94e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.92 E-value: 4.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------------FAYVAQQAWI-LNATLRDNIL 644
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrrrIGYVPQEPALyPDLTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 F-------GKEYDEERYNSVLNSCclrpdlailpssDLTE-IGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD 716
Cdd:COG1131 96 FfarlyglPRKEARERIDELLELF------------GLTDaADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 717 AhVGNHIFNSAIRKHLKS-KTVLFVTHQL---QYLvdCDEVIFMKEGCITERGTHEELMN 772
Cdd:COG1131 164 P-EARRELWELLRELAAEgKTVLLSTHYLeeaERL--CDRVAIIDKGRIVADGTPDELKA 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
578-778 |
1.05e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 116.98 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 644
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvtraslrrnIAVVFQDAGLFNRSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 FGKE--YDEErynsvlnsccLRPDLAILPSSDL---------TEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:PRK13657 431 VGRPdaTDEE----------MRAAAERAQAHDFierkpdgydTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 714 ALDAHVGNHIfNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:PRK13657 501 ALDVETEAKV-KAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFA 564
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
563-781 |
1.45e-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: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 563 EGKHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVA 629
Cdd:TIGR01192 336 EFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIdintvtreslrksIATVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 630 QQAWILNATLRDNILFGKE--YDEERYNSVLNSCCLRPDLAILPSSDlTEIGERGANLSGGQRQRISLARALYSDRSIYI 707
Cdd:TIGR01192 416 QDAGLFNRSIRENIRLGREgaTDEEVYEAAKAAAAHDFILKRSNGYD-TLVGERGNRLSGGERQRLAIARAILKNAPILV 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767925452 708 LDDPLSALDAHVGNHIFNsAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIF 781
Cdd:TIGR01192 495 LDEATSALDVETEARVKN-AIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL 567
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
914-1310 |
1.63e-26 |
|
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: 116.35 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 914 YASIYALSMAVMLILKAIRGvvfvkgtlrassrlhdELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF 993
Cdd:TIGR02203 72 FVSTYLLSWVSNKVVRDIRV----------------RMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 994 IQNVILVFFCVGMIAgVFPWFLVAVgpLVILFSVLHIVSRVLIRELKRLDNITQSPF--LSHITS-SIQGLATIHAYNkG 1070
Cdd:TIGR02203 136 VRETLTVIGLFIVLL-YYSWQLTLI--VVVMLPVLSILMRRVSKRLRRISKEIQNSMgqVTTVAEeTLQGYRVVKLFG-G 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1071 QEF-LHRYQELlddnqapfflfTCAMRWLAVRLD------------LISIALITTtgLMIVLMHGQIPPAYAGLAISYAV 1137
Cdd:TIGR02203 212 QAYeTRRFDAV-----------SNRNRRLAMKMTsagsisspitqlIASLALAVV--LFIALFQAQAGSLTAGDFTAFIT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1138 QLTGLFQFTVRLA---SETEARFTSVERINHYIKT-LSLEAPARIKNKApspdwpqEGEVTFENAEMRYRENLPLVLKKV 1213
Cdd:TIGR02203 279 AMIALIRPLKSLTnvnAPMQRGLAAAESLFTLLDSpPEKDTGTRAIERA-------RGDVEFRNVTFRYPGRDRPALDSI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1214 SFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DP 1290
Cdd:TIGR02203 352 SLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT 431
|
410 420
....*....|....*....|
gi 767925452 1291 fNQYTEDQIWDALERTHMKE 1310
Cdd:TIGR02203 432 -EQADRAEIERALAAAYAQD 450
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
570-772 |
1.81e-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: 116.00 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 570 GHLRLQR-----------TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------F 625
Cdd:COG4618 329 GRLSVENltvvppgskrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAdlsqwdreelgrhI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 626 AYVAQQAWILNATLRDNI-LFGKEYDEErynsVLNSCclrpDLA-----ILpssDL-----TEIGERGANLSGGQRQRIS 694
Cdd:COG4618 409 GYLPQDVELFDGTIAENIaRFGDADPEK----VVAAA----KLAgvhemIL---RLpdgydTRIGEGGARLSGGQRQRIG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 695 LARALYSDRSIYILDDPLSALDAhVGNHIFNSAIRkHLKS--KTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDD-EGEAALAAAIR-ALKArgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
578-772 |
2.67e-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: 109.36 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWI-LNATLRDNI 643
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaslsrrelarrIAYVPQEPPApFGLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 644 LFG-----------KEYDEERYNSVLNSCclrpdlailpssDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDP 711
Cdd:COG1120 97 ALGryphlglfgrpSAEDREAVEEALERT------------GLEHLADRPVDeLSGGERQRVLIARALAQEPPLLLLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 712 LSALDAHvgnHIFN--SAIRK--HLKSKTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEELMN 772
Cdd:COG1120 165 TSHLDLA---HQLEvlELLRRlaRERGRTVVMVLHDLnlaaRY---ADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
578-765 |
2.69e-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: 107.14 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIaisgtfayvaqqawilnatlrdnILFGKEYDEerynsv 657
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI-----------------------LLDGKDLAS------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 658 LNSCCLRPDLAILPSS----DLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIR-KH 731
Cdd:cd03214 66 LSPKELARKIAYVPQAlellGLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRlAR 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 767925452 732 LKSKTVLFVTHQL----QYlvdCDEVIFMKEGCITERG 765
Cdd:cd03214 146 ERGKTVVMVLHDLnlaaRY---ADRVILLKDGRIVAQG 180
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
578-761 |
4.19e-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: 106.15 E-value: 4.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 644
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSGSIAENIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 fgkeydeerynsvlnscclrpdlailpssdlteigerganlSGGQRQRISLARALYSDRSIYILDDPLSALDaHVGNHIF 724
Cdd:cd03246 98 -----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLD-VEGERAL 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 767925452 725 NSAIRkHLKSK--TVLFVTHQLQYLVDCDEVIFMKEGCI 761
Cdd:cd03246 136 NQAIA-ALKAAgaTRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1191-1306 |
4.61e-26 |
|
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: 107.68 E-value: 4.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1191 GEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 1270
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 767925452 1271 SIIPQEPVLFSGTVRSNLDPFNQYTEDQ-IWDALERT 1306
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDErILRAAELA 117
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
542-771 |
5.51e-26 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 114.37 E-value: 5.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 542 LAEQKGHLLLDS-DERPSPEEeegkhihlghlrlQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIA 620
Cdd:TIGR01842 310 LPEPEGHLSVENvTIVPPGGK-------------KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 621 ISG-------------TFAYVAQQAWILNATLRDNIL-FGKEYDEErynSVLNSCCLRP--DLAI-LPSSDLTEIGERGA 683
Cdd:TIGR01842 377 LDGadlkqwdretfgkHIGYLPQDVELFPGTVAENIArFGENADPE---KIIEAAKLAGvhELILrLPDGYDTVIGPGGA 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 684 NLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVGNHIFNSAIrKHLKSK--TVLFVTHQLQYLVDCDEVIFMKEGCI 761
Cdd:TIGR01842 454 TLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE-EGEQALANAI-KALKARgiTVVVITHRPSLLGCVDKILVLQDGRI 531
|
250
....*....|
gi 767925452 762 TERGTHEELM 771
Cdd:TIGR01842 532 ARFGERDEVL 541
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
564-765 |
6.04e-26 |
|
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: 107.59 E-value: 6.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 564 GKHIHLGHLRlQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAY 627
Cdd:cd03257 8 SVSFPTGGGS-VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkirrkeIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 628 VAQQA-----------WILNATLRdnILFGKEYDEERYNSVLNSCCLRPdlaiLPSSDLTEigeRGANLSGGQRQRISLA 696
Cdd:cd03257 87 VFQDPmsslnprmtigEQIAEPLR--IHGKLSKKEARKEAVLLLLVGVG----LPEEVLNR---YPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 697 RALYSDRSIYILDDPLSALDAHVGNHIFNsaIRKHLKSK---TVLFVTHQL---QYLvdCDEVIFMKEGCITERG 765
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILD--LLKKLQEElglTLLFITHDLgvvAKI--ADRVAVMYAGKIVEEG 228
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
916-1297 |
7.22e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 115.20 E-value: 7.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 916 SIYALSM--AVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF 993
Cdd:TIGR00958 203 AIFFMCLlsIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 994 IQNVILVFFCVGMIAGVFPWF----LVAVGPLVILFSVLHIVSRVLIRELKrlDNITQSPFLSHitSSIQGLATIHAY-N 1068
Cdd:TIGR00958 283 LRNLVMLLGLLGFMLWLSPRLtmvtLINLPLVFLAEKVFGKRYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFaA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1069 KGQEfLHRYQELLDDnqapfflftcaMRWLAVRLDLISIALITTTGLM------IVL-------MHGQIPpayAGLAIS- 1134
Cdd:TIGR00958 359 EEGE-ASRFKEALEE-----------TLQLNKRKALAYAGYLWTTSVLgmliqvLVLyyggqlvLTGKVS---SGNLVSf 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1135 --YAVQLTGLFQFTVRLASETEARFTSVERINHYI-KTLSLEAPARIknkAPSPDwpqEGEVTFENAEMRY--RENLPlV 1209
Cdd:TIGR00958 424 llYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLdRKPNIPLTGTL---APLNL---EGLIEFQDVSFSYpnRPDVP-V 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1210 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLD 1289
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIA 576
|
....*...
gi 767925452 1290 PFNQYTED 1297
Cdd:TIGR00958 577 YGLTDTPD 584
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
539-789 |
1.13e-25 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 113.66 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 539 QAVLAEQKGHLLLD-------SDERPSpeeeEGKHIHLGHLRL-----QRTLHSIDLEIQEGKLVGICGSVGSGKTSLIS 606
Cdd:PRK10790 310 QAVVAGERVFELMDgprqqygNDDRPL----QSGRIDIDNVSFayrddNLVLQNINLSVPSRGFVALVGHTGSGKSTLAS 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 607 AILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAILPSS 673
Cdd:PRK10790 386 LLMGYYPLTEGEIRLDGrplsslshsvlrqGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDG 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 674 DLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNS--AIRKHlksKTVLFVTHQLQYLVDCD 751
Cdd:PRK10790 466 LYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAlaAVREH---TTLVVIAHRLSTIVEAD 542
|
250 260 270
....*....|....*....|....*....|....*...
gi 767925452 752 EVIFMKEGCITERGTHEELMNLNGDYATIFNNLLLGET 789
Cdd:PRK10790 543 TILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEE 580
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
576-776 |
1.34e-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: 107.25 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGtFAYVAQQAWILNA--------------TLRD 641
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG-EDVRKEPREARRQigvlpderglydrlTVRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 642 NI-LFGKEYDEERYNsvlnsccLRPDLA-ILPSSDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSALDAh 718
Cdd:COG4555 94 NIrYFAELYGLFDEE-------LKKRIEeLIELLGLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 719 VGNHIFNSAIRKHLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMNLNGD 776
Cdd:COG4555 166 MARRLLREILRALKKEgKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
567-761 |
1.36e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.05 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 567 IHLGHLRLQRT----LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVA 629
Cdd:COG4619 1 LELEGLSFRVGgkpiLSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppewrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 630 QQAWILNATLRDNILF-----GKEYDEERYNSVLNSCCLRPDLAilpssdlteigERGA-NLSGGQRQRISLARALYSDR 703
Cdd:COG4619 81 QEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPDIL-----------DKPVeRLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767925452 704 SIYILDDPLSALDAHvgN-HIFNSAIRKHLKSK--TVLFVTH---QLQYLvdCDEVIFMKEGCI 761
Cdd:COG4619 150 DVLLLDEPTSALDPE--NtRRVEELLREYLAEEgrAVLWVSHdpeQIERV--ADRVLTLEAGRL 209
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
865-1167 |
2.44e-25 |
|
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: 107.69 E-value: 2.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 865 LFMLNVGSTAFSTWWLSYWikqgsgntTVTRGNETSvsdsmkdnPHMQYYASIYALSMAVMLILKAIRGVVFVKGTLRAS 944
Cdd:cd18559 7 LVLCNHVFSGPSNLWLLLW--------FDDPVNGPQ--------EHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 945 SRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF---IQNVILVFFcvgMIAGVFPWFLVAVgPL 1021
Cdd:cd18559 71 RAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWmgpLQNVIGLYL---LILLAGPMAAVGI-PL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1022 VILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRyQELLDDNQAPFFLFTCAMRWLAVR 1101
Cdd:cd18559 147 GLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQ-VDAKRDNELAYLPSIVYLRALAVR 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767925452 1102 LDLISIALITTTGLMIVLMHGQIpPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 1167
Cdd:cd18559 226 LWCVGPCIVLFASFFAYVSRHSL-AGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
578-756 |
4.17e-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: 105.94 E-value: 4.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------FAYVAQQA----WilnATLRDNILF 645
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgpdRGVVFQEPallpW---LTVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 646 G-------KEYDEERYNSVLNSCCLRPDLAILPSsdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDA- 717
Cdd:COG1116 104 GlelrgvpKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDAl 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767925452 718 ---HVGNHIFNsaIRKHLKsKTVLFVTHqlqylvDCDEVIFM 756
Cdd:COG1116 173 treRLQDELLR--LWQETG-KTVLFVTH------DVDEAVFL 205
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
578-761 |
7.21e-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: 102.86 E-value: 7.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAIsgtfayvaqqawilnatlrdnilFGKEYDEERyNSV 657
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-----------------------LGKDIKKEP-EEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 658 LNSCCLRPDLAILPSsDLTeiGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVGNHIFNSAIRKHLKS-KT 736
Cdd:cd03230 72 KRRIGYLPEEPSLYE-NLT--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELLRELKKEgKT 147
|
170 180
....*....|....*....|....*.
gi 767925452 737 VLFVTHQLQYLVD-CDEVIFMKEGCI 761
Cdd:cd03230 148 ILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
578-770 |
7.65e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 107.54 E-value: 7.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGqmtlLE----GSIAISGT--F----------AYVAQQAwilnA---- 637
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAG----LEtpdsGRIVLNGRdlFtnlpprerrvGFVFQHY----Alfph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 638 -TLRDNILFG-------KEYDEERYNSVLnscclrpDLAilpssDLTEIGER-GANLSGGQRQRISLARALYSDRSIYIL 708
Cdd:COG1118 90 mTVAENIAFGlrvrppsKAEIRARVEELL-------ELV-----QLEGLADRyPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767925452 709 DDPLSALDAHVgnhifnsaiRKHLKSK----------TVLFVTHQLQ--YLVdCDEVIFMKEGCITERGTHEEL 770
Cdd:COG1118 158 DEPFGALDAKV---------RKELRRWlrrlhdelggTTVFVTHDQEeaLEL-ADRVVVMNQGRIEQVGTPDEV 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
578-753 |
7.95e-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: 103.71 E-value: 7.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------------FAYVAQQ-AWILNATLRDNIL 644
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdaredyrrrLAYLGHAdGLKPELTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 F-----GKEYDEERYNSVLnscclrpdlAILpssDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDAH 718
Cdd:COG4133 98 FwaalyGLRADREAIDEAL---------EAV---GLAGLADLpVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 767925452 719 vGNHIFNSAIRKHLKS-KTVLFVTHQLQYLVDCDEV 753
Cdd:COG4133 166 -GVALLAELIAAHLARgGAVLLTTHQPLELAAARVL 200
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
577-759 |
9.47e-25 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 103.70 E-value: 9.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 577 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAYVAQQawILNATL 639
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltklslkelrrkvglvFQNPDDQ--FFGPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 640 RDNILFGKE---YDEERYNSVLNSCCLRPDLAILPSSDLteigergANLSGGQRQRISLARALYSDRSIYILDDPLSALD 716
Cdd:cd03225 94 EEEVAFGLEnlgLPEEEIEERVEEALELVGLEGLRDRSP-------FTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767925452 717 AHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEG 759
Cdd:cd03225 167 PAGRRELLELLKKLKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
575-761 |
1.22e-24 |
|
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: 103.37 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQaWIL--NATLRD 641
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMVFQD-YALfpHLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 642 NILFG----KEYDEERYNSVLNScclrpdLAILpssDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALD 716
Cdd:cd03259 92 NIAFGlklrGVPKAEIRARVREL------LELV---GLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767925452 717 AHVgnhifNSAIRKHLKS------KTVLFVTH-QLQYLVDCDEVIFMKEGCI 761
Cdd:cd03259 163 AKL-----REELREELKElqrelgITTIYVTHdQEEALALADRIAVMNEGRI 209
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
918-1307 |
2.13e-24 |
|
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: 109.91 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 918 YALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTG---RILNRFSKDMDEVdVRlpfqaeMFI 994
Cdd:COG5265 84 YGLLRLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGglsRDIERGTKGIEFL-LR------FLL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 995 QNVILVFFCVGMIAGVF-----PWF----LVAVGpLVILFSVLHIVSRV-LIRELKRLDNITQSpflsHITSSIQGLATI 1064
Cdd:COG5265 157 FNILPTLLEIALVAGILlvkydWWFalitLVTVV-LYIAFTVVVTEWRTkFRREMNEADSEANT----RAVDSLLNYETV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1065 HAYNkGQEF-LHRYQELLDDnqapfflFTCAMRWLAVRLDLISI--ALITTTGLMIVL-------MHGQIPPAYAGLAIS 1134
Cdd:COG5265 232 KYFG-NEAReARRYDEALAR-------YERAAVKSQTSLALLNFgqALIIALGLTAMMlmaaqgvVAGTMTVGDFVLVNA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1135 YAVQLT---GLFQFTVRlasETEARFTSVERInhyiKTLsLEAPARIKNKAPSPDWP-QEGEVTFENAEMRYRENLPlVL 1210
Cdd:COG5265 304 YLIQLYiplNFLGFVYR---EIRQALADMERM----FDL-LDQPPEVADAPDAPPLVvGGGEVRFENVSFGYDPERP-IL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1211 KKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLdp 1290
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI-- 452
|
410 420
....*....|....*....|..
gi 767925452 1291 fnQY-----TEDQIWDALERTH 1307
Cdd:COG5265 453 --AYgrpdaSEEEVEAAARAAQ 472
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
578-756 |
2.87e-24 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 102.55 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------FAYVAQQA----WilnATLRDNILF 645
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQQDallpW---LTVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 646 GkeydeerynsvlnscclrPDLAILPSSDLTEIGER---------GAN-----LSGGQRQRISLARALYSDRSIYILDDP 711
Cdd:cd03293 97 G------------------LELQGVPKAEARERAEEllelvglsgFENayphqLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767925452 712 LSALDAHVGNHIFN--SAIRKHLKsKTVLFVTHqlqylvDCDEVIFM 756
Cdd:cd03293 159 FSALDALTREQLQEelLDIWRETG-KTVLLVTH------DIDEAVFL 198
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1191-1309 |
2.95e-24 |
|
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: 104.17 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1191 GEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGcIKIDGVRISDIGLADLRSKL 1270
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGD-IQIDGVSWNSVPLQKWRKAF 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 767925452 1271 SIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMK 1309
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLK 118
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
574-766 |
3.35e-24 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 102.11 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 574 LQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLR 640
Cdd:cd03369 20 LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 641 DNILFGKEYDEERYNSVLnscclrpdlailpssdltEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVg 720
Cdd:cd03369 100 SNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767925452 721 NHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGT 766
Cdd:cd03369 161 DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
578-772 |
4.68e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 108.07 E-value: 4.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYVAQ----QawiLNA 637
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdltklsrrslrelrrrVQMVFQdpysS---LNP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 638 --TLRDNILFG--------KEYDEERYNSVLNSCCLRPDLAilpssdlteiGERGANLSGGQRQRISLARALYSDRSIYI 707
Cdd:COG1123 358 rmTVGDIIAEPlrlhgllsRAERRERVAELLERVGLPPDLA----------DRYPHELSGGQRQRVAIARALALEPKLLI 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 708 LDDPLSALDAHVGNHIFN--SAIRKHLKsKTVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEELMN 772
Cdd:COG1123 428 LDEPTSALDVSVQAQILNllRDLQRELG-LTYLFISHDLA-VVRyiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
575-772 |
5.29e-24 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 102.19 E-value: 5.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYVAQQAWILNA- 637
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSGALFDSl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 638 TLRDNILF--------GKEYDEERYNSVLNSCCLRPDLAILPssdlteigergANLSGGQRQRISLARALYSDRSIYILD 709
Cdd:cd03261 93 TVFENVAFplrehtrlSEEEIREIVLEKLEAVGLRGAEDLYP-----------AELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767925452 710 DPLSALDAhVGNHIFNSAIRKHLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:cd03261 162 EPTAGLDP-IASGVIDDLIRSLKKELglTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
578-713 |
6.87e-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: 99.26 E-value: 6.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNA-TLRDNI 643
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkeIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767925452 644 LFG-------KEYDEERYNSVLNScclrpdLAILPSSDlTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:pfam00005 81 RLGlllkglsKREKDARAEEALEK------LGLGDLAD-RPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1193-1310 |
1.52e-23 |
|
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: 100.77 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 1272
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 767925452 1273 IPQEPVLFSGTVRSNLdpfnQY-----TEDQIWDALERTHMKE 1310
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHD 118
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1193-1310 |
6.30e-23 |
|
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: 99.23 E-value: 6.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 1272
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 767925452 1273 IPQEPVLFSGTVRSNLdpfnQY-----TEDQIWDALERTHMKE 1310
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHE 119
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
576-772 |
1.01e-22 |
|
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: 98.57 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFA-----------YVAQQ-AWILNATLRDNI 643
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAtdvpvqernvgFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 644 LFGKEYDEERYnsvlnscclRPDLA--------ILPSSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:cd03296 96 AFGLRVKPRSE---------RPPEAeirakvheLLKLVQLDWLADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 715 LDAHVgnhifnsaiRKHLKS----------KTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:cd03296 167 LDAKV---------RKELRRwlrrlhdelhVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
572-765 |
3.82e-22 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 96.21 E-value: 3.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 572 LRLQRTLHSIDLEIQ---EGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAYVAQQ 631
Cdd:cd03297 4 VDIEKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlppqqrkIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 632 AWIL-NATLRDNILFGkeydeerynsvLNSCCLRPDL----AILPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSI 705
Cdd:cd03297 84 YALFpHLNVRENLAFG-----------LKRKRNREDRisvdELLDLLGLDHLLNRYpAQLSGGEKQRVALARALAAQPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 706 YILDDPLSALDAHVGNHIFN--SAIRKHLKsKTVLFVTH---QLQYLvdCDEVIFMKEGCITERG 765
Cdd:cd03297 153 LLLDEPFSALDRALRLQLLPelKQIKKNLN-IPVIFVTHdlsEAEYL--ADRIVVMEDGRLQYIG 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
565-759 |
4.12e-22 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 96.02 E-value: 4.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 565 KHIHLGHLRLQrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAY 627
Cdd:cd03255 8 KTYGGGGEKVQ-ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrrrhIGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 628 VAQQAWILNA-TLRDNILFG-------KEYDEERYNSVLNSCCLRPDLAILPSsdlteigergaNLSGGQRQRISLARAL 699
Cdd:cd03255 87 VFQSFNLLPDlTALENVELPlllagvpKKERRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 700 YSDRSIYILDDPLSALDAHVGNHIFNsAIRK--HLKSKTVLFVTHQLQYLVDCDEVIFMKEG 759
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVME-LLRElnKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
578-771 |
4.17e-22 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 96.63 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG------TFAYVAQQAWIL---------NATLRDN 642
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkkNLRELRRKVGLVfqnpddqlfAPTVEED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 643 ILFG-------KEYDEERYNSVLNSCclrpdlailpssDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:COG1122 97 VAFGpenlglpREEIRERVEEALELV------------GLEHLADRPpHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 715 LDAHVGNHIFNsAIRK-HLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 771
Cdd:COG1122 165 LDPRGRRELLE-LLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
855-1314 |
7.37e-22 |
|
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: 101.21 E-value: 7.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 855 GPLAFLVIMALfmLNVGSTAFSTWWLSY----WIKQGSGNTTVTRgnetsvsdsmkdnphmqyYASIYALSMAVMLILKA 930
Cdd:TIGR02857 3 RALALLALLGV--LGALLIIAQAWLLARvvdgLISAGEPLAELLP------------------ALGALALVLLLRALLGW 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 931 IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDvrlPFQAEMFIQNVILVFFCVGMIAGV 1010
Cdd:TIGR02857 63 LQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALD---GYFARYLPQLVLAVIVPLAILAAV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1011 FP--W----FLVAVGPLVILFSVL--HIVSRVLIRELKRLDNITqspflSHITSSIQGLATIHAYNKGqeflHRYQELLD 1082
Cdd:TIGR02857 140 FPqdWisglILLLTAPLIPIFMILigWAAQAAARKQWAALSRLS-----GHFLDRLRGLPTLKLFGRA----KAQAAAIR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1083 DNQAPF-----------FLFTCAMRWLAVrldlISIALITTT-GLMivLMHGQIPPAYAGLAISYAVQltglFQFTVR-L 1149
Cdd:TIGR02857 211 RSSEEYrertmrvlriaFLSSAVLELFAT----LSVALVAVYiGFR--LLAGDLDLATGLFVLLLAPE----FYLPLRqL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1150 ASETEARFTSVERINHyIKTLsLEAPARIK-NKAPSPdWPQEGEVTFENAEMRYrENLPLVLKKVSFTIKPKEKIGIVGR 1228
Cdd:TIGR02857 281 GAQYHARADGVAAAEA-LFAV-LDAAPRPLaGKAPVT-AAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGP 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1229 TGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALER 1305
Cdd:TIGR02857 357 SGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRP--DASDAEIREALER 434
|
....*....
gi 767925452 1306 THMKECDSS 1314
Cdd:TIGR02857 435 AGLDEFVAA 443
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
576-770 |
1.05e-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: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQaWIL--NATLRDN 642
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtdlppkdrnIAMVFQS-YALypHMTVYEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 643 ILFG----KEYDEERYNSVLNScclrpdLAILpssDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:COG3839 96 IAFPlklrKVPKAEIDRRVREA------AELL---GLEDLLDRkPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 718 HVGNHifnsaIRKHLKS------KTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:COG3839 167 KLRVE-----MRAEIKRlhrrlgTTTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
578-759 |
1.28e-21 |
|
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: 93.41 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT---------------FAYVAQQaWIL--NATLR 640
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdltdledelpplrrrIGMVFQD-FALfpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 641 DNILFGkeydeerynsvlnscclrpdlailpssdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAhvg 720
Cdd:cd03229 95 ENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDP--- 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767925452 721 nhIFNSAIRKHLKS------KTVLFVTHQLQYLVD-CDEVIFMKEG 759
Cdd:cd03229 134 --ITRREVRALLKSlqaqlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
576-778 |
5.66e-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: 99.26 E-value: 5.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDN 642
Cdd:TIGR03797 467 LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGqdlagldvqavrrQLGVVLQNGRLMSGSIFEN 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 643 ILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD----AH 718
Cdd:TIGR03797 547 IAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDnrtqAI 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 719 VgnhifnSAIRKHLKSkTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:TIGR03797 627 V------SESLERLKV-TRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFA 679
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
578-763 |
8.97e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 92.41 E-value: 8.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISaILGqmTLL---EGSIAISGT-----------------FAYVAQQAWIL-N 636
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILG--GLDrptSGEVLIDGQdisslserelarlrrrhIGFVFQFFNLLpE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 637 ATLRDNILF-------GKEYDEERYNSVLnscclrpdlailpssDLTEIGERG----ANLSGGQRQRISLARALYSDRSI 705
Cdd:COG1136 101 LTALENVALplllagvSRKERRERARELL---------------ERVGLGDRLdhrpSQLSGGQQQRVAIARALVNRPKL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 706 YILDDPLSALDAHVGNHIFNsAIRKHLKS--KTVLFVTHQLQYLVDCDEVIFMKEGCITE 763
Cdd:COG1136 166 ILADEPTGNLDSKTGEEVLE-LLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1193-1288 |
1.07e-20 |
|
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: 92.55 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 1272
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90
....*....|....*.
gi 767925452 1273 IPQEPVLFSGTVRSNL 1288
Cdd:cd03252 81 VLQENVLFNRSIRDNI 96
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
578-770 |
1.22e-20 |
|
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: 92.26 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYVAQQAWILNA-TLR 640
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllsgkelrkarrrIGMIFQHFNLLSSrTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 641 DNILF-------GKEYDEERYNSVLNscclrpdlailpssdLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILD 709
Cdd:cd03258 101 ENVALpleiagvPKAEIEERVLELLE---------------LVGLEDKAdaypAQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767925452 710 DPLSALDAHVGNHIFN--SAIRKHLKSkTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 770
Cdd:cd03258 166 EATSALDPETTQSILAllRDINRELGL-TIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
576-772 |
1.73e-20 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 96.90 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILG---QMTLLEGSIAISGT-------------FAYVAQQAWI-LN-A 637
Cdd:COG1123 20 PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRdllelsealrgrrIGMVFQDPMTqLNpV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 638 TLRDNILFGKEYD----EERYNSVLnscclrpdlAILPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:COG1123 100 TVGDQIAEALENLglsrAEARARVL---------ELLEAVGLERRLDRYpHQLSGGQRQRVAIAMALALDPDLLIADEPT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925452 713 SALDAHVGNHIFnSAIRKHLK--SKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:COG1123 171 TALDVTTQAEIL-DLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
578-761 |
1.92e-20 |
|
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: 91.76 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNIL 644
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhsKVSLVGQEPVLFARSLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 FG-KEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGNHI 723
Cdd:cd03248 110 YGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SEQQ 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 767925452 724 FNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCI 761
Cdd:cd03248 189 VQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1210-1323 |
2.21e-20 |
|
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: 88.86 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1210 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSG-TVRSNL 1288
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 767925452 1289 -------DPFNQYTEDQIWDALERTHMKECDSSHLKNKFCSL 1323
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGLGDLADRPVGERPGTL 122
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1193-1288 |
2.40e-20 |
|
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: 91.83 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRY--RENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 1270
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90
....*....|....*...
gi 767925452 1271 SIIPQEPVLFSGTVRSNL 1288
Cdd:cd03249 80 GLVSQEPVLFDGTIAENI 97
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
239-467 |
2.54e-20 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350042 [Multi-domain] Cd Length: 288 Bit Score: 93.00 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 239 TWALNyRTGVRLRGAILTMAFKK--ILKLKNIKEKSLGELINICSNDGQRMfeAAAVGSL--LAGGPV-VAI-LGMIY-- 310
Cdd:cd18598 59 NFQMN-KVSLKVRAALVTAVYRKalRVRSSSLSKFSTGEIVNLMSTDADRI--VNFCPSFhdLWSLPLqIIVaLYLLYqq 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 311 -NVIILGptgflGSAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEER 389
Cdd:cd18598 136 vGVAFLA-----GLVFALVLIPINKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKEL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 390 RILEKAGYFQSITV---GVAPIVVviaSVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 466
Cdd:cd18598 211 KALKGRKYLDALCVyfwATTPVLI---SILTFATYVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKR 287
|
.
gi 767925452 467 F 467
Cdd:cd18598 288 L 288
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
578-770 |
3.20e-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: 3.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQAwilnA-----TLRD 641
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQDY----AlfphlTVAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 642 NILFG-------KEYDEERYNSVLnscclrpdlailpssDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILDD 710
Cdd:COG3842 97 NVAFGlrmrgvpKAEIRARVAELL---------------ELVGLEGLAdrypHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925452 711 PLSALDAHVGNHIfNSAIRKHLKS--KTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:COG3842 162 PLSALDAKLREEM-REELRRLQRElgITFIYVTHdQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
567-776 |
3.22e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 90.97 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 567 IHLGHLRLQrtlhsIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVAQ-------QAWILN 636
Cdd:COG3840 9 YRYGDFPLR-----FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdlTALPPAErpvsmlfQENNLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 637 A--TLRDNILFGkeydeerynsvlnsccLRPDL-----------AILPSSDLTEIGER-GANLSGGQRQRISLARALYSD 702
Cdd:COG3840 84 PhlTVAQNIGLG----------------LRPGLkltaeqraqveQALERVGLAGLLDRlPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 703 RSIYILDDPLSALDAhvgnhifnsAIRK---HLKSK-------TVLFVTHQLQylvD----CDEVIFMKEGCITERGTHE 768
Cdd:COG3840 148 RPILLLDEPFSALDP---------ALRQemlDLVDElcrerglTVLMVTHDPE---DaariADRVLLVADGRIAADGPTA 215
|
....*...
gi 767925452 769 ELMNLNGD 776
Cdd:COG3840 216 ALLDGEPP 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
575-770 |
3.65e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 91.35 E-value: 3.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAIlgqmTLLE---------GSIAISGTFAYVAQQAWILNatLRDNILF 645
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI----NLLEqpeagtirvGDITIDTARSLSQQKGLIRQ--LRQHVGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 646 -GKEYDEERYNSVLNSCCLRP--------DLAI-LPSSDLTEIGERGAN------LSGGQRQRISLARALYSDRSIYILD 709
Cdd:PRK11264 90 vFQNFNLFPHRTVLENIIEGPvivkgepkEEATaRARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925452 710 DPLSALDAHVGNHIFNSaIRKHLKSK-TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 770
Cdd:PRK11264 170 EPTSALDPELVGEVLNT-IRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
578-770 |
4.11e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.61 E-value: 4.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQ-AWILNATLRDNILF 645
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 646 GKEYDEERYnsvlnscclRPDLAILPSS--------DLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALD 716
Cdd:PRK10851 98 GLTVLPRRE---------RPNAAAIKAKvtqllemvQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767925452 717 AHVGNHIfNSAIRK-HLKSK-TVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:PRK10851 169 AQVRKEL-RRWLRQlHEELKfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
530-775 |
1.49e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 95.81 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 530 VRQLQRTEHQAVLAEQKGHLL--------LDSDERPSPEEEEGKHIHLG--HLR----LQRTLHSIDLEIQEGKLVGICG 595
Cdd:PLN03232 1190 LRQASKAENSLNSVERVGNYIdlpseataIIENNRPVSGWPSRGSIKFEdvHLRyrpgLPPVLHGLSFFVSPSEKVGVVG 1269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 596 SVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNILFGKEYDEERYNSVLNSCC 662
Cdd:PLN03232 1270 RTGAGKSSMLNALFRIVELEKGRIMIDDcdvakfgltdlrrVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAH 1349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 663 LRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVgNHIFNSAIRKHLKSKTVLFVTH 742
Cdd:PLN03232 1350 IKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT-DSLIQRTIREEFKSCTMLVIAH 1428
|
250 260 270
....*....|....*....|....*....|...
gi 767925452 743 QLQYLVDCDEVIFMKEGCITERGTHEELMNLNG 775
Cdd:PLN03232 1429 RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
578-770 |
2.20e-19 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 88.39 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAI-----LGQMTLLEGSIAISG---------------TFAYVAQQAWILNA 637
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGkdiydldvdvlelrrRVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 638 TLRDNILFG--------KEYDEERYNSVLnscclrpDLAILPssdlTEIGER--GANLSGGQRQRISLARALYSDRSIYI 707
Cdd:cd03260 96 SIYDNVAYGlrlhgiklKEELDERVEEAL-------RKAALW----DEVKDRlhALGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767925452 708 LDDPLSALDAhVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEEL 770
Cdd:cd03260 165 LDEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1158-1305 |
2.46e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 93.74 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1158 TSVERINHYIktlslEAPARIKNKAPSPDWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLG 1237
Cdd:PRK11160 309 ASARRINEIT-----EQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 1238 MALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALER 1305
Cdd:PRK11160 384 QLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQ 452
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
578-759 |
3.90e-19 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 86.84 E-value: 3.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTL--LEGSIAISGT----------FAYVAQQ-AWILNATLRDNIL 644
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRpldkrsfrkiIGYVPQDdILHPTLTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 FgkeydeerynsvlnSCCLRpdlailpssdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIF 724
Cdd:cd03213 105 F--------------AAKLR-------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 767925452 725 nSAIRKHLKS-KTVLFVTHQLQYLV--DCDEVIFMKEG 759
Cdd:cd03213 152 -SLLRRLADTgRTIICSIHQPSSEIfeLFDKLLLLSQG 188
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
574-775 |
6.05e-19 |
|
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: 93.86 E-value: 6.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 574 LQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLR 640
Cdd:TIGR00957 1298 LDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLniakiglhdlrfkITIIPQDPVLFSGSLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 641 DNILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 720
Cdd:TIGR00957 1378 MNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 721 NHIfNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNG 775
Cdd:TIGR00957 1458 NLI-QSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRG 1511
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
565-770 |
8.95e-19 |
|
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: 87.24 E-value: 8.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 565 KHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYV 628
Cdd:cd03256 4 ENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 629 AQQ-AWILNATLRDNILFGK-------------EYDEERYNSvlnscclrpdLAILPSSDLTE-IGERGANLSGGQRQRI 693
Cdd:cd03256 84 FQQfNLIERLSVLENVLSGRlgrrstwrslfglFPKEEKQRA----------LAALERVGLLDkAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 694 SLARALYSDRSIYILDDPLSALD---AHVGNHIFNSAIRKHlkSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEE 769
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDpasSRQVMDLLKRINREE--GITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAE 231
|
.
gi 767925452 770 L 770
Cdd:cd03256 232 L 232
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
244-466 |
1.55e-18 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 87.66 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 244 YRTGVRLRGAILTMAFKKILKLKNIKEKS--LGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFL 321
Cdd:cd18559 63 SIGGIFASRAVHLDLYHKALRSPISFFERtpSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 322 GSAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGYFQSI 401
Cdd:cd18559 143 GIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRAL 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767925452 402 TVGVAPIVVVIASVVTFSVHMTLGFD--LTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 466
Cdd:cd18559 223 AVRLWCVGPCIVLFASFFAYVSRHSLagLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
566-771 |
1.69e-18 |
|
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: 89.00 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 566 HIHLGHLRLQrtlhsIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAYV 628
Cdd:COG4148 8 RLRRGGFTLD-----VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsargiflpphrrrIGYV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 629 AQQAwILNATL--RDNILFGkeydeeRYNSVLNSCCLRPDLAIlpssDLTEIG---ERG-ANLSGGQRQRISLARALYSD 702
Cdd:COG4148 83 FQEA-RLFPHLsvRGNLLYG------RKRAPRAERRISFDEVV----ELLGIGhllDRRpATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 703 RSIYILDDPLSALDAHvgnhifnsaiRKH--------LKSKT---VLFVTHQL---QYLvdCDEVIFMKEGCITERGTHE 768
Cdd:COG4148 152 PRLLLMDEPLAALDLA----------RKAeilpylerLRDELdipILYVSHSLdevARL--ADHVVLLEQGRVVASGPLA 219
|
...
gi 767925452 769 ELM 771
Cdd:COG4148 220 EVL 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
554-743 |
2.67e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 90.25 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 554 DERPSPEEEEGKHIHLGHLRLQR-----TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGqmtlL----EGSIAI--S 622
Cdd:COG4178 350 EAASRIETSEDGALALEDLTLRTpdgrpLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG----LwpygSGRIARpaG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 623 GTFAYVAQQAWILNATLRDNILF---GKEYDEERYNSVLNSCCLrPDLAilpsSDLTEIGERGANLSGGQRQRISLARAL 699
Cdd:COG4178 426 ARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGL-GHLA----ERLDEEADWDQVLSLGEQQRLAFARLL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767925452 700 YSDRSIYILDDPLSALDAHVGNHIFnSAIRKHLKSKTVLFVTHQ 743
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALY-QLLREELPGTTVISVGHR 543
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
574-780 |
3.13e-18 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 86.12 E-value: 3.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 574 LQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLR 640
Cdd:cd03288 33 LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIdisklplhtlrsrLSIILQDPILFSGSIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 641 DNILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 720
Cdd:cd03288 113 FNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 721 NhIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELM-NLNGDYATI 780
Cdd:cd03288 193 N-ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASL 252
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1193-1288 |
3.40e-18 |
|
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: 83.52 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGlADLRSKLSI 1272
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90
....*....|....*.
gi 767925452 1273 IPQEPVLFSGTVRSNL 1288
Cdd:cd03247 80 LNQRPYLFDTTLRNNL 95
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
577-765 |
5.17e-18 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 84.23 E-value: 5.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 577 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-----------TFAYVAQQ-AWILNATLRDNIL 644
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 FG-------KEYDEERYNSVlnscclrpdlailpsSDLTEIGE----RGANLSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:cd03301 95 FGlklrkvpKDEIDERVREV---------------AELLQIEHlldrKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 714 ALDAHVgnhifNSAIRKHLKS------KTVLFVTH-QLQYLVDCDEVIFMKEGCITERG 765
Cdd:cd03301 160 NLDAKL-----RVQMRAELKRlqqrlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
580-772 |
6.47e-18 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 84.66 E-value: 6.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 580 SIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWIL-NATLRDNI-- 643
Cdd:cd03295 19 NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFpHMTVEENIal 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 644 ---LFG--KEYDEERYNSVLNSCCLRPdlailpssdlTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:cd03295 99 vpkLLKwpKEKIRERADELLALVGLDP----------AEFADRyPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 718 hvgnhIFNSAIR---KHLKS---KTVLFVTHQLQ-YLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:cd03295 169 -----ITRDQLQeefKRLQQelgKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
565-756 |
7.38e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 84.91 E-value: 7.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 565 KHIHL---GHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------FAYVAQQ-- 631
Cdd:COG4525 7 RHVSVrypGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVpvtgpgadRGVVFQKda 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 632 --AWiLNAtlRDNILFGKeydeeRYNSVLNSCCLRPDLAILPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYIL 708
Cdd:COG4525 87 llPW-LNV--LDNVAFGL-----RLRGVPKAERRARAEELLALVGLADFARRRiWQLSGGMRQRVGIARALAADPRFLLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767925452 709 DDPLSALDA----HVGNHIFNSAIRKHlksKTVLFVTHqlqylvDCDEVIFM 756
Cdd:COG4525 159 DEPFGALDAltreQMQELLLDVWQRTG---KGVFLITH------SVEEALFL 201
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
578-754 |
9.66e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 82.67 E-value: 9.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG--TFAYVAQQ---AWILNATLRDNI---LFGKEY 649
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVamgRWARRG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 650 DEERYN----SVLNSCCLRPDLAILPSSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN 725
Cdd:NF040873 88 LWRRLTrddrAAVDDALERVGLADLAGRQLGE-------LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180
....*....|....*....|....*....
gi 767925452 726 SAIRKHLKSKTVLFVTHQLQYLVDCDEVI 754
Cdd:NF040873 161 LLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
950-1305 |
1.07e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 88.48 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 950 ELFRRILRSPMKFFDTTPTGRILNRFSKDMDEV-DVRLPFQAEMFIQNVILVFFCVgmIAGVFPWFLVAVgpLVILFSVL 1028
Cdd:PRK13657 94 EYFERIIQLPLAWHSQRGSGRALHTLLRGTDALfGLWLEFMREHLATLVALVVLLP--LALFMNWRLSLV--LVVLGIVY 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1029 HIVSRVLIRELKRLDNITQ---SPFLSHITSSIQGLATIHAYNKGQ---EFLHRYQELLDDNQAPfflftcAMRWLAVRL 1102
Cdd:PRK13657 170 TLITTLVMRKTKDGQAAVEehyHDLFAHVSDAIGNVSVVQSYNRIEaetQALRDIADNLLAAQMP------VLSWWALAS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1103 DL------ISIALITTTGLMIVLmHGQIPP----AYAGLAISYAVQLTGLFQFTVRLasetearFTSVERINHYIKTLsl 1172
Cdd:PRK13657 244 VLnraastITMLAILVLGAALVQ-KGQLRVgevvAFVGFATLLIGRLDQVVAFINQV-------FMAAPKLEEFFEVE-- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1173 EAPARIKNKAPSPDWPQ-EGEVTFENAEMRYrENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCI 1251
Cdd:PRK13657 314 DAVPDVRDPPGAIDLGRvKGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 1252 KIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL-----DPfnqyTEDQIWDALER 1305
Cdd:PRK13657 393 LIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAAAER 447
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
578-772 |
1.16e-17 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 84.62 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAYVAQQ-AWILNATL 639
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaamsrkelrelrrkkISMVFQSfALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 640 RDNILFG-------KEYDEERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:cd03294 120 LENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767925452 713 SALDahvgnhifnSAIRKHLKS----------KTVLFVTHqlqylvDCDEVI-------FMKEGCITERGTHEELMN 772
Cdd:cd03294 189 SALD---------PLIRREMQDellrlqaelqKTIVFITH------DLDEALrlgdriaIMKDGRLVQVGTPEEILT 250
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
563-762 |
1.36e-17 |
|
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: 82.69 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 563 EGKHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG----------TFAYVAQQA 632
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 633 wilnatlrDNILFGkeydeeryNSVLNSCCLRPDLA---------ILPSSDLTEIGERG-ANLSGGQRQRISLARALYSD 702
Cdd:cd03226 81 --------DYQLFT--------DSVREELLLGLKELdagneqaetVLKDLDLYALKERHpLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767925452 703 RSIYILDDPLSALDAH----VGNHIfnsairKHLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCIT 762
Cdd:cd03226 145 KDLLIFDEPTSGLDYKnmerVGELI------RELAAqgKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
581-771 |
2.57e-17 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 85.16 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 581 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAYVAQQAWIL-NATLRDN 642
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiflppekrrIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 643 ILFGK-----EYDEERYNSVLNSCCLRPDLAILPssdlteigergANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:TIGR02142 96 LRYGMkrarpSERRISFERVIELLGIGHLLGRLP-----------GRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767925452 718 HVGNHI--FNSAIRKHLKSKtVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 771
Cdd:TIGR02142 165 PRKYEIlpYLERLHAEFGIP-ILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVW 220
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
850-1310 |
2.68e-17 |
|
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: 87.16 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 850 IQAAGGPLAFLVIMALFmlnvgSTAFSTWWLSYwIkqgsgNTTVTRGNETSVSdsmkdnphmqyYASIYALSMAVMLILK 929
Cdd:COG4615 8 LRESRWLLLLALLLGLL-----SGLANAGLIAL-I-----NQALNATGAALAR-----------LLLLFAGLLVLLLLSR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 930 AIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMD---EVDVRLPFqaemFIQNVILVFFCVGM 1006
Cdd:COG4615 66 LASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRtisQAFVRLPE----LLQSVALVLGCLAY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1007 IAgvfpW-----FLVAVGPLVILFSVLHIVSRVLIRELKRLDNiTQSPFLSHITSSIQGLA--TIHAyNKGQEFLHRY-- 1077
Cdd:COG4615 142 LA----WlspplFLLTLVLLGLGVAGYRLLVRRARRHLRRARE-AEDRLFKHFRALLEGFKelKLNR-RRRRAFFDEDlq 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1078 ---QELLDDNQAPFFLFTCAMRWlavrldlISIALITTTGLmIVLMHGQIPPAYAGLAISYAvqLTGLF------QFTVR 1148
Cdd:COG4615 216 ptaERYRDLRIRADTIFALANNW-------GNLLFFALIGL-ILFLLPALGWADPAVLSGFV--LVLLFlrgplsQLVGA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1149 LASETEARfTSVERINHYikTLSLEAPARIKNKAPSPDWPQE-GEVTFENAEMRYR---ENLPLVLKKVSFTIKPKEKIG 1224
Cdd:COG4615 286 LPTLSRAN-VALRKIEEL--ELALAAAEPAAADAAAPPAPADfQTLELRGVTYRYPgedGDEGFTLGPIDLTIRRGELVF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1225 IVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFsgtvRSNLDPFNQYTEDQIWDALE 1304
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADPARARELLE 438
|
....*.
gi 767925452 1305 RTHMKE 1310
Cdd:COG4615 439 RLELDH 444
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
578-772 |
3.52e-17 |
|
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: 82.38 E-value: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQ-AWILNATLRDNILF 645
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 646 G----KEYDEERYNSVLNsccLRPDLAIlpssdlTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVg 720
Cdd:cd03299 95 GlkkrKVDKKEIERKVLE---IAEMLGI------DHLLNRKpETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 721 nhifNSAIRKHLK------SKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:cd03299 165 ----KEKLREELKkirkefGVTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1190-1288 |
3.57e-17 |
|
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: 82.13 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1190 EGEVTFENAEMRYReNLP--LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLR 1267
Cdd:cd03248 9 KGIVKFQNVTFAYP-TRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100
....*....|....*....|.
gi 767925452 1268 SKLSIIPQEPVLFSGTVRSNL 1288
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNI 108
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
953-1304 |
4.89e-17 |
|
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: 86.72 E-value: 4.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 953 RRILRSPMKFFDTTPTGRILNRFSKDMDEVDVrlpfqaemfIQNVIL-VFFCVGMIAGVfPWFLVAVGPLVILFSVLHIV 1031
Cdd:TIGR01193 237 KHLFELPMSFFSTRRTGEIVSRFTDASSIIDA---------LASTILsLFLDMWILVIV-GLFLVRQNMLLFLLSLLSIP 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1032 SRVLI-----RELKRLDN---ITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCA---MRWLAV 1100
Cdd:TIGR01193 307 VYAVIiilfkRTFNKLNHdamQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKAdqgQQAIKA 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1101 RLDLISIALITTTGLMIVLMH----GQIPpAYAGLaISYavqLTGLFQFTVRLASETEARFTSVERINHYIKTLSLEAPA 1176
Cdd:TIGR01193 387 VTKLILNVVILWTGAYLVMRGkltlGQLI-TFNAL-LSY---FLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINK 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1177 RIKNKAPSPDwpqeGEVTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGV 1256
Cdd:TIGR01193 462 KKRTELNNLN----GDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF 536
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 767925452 1257 RISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQ--YTEDQIWDALE 1304
Cdd:TIGR01193 537 SLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKenVSQDEIWAACE 586
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1196-1287 |
5.03e-17 |
|
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: 80.34 E-value: 5.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1196 ENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQ 1275
Cdd:cd03246 4 ENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90
....*....|..
gi 767925452 1276 EPVLFSGTVRSN 1287
Cdd:cd03246 84 DDELFSGSIAEN 95
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
580-795 |
5.27e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.39 E-value: 5.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 580 SIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVAQ-------QAWIL--NATLRDNILFG- 646
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvTHRSIQQrdicmvfQSYALfpHMSLGENVGYGl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 647 ---KEYDEERYNSVlnscclRPDLAILpssDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDAHvgnh 722
Cdd:PRK11432 104 kmlGVPKEERKQRV------KEALELV---DLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDAN---- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 723 ifnsaIRKHLKSK----------TVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL---------MNLNGDyATIFN 782
Cdd:PRK11432 171 -----LRRSMREKirelqqqfniTSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELyrqpasrfmASFMGD-ANIFP 244
|
250
....*....|...
gi 767925452 783 NLLLGETppVEIN 795
Cdd:PRK11432 245 ATLSGDY--VDIY 255
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
572-765 |
6.01e-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: 81.00 E-value: 6.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 572 LRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVAQQAwiLNATLRDNILFGKE 648
Cdd:cd03298 8 FSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvTAAPPADRP--VSMLFQENNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 649 YDEERYnsvlnscclrpDLAILPSSDLTEIgERGA-------------------NLSGGQRQRISLARALYSDRSIYILD 709
Cdd:cd03298 86 TVEQNV-----------GLGLSPGLKLTAE-DRQAievalarvglaglekrlpgELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767925452 710 DPLSALDAHVGNHIFNSAIRKHLKSK-TVLFVTHQLQYLVDCDE-VIFMKEGCITERG 765
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLHAETKmTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
578-772 |
6.06e-17 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 81.95 E-value: 6.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYVAQQAwilnA---- 637
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQditglsekelyelrrrIGMLFQGG----Alfds 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 638 -TLRDNILFG-KEYD-------EERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDRSIYIL 708
Cdd:COG1127 97 lTVFENVAFPlREHTdlseaeiRELVLEKLELVGLPGAADKMPSE-----------LSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767925452 709 DDPLSALDAHVGNHIFN--SAIRKHLKSkTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:COG1127 166 DEPTAGLDPITSAVIDEliRELRDELGL-TSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
578-771 |
1.43e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 85.95 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNI- 643
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfglmdlrkVLGIIPQAPVLFSGTVRFNLd 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 644 LFGKEYDEERYNSvLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDahVG-NH 722
Cdd:PLN03130 1335 PFNEHNDADLWES-LERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD--VRtDA 1411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767925452 723 IFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELM 771
Cdd:PLN03130 1412 LIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLL 1460
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
565-772 |
4.97e-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: 78.63 E-value: 4.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 565 KHIHLGHLRLQrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQ 630
Cdd:cd03224 4 ENLNAGYGKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 631 -QAWILNATLRDNILFG-----KEYDEERYNSVLNsccLRPDLAilpssdlTEIGERGANLSGGQRQRISLARALYSDRS 704
Cdd:cd03224 83 gRRIFPELTVEENLLLGayarrRAKRKARLERVYE---LFPRLK-------ERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 705 IYILDDPLSALDAHVGNHIFNsAIRKhLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFE-AIRE-LRDEgvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
575-763 |
5.13e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 79.73 E-value: 5.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG----------------TFAYVAQQA------ 632
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplaklnraqrkafrrDIQMVFQDSisavnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 633 -----WILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAilpssdlteiGERGANLSGGQRQRISLARALYSDRSIYI 707
Cdd:PRK10419 105 rktvrEIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVL----------DKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 708 LDDPLSALDAHVGNHIFnsAIRKHLKSKT---VLFVTHQLQyLVD--CDEVIFMKEGCITE 763
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVI--RLLKKLQQQFgtaCLFITHDLR-LVErfCQRVMVMDNGQIVE 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
578-761 |
5.43e-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: 78.34 E-value: 5.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWilnATLRDNI--LFgkeydeERYN 655
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNI---NELRQKVgmVF------QQFN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 656 -----SVLNSCCLRPDLAI-LPSSDLTEIGER-----G---------ANLSGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:cd03262 87 lfphlTVLENITLAPIKVKgMSKAEAEERALEllekvGladkadaypAQLSGGQQQRVAIARALAMNPKVMLFDEPTSAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767925452 716 DAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCI 761
Cdd:cd03262 167 DPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
575-772 |
7.03e-16 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 78.43 E-value: 7.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQ-AWILNATLRDN 642
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlpphkrpVNTVFQNyALFPHLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 643 ILFG-------KEYDEERYNSVLnscclrpDLAilpssDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:cd03300 93 IAFGlrlkklpKAEIKERVAEAL-------DLV-----QLEGYANRKpSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 715 LDAHvgnhifnsaIRKHLKSK----------TVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:cd03300 161 LDLK---------LRKDMQLElkrlqkelgiTFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
578-772 |
7.89e-16 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 79.51 E-value: 7.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILgQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNI- 643
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGVIPQKVFIFSGTFRKNLd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 644 LFGKEYDEERYNsVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhvgnhI 723
Cdd:cd03289 99 PYGKWSDEEIWK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-----I 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767925452 724 FNSAIRKHLKSK----TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:cd03289 173 TYQVIRKTLKQAfadcTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1209-1304 |
8.11e-16 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 78.32 E-value: 8.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG---LADLRSKLSIIPQEPvlfsgtvR 1285
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDP-------M 92
|
90 100
....*....|....*....|
gi 767925452 1286 SNLDPfnQYT-EDQIWDALE 1304
Cdd:cd03257 93 SSLNP--RMTiGEQIAEPLR 110
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1210-1310 |
1.20e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 81.81 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1210 LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrLVELSG-----GCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTV 1284
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSL------LNALLGflpyqGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTL 439
|
90 100
....*....|....*....|....*....
gi 767925452 1285 RSNL---DPfnQYTEDQIWDALERTHMKE 1310
Cdd:PRK11174 440 RDNVllgNP--DASDEQLQQALENAWVSE 466
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
575-790 |
1.90e-15 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 77.92 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG----------------TFAYVAQQA------ 632
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqldrkqrrafrrDVQLVFQDSpsavnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 633 -----WILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAilpssdlteiGERGANLSGGQRQRISLARALYSDRSIYI 707
Cdd:TIGR02769 104 rmtvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDA----------DKLPRQLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 708 LDDPLSALDAHVGNHIFnsAIRKHLKSK---TVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEELMNLNGDYATIFN 782
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVIL--ELLRKLQQAfgtAYLFITHDLR-LVQsfCQRVAVMDKGQIVEECDVAQLLSFKHPAGRNLQ 250
|
....*...
gi 767925452 783 NLLLGETP 790
Cdd:TIGR02769 251 SAVLPEHP 258
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
578-791 |
2.55e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.72 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYVAQQAWILNATLRD 641
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsklqgirklvgIVFQNPETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 642 NILFGKEydeerynsvlnSCCLRP-DLAILPSSDLTEIG------ERGANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:PRK13644 98 DLAFGPE-----------NLCLPPiEIRKRVDRALAEIGlekyrhRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 715 LDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEelmnlngdyaTIFNNL---LLGETPP 791
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPE----------NVLSDVslqTLGLTPP 236
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
913-1163 |
3.07e-15 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 77.98 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 913 YYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 992
Cdd:cd07346 40 WIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 993 FIQNVILVFFCVGMIAgVFPW--FLVAVGPLVILFSVLHIVSRvLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKG 1070
Cdd:cd07346 120 LLSDVLTLIGALVILF-YLNWklTLVALLLLPLYVLILRYFRR-RIRKASREVRESLAELSAFLQESLSGIRVVKAFAAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1071 QEFLHRYQELLDDNqapFFLFTCAMRWLAvrLDLISIALITTTGLMIVL-------MHGQIPPAYAGLAISYAVQLTGLF 1143
Cdd:cd07346 198 EREIERFREANRDL---RDANLRAARLSA--LFSPLIGLLTALGTALVLlyggylvLQGSLTIGELVAFLAYLGMLFGPI 272
|
250 260
....*....|....*....|
gi 767925452 1144 QFTVRLASETEARFTSVERI 1163
Cdd:cd07346 273 QRLANLYNQLQQALASLERI 292
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
581-743 |
4.01e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.68 E-value: 4.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 581 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVAQQAWIL---NA-----TLRDNILFGKEy 649
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiDDPDVAEACHYLghrNAmkpalTVAENLEFWAA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 650 deerynsVLNSCCLRPD--LAILPSSDLTEIgeRGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGNHIFNSA 727
Cdd:PRK13539 100 -------FLGGEELDIAaaLEAVGLAPLAHL--PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFAEL 169
|
170
....*....|....*..
gi 767925452 728 IRKHLKSK-TVLFVTHQ 743
Cdd:PRK13539 170 IRAHLAQGgIVIAATHI 186
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
670-1288 |
4.36e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 81.23 E-value: 4.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 670 LPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDaHVGNHIFNSAIR--KHLKSKTVLFVTHQLQYL 747
Cdd:PTZ00265 565 LPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINnlKGNENRITIIIAHRLSTI 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 748 -------------------VDCDEVIFMKEGC----------------------------ITERGTHEELM-NLNGDYAT 779
Cdd:PTZ00265 644 ryantifvlsnrergstvdVDIIGEDPTKDNKennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMkNKNGIYYT 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 780 IFNNLllgetppvEINSKKETSGSQKKSQDKgpKTGSVK-KEKAVKPEEGQLVQLEEKGQGSVPWSVYGVYIQA----AG 854
Cdd:PTZ00265 724 MINNQ--------KVSSKKSSNNDNDKDSDM--KSSAYKdSERGYDPDEMNGNSKHENESASNKKSCKMSDENAsennAG 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 855 GPLAFL----------------------------VIMALFMLNVGS--TAFSTWWLSYwikqgsgnttvtrgnetsVSdS 904
Cdd:PTZ00265 794 GKLPFLrnlfkrkpkapnnlrivyreifsykkdvTIIALSILVAGGlyPVFALLYAKY------------------VS-T 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 905 MKDNPHMQYYA---SIYALSMAV-MLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDT---TPtGRILNRFSK 977
Cdd:PTZ00265 855 LFDFANLEANSnkySLYILVIAIaMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINR 933
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 978 DMDEVDVRLPFQAEMFIQNVILvfFCVGMIAGVFPWFLVA---VGPLVILFSVLHIVSRVLIR---ELKRL--------- 1042
Cdd:PTZ00265 934 DVHLLKTGLVNNIVIFTHFIVL--FLVSMVMSFYFCPIVAavlTGTYFIFMRVFAIRARLTANkdvEKKEInqpgtvfay 1011
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1043 ---DNITQSP-------FLSHITSSIQGL---------ATIHAYNKGQEFLHRYQELL--DDNQAPFFLFTCAMrWLAVR 1101
Cdd:PTZ00265 1012 nsdDEIFKDPsfliqeaFYNMNTVIIYGLedyfcnlieKAIDYSNKGQKRKTLVNSMLwgFSQSAQLFINSFAY-WFGSF 1090
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1102 ldLISIALITTTGLMIVLMHGQIPPAYAGLAISyavqltglfqftvrLASETEARFTSVERINHYIKTLSL-----EAPA 1176
Cdd:PTZ00265 1091 --LIRRGTILVDDFMKSLFTFLFTGSYAGKLMS--------------LKGDSENAKLSFEKYYPLIIRKSNidvrdNGGI 1154
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1177 RIKNKAPSpdwpqEGEVTFENAEMRY--RENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVEL-------- 1246
Cdd:PTZ00265 1155 RIKNKNDI-----KGKIEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivf 1228
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1247 ----------------------------------------------SGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLF 1280
Cdd:PTZ00265 1229 knehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLF 1308
|
....*...
gi 767925452 1281 SGTVRSNL 1288
Cdd:PTZ00265 1309 NMSIYENI 1316
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
911-1146 |
4.46e-15 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 77.43 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 911 MQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvrlpfqA 990
Cdd:cd18544 40 LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEAL-------N 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 991 EMFIQNVILVFFCVGMIAGVF----------PWFLVAVGPLVILFSVLH-IVSRVLIRELKRLdnitqspfLSHITS--- 1056
Cdd:cd18544 113 ELFTSGLVTLIGDLLLLIGILiamfllnwrlALISLLVLPLLLLATYLFrKKSRKAYREVREK--------LSRLNAflq 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1057 -SIQGLATIHAYNKGQEFLHRYQELlddNQApffLFTCAMRwlAVRLDLI---SIALITTTGLMIVLMHGqippayAGLA 1132
Cdd:cd18544 185 eSISGMSVIQLFNREKREFEEFDEI---NQE---YRKANLK--SIKLFALfrpLVELLSSLALALVLWYG------GGQV 250
|
250
....*....|....
gi 767925452 1133 ISYAVQLTGLFQFT 1146
Cdd:cd18544 251 LSGAVTLGVLYAFI 264
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
578-770 |
4.71e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 78.20 E-value: 4.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAIlgqmTLLE----GSIAISGT--------------------FayvaQQAW 633
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI----NLLErptsGSVLVDGVdltalserelraarrkigmiF----QHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 634 ILNA-TLRDNILF-------GKEYDEERYNSVLnscclrpdlailpssDLTEIGERG----ANLSGGQRQRISLARALYS 701
Cdd:COG1135 93 LLSSrTVAENVALpleiagvPKAEIRKRVAELL---------------ELVGLSDKAdaypSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767925452 702 DRSIYILDDPLSALDAHVGNHIFN--SAIRKHLKsKTVLFVTHQLqylvD-----CDEVIFMKEGCITERGTHEEL 770
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDllKDINRELG-LTIVLITHEM----DvvrriCDRVAVLENGRIVEQGPVLDV 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
575-771 |
4.74e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.12 E-value: 4.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI-------------AISGTFAYVAQQAWI-LNATLR 640
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVlvagddvealsarAASRRVASVPQDTSLsFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 641 DNILFGKEYDEERYN-------SVLNSCCLRPDLAILPSSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:PRK09536 96 QVVEMGRTPHRSRFDtwtetdrAAVERAMERTGVAQFADRPVTS-------LSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 714 ALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 771
Cdd:PRK09536 169 SLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1167-1288 |
5.22e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 79.76 E-value: 5.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1167 IKTLSLEAPARIKNKAPSPDwpQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVEL 1246
Cdd:PRK10789 290 IRAMLAEAPVVKDGSEPVPE--GRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDV 367
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 767925452 1247 SGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL 1288
Cdd:PRK10789 368 SEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI 409
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
578-770 |
5.56e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 75.80 E-value: 5.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAIlgqmTLLE----GSIAISGTfaYVAQQAWILNAtLRDNI--LFgkeyde 651
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCI----NLLEepdsGTITVDGE--DLTDSKKDINK-LRRKVgmVF------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 652 ERYN-----SVLNSCCLRPdlaI----LPSSDLTEIGER-----G---------ANLSGGQRQRISLARALYSDRSIYIL 708
Cdd:COG1126 84 QQFNlfphlTVLENVTLAP---IkvkkMSKAEAEERAMEllervGladkadaypAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 709 DDPLSALD----AHVGNHIfnsairKHLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 770
Cdd:COG1126 161 DEPTSALDpelvGEVLDVM------RDLAKEgmTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
581-743 |
5.60e-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: 75.09 E-value: 5.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 581 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------------FAYVAQQAWILNA-TLRDNILFgk 647
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdephenILYLGHLPGLKPElSALENLHF-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 648 eydeerYNSVLNSCCLRPDLAiLPSSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGNHIFNS 726
Cdd:TIGR01189 97 ------WAAIHGGAQRTIEDA-LAAVGLTGFEDLPAAqLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVALLAG 168
|
170
....*....|....*...
gi 767925452 727 AIRKHL-KSKTVLFVTHQ 743
Cdd:TIGR01189 169 LLRAHLaRGGIVLLTTHQ 186
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
578-772 |
6.81e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 76.57 E-value: 6.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKtSLISAIL-GQMTLLEGSIAISG------TFAYVAQQAWI---------LNATLRD 641
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGK-STISKILtGLLKPQSGEIKIDGitiskeNLKEIRKKIGIifqnpdnqfIGATVED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 642 NILFGKEydeerynsvlNSCCLRPDLA--ILPSSDLTEIGE----RGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:PRK13632 104 DIAFGLE----------NKKVPPKKMKdiIDDLAKKVGMEDyldkEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 716 DAHVGNHI--FNSAIRKHlKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:PRK13632 174 DPKGKREIkkIMVDLRKT-RKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
578-773 |
6.83e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 78.07 E-value: 6.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-TFAYVAQQAWILNA-----------TLRDNILF 645
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqDITHVPAENRHVNTvfqsyalfphmTVFENVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 646 G----KEYDEERYNSVLNScclrpdlaiLPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 720
Cdd:PRK09452 110 GlrmqKTPAAEITPRVMEA---------LRMVQLEEFAQRKpHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLR 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 721 NHIFNSAirKHLKSK---TVLFVTH-QLQYLVDCDEVIFMKEGCITERGT----HEELMNL 773
Cdd:PRK09452 181 KQMQNEL--KALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTpreiYEEPKNL 239
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
578-759 |
7.86e-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: 73.62 E-value: 7.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTfayvaqqawilnatlrdnilfgkeydEERYNSv 657
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--------------------------EVSFAS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 658 lnscclrPDLAIlpssdlteigERGAN----LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNsAIRKhLK 733
Cdd:cd03216 69 -------PRDAR----------RAGIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK-VIRR-LR 129
|
170 180
....*....|....*....|....*....
gi 767925452 734 S--KTVLFVTHQLQYLVD-CDEVIFMKEG 759
Cdd:cd03216 130 AqgVAVIFISHRLDEVFEiADRVTVLRDG 158
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
571-759 |
9.68e-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: 73.62 E-value: 9.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 571 HLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVA----QQA 632
Cdd:cd03215 9 GLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrkREG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 633 WILNATLRDNILfgkeydeerynsvlnscclrpdLAILpssdlteigerganLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:cd03215 89 LVLDLSVAENIA----------------------LSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767925452 713 SALDahVG--NHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEG 759
Cdd:cd03215 133 RGVD--VGakAEIYRLIRELADAGKAVLLISSELDELLGlCDRILVMYEG 180
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
575-765 |
1.03e-14 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 74.56 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTF------------AYVAQQAWILNATLRDN 642
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSyqkniealrrigALIEAPGFYPNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 643 I-LFGKEYD--EERYNSVLNSCCLRpdlailpssdlTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhV 719
Cdd:cd03268 93 LrLLARLLGirKKRIDEVLDVVGLK-----------DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP-D 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767925452 720 GNHIFNSAIRKHLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 765
Cdd:cd03268 161 GIKELRELILSLRDQgITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
956-1310 |
1.13e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.99 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 956 LRSPMKFFDTTPTGRILNRFSKDMdEVdVRlpfqaEMFIQNVILVFFCVGMIAGV------FPW--FLVAVG--PLVILF 1025
Cdd:PRK10790 109 LRQPLSAFDTQPVGQLISRVTNDT-EV-IR-----DLYVTVVATVLRSAALIGAMlvamfsLDWrmALVAIMifPAVLVV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1026 SVLH------IVSRVlirelkrldnitqSPFLSHITS----SIQGLATIHAYNKGQEFLHRyqeLLDDNQAPFflftcAM 1095
Cdd:PRK10790 182 MVIYqrystpIVRRV-------------RAYLADINDgfneVINGMSVIQQFRQQARFGER---MGEASRSHY-----MA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1096 RWLAVRLD------LISI--ALITTtGLMivLMHGQIPPAYAGLAISYA-VQLTG-----LFQFTVRLASETEArFTSVE 1161
Cdd:PRK10790 241 RMQTLRLDgfllrpLLSLfsALILC-GLL--MLFGFSASGTIEVGVLYAfISYLGrlnepLIELTTQQSMLQQA-VVAGE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1162 RInhyiktlsLEAPARIKNKAPSPDWP-QEGEVTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMAL 1240
Cdd:PRK10790 317 RV--------FELMDGPRQQYGNDDRPlQSGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLL 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1241 FRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKE 1310
Cdd:PRK10790 388 MGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAE 457
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
581-759 |
1.47e-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: 72.10 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 581 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--FAYVAQqawilnatlrdnilfgkeydeerynsvl 658
Cdd:cd03221 19 ISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTvkIGYFEQ---------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 659 nscclrpdlailpssdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDahvgnhIFN-SAIRKHLKS--K 735
Cdd:cd03221 71 --------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD------LESiEALEEALKEypG 118
|
170 180
....*....|....*....|....*.
gi 767925452 736 TVLFVTHQlQYLVD--CDEVIFMKEG 759
Cdd:cd03221 119 TVILVSHD-RYFLDqvATKIIELEDG 143
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
593-770 |
1.79e-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: 76.38 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 593 ICGSVGSGKTSLISAILGQMTLLEGSIAISGT-FAYVAQ---------QAWIL--NATLRDNILFG----KEYDEERYNS 656
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEdVTNVPPhlrhinmvfQSYALfpHMTVEENVAFGlkmrKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 657 VLnscclrpdlAILPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKHLK-S 734
Cdd:TIGR01187 81 VL---------EALRLVQLEEFADRKpHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlG 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 767925452 735 KTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:TIGR01187 152 ITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
578-759 |
2.91e-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: 73.08 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---------TFAYVAQQAWI-LNATLRDNILF-- 645
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLPEERGLyPKMKVIDQLVYla 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 646 -----GKEYDEERYNSVLNscclRPDLAILPSSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVG 720
Cdd:cd03269 96 qlkglKKEEARRRIDEWLE----RLELSEYANKRVEE-------LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767925452 721 NHIFNSAIRKHL-KSKTVLFVTHQLQyLVD--CDEVIFMKEG 759
Cdd:cd03269 164 VELLKDVIRELArAGKTVILSTHQME-LVEelCDRVLLLNKG 204
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
576-777 |
2.94e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.28 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMT----------LLEGSIAISGTFA-----------YVAQQAWI 634
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksagshieLLGRTVQREGRLArdirksrantgYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 635 LNA-TLRDNILFGKEYDEERYNSvlnscCLR---PDLAILPSSDLTEIG------ERGANLSGGQRQRISLARALYSDRS 704
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTPFWRT-----CFSwftREQKQRALQALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767925452 705 IYILDDPLSALDAHVGnHIFNSAIR--KHLKSKTVLFVTHQLQY-LVDCDEVIFMKEGCITERGTHEELMNLNGDY 777
Cdd:PRK09984 173 VILADEPIASLDPESA-RIVMDTLRdiNQNDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQFDNERFDH 247
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
582-765 |
3.31e-14 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 72.97 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 582 DLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQAWIL-NATLRDNILFG--- 646
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQshtglapyqrpVSMLFQENNLFaHLTVRQNIGLGlhp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 647 ----KEYDEERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 722
Cdd:TIGR01277 98 glklNAEQQEKVVDAAQQVGIADYLDRLPEQ-----------LSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767925452 723 IFnsAIRKHL---KSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 765
Cdd:TIGR01277 167 ML--ALVKQLcseRQRTLLMVTHHLSDARAiASQIAVVSQGKIKVVS 211
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
578-772 |
5.13e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 73.72 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------FAYVAQQ------------------AW 633
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdYKYRCKHirmifqdpntslnprlniGQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 634 ILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLteigerganlSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:COG4167 109 ILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHML----------SSGQKQRVALARALILQPKIIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767925452 714 ALDAHVGNHIFNsaIRKHLKSK---TVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEELMN 772
Cdd:COG4167 179 ALDMSVRSQIIN--LMLELQEKlgiSYIYVSQHLG-IVKhiSDKVLVMHQGEVVEYGKTAEVFA 239
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
951-1307 |
5.81e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.60 E-value: 5.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 951 LFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD----------VRlpfQAEMFIQNVILVFFcvgmiagvFPWFLVavgp 1020
Cdd:PRK11176 104 LFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVAssssgalitvVR---EGASIIGLFIMMFY--------YSWQLS---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1021 lVILFSVLHIVSrVLIREL-KRLDNIT---QSPfLSHITSS----IQGLATIHAYNkGQEF-LHRYQELLDDnqapfflf 1091
Cdd:PRK11176 169 -LILIVIAPIVS-IAIRVVsKRFRNISknmQNT-MGQVTTSaeqmLKGHKEVLIFG-GQEVeTKRFDKVSNR-------- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1092 tcaMRWLAVRL---DLIS---IALITTTGLMIVLMHGQIPPAYAGL-AISYAVQLTGLFQFTVRLASETE--ARFtsvER 1162
Cdd:PRK11176 237 ---MRQQGMKMvsaSSISdpiIQLIASLALAFVLYAASFPSVMDTLtAGTITVVFSSMIALMRPLKSLTNvnAQF---QR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1163 INHYIKTL----SLEAPariKNKAPSPDWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGM 1238
Cdd:PRK11176 311 GMAACQTLfailDLEQE---KDEGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIAN 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 1239 ALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL--DPFNQYTEDQIWDALERTH 1307
Cdd:PRK11176 388 LLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIayARTEQYSREQIEEAARMAY 458
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
578-772 |
6.94e-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: 77.26 E-value: 6.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILgQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNIL 644
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvswnsvtlqtwrkAFGVIPQKVFIFSGTFRKNLD 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 FGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhvgnhIF 724
Cdd:TIGR01271 1314 PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP-----VT 1388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767925452 725 NSAIRKHLKSK----TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:TIGR01271 1389 LQIIRKTLKQSfsncTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLN 1440
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
578-770 |
7.01e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.24 E-value: 7.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILG-QMTLLE--GSIAISGT----------FAYVAQQAWILNA-TLRDNI 643
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrSPKGVKgsGSVLLNGMpidakemraiSAYVQQDDLFIPTlTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 644 LF----------GKEYDEERYNSVLNscclrpDLAILPSSDlTEIGERGA--NLSGGQRQRISLARALYSDRSIYILDDP 711
Cdd:TIGR00955 121 MFqahlrmprrvTKKEKRERVDEVLQ------ALGLRKCAN-TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925452 712 LSALDAHVGNHIFnsAIRKHL--KSKTVLFVTHQLQYLVDC--DEVIFMKEGCITERGTHEEL 770
Cdd:TIGR00955 194 TSGLDSFMAYSVV--QVLKGLaqKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQA 254
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
578-773 |
7.07e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.81 E-value: 7.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFayvaqqAWIL--------NATLRDNILFG--- 646
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV------SALLelgagfhpELTGRENIYLNgrl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 647 -----KEYDeERYNSVLnscclrpdlailpssDLTEIGE------RgaNLSGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:COG1134 116 lglsrKEID-EKFDEIV---------------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVG 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767925452 716 DAHvgnhiFN----SAIRKHLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMNL 773
Cdd:COG1134 178 DAA-----FQkkclARIRELRESgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
575-776 |
7.21e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 73.51 E-value: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGtFAYVAQQAW----------------ILNAT 638
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSEETVWdvrrqvgmvfqnpdnqFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 639 LRDNILFGKE-----YDE--ERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDRSIYILDDP 711
Cdd:PRK13635 99 VQDDVAFGLEnigvpREEmvERVDQALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767925452 712 LSALDAhVGNHIFNSAIRkHLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGD 776
Cdd:PRK13635 168 TSMLDP-RGRREVLETVR-QLKEQkgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1195-1277 |
7.77e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 73.49 E-value: 7.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1195 FENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIP 1274
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89
|
...
gi 767925452 1275 QEP 1277
Cdd:PRK13632 90 QNP 92
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
568-772 |
8.26e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.43 E-value: 8.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 568 HLGHLRLqrtLHSIDLEIQEGKLVGICGSVGSGKTSLISAI--LGQMT---LLEGSIAISGTFA----------YVAQQA 632
Cdd:PRK09493 10 HFGPTQV---LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITsgdLIVDGLKVNDPKVderlirqeagMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 633 WIL-NATLRDNILFG--------KEYDEERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDR 703
Cdd:PRK09493 87 YLFpHLTALENVMFGplrvrgasKEEAEKQARELLAKVGLAERAHHYPSE-----------LSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 704 SIYILDDPLSALDAHVGNHIFNsaIRKHLKSK--TVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELMN 772
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLK--VMQDLAEEgmTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
578-772 |
1.10e-13 |
|
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: 72.42 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEG-SIAISGT-------------FAYV--AQQAWIL-NATLR 640
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGErrggedvwelrkrIGLVspALQLRFPrDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 641 DNIL---FG-----KEYDEERYNSVLnscclrpdlAILPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDP 711
Cdd:COG1119 99 DVVLsgfFDsiglyREPTDEQRERAR---------ELLELLGLAHLADRPfGTLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767925452 712 LSALDAHvGNHIFNSAIRK--HLKSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELMN 772
Cdd:COG1119 170 TAGLDLG-ARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLT 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
571-773 |
1.13e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.44 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 571 HLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYV----AQQA 632
Cdd:COG1129 261 GLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVpedrKGEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 633 WILNATLRDNILFGkeydeeRYNSVLNSCCLRP------------DLAILPSSDLTEIGergaNLSGGQRQRISLARALY 700
Cdd:COG1129 341 LVLDLSIRENITLA------SLDRLSRGGLLDRrreralaeeyikRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 701 SDRSIYILDDPLSALDahVGNH--IFNsAIRKhLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCIT-----ERGTHEEL 770
Cdd:COG1129 411 TDPKVLILDEPTRGID--VGAKaeIYR-LIRE-LAAegKAVIVISSELPELLGlSDRILVMREGRIVgeldrEEATEEAI 486
|
...
gi 767925452 771 MNL 773
Cdd:COG1129 487 MAA 489
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
575-756 |
1.20e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.42 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI-----AISGTFA---YVAQQAWILN-ATLRDNILF 645
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSItldgkPVEGPGAergVVFQNEGLLPwRNVQDNVAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 646 GKEY----DEERYNSVLnscclrpdlAILPSSDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 720
Cdd:PRK11248 94 GLQLagveKMQRLEIAH---------QMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 767925452 721 NHIFNSAIRK-HLKSKTVLFVTHqlqylvDCDEVIFM 756
Cdd:PRK11248 165 EQMQTLLLKLwQETGKQVLLITH------DIEEAVFM 195
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
578-754 |
1.37e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.67 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 644
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 F-----GKEYDEERynsvlnsccLRPDLAI--LPSSDLTEigeRGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:PRK10247 103 FpwqirNQQPDPAI---------FLDDLERfaLPDTILTK---NIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 767925452 718 HvGNHIFNSAIRKHLKSK--TVLFVTHQLQYLVDCDEVI 754
Cdd:PRK10247 171 S-NKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVI 208
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1194-1275 |
1.50e-13 |
|
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: 69.58 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1194 TFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSII 1273
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
..
gi 767925452 1274 PQ 1275
Cdd:cd00267 79 PQ 80
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
578-765 |
1.60e-13 |
|
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: 71.24 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAY-----VAQQAWILNA--------TLRDNIL 644
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVkepaeARRRLGFVSDstglydrlTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 -FGKEYDEERYNsvlnsccLRPDLAILpsSDLTEIGE----RGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhV 719
Cdd:cd03266 101 yFAGLYGLKGDE-------LTARLEEL--ADRLGMEElldrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV-M 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767925452 720 GNHIFNSAIRkHLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 765
Cdd:cd03266 171 ATRALREFIR-QLRAlgKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
583-761 |
1.95e-13 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 71.15 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 583 LEIQEGKLVGICGSVGSGKTSLISAILGQM---TLLEGSIAISGT----------FAYVAQQ-AWILNATLRDNILF--- 645
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQprkpdqfqkcVAYVRQDdILLPGLTVRETLTYtai 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 646 ---GKEYDEERYNSVLNSCCLRpDLAILPSSdlteiGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 722
Cdd:cd03234 108 lrlPRKSSDAIRKKRVEDVLLR-DLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767925452 723 IFnsAIRKHL--KSKTVLFVTHQ-----LQYLvdcDEVIFMKEGCI 761
Cdd:cd03234 182 LV--STLSQLarRNRIVILTIHQprsdlFRLF---DRILLLSSGEI 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1195-1319 |
2.32e-13 |
|
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: 70.57 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1195 FENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIP 1274
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767925452 1275 QEP--VLFSGTVRSNL--DPFN-QYTEDQIWDALERThMKECDSSHLKNK 1319
Cdd:cd03225 82 QNPddQFFGPTVEEEVafGLENlGLPEEEIEERVEEA-LELVGLEGLRDR 130
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
625-772 |
2.38e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.45 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 625 FAYVAQQAWILNATLRDNILFGKE-YDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDR 703
Cdd:PTZ00265 1298 FSIVSQEPMLFNMSIYENIKFGKEdATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREP 1377
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 704 SIYILDDPLSALDAHVGNHIFNSAIR-KHLKSKTVLFVTHQLQYLVDCDEVIFM----KEGCITE-RGTHEELMN 772
Cdd:PTZ00265 1378 KILLLDEATSSLDSNSEKLIEKTIVDiKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLS 1452
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
566-772 |
2.95e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 71.30 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 566 HIHLGHLRLqrtLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---------------------- 623
Cdd:COG4559 8 SVRLGGRTL---LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarrravlpqhs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 624 --TFAYVAQQ-------AWILNATLRDNILfgkeydeerynsvlnscclrpdLAILPSSDLTEIGERG-ANLSGGQRQRI 693
Cdd:COG4559 85 slAFPFTVEEvvalgraPHGSSAAQDRQIV----------------------REALALVGLAHLAGRSyQTLSGGEQQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 694 SLARAL-------YSDRSIYILDDPLSALD-AHVgNHIFNSAirKHLKSK--TVLFVTHQL----QYlvdCDEVIFMKEG 759
Cdd:COG4559 143 QLARVLaqlwepvDGGPRWLFLDEPTSALDlAHQ-HAVLRLA--RQLARRggGVVAVLHDLnlaaQY---ADRILLLHQG 216
|
250
....*....|...
gi 767925452 760 CITERGTHEELMN 772
Cdd:COG4559 217 RLVAQGTPEEVLT 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
567-743 |
8.25e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.68 E-value: 8.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 567 IHLGHLRLQRTL-HSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------FAYVAQQAWI--LNA 637
Cdd:PRK13538 5 RNLACERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpirrqrDEYHQDLLYLghQPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 638 -----TLRDNILF----GKEYDEERYNSVLNSCCL--RPDLAIlpssdlteigergANLSGGQRQRISLARALYSDRSIY 706
Cdd:PRK13538 85 iktelTALENLRFyqrlHGPGDDEALWEALAQVGLagFEDVPV-------------RQLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 767925452 707 ILDDPLSALDAHvGNHIFNSAIRKHLKSK-TVLFVTHQ 743
Cdd:PRK13538 152 ILDEPFTAIDKQ-GVARLEALLAQHAEQGgMVILTTHQ 188
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
578-743 |
9.32e-13 |
|
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: 67.56 E-value: 9.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAI---SGTFaYVAQQAWILNATLRDNIlfgkeydeery 654
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpegEDLL-FLPQRPYLPLGTLREQL----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 655 nsvlnscclrpdlaILPSSDlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnSAIRKHLks 734
Cdd:cd03223 85 --------------IYPWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY-QLLKELG-- 138
|
....*....
gi 767925452 735 KTVLFVTHQ 743
Cdd:cd03223 139 ITVISVGHR 147
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
581-770 |
1.05e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.21 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 581 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQ-AWILNATLRDNILFG-- 646
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvppaergVGMVFQSyALYPHLSVAENMSFGlk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 647 -----KEYDEERYNSVLnscclrpdlAILPSSDLTEigERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA--HV 719
Cdd:PRK11000 102 lagakKEEINQRVNQVA---------EVLQLAHLLD--RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767925452 720 GNHIFNSAIRKHLKSkTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:PRK11000 171 QMRIEISRLHKRLGR-TMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1173-1277 |
1.08e-12 |
|
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: 72.24 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1173 EAPARIKNKAPSPDWPQEGE--VTFENAEMRYRENLP---LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS 1247
Cdd:COG1123 239 AVPRLGAARGRAAPAAAAAEplLEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT 318
|
90 100 110
....*....|....*....|....*....|...
gi 767925452 1248 GGCIKIDGVRISDIG---LADLRSKLSIIPQEP 1277
Cdd:COG1123 319 SGSILFDGKDLTKLSrrsLRELRRRVQMVFQDP 351
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
569-769 |
1.13e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.06 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 569 LGHLRLQrtlhsIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAYVAQQ 631
Cdd:PRK11144 10 LGDLCLT-----VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppekrrIGYVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 632 AWIL-NATLRDNILFG-KEYDEERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDRSIYILD 709
Cdd:PRK11144 85 ARLFpHYKVRGNLRYGmAKSMVAQFDKIVALLGIEPLLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 710 DPLSALDAHvgnhifnsaiRKH-----LK--SKTV----LFVTHQLQYLVD-CDEVIFMKEGCITERGTHEE 769
Cdd:PRK11144 154 EPLASLDLP----------RKRellpyLErlAREInipiLYVSHSLDEILRlADRVVVLEQGKVKAFGPLEE 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
578-742 |
1.35e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.02 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG--TFAYVAQQAWIL-NATLRDNIL--FGKEYD-E 651
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDdDLTVLDTVLdgDAELRAlE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 652 ERYNSVLNSCCLRPDLAILPSSDLTEIGERGA--------------------------NLSGGQRQRISLARALYSDRSI 705
Cdd:COG0488 94 AELEELEAKLAEPDEDLERLAELQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARALLSEPDL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767925452 706 YILDDPLSALDAHvgnhifnsAIR---KHLKS--KTVLFVTH 742
Cdd:COG0488 174 LLLDEPTNHLDLE--------SIEwleEFLKNypGTVLVVSH 207
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
578-765 |
1.44e-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: 68.71 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGtfayvaQQAWIL--------NATLRDNILFG--- 646
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSLLglgggfnpELTGRENIYLNgrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 647 ----KEYDEERYNSVLnscclrpdlailpssDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAH 718
Cdd:cd03220 112 lglsRKEIDEKIDEII---------------EFSELGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767925452 719 vgnhiF----NSAIRKHLK-SKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 765
Cdd:cd03220 177 -----FqekcQRRLRELLKqGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1213-1309 |
1.70e-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: 70.08 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1213 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE---LSGGCIKIDGVRISDIGLADLR----SKLSIIPQEPVlfsgtvr 1285
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRkirgREIQMIFQDPM------- 96
|
90 100
....*....|....*....|....*
gi 767925452 1286 SNLDPFnqYT-EDQIWDALeRTHMK 1309
Cdd:COG0444 97 TSLNPV--MTvGDQIAEPL-RIHGG 118
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
578-770 |
1.78e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 69.75 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFayvaqqawiLNATLRDNIlfGkeY-DEERyns 656
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP---------LDPEDRRRI--G--YlPEER--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 657 vlnscCLRPDLAI------------LPSSDLT----------EIGERGA----NLSGGQRQRISLARALYSDRSIYILDD 710
Cdd:COG4152 81 -----GLYPKMKVgeqlvylarlkgLSKAEAKrradewlerlGLGDRANkkveELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925452 711 PLSALDAhVGNHIFNSAIRKHLKS-KTVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEEL 770
Cdd:COG4152 156 PFSGLDP-VNVELLKDVIRELAAKgTTVIFSSHQME-LVEelCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
578-772 |
1.92e-12 |
|
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: 68.34 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTF--------------AYVAQQAWIL-NATLRDN 642
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhkrarlgiGYLPQEASIFrKLTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 643 IL-------FGKEYDEERYNSVLNscclrpDLAILPSSDlteigERGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:cd03218 96 ILavleirgLSKKEREEKLEELLE------EFHITHLRK-----SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 716 DAHVGNHIfnSAIRKHLKSKT--VLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:cd03218 165 DPIAVQDI--QKIIKILKDRGigVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
581-759 |
2.20e-12 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 67.92 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 581 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG----TFAYVAQQA-----------WILnaTLRDNILF 645
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirTDRKAARQSlgycpqfdalfDEL--TVREHLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 646 -----GKEYDEERYNSvlnscclrpdLAILPSSDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 719
Cdd:cd03263 99 yarlkGLPKSEIKEEV----------ELLLRVLGLTDKANKRArTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767925452 720 GNHIFNsAIRKHLKSKTVLFVTHQLQ---YLvdCDEVIFMKEG 759
Cdd:cd03263 169 RRAIWD-LILEVRKGRSIILTTHSMDeaeAL--CDRIAIMSDG 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1193-1308 |
2.22e-12 |
|
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: 71.09 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG---GCIKIDGVRISDIGLADLRSK 1269
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 767925452 1270 LSIIPQEPvlfsgtvRSNLDPFNqyTEDQIWDALERTHM 1308
Cdd:COG1123 85 IGMVFQDP-------MTQLNPVT--VGDQIAEALENLGL 114
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
576-770 |
2.64e-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: 67.78 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG------------TFAYVAQQAWILNA-TLRDN 642
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 643 I-LFGKEYD---EERYNSVLNscclrpdlaILPSSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:cd03265 94 LyIHARLYGvpgAERRERIDE---------LLDFVGLLEAADRlVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 718 HVGNHIFnSAIRKHLKSK--TVLFVTHqlqYLVD----CDEVIFMKEGCITERGTHEEL 770
Cdd:cd03265 165 QTRAHVW-EYIEKLKEEFgmTILLTTH---YMEEaeqlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
685-772 |
2.78e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 70.87 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 685 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNsaIRKHLKSK---TVLFVTHQLQ---YLvdCDEVIFMKE 758
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILD--LLRDLQREhglAYLFISHDLAvvrAL--AHRVMVMKD 501
|
90
....*....|....
gi 767925452 759 GCITERGTHEELMN 772
Cdd:COG4172 502 GKVVEQGPTEQVFD 515
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
576-772 |
3.24e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 68.92 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------------TFAYVAQQawILN 636
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkkvglVFQYPEYQ--LFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 637 ATLRDNILFGK----EYDEERYNSVLNSCclrpDLAILPSSDLTEigERGANLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:PRK13637 99 ETIEKDIAFGPinlgLSEEEIENRVKRAM----NIVGLDYEDYKD--KSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 713 SALDAHVGNHIFNSAIRKHLKSK-TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFK 234
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
575-772 |
3.45e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 68.19 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------FAYVAQQAWIL---NA-----TLR 640
Cdd:COG4604 14 KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvattpSRELAKRLAILrqeNHinsrlTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 641 DNILFG---------KEYDEERYNSVLNSCclrpdlailpssDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDD 710
Cdd:COG4604 94 ELVAFGrfpyskgrlTAEDREIIDEAIAYL------------DLEDLADRYLDeLSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925452 711 PLSALDahvgnhIFNS-AIRKHLKS------KTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEELMN 772
Cdd:COG4604 162 PLNNLD------MKHSvQMMKLLRRladelgKTVVIVLHDInfasCY---ADHIVAMKDGRVVAQGTPEEIIT 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
578-780 |
3.78e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.58 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTfAYVAQQAWILN----------------ATLRD 641
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWNLRrkigmvfqnpdnqfvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 642 NILFGKEYDEERYNSVLNscclRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 721
Cdd:PRK13642 102 DVAFGMENQGIPREEMIK----RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 722 HIFNsaIRKHLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATI 780
Cdd:PRK13642 178 EIMR--VIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEI 237
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
578-772 |
4.41e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.07 E-value: 4.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAY----------VAQQAWILNATLRDNILFgK 647
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLRLLRTRLTMVF-Q 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 648 EYDEERYNSVLNSCCLRPDLAI-LPSSDLTE----------IGERG-----ANLSGGQRQRISLARALYSDRSIYILDDP 711
Cdd:PRK10619 100 HFNLWSHMTVLENVMEAPIQVLgLSKQEAREravkylakvgIDERAqgkypVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 712 LSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELMN 772
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
578-772 |
5.04e-12 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 67.31 E-value: 5.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQAWIL-NATLRDN 642
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIFpSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 643 ILFG------KEYDEERYNSVLNsccLRPDLAilpssdlteigER----GANLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:COG0410 99 LLLGayarrdRAEVRADLERVYE---LFPRLK-----------ERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925452 713 SALDAHVGNHIFNsAIRKhLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:COG0410 165 LGLAPLIVEEIFE-IIRR-LNREgvTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
578-772 |
5.83e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.19 E-value: 5.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI-------------------------------------A 620
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvleklviqktrfkkikkikE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 621 ISGTFAYVAQQA--WILNATLRDNILFG-------KEYDEERYNSVLNSCCLrpDLAILPSSDLteigergaNLSGGQRQ 691
Cdd:PRK13651 103 IRRRVGVVFQFAeyQLFEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESYLQRSPF--------ELSGGQKR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 692 RISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG-THEE 769
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEwTKRTIFFKDGKIIKDGdTYDI 252
|
...
gi 767925452 770 LMN 772
Cdd:PRK13651 253 LSD 255
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
578-742 |
6.11e-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: 66.66 E-value: 6.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT---------FAYVAQQ--------AWILNATLR 640
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraIPYLRRKigvvfqdfRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 641 DNILFGKEYDE-------ERYNSVLNSCCLRPDLAILPssdlteigergANLSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:cd03292 97 ENVAFALEVTGvppreirKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180
....*....|....*....|....*....
gi 767925452 714 ALDAHVGNHIFNSAIRKHLKSKTVLFVTH 742
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
575-761 |
7.34e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.01 E-value: 7.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRT-LHSIDLEIQEGKLVGICGSVGSGKTSLISAILG-----QMTLLEGSIAIsgtfayvaqqawilnATLRDNILFgkE 648
Cdd:PRK11247 24 ERTvLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGletpsAGELLAGTAPL---------------AEAREDTRL--M 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 649 YDEER---YNSVLNSCCL------RPD-LAILPSSDLTE-IGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:PRK11247 87 FQDARllpWKKVIDNVGLglkgqwRDAaLQALAAVGLADrANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767925452 718 HVG---NHIFNSAIRKHlkSKTVLFVTHQLQYLVD-CDEVIFMKEGCI 761
Cdd:PRK11247 167 LTRiemQDLIESLWQQH--GFTVLLVTHDVSEAVAmADRVLLIEEGKI 212
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
567-742 |
8.76e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 65.97 E-value: 8.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 567 IHLGHLRLqrtLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQmtlLEGSIAISGtfayvaqQAWI-------LNATL 639
Cdd:COG4136 9 ITLGGRPL---LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGT---LSPAFSASG-------EVLLngrrltaLPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 640 R------------------DNILFG---KEYDEERYNSVLNScclrpdlaiLPSSDLTEIGERG-ANLSGGQRQRISLAR 697
Cdd:COG4136 76 RrigilfqddllfphlsvgENLAFAlppTIGRAQRRARVEQA---------LEEAGLAGFADRDpATLSGGQRARVALLR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767925452 698 ALYSDRSIYILDDPLSALDAH----VGNHIFNSAIRKHLkskTVLFVTH 742
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAAlraqFREFVFEQIRQRGI---PALLVTH 192
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
578-749 |
1.02e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 65.84 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYVAQQAWIL-NATLR 640
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlkrreipylrrrIGVVFQDFRLLpDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 641 DNILF-----GKEYDE--ERYNSVLnscclrpdlailpssDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILD 709
Cdd:COG2884 98 ENVALplrvtGKSRKEirRRVREVL---------------DLVGLSDKAkalpHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767925452 710 DPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQyLVD 749
Cdd:COG2884 163 EPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE-LVD 201
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1193-1294 |
1.10e-11 |
|
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: 65.57 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRY---RENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlrsK 1269
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100
....*....|....*....|....*...
gi 767925452 1270 LSIIPQEPVLFSGTVRSNL---DPFNQY 1294
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgKPFDEE 95
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
585-768 |
1.25e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.55 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 585 IQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGtfAYVAQQAWILNA---------------TLRDNIL-FGKE 648
Cdd:PRK13536 64 VASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLARArigvvpqfdnldlefTVRENLLvFGRY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 649 YdeeRYNSvlnscclRPDLAILPSsdLTEIGE-------RGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGN 721
Cdd:PRK13536 142 F---GMST-------REIEAVIPS--LLEFARleskadaRVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-AR 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767925452 722 HIFNSAIRKHL-KSKTVLFVTHQLQYLVD-CDEVIFMKEGC-ITERGTHE 768
Cdd:PRK13536 209 HLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGRkIAEGRPHA 258
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
576-772 |
1.80e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.57 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGqMTLLEGSIAISGTFAYVAQ---------------------QAWI 634
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNG-LIISETGQTIVGDYAIPANlkkikevkrlrkeiglvfqfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 635 LNATLRDNILFGK----EYDEERYNSVlnscclrPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDD 710
Cdd:PRK13645 104 FQETIEKDIAFGPvnlgENKQEAYKKV-------PELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767925452 711 PLSALDAHVGNHIFNSAIR-KHLKSKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERlNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
578-772 |
1.97e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 66.36 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTS---LISAILGQMTLLEGSIAISGTfAYVAQQAW----------------ILNAT 638
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGI-TLTAKTVWdirekvgivfqnpdnqFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 639 LRDNILFGKEydeerynsvlNSCCLRPDLAILPSSDLTEIG------ERGANLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:PRK13640 102 VGDDVAFGLE----------NRAVPRPEMIKIVRDVLADVGmldyidSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 713 SALDAHVGNHIFnSAIRKHLKSK--TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:PRK13640 172 SMLDPAGKEQIL-KLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
581-772 |
1.98e-11 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 65.54 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 581 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIA-----ISG-------------TFayvaQQAWIL-NATLRD 641
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgedITGlppheiarlgigrTF----QIPRLFpELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 642 NILFGKEYDEERYNSVLNSCCLRPDL-----AILpssDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREEREAreraeELL---ERVGLADLAdrpaGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 713 SALD----AHVGNHIfnSAIRKHlkSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:cd03219 172 AGLNpeetEELAELI--RELRER--GITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
578-761 |
2.02e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.60 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISaILGQMtllegSIAISGTFAYVAQQAWILN----ATLRDN----------- 642
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCL-----DKPTSGTYRVAGQDVATLDadalAQLRREhfgfifqryhl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 643 --------------ILFGKEYDEERYNSVlnscclrpdlAILPSSDLTE-IGERGANLSGGQRQRISLARALYSDRSIYI 707
Cdd:PRK10535 98 lshltaaqnvevpaVYAGLERKQRLLRAQ----------ELLQRLGLEDrVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767925452 708 LDDPLSALDAHVGNHIFnsAIRKHLKSK--TVLFVTHQLQYLVDCDEVIFMKEGCI 761
Cdd:PRK10535 168 ADEPTGALDSHSGEEVM--AILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
578-770 |
2.13e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.18 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQ-AWILNATLRDNILF 645
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelepadrdIAMVFQNyALYPHMSVRENMAY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 646 G-------KEYDEERynsvlnscclrpdlaILPSSDLTEIGE----RGANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:PRK11650 100 GlkirgmpKAEIEER---------------VAEAARILELEPlldrKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 715 LDAHVGNHIfNSAIRK-HLKSKTV-LFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:PRK11650 165 LDAKLRVQM-RLEIQRlHRRLKTTsLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
575-744 |
2.31e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.83 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAiLGQMTLLEGSIAISGTFAYVAQQAWILNATL------------RDN 642
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYERRVNLnrlrrqvsmvhpKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 643 ILFGKEYDEERYNSVLNSccLRPDLAI-------LPSSDL-----TEIGERGANLSGGQRQRISLARALYSDRSIYILDD 710
Cdd:PRK14258 99 LFPMSVYDNVAYGVKIVG--WRPKLEIddivesaLKDADLwdeikHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 767925452 711 PLSALDA----HVGNHIFNSAIRKHLkskTVLFVTHQL 744
Cdd:PRK14258 177 PCFGLDPiasmKVESLIQSLRLRSEL---TMVIVSHNL 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
583-815 |
2.46e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 67.37 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 583 LEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNATLRDNILFGKEYDEERYNSVLNSCC 662
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 663 LRPDLAILPSSD--------LTEIG-ERGAN-----LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAI 728
Cdd:PRK10070 129 FGMELAGINAEErrekaldaLRQVGlENYAHsypdeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 729 RKHLK-SKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELMN--LNGDYATIFNNLLLGETPPVEINSKKETSGSQ 804
Cdd:PRK10070 209 KLQAKhQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNnpANDYVRTFFRGVDISQVFSAKDIARRTPNGLI 288
|
250
....*....|.
gi 767925452 805 KKSQDKGPKTG 815
Cdd:PRK10070 289 RKTPGFGPRSA 299
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1213-1277 |
2.50e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 66.68 E-value: 2.50e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767925452 1213 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG---LADLRSKLSIIPQEP 1277
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP 104
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
569-743 |
2.87e-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: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 569 LGHLRLQRTLHS-IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------------FAYVAQQAWIL 635
Cdd:cd03231 6 LTCERDGRALFSgLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiargLLYLGHAPGIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 636 NA-TLRDNILFgkeydeerynsvlnSCCLRPDLAI---LPSSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDD 710
Cdd:cd03231 86 TTlSVLENLRF--------------WHADHSDEQVeeaLARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|....
gi 767925452 711 PLSALDAHvGNHIFNSAIRKHL-KSKTVLFVTHQ 743
Cdd:cd03231 152 PTTALDKA-GVARFAEAMAGHCaRGGMVVLTTHQ 184
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
578-763 |
2.97e-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: 64.76 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--FAyvaqqawiLN----ATLR-DNILFgkeyd 650
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlFA--------LDedarARLRaRHVGF----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 651 eerynsVLNSCCLRPDL-AI----LPssdLTEIGERGA----------------------NLSGGQRQRISLARALYSDR 703
Cdd:COG4181 95 ------VFQSFQLLPTLtALenvmLP---LELAGRRDArararallervglghrldhypaQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 704 SIYILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLF-VTHQLQYLVDCDEVIFMKEGCITE 763
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVlVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
575-771 |
3.15e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 65.42 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNA-TLR 640
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlarrLALLPQHHLTPEGiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 641 DNILFGK-----------EYDEERYNSVLNScclrpdlailpsSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYIL 708
Cdd:PRK11231 95 ELVAYGRspwlslwgrlsAEDNARVNQAMEQ------------TRINHLADRRlTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767925452 709 DDPLSALDAhvgNHIFN--SAIRK-HLKSKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELM 771
Cdd:PRK11231 163 DEPTTYLDI---NHQVElmRLMRElNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
915-1080 |
4.73e-11 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 65.50 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 915 ASIYALSMAVMLILkairGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvrlpfqAEMFI 994
Cdd:cd18547 52 LGLYLLSALFSYLQ----NRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNI-------SQALS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 995 QNVILVFFCVGMIAGVF-------PWF-LVAVGPLVILFSVLHIV---SRVLIREL-KRLDNITqspflSHITSSIQGLA 1062
Cdd:cd18547 121 QSLTQLISSILTIVGTLimmlyisPLLtLIVLVTVPLSLLVTKFIakrSQKYFRKQqKALGELN-----GYIEEMISGQK 195
|
170
....*....|....*...
gi 767925452 1063 TIHAYNKGQEFLHRYQEL 1080
Cdd:cd18547 196 VVKAFNREEEAIEEFDEI 213
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
578-757 |
5.40e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.90 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------FAYVAQQA---WILNATLRDNIL 644
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQSEevdWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 645 FG-----------KEYDEERYNSVLNscclRPDLAILPSSdltEIGErganLSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:PRK15056 103 MGryghmgwlrraKKRDRQIVTAALA----RVDMVEFRHR---QIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767925452 714 ALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMK 757
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEfCDYTVMVK 216
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
575-772 |
5.57e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.41 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAIlGQMTLLEGSIAISGTFAY---------------------VAQQAW 633
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 634 ILNATLRDNILFGKEYDEERYNSVLNSCCLRpdlAILPSSDLTEIGER----GANLSGGQRQRISLARALYSDRSIYILD 709
Cdd:PRK14239 97 PFPMSIYENVVYGLRLKGIKDKQVLDEAVEK---SLKGASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767925452 710 DPLSALDAHVGNHIFNSAIRkhLKSK-TVLFVTHQLQYLVD-CDEVIFMKEGCITERG-THEELMN 772
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLG--LKDDyTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNdTKQMFMN 237
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
575-765 |
5.74e-11 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 63.75 E-value: 5.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGkLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG------------TFAYVAQQAwilnaTLRDN 642
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQEF-----GVYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 643 IlfgKEYDEERYNSVLNSC----CLRPDLAILPSSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDa 717
Cdd:cd03264 87 F---TVREFLDYIAWLKGIpskeVKARVDEVLELVNLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767925452 718 hVGNHI-FNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 765
Cdd:cd03264 163 -PEERIrFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
575-770 |
5.84e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 65.04 E-value: 5.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAI------SGT---------------FAYVAQQaw 633
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKknkklkplrkkvgivFQFPEHQ-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 634 ILNATLRDNILFG-------KEYDEERYNSVLNSCCLRPDLaiLPSSDLteigergaNLSGGQRQRISLARALYSDRSIY 706
Cdd:PRK13634 98 LFEETVEKDICFGpmnfgvsEEDAKQKAREMIELVGLPEEL--LARSPF--------ELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 707 ILDDPLSALDAHVGNHIFNSAIRKHL-KSKTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEEL 770
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMedaaRY---ADQIVVMHKGTVFLQGTPREI 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
577-772 |
6.30e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 64.77 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 577 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI-----AISG-TFAYVAQQAWIL---------NATLRD 641
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDdNFEKLRKHIGIVfqnpdnqfvGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 642 NILFGKE-----YDE--ERYNSVLNscclrpDLAILPSSDlteigERGANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:PRK13648 104 DVAFGLEnhavpYDEmhRRVSEALK------QVDMLERAD-----YEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 715 LDAHVGNHIFNsaIRKHLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:PRK13648 173 LDPDARQNLLD--LVRKVKSEhniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1210-1277 |
6.34e-11 |
|
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: 66.63 E-value: 6.34e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 1210 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVElSGGCIKIDGVRISDIG---LADLRSKLSIIPQEP 1277
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP 371
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1193-1276 |
7.05e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 63.53 E-value: 7.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENlPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSK 1269
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
....*..
gi 767925452 1270 LSIIPQE 1276
Cdd:COG2884 81 IGVVFQD 87
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
582-780 |
7.92e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.45 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 582 DLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVAQQ-AWIL--------NATLRDNILFGkey 649
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhTTTPPSRRpVSMLfqennlfsHLTVAQNIGLG--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 650 deerynsvlnsccLRPDL-----------AILPSSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:PRK10771 96 -------------LNPGLklnaaqreklhAIARQMGIEDLLARlPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 718 HVGNHIFN----SAIRKHLkskTVLFVTHQLQylvDCDEV----IFMKEGCITERGTHEELMNLNGDYATI 780
Cdd:PRK10771 163 ALRQEMLTlvsqVCQERQL---TLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELLSGKASASAL 227
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
179-447 |
1.01e-10 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 64.20 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 179 LILSIVCLMITQLAGFSGPAFMvKHLLE-YTQATESNLQYSLLLVLGLLLTEIVRSWSLALTWALNYRTGVRLRGAILTM 257
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVL-GRILDvLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 258 AFKKILKLKNI--KEKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPT-GFLGSAVFILFYPAMM 334
Cdd:pfam00664 80 LFKKILRQPMSffDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 335 FASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGYFQSITVGVAPIVVVIAS 414
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSY 239
|
250 260 270
....*....|....*....|....*....|....*
gi 767925452 415 VVT--FSVHMTLGFDLTAAQAFTVVTVFNSMTFAL 447
Cdd:pfam00664 240 ALAlwFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
576-772 |
1.16e-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: 65.59 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILG--QMTLLEGSI----AISGTFAYVAQQA----------------- 632
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvALCEKCGYVERPSkvgepcpvcggtlepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 633 ---WILNATLRDNI-------------LFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTE---IGER----GANLSGGQ 689
Cdd:TIGR03269 94 vdfWNLSDKLRRRIrkriaimlqrtfaLYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEmvqLSHRithiARDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 690 RQRISLARALYSDRSIYILDDPLSALDAHVGNhIFNSAIRKHLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGT 766
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASgiSMVLTSHWPEVIEDlSDKAIWLENGEIKEEGT 252
|
....*.
gi 767925452 767 HEELMN 772
Cdd:TIGR03269 253 PDEVVA 258
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
555-765 |
1.68e-10 |
|
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: 62.74 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 555 ERPSPEEEEGKHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG----------- 623
Cdd:cd03267 14 SKEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwkrrkkfl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 624 -----TFAYVAQQAWILNAtlRDNILFGKE-YD--EERYNSVLNSCClrpdlailpssDLTEIGE------RgaNLSGGQ 689
Cdd:cd03267 94 rrigvVFGQKTQLWWDLPV--IDSFYLLAAiYDlpPARFKKRLDELS-----------ELLDLEElldtpvR--QLSLGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 690 RQRISLARALYSDRSIYILDDPLSALDAHVGNhifnsAIRKHLKS------KTVLFVTHqlqYLVD----CDEVIFMKEG 759
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQE-----NIRNFLKEynrergTTVLLTSH---YMKDiealARRVLVIDKG 230
|
....*.
gi 767925452 760 CITERG 765
Cdd:cd03267 231 RLLYDG 236
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
580-771 |
2.04e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.88 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 580 SIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAIS------GTFAYVAQQ------------------AWIL 635
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfGDYSYRSQRirmifqdpstslnprqriSQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 636 NATLRDNILFGKEYDEERYNSVLNSCCLRPDLA-ILPSSdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:PRK15112 111 DFPLRLNTDLEPEQREKQIIETLRQVGLLPDHAsYYPHM-----------LAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 715 LDAHVGNHIFNSAIRkhLKSK---TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 771
Cdd:PRK15112 180 LDMSMRSQLINLMLE--LQEKqgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1196-1289 |
2.22e-10 |
|
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: 60.87 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1196 ENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGlADLRSKLSIIPQ 1275
Cdd:cd03230 4 RNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLPE 80
|
90
....*....|....*
gi 767925452 1276 EPVLFSG-TVRSNLD 1289
Cdd:cd03230 81 EPSLYENlTVRENLK 95
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
905-1027 |
2.26e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 63.33 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 905 MKDNPHMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDV 984
Cdd:cd18572 29 DGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSD 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767925452 985 RLPFQAEMFIQNVILVFFCVGMIAGVfPWFL-----VAVGPLVILFSV 1027
Cdd:cd18572 109 PLSTNLNVFLRNLVQLVGGLAFMFSL-SWRLtllafITVPVIALITKV 155
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
577-770 |
2.34e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 63.21 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 577 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTfAYVAQQAW----------------ILNATLR 640
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdirhkigmvfqnpdnqFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 641 DNILFGKE-----YDE--ERYNSVLNscclrpdlaILPSSDLTEigERGANLSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:PRK13650 101 DDVAFGLEnkgipHEEmkERVNEALE---------LVGMQDFKE--REPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 714 ALDAHVGNHIFNS--AIRKHLKsKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:PRK13650 170 MLDPEGRLELIKTikGIRDDYQ-MTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
578-772 |
2.36e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 63.26 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-----------------TFAYVAQ--QAWILNAT 638
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 639 LRDNILFG--------KEYDEERYNSVLNSCCLRPDLAILPssdlteigergANLSGGQRQRISLARALYSDRSIYILDD 710
Cdd:PRK13646 103 VEREIIFGpknfkmnlDEVKNYAHRLLMDLGFSRDVMSQSP-----------FQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767925452 711 PLSALDAHVGNHIFNSAIRKHLK-SKTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEELMN 772
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMnevaRY---ADEVIVMKEGSIVSQTSPKELFK 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
683-772 |
3.57e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.34 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 683 ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnsAIRKHLKSK---TVLFVTHQLQYLVD-CDEVIFMKE 758
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL--ALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQ 501
|
90
....*....|....
gi 767925452 759 GCITERGTHEELMN 772
Cdd:PRK15134 502 GEVVEQGDCERVFA 515
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
581-743 |
4.27e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.13 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 581 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISgtfayVAQQAWILNATLRDNILFGKEYDEERYnsVLNS 660
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLIDAIGRKGDFKDAVE--LLNA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 661 CCLrpdlailpsSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD---AHVGNHIFNSAIRKHlkSKTV 737
Cdd:COG2401 122 VGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQKLARRA--GITL 190
|
....*.
gi 767925452 738 LFVTHQ 743
Cdd:COG2401 191 VVATHH 196
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
578-766 |
5.05e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 61.37 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTfaYVAQQAWILNATLRDNILfGKEYDEER---- 653
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ--PMSKLSSAAKAELRNQKL-GFIYQFHHllpd 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 654 YNSVLNSCC------LRPDLAILPSSD-LTEIG------ERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 720
Cdd:PRK11629 102 FTALENVAMplligkKKPAEINSRALEmLAAVGlehranHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767925452 721 NHIFNSAIRKHLKSKTV-LFVTHQLQYLVDCDEVIFMKEGCITERGT 766
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAfLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
578-766 |
5.75e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 62.51 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAIlgqmTLLE----GSIAISGT----------------FAYVAQQAWILNA 637
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCI----NLLErptsGRVLVDGQdltalsekelrkarrqIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 638 -TLRDNILF-------GKEYDEERYNSVLnscclrpdlailpssDLTEIGERG----ANLSGGQRQRISLARALYSDRSI 705
Cdd:PRK11153 97 rTVFDNVALplelagtPKAEIKARVTELL---------------ELVGLSDKAdrypAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 706 YILDDPLSALDAHVGNHIFN--SAIRKHLKSkTVLFVTHQLQyLVD--CDEVIFMKEGCITERGT 766
Cdd:PRK11153 162 LLCDEATSALDPATTRSILEllKDINRELGL-TIVLITHEMD-VVKriCDRVAVIDAGRLVEQGT 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1196-1284 |
6.44e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.99 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1196 ENAEMRYRENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD--IGLADLRSKL 1270
Cdd:PRK13637 6 ENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKV 85
|
90
....*....|....*.
gi 767925452 1271 SIIPQEP--VLFSGTV 1284
Cdd:PRK13637 86 GLVFQYPeyQLFEETI 101
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
566-757 |
6.92e-10 |
|
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: 59.30 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 566 HIHLGHLRLQRTlhSIDLEIQEGKLVGICGSVGSGKTSLISAIlgqmtllegsiaisgtfayvaqqawILNATLRDNILF 645
Cdd:cd03227 1 KIVLGRFPSYFV--PNDVTFGEGSLTIITGPNGSGKSTILDAI-------------------------GLALGGAQSATR 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 646 GKEYDEERYNSvlnsCCLRPDLAILPSSdlteigerganLSGGQRQRISLARAL----YSDRSIYILDDPLSALDAHVGN 721
Cdd:cd03227 54 RRSGVKAGCIV----AAVSAELIFTRLQ-----------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQ 118
|
170 180 190
....*....|....*....|....*....|....*..
gi 767925452 722 HIFNsAIRKHLKSK-TVLFVTHQLQYLVDCDEVIFMK 757
Cdd:cd03227 119 ALAE-AILEHLVKGaQVIVITHLPELAELADKLIHIK 154
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1193-1288 |
7.18e-10 |
|
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: 59.51 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG--LADLRSKL 1270
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRI 78
|
90
....*....|....*....
gi 767925452 1271 SIIPQEPVLFSG-TVRSNL 1288
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI 97
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
907-1120 |
7.29e-10 |
|
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: 62.08 E-value: 7.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 907 DNPHMQYYASIYALSM----AVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTP--TGRILNRFSKDMD 980
Cdd:cd18578 43 DDDELRSEANFWALMFlvlaIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDAS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 981 EV----DVRLPfqaeMFIQNVILVFFCVGmIAGVFPWFL----VAVGPLVILFSVLHIvsRVLIR-ELKRLDNITQSpfl 1051
Cdd:cd18578 123 DVrglvGDRLG----LILQAIVTLVAGLI-IAFVYGWKLalvgLATVPLLLLAGYLRM--RLLSGfEEKNKKAYEES--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1052 SHITS-SIQGLATIHAYNKGQEFLHRYQELLDDNQ-------------------APFFLFTCAMRWLAVrldLISIALIT 1111
Cdd:cd18578 193 SKIASeAVSNIRTVASLTLEDYFLEKYEEALEEPLkkglrralisglgfglsqsLTFFAYALAFWYGGR---LVANGEYT 269
|
....*....
gi 767925452 1112 TTGLMIVLM 1120
Cdd:cd18578 270 FEQFFIVFM 278
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
578-763 |
7.42e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.16 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--FAYVAQQAWIL--NATLRDNILFGKEYDEER 653
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETvkIGYFDQHQEELdpDKTVLDELRDGAPGGTEQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 654 Y-NSVLNSCCLRPDLAilpssdLTEIGergaNLSGGQRQRISLARALYSDRSIYILDDPlsaldahvGNH-------IFN 725
Cdd:COG0488 411 EvRGYLGRFLFSGDDA------FKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEP--------TNHldietleALE 472
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767925452 726 SAIRKHlkSKTVLFVTHQlQYLVD--CDEVIFMKEGCITE 763
Cdd:COG0488 473 EALDDF--PGTVLLVSHD-RYFLDrvATRILEFEDGGVRE 509
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
566-772 |
9.30e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 60.94 E-value: 9.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 566 HIHLGHLRLqrtLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---------------------- 623
Cdd:PRK13548 9 SVRLGGRTL---LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarrravlpqhs 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 624 --TFAYVAQQ-------AWILNATLRDNILfgkeydeeryNSVLNSCclrpDLAILPSSDLTEigerganLSGGQRQRIS 694
Cdd:PRK13548 86 slSFPFTVEEvvamgraPHGLSRAEDDALV----------AAALAQV----DLAHLAGRDYPQ-------LSGGEQQRVQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 695 LARAL------YSDRSIYILDDPLSALD-AH---VGNHIFNSAIRKHLkskTVLFVTHQL----QYlvdCDEVIFMKEGC 760
Cdd:PRK13548 145 LARVLaqlwepDGPPRWLLLDEPTSALDlAHqhhVLRLARQLAHERGL---AVIVVLHDLnlaaRY---ADRIVLLHQGR 218
|
250
....*....|..
gi 767925452 761 ITERGTHEELMN 772
Cdd:PRK13548 219 LVADGTPAEVLT 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
581-770 |
9.96e-10 |
|
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: 61.61 E-value: 9.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 581 IDLEIQEGKLVGICGSVGSGKTSLISAILGqmtLLE------GSIAISGT-----------------FAYVAQQA----- 632
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILG---LLPppgitsGEILFDGEdllklsekelrkirgreIQMIFQDPmtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 633 ------WILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAIL---PSsdlteigergaNLSGGQRQRISLARALYSDR 703
Cdd:COG0444 101 pvmtvgDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLdryPH-----------ELSGGMRQRVMIARALALEP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 704 SIYILDDPLSALDAHVGNHIFN--SAIRKHLKSkTVLFVTHQL---QYLvdCDEVIFMKEGCITERGTHEEL 770
Cdd:COG0444 170 KLLIADEPTTALDVTIQAQILNllKDLQRELGL-AILFITHDLgvvAEI--ADRVAVMYAGRIVEEGPVEEL 238
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
281-770 |
1.01e-09 |
|
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: 62.89 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 281 SNDGQRMFEAAAVGSLLAGGPVVAILGMIYnVIILGPTGFLGSAVFI----LFYpaMMFASRLTAYFRRkcVAATDERVQ 356
Cdd:COG4615 112 TEDVRTISQAFVRLPELLQSVALVLGCLAY-LAWLSPPLFLLTLVLLglgvAGY--RLLVRRARRHLRR--AREAEDRLF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 357 K-MNEVLTYIKFIKM--------YAwvKAFSQSVQKIREEERRilekAGYFQSITVGVAPIV--VVIASVVTFSVHMtlg 425
Cdd:COG4615 187 KhFRALLEGFKELKLnrrrrrafFD--EDLQPTAERYRDLRIR----ADTIFALANNWGNLLffALIGLILFLLPAL--- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 426 FDLTAAQAFTVVTVF----NSMTFALKVTPfsvkSLSEASVAVDRFKSLFLMEEvhmiknkPASPHikiEMKNATLAWDS 501
Cdd:COG4615 258 GWADPAVLSGFVLVLlflrGPLSQLVGALP----TLSRANVALRKIEELELALA-------AAEPA---AADAAAPPAPA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 502 SHSSIQnspkltpkmkkdkrasrgkkekvrqLQRTEHQavlaeqkghllldsderpSPEEEEGKHIHLGhlrlqrtlhSI 581
Cdd:COG4615 324 DFQTLE-------------------------LRGVTYR------------------YPGEDGDEGFTLG---------PI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 582 DLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGtfAYVAQQAWilnATLRDNI--------LFGKEY---- 649
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG--QPVTADNR---EAYRQLFsavfsdfhLFDRLLgldg 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 650 --DEERynsvlnsccLRPDLAILPSSDLTEIgERGA----NLSGGQRQRISLARALYSDRSIYILD------DPlsalda 717
Cdd:COG4615 427 eaDPAR---------ARELLERLELDHKVSV-EDGRfsttDLSQGQRKRLALLVALLEDRPILVFDewaadqDP------ 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 718 hVGNHIFNSAIRKHLKS--KTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:COG4615 491 -EFRRVFYTELLPELKArgKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAAL 544
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
578-768 |
1.08e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 60.41 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAilgqMTLLEgsIAISGTFAyVAQQAWILNAT--------LRDNI--LFgk 647
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRV----LNLLE--MPRSGTLN-IAGNHFDFSKTpsdkaireLRRNVgmVF-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 648 eydeERYN-----SVLNSCCLRP--------------DLAILPSSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYI 707
Cdd:PRK11124 89 ----QQYNlwphlTVQQNLIEAPcrvlglskdqalarAEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767925452 708 LDDPLSALDAHVGNHIFNsaIRKHLKSK--TVLFVTHQlqylVD-----CDEVIFMKEGCITERGTHE 768
Cdd:PRK11124 165 FDEPTAALDPEITAQIVS--IIRELAETgiTQVIVTHE----VEvarktASRVVYMENGHIVEQGDAS 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
575-772 |
1.13e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.29 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQAWILNA-TL 639
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararrgIGYLPQEASIFRRlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 640 RDNIL--------FGKEYDEERYNSVL---NSCCLRPDLailpssdlteigerGANLSGGQRQRISLARALYSDRSIYIL 708
Cdd:PRK10895 96 YDNLMavlqirddLSAEQREDRANELMeefHIEHLRDSM--------------GQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767925452 709 DDPLSALDAHVGNHIfnSAIRKHLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:PRK10895 162 DEPFAGVDPISVIDI--KRIIEHLRDSglGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
578-785 |
1.26e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.26 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLIsaiLGQMTLLE---GSIAISG-------------TFAYVAQQAWILNATLRD 641
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLL---LTFMRMVEvcgGEIRVNGreigayglrelrrQFSMIPQDPVLFDGTVRQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 642 NILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLS-----ALD 716
Cdd:PTZ00243 1403 NVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILMDEATanidpALD 1482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 717 AHVGNHIFnSAIRKHlkskTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEEL-MNLNgdyaTIFNNLL 785
Cdd:PTZ00243 1483 RQIQATVM-SAFSAY----TVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQ----SIFHSMV 1543
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
581-765 |
1.58e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 60.97 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 581 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG----TFAYVAQQAWIL---------NATLRDNIL-FG 646
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpSRARHARQRVGVvpqfdnldpDFTVRENLLvFG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 647 keydeeRYNSVLNSCC--LRPDL---AILPSSDLTEIGErganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGN 721
Cdd:PRK13537 106 ------RYFGLSAAAAraLVPPLlefAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-AR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767925452 722 HIFNSAIRKHLKS-KTVLFVTHqlqylvdcdeviFMKEG-------CITERG 765
Cdd:PRK13537 175 HLMWERLRSLLARgKTILLTTH------------FMEEAerlcdrlCVIEEG 214
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
576-766 |
1.73e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.52 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILG-----QMTLLEGSIAISGTfayvAQQAWILNATLRDNILFGKEYD 650
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSST----SKQKEIKPVRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 651 EERYNSVLNSCCLRP--------DLAILPSSDLTEIG------ERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:PRK13643 96 QLFEETVLKDVAFGPqnfgipkeKAEKIAAEKLEMVGladefwEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767925452 716 DAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGT 766
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
581-771 |
1.82e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 60.90 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 581 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-FAYVAQQAW-------------------------- 633
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQdITGLSGRELrplrrrmqmvfqdpyaslnprmtvgd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 634 ILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAilpssdlteigERGAN-LSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:COG4608 117 IIAEPLRIHGLASKAERRERVAELLELVGLRPEHA-----------DRYPHeFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 713 SALDAHVGNHIFNsaIRKHLKSK---TVLFVTHQL---QYLvdCDEVIFMKEGCITERGTHEELM 771
Cdd:COG4608 186 SALDVSIQAQVLN--LLEDLQDElglTYLFISHDLsvvRHI--SDRVAVMYLGKIVEIAPRDELY 246
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
576-772 |
2.03e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 60.13 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILN---------------ATLR 640
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSkvglvfqdpddqvfsSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 641 DNILFGKEYDEERYNSVLNscclRPDLAiLPSSDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 719
Cdd:PRK13647 99 DDVAFGPVNMGLDKDEVER----RVEEA-LKAVRMWDFRDKPPyHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767925452 720 GNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:PRK13647 174 QETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
576-771 |
2.15e-09 |
|
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: 61.74 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGqmtLLEGSiaiSGTFAYVAQQAWIL----------NATLRDNILF 645
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAG---VLEPT---SGEVNVRVGDEWVDmtkpgpdgrgRAKRYIGILH 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 646 gKEYDEERYNSVLN------SCCLRPDLA------ILPSSDLTE-----IGERGAN-LSGGQRQRISLARALYSDRSIYI 707
Cdd:TIGR03269 372 -QEYDLYPHRTVLDnlteaiGLELPDELArmkaviTLKMVGFDEekaeeILDKYPDeLSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 708 LDDPLSALD----AHVGNHIFNSaiRKHLkSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 771
Cdd:TIGR03269 451 LDEPTGTMDpitkVDVTHSILKA--REEM-EQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
897-1083 |
2.41e-09 |
|
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: 60.18 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 897 NETSVSDSMKDnphMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFS 976
Cdd:cd18577 35 GESSPDEFLDD---VNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 977 KDMDEVdvrlpfQ---AE---MFIQNVILVF--FCVGMIAGvfpW----FLVAVGPLVILfsVLHIVSRVLIR-ELKRLD 1043
Cdd:cd18577 112 SDTNLI------QdgiGEklgLLIQSLSTFIagFIIAFIYS---WkltlVLLATLPLIAI--VGGIMGKLLSKyTKKEQE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767925452 1044 NITQSpfLSHITSSIQGLATIHAYNKGQEFLHRYQELLDD 1083
Cdd:cd18577 181 AYAKA--GSIAEEALSSIRTVKAFGGEEKEIKRYSKALEK 218
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
578-761 |
2.56e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 59.71 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVAQQA-WIL------------NATLRD 641
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvTKLPEYKRAkYIGrvfqdpmmgtapSMTIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 642 NILF----GKEY---------DEERYnsvlnscclRPDLAILpssDL-------TEIGergaNLSGGQRQRISLARALYS 701
Cdd:COG1101 102 NLALayrrGKRRglrrgltkkRRELF---------RELLATL---GLglenrldTKVG----LLSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 702 DRSIYILDDPLSALD---AHVGNHIFNSAIR-KHLkskTVLFVTHQLQYLVDC-DEVIFMKEGCI 761
Cdd:COG1101 166 KPKLLLLDEHTAALDpktAALVLELTEKIVEeNNL---TTLMVTHNMEQALDYgNRLIMMHEGRI 227
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
580-743 |
3.39e-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: 61.30 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 580 SIDLEIQEGKLVGICGSVGSGKTSLISaILGQMTLLEG---SIAISGTFAYVAQQAWILNATLRDNILFGKEYDEERYNS 656
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRG 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 657 VLNScclrpDL-AILPSSDLTEIGERGAN----------LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN 725
Cdd:TIGR00954 549 LSDK-----DLeQILDNVQLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYR 623
|
170
....*....|....*...
gi 767925452 726 SAIRKHLkskTVLFVTHQ 743
Cdd:TIGR00954 624 LCREFGI---TLFSVSHR 638
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1139-1288 |
3.65e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.58 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1139 LTGLFQFTVRLASETEarftsverinhYIKtlSLEAPA---RIKNKAPSPDWPQEGE-------VTFENAEMRY--RENL 1206
Cdd:PTZ00265 332 LISMFMLTIILPNITE-----------YMK--SLEATNslyEIINRKPLVENNDDGKklkdikkIQFKNVRFHYdtRKDV 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1207 PlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKI-DGVRISDIGLADLRSKLSIIPQEPVLFSGTVR 1285
Cdd:PTZ00265 399 E-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIK 477
|
...
gi 767925452 1286 SNL 1288
Cdd:PTZ00265 478 NNI 480
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1193-1287 |
4.37e-09 |
|
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: 58.47 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLPLVlKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 1272
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90
....*....|....*.
gi 767925452 1273 IPQEPVLFSG-TVRSN 1287
Cdd:cd03295 80 VIQQIGLFPHmTVEEN 95
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1196-1277 |
4.48e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 59.26 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1196 ENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQ 1275
Cdd:PRK13635 9 EHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQ 88
|
..
gi 767925452 1276 EP 1277
Cdd:PRK13635 89 NP 90
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
927-1081 |
4.54e-09 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 59.14 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 927 ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkDMDEVDVRLPFQAEMFIQNVILVFFCVGM 1006
Cdd:cd18782 57 VLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTALTTLLDVLFSVIYIAV 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 1007 IAgVFPWFL----VAVGPLVILFSVLhiVSRVLIRELKRLdNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELL 1081
Cdd:cd18782 136 LF-SYSPLLtlvvLATVPLQLLLTFL--FGPILRRQIRRR-AEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRY 210
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
578-783 |
8.11e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 58.12 E-value: 8.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAiLGQMTLL------EGSIAISGTFAY---------------VAQQAWILN 636
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRC-LNRMNDLipgarvEGEILLDGEDIYdpdvdvvelrrrvgmVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 637 ATLRDNILFGkeydeerynsvlnsccLRpDLAILPSSDLTEIGER------------------GANLSGGQRQRISLARA 698
Cdd:COG1117 106 KSIYDNVAYG----------------LR-LHGIKSKSELDEIVEEslrkaalwdevkdrlkksALGLSGGQQQRLCIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 699 LYSDRSIYILDDPLSALD----AHVGNHIFNsairkhLKSK-TVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEElmn 772
Cdd:COG1117 169 LAVEPEVLLMDEPTSALDpistAKIEELILE------LKKDyTIVIVTHNMQQAARVsDYTAFFYLGELVEFGPTEQ--- 239
|
250
....*....|.
gi 767925452 773 lngdyatIFNN 783
Cdd:COG1117 240 -------IFTN 243
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
578-770 |
8.68e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.18 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAW----------------ILNATLRD 641
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdirnkagmvfqnpdnqIVATIVEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 642 NILFGKEydeerynsvlnscclrpDLAILPSsdltEIGERGAN-----------------LSGGQRQRISLARALYSDRS 704
Cdd:PRK13633 106 DVAFGPE-----------------NLGIPPE----EIRERVDEslkkvgmyeyrrhaphlLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 705 IYILDDPLSALDAHVGNHIFNSAirKHLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTI--KELNKKygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
919-1083 |
9.68e-09 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 58.34 E-value: 9.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 919 ALSMAVMLILKAIrgVVFVKGTL------RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 992
Cdd:cd18557 39 ALILLAIYLLQSV--FTFVRYYLfniageRIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 993 FIQNVILVFFCVGMIA----GVFPWFLVAVGPLVILFSVLHIVSRVLIREL-KRLDNITQspflsHITSSIQGLATIHAY 1067
Cdd:cd18557 117 LLRNILQVIGGLIILFilswKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVqDALAKAGQ-----VAEESLSNIRTVRSF 191
|
170
....*....|....*.
gi 767925452 1068 NKGQEFLHRYQELLDD 1083
Cdd:cd18557 192 SAEEKEIRRYSEALDR 207
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
686-799 |
9.90e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.82 E-value: 9.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 686 SGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN--SAIRKHLKSKTVlFVTHQLQyLVD--CDEVIFMKEGCI 761
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNlmMDLQQELGLSYV-FISHDLS-VVEhiADEVMVMYLGRC 233
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 767925452 762 TERGTHEelmnlngdyaTIFNN-------LLLGETPPVEINSKKE 799
Cdd:PRK11308 234 VEKGTKE----------QIFNNprhpytqALLSATPRLNPDDRRE 268
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
581-771 |
1.13e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 581 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQ----AWILNATLRDN 642
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgMAYITESrrdnGFFPNFSIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 643 ILFGK---------------EYDEERYNSVLnscclRPDLAILPSSDLTEIGErganLSGGQRQRISLARALYSDRSIYI 707
Cdd:PRK09700 362 MAISRslkdggykgamglfhEVDEQRTAENQ-----RELLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 708 LDDPLSALDAHVGNHIFnSAIRKHLKS-KTVLFVTHQL-QYLVDCDEVIFMKEGCITE------RGTHEELM 771
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIY-KVMRQLADDgKVILMVSSELpEIITVCDRIAVFCEGRLTQiltnrdDMSEEEIM 503
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1195-1342 |
1.24e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 59.31 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1195 FENAEMRYreNLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSlgmaLFRLV----ELSGGCIKID-GVRIsdigladlrsk 1269
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKST----LLKILagelEPDSGEVSIPkGLRI----------- 63
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767925452 1270 lSIIPQEPVLFSG-TVRSN-LDPFNQYteDQIWDALERTHMKECDSSHLKNKFCSLQKMFHRHGPTALDFR-RRVL 1342
Cdd:COG0488 64 -GYLPQEPPLDDDlTVLDTvLDGDAEL--RALEAELEELEAKLAEPDEDLERLAELQEEFEALGGWEAEARaEEIL 136
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
914-1122 |
1.34e-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: 57.86 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 914 YASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvrlpfqAEMF 993
Cdd:cd18545 42 IALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSL-------SDLL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 994 ---IQNVILVFFCVGMIAGVFPWF-----LVAVGPLVILFSVLhIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIH 1065
Cdd:cd18545 115 sngLINLIPDLLTLVGIVIIMFSLnvrlaLVTLAVLPLLVLVV-FLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQ 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1066 AYNKGQEFLHRYQELLDDNQAPFflftcaMRwlAVRL-DLI--SIALITTTGLMIVLMHG 1122
Cdd:cd18545 194 SFAREDENEEIFDELNRENRKAN------MR--AVRLnALFwpLVELISALGTALVYWYG 245
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
917-1085 |
1.40e-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: 57.84 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 917 IYALSMAVMLILKA----IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkdmdevDVrlpfqaeM 992
Cdd:cd18570 43 IISIGLILLYLFQSllsyIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN------DA-------N 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 993 FIQNVI-----------LVFFCVGMIAGVFPW--FLVAVGPLVILFSVLHIVSRVLIRELKRLdNITQSPFLSHITSSIQ 1059
Cdd:cd18570 110 KIREAIssttislfldlLMVIISGIILFFYNWklFLITLLIIPLYILIILLFNKPFKKKNREV-MESNAELNSYLIESLK 188
|
170 180
....*....|....*....|....*.
gi 767925452 1060 GLATIHAYNKGQEFLHRYQELLDDNQ 1085
Cdd:cd18570 189 GIETIKSLNAEEQFLKKIEKKFSKLL 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1210-1290 |
1.44e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.10 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1210 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI---SDIGLADLRSKLSIIPQEPVlfsgtvrS 1286
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPY-------A 412
|
....
gi 767925452 1287 NLDP 1290
Cdd:PRK10261 413 SLDP 416
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1193-1305 |
1.51e-08 |
|
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: 56.33 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGlADLRSKLSI 1272
Cdd:COG4133 3 LEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAY 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767925452 1273 IPQEPVLFSG-TVRSNLDpF------NQYTEDQIWDALER 1305
Cdd:COG4133 80 LGHADGLKPElTVRENLR-FwaalygLRADREAIDEALEA 118
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
578-770 |
2.07e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.98 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNA-------------------- 637
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiklrkevgmvfqqpnpfphl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 638 TLRDNILFGKEY----DEERYNSVLNSCCLRPDLailpssdLTEIGER----GANLSGGQRQRISLARALYSDRSIYILD 709
Cdd:PRK14246 106 SIYDNIAYPLKShgikEKREIKKIVEECLRKVGL-------WKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 710 DPLSALDAhVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 770
Cdd:PRK14246 179 EPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1193-1287 |
2.12e-08 |
|
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: 56.44 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSlgmaLFRLVEL----SGGCIKIDGVRISDIGLADL 1266
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKST----LIRCINGlerpTSGSVLVDGTDLTLLSGKEL 77
|
90 100
....*....|....*....|....*
gi 767925452 1267 ---RSKLSIIPQEPVLFSG-TVRSN 1287
Cdd:cd03258 78 rkaRRRIGMIFQHFNLLSSrTVFEN 102
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
913-1122 |
2.18e-08 |
|
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: 57.05 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 913 YYASIYALSMAVMLILKAIRgvvfvkgtlrassrlhDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 992
Cdd:cd18552 56 SYLQTYLMAYVGQRVVRDLR----------------NDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 993 FIQNVILVFFCVG-MIagVFPWFL----VAVGPLVILfsvlhiVSRVLIRELKRLDNITQSpFLSHITS----SIQGLAT 1063
Cdd:cd18552 120 LVRDPLTVIGLLGvLF--YLDWKLtliaLVVLPLAAL------PIRRIGKRLRKISRRSQE-SMGDLTSvlqeTLSGIRV 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 1064 IHAYNKGQEFLHRYQELLDDNqapfflFTCAMRWLAVRlDLIS--IALITTTGLMIVLMHG 1122
Cdd:cd18552 191 VKAFGAEDYEIKRFRKANERL------RRLSMKIARAR-ALSSplMELLGAIAIALVLWYG 244
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1209-1288 |
2.28e-08 |
|
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: 56.29 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLSIIPQEPVLFSG-TVRS 1286
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
..
gi 767925452 1287 NL 1288
Cdd:cd03224 95 NL 96
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
576-759 |
2.48e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 58.30 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILG--QMTLLEGSIAISGT--------------FAYVAQQ-AWILNAT 638
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSplkasnirdteragIVIIHQElTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 639 LRDNILFGKEYDEE----RYNSVLNSC-CLRPDLAILPSSDLTEIGERGanlsGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:TIGR02633 95 VAENIFLGNEITLPggrmAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767925452 714 ALDAHVGNHIFNsaIRKHLKSKTV--LFVTHQLQYL-VDCDEVIFMKEG 759
Cdd:TIGR02633 171 SLTEKETEILLD--IIRDLKAHGVacVYISHKLNEVkAVCDTICVIRDG 217
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
919-1163 |
2.56e-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: 57.13 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 919 ALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVI 998
Cdd:cd18563 50 AGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNIL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 999 LVFFCVGMIAGVFPWFLVAV---GPLVILFSVLH--IVSRVLIRELKRLDNITqspflSHITSSIQGLATIHAYnkGQE- 1072
Cdd:cd18563 130 MIIGIGVVLFSLNWKLALLVlipVPLVVWGSYFFwkKIRRLFHRQWRRWSRLN-----SVLNDTLPGIRVVKAF--GQEk 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1073 -----FLHRYQELLDDNqapfflftcamrwlaVRLDLIS------IALITTTGLMIV-------LMHGQIPP----AYag 1130
Cdd:cd18563 203 reikrFDEANQELLDAN---------------IRAEKLWatffplLTFLTSLGTLIVwyfggrqVLSGTMTLgtlvAF-- 265
|
250 260 270
....*....|....*....|....*....|...
gi 767925452 1131 laISYAVQLTGLFQFTVRLASETEARFTSVERI 1163
Cdd:cd18563 266 --LSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1209-1280 |
2.69e-08 |
|
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: 55.61 E-value: 2.69e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD--IGLADLRSKLSIIPQEPVLF 1280
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKVGMVFQQFNLF 88
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
923-1028 |
2.92e-08 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 56.67 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 923 AVMLILKAIRGVV-FVKGTL------RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQ 995
Cdd:cd18542 43 LLILGVALLRGVFrYLQGYLaekasqKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVR 122
|
90 100 110
....*....|....*....|....*....|....*.
gi 767925452 996 NVILVFFCVGMIAGVFP---WFLVAVGPLVILFSVL 1028
Cdd:cd18542 123 AVLLFIGALIIMFSINWkltLISLAIIPFIALFSYV 158
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
575-756 |
3.03e-08 |
|
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: 55.02 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQmtllEGSIAISGTFAYVAQQAWILNATLRDNILFGKEYdeery 654
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFLPKFSRNKLIFIDQLQFLIDVGLGY----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 655 nsvlnscclrpdlailpssdLTeIGERGANLSGGQRQRISLARALYSD--RSIYILDDPLSALDAHVGNHIFNSAIRKHL 732
Cdd:cd03238 79 --------------------LT-LGQKLSTLSGGELQRVKLASELFSEppGTLFILDEPSTGLHQQDINQLLEVIKGLID 137
|
170 180
....*....|....*....|....
gi 767925452 733 KSKTVLFVTHQLQYLVDCDEVIFM 756
Cdd:cd03238 138 LGNTVILIEHNLDVLSSADWIIDF 161
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
578-814 |
3.10e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.17 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAI----------SGTFAYVAQQAWILNA---------- 637
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELITNPYSKKIKNFkelrrrvsmv 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 638 -----------TLRDNILFG-------KEYDEERYNSVLNSCCLRPDLAilpssdlteigERGA-NLSGGQRQRISLARA 698
Cdd:PRK13631 122 fqfpeyqlfkdTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSYL-----------ERSPfGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 699 LYSDRSIYILDDPLSALDAHvGNHIFNSAIRKHLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTheelmnlngD 776
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAKANnKTVFVITHTMEHVLEvADEVIVMDKGKILKTGT---------P 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 767925452 777 YATIFNNLLLGET----PPV--EINSKKETSGSQKKSQDKGPKT 814
Cdd:PRK13631 261 YEIFTDQHIINSTsiqvPRViqVINDLIKKDPKYKKLYQKQPRT 304
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
918-1122 |
3.11e-08 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 56.72 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 918 YALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF 993
Cdd:cd18576 38 IALLLLGLFLLQAVfsffRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 994 IQNVILVFFCVGMIAGVFP---WFLVAVGPLVILFSVlhIVSRVlIREL--KRLDNITQSpfLSHITSSIQGLATIHAYN 1068
Cdd:cd18576 118 LRQILTLIGGVVLLFFISWkltLLMLATVPVVVLVAV--LFGRR-IRKLskKVQDELAEA--NTIVEETLQGIRVVKAFT 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 1069 KGQEFLHRYQELLDDnqapffLFTCAMRWLAVRLDLIS-IALITTTGLMIVLMHG 1122
Cdd:cd18576 193 REDYEIERYRKALER------VVKLALKRARIRALFSSfIIFLLFGAIVAVLWYG 241
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1209-1288 |
3.29e-08 |
|
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: 55.65 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGC-----IKIDGVRISDIGLAD--LRSKLSIIPQEPVLFS 1281
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApdegeVLLDGKDIYDLDVDVleLRRRVGMVFQKPNPFP 94
|
....*..
gi 767925452 1282 GTVRSNL 1288
Cdd:cd03260 95 GSIYDNV 101
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
576-740 |
3.64e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.66 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNA---------------TLR 640
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREavaivpegrrvfsrmTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 641 DNILFG-----KEYDEERYNSVLNsccLRPDLailpssdLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:PRK11614 99 ENLAMGgffaeRDQFQERIKWVYE---LFPRL-------HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180
....*....|....*....|....*
gi 767925452 716 DAHVGNHIFNSAIRKHLKSKTVLFV 740
Cdd:PRK11614 169 APIIIQQIFDTIEQLREQGMTIFLV 193
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
576-770 |
3.71e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQAWIL-NATLR 640
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLFpNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 641 DNILFG---KEYDEERYNSVLN--SCCLRPDLAilpssdlteigerGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:PRK15439 105 ENILFGlpkRQASMQKMKQLLAalGCQLDLDSS-------------AGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767925452 716 DAHVGNHIFnSAIRKhLKSKTV--LFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 770
Cdd:PRK15439 172 TPAETERLF-SRIRE-LLAQGVgiVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
584-749 |
4.30e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 55.88 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 584 EIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-TFAYVAQQAWILNATLRDNILFGKE---YDEERYNS-VL 658
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKADYEGTVRDLLSSITkdfYTHPYFKTeIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 659 NSCCLRPdlaiLPSSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKHL--KSKT 736
Cdd:cd03237 101 KPLQIEQ----ILDREVPE-------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA-SKVIRRFAenNEKT 168
|
170
....*....|....*.
gi 767925452 737 VLFVTHQL---QYLVD 749
Cdd:cd03237 169 AFVVEHDIimiDYLAD 184
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
578-770 |
4.37e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 57.34 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYV--AQQAWI------LN----ATLRDN 642
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvRFRSPrdAQAAGIaiihqeLNlvpnLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 643 ILFGKEY------D----EERYNSVLNscclRPDLAILPSsdlTEIGErganLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:COG1129 100 IFLGREPrrggliDwramRRRARELLA----RLGLDIDPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 713 SALDAHVGNHIFNsAIRKhLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 770
Cdd:COG1129 169 ASLTEREVERLFR-IIRR-LKAQgvAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
555-749 |
5.61e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 5.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 555 ERPSPEEEEGKHIHLGHLRLQRTLHSIDL-----EIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVA 629
Cdd:PRK13409 327 EERPPRDESERETLVEYPDLTKKLGDFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 630 Q----------QAWILNATlrdnilfgKEYDEERYNSVLnsccLRP-DLAILPSSDLTEigerganLSGGQRQRISLARA 698
Cdd:PRK13409 407 QyikpdydgtvEDLLRSIT--------DDLGSSYYKSEI----IKPlQLERLLDKNVKD-------LSGGELQRVAIAAC 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767925452 699 LYSDRSIYILDDPLSALDAH----VGnhifnSAIRKHL--KSKTVLFVTHQLqYLVD 749
Cdd:PRK13409 468 LSRDADLYLLDEPSAHLDVEqrlaVA-----KAIRRIAeeREATALVVDHDI-YMID 518
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1209-1277 |
6.96e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.02 E-value: 6.96e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVElSGGCIKIDGVRISDIG---LADLRSKLSIIPQEP 1277
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP 371
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
576-772 |
7.43e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.18 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTL-HSIDLEIQEGKLVGICGSVGSGKTSLI------------SAILGQMTLLE-GSIAISGTFAYVAQQawiLNA---- 637
Cdd:PRK10575 24 RTLlHPLSLTFPAGKVTGLIGHNGSGKSTLLkmlgrhqppsegEILLDAQPLESwSSKAFARKVAYLPQQ---LPAaegm 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 638 TLRDNILFGK-----------EYDEERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDRSIY 706
Cdd:PRK10575 101 TVRELVAIGRypwhgalgrfgAADREKVEEAISLVGLKPLAHRLVDS-----------LSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767925452 707 ILDDPLSALD-AHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:PRK10575 170 LLDEPTSALDiAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1209-1259 |
1.19e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 54.32 E-value: 1.19e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvRIS 1259
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVS 90
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
857-1122 |
1.42e-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: 54.80 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 857 LAFLVIMALFMLNVGSTafstwwLSYWIKQGSGNttvtrGNETSVSdsmkdnphmQYYASIYALSmAVMLILKAIRgVVF 936
Cdd:cd18575 2 LIALLIAAAATLALGQG------LRLLIDQGFAA-----GNTALLN---------RAFLLLLAVA-LVLALASALR-FYL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 937 VkGTL--RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAgVFPWF 1014
Cdd:cd18575 60 V-SWLgeRVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLF-ITSPK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1015 LVAVGPLVILFSVLHIVsrVLIRELKRLDNITQSPFL---SHITSSIQGLATIHAYNKGQEFLHRYQELLDDNqapfflF 1091
Cdd:cd18575 138 LTLLVLLVIPLVVLPII--LFGRRVRRLSRASQDRLAdlsAFAEETLSAIKTVQAFTREDAERQRFATAVEAA------F 209
|
250 260 270
....*....|....*....|....*....|..
gi 767925452 1092 TCAMRWLAVRLDLISIA-LITTTGLMIVLMHG 1122
Cdd:cd18575 210 AAALRRIRARALLTALViFLVFGAIVFVLWLG 241
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
578-772 |
1.68e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 53.88 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQAWIL-NATLRDN 642
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIFrKLTVEDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 643 IL-------FGKEYDEERYNSVLNscclrpDLailpssDLTEIGE-RGANLSGGQRQRISLARALYSDRSIYILD----- 709
Cdd:COG1137 99 ILavlelrkLSKKEREERLEELLE------EF------GITHLRKsKAYSLSGGERRRVEIARALATNPKFILLDepfag 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 710 -DPLSALDahvgnhifnsaIRK---HLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:COG1137 167 vDPIAVAD-----------IQKiirHLKERgiGVLITDHNVRETLGiCDRAYIISEGKVLAEGTPEEILN 225
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
913-1124 |
1.83e-07 |
|
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: 54.34 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 913 YYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 992
Cdd:cd18541 41 RYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 993 FIQNVILVFFCVGMIAGVFPWF-LVAVGPLVILFsvlhIVSRVLIRELKRLDNITQSPFlSHITSSIQ----GLATIHAY 1067
Cdd:cd18541 121 LVDALFLGVLVLVMMFTISPKLtLIALLPLPLLA----LLVYRLGKKIHKRFRKVQEAF-SDLSDRVQesfsGIRVIKAF 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767925452 1068 NKGQEFLHRYQELLDDNQApfflftcamRWLA-VRLD---LISIALITTTGLMIVL-------MHGQI 1124
Cdd:cd18541 196 VQEEAEIERFDKLNEEYVE---------KNLRlARVDalfFPLIGLLIGLSFLIVLwyggrlvIRGTI 254
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
575-716 |
1.94e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 54.84 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-FAYVAQ---------QAWIL--NATLRDN 642
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdLSHVPPyqrpinmmfQSYALfpHMTVEQN 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 643 ILFGKEYDEERYNSVLNSCClrpdlAILPSSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALD 716
Cdd:PRK11607 112 IAFGLKQDKLPKAEIASRVN-----EMLGLVHMQEFAKRKPHqLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
900-1083 |
2.60e-07 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 54.06 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 900 SVSDSMKDNPHMQYYASIYALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRF 975
Cdd:cd18573 25 VASKESGDIEIFGLSLKTFALALLGVFVVGAAanfgRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 976 SKDMDEVdvrlpfqAEMFIQNV-------ILVFFCVGMIAGVFP---WFLVAVGPLVILFSVlhivsrVLIRELKRLDNI 1045
Cdd:cd18573 105 SSDTSVV-------GKSLTQNLsdglrslVSGVGGIGMMLYISPkltLVMLLVVPPIAVGAV------FYGRYVRKLSKQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767925452 1046 TQSPfLSHITSS----IQGLATIHAYNKGQEFLHRYQELLDD 1083
Cdd:cd18573 172 VQDA-LADATKVaeerLSNIRTVRAFAAERKEVERYAKKVDE 212
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
565-763 |
2.67e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.24 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 565 KHIHLGHLRLQrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGqmtLLEGSiaiSGTFAYVAQQAWILN----ATLR 640
Cdd:PRK10584 14 KSVGQGEHELS-ILTGVELVVKRGETIALIGESGSGKSTLLAILAG---LDDGS---SGEVSLVGQPLHQMDeearAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 641 -DNILFgkeydeerynsVLNSCCLRPDLAILPSSDLTEI----------------------GER----GANLSGGQRQRI 693
Cdd:PRK10584 87 aKHVGF-----------VFQSFMLIPTLNALENVELPALlrgessrqsrngakalleqlglGKRldhlPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925452 694 SLARALYSDRSIYILDDPLSALDAHVGNHIFN---SAIRKHlkSKTVLFVTHQLQYLVDCDEVIFMKEGCITE 763
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADllfSLNREH--GTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1209-1268 |
2.91e-07 |
|
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: 52.82 E-value: 2.91e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRS 1268
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARLRA 89
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
578-754 |
3.10e-07 |
|
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: 53.39 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQ--MTLLEGSIAISGTFAYVAQQAWI----------LNATLRDN--- 642
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPalARRLHLKKEQPGNHDRIEGLEHIdkvividqspIGRTPRSNpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 643 ---------ILF-----GKEYDEE----RYN-----SVLNSCC------------LRPDLAILPSSDLTEI--GERGANL 685
Cdd:cd03271 91 ytgvfdeirELFcevckGKRYNREtlevRYKgksiaDVLDMTVeealeffenipkIARKLQTLCDVGLGYIklGQPATTL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925452 686 SGGQRQRISLARALySDRS----IYILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVI 754
Cdd:cd03271 171 SGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWII 242
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
570-759 |
3.16e-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: 52.25 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 570 GHLRLqrtLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMT--LLEGSIAISG-----TFA----YVAQQ-AWILNA 637
Cdd:cd03232 18 GKRQL---LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGrpldkNFQrstgYVEQQdVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 638 TLRDNILFgkeydeerynsvlnSCCLRpdlailpssdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:cd03232 95 TVREALRF--------------SALLR-------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767925452 718 HVGNHIFNsAIRKHLKS-KTVLFVTHQ-----LQYLvdcDEVIFMKEG 759
Cdd:cd03232 142 QAAYNIVR-FLKKLADSgQAILCTIHQpsasiFEKF---DRLLLLKRG 185
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1193-1322 |
3.62e-07 |
|
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: 52.49 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLP--LVLKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVE-LSGGCIKIDGV---RISDIGLADL 1266
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILGGLDrPTSGEVRVDGTdisKLSEKELAAF 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 1267 R-SKLSIIPQEPVLFSG-TVRSNLD-------PFNQYTEDQIWDALERTHMKecdssHLKNKFCS 1322
Cdd:cd03255 80 RrRHIGFVFQSFNLLPDlTALENVElplllagVPKKERRERAEELLERVGLG-----DRLNHYPS 139
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1193-1280 |
3.76e-07 |
|
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: 52.47 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLP--LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGladlrSKL 1270
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90
....*....|
gi 767925452 1271 SIIPQEPVLF 1280
Cdd:cd03293 76 GYVFQQDALL 85
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1195-1310 |
4.55e-07 |
|
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: 52.15 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1195 FENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIsdiglADLRSKLSIIP 1274
Cdd:cd03235 2 VEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYVP 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767925452 1275 QE-------PVLFSGTVRSNLDP----FNQYTEDQ---IWDALERTHMKE 1310
Cdd:cd03235 75 QRrsidrdfPISVRDVVLMGLYGhkglFRRLSKADkakVDEALERVGLSE 124
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
576-759 |
4.59e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.02 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQAWILNA-TLR 640
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqlgIGIIYQELSVIDElTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 641 DNILFGK------------EYDEERynSVLNSCCLRPDLAIlpssdltEIGERGANLSGGQRQRISLARALYSDRSIYIL 708
Cdd:PRK09700 99 ENLYIGRhltkkvcgvniiDWREMR--VRAAMMLLRVGLKV-------DLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767925452 709 DDPLSALDAHVGNHIFnsAIRKHLKS--KTVLFVTHQLQYLVD-CDEVIFMKEG 759
Cdd:PRK09700 170 DEPTSSLTNKEVDYLF--LIMNQLRKegTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
578-770 |
4.91e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.54 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAI-----LGQMTLLEGSIAISGTFAY--------VAQQAWIL--------N 636
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYspdvdpieVRREVGMVfqypnpfpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 637 ATLRDNILFG----------KEYDEerynsvlnscclRPDLAILPSSDLTEIGER----GANLSGGQRQRISLARALYSD 702
Cdd:PRK14267 100 LTIYDNVAIGvklnglvkskKELDE------------RVEWALKKAALWDEVKDRlndyPSNLSGGQRQRLVIARALAMK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 703 RSIYILDDPLSALDAhVGNHIFNSAIRKHLKSKTVLFVTHQ-LQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:PRK14267 168 PKILLMDEPTANIDP-VGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
685-770 |
5.39e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 53.92 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 685 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnsAIRKHLKSKT---VLFVTHQLQyLVD--CDEVIFMKEG 759
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQIL--DLLKDLQRELgmaLLLITHDLG-VVRrfADRVAVMRQG 233
|
90
....*....|.
gi 767925452 760 CITERGTHEEL 770
Cdd:COG4172 234 EIVEQGPTAEL 244
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
554-749 |
6.49e-07 |
|
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: 53.63 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 554 DERPSPEEEEGKHIhLGHLRLQRTLHSIDLEIQEGKL-----VGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYV 628
Cdd:COG1245 328 EVHAPRREKEEETL-VEYPDLTKSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 629 AQqaWILN-------ATLRDNIlfGKEYDEERYNSVLnsccLRPdLAI--LPSSDLTEigerganLSGGQRQRISLARAL 699
Cdd:COG1245 407 PQ--YISPdydgtveEFLRSAN--TDDFGSSYYKTEI----IKP-LGLekLLDKNVKD-------LSGGELQRVAIAACL 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767925452 700 YSDRSIYILDDPLSALDA----HVGnhifnSAIRKHLKS--KTVLFVTHQLqYLVD 749
Cdd:COG1245 471 SRDADLYLLDEPSAHLDVeqrlAVA-----KAIRRFAENrgKTAMVVDHDI-YLID 520
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1209-1309 |
7.15e-07 |
|
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: 51.73 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI---SDIGLADLRSKLSIIPQEPVLFSG-TV 1284
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRRMGMLFQSGALFDSlTV 94
|
90 100
....*....|....*....|....*.
gi 767925452 1285 RSNLD-PFNQYTEDQIWDALERTHMK 1309
Cdd:cd03261 95 FENVAfPLREHTRLSEEEIREIVLEK 120
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1193-1277 |
7.67e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 52.06 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLPLVLKKVSFTIkPKEK-IGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLS 1271
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNI-PKGQwTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
....*.
gi 767925452 1272 IIPQEP 1277
Cdd:PRK13648 87 IVFQNP 92
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
916-1083 |
7.72e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 52.51 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 916 SIYALSMAVMLILKA----IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkdmDEVDVRlpfqaE 991
Cdd:cd18555 42 NVLGIGILILFLLYGlfsfLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRAN---SNVYIR-----Q 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 992 MFIQNVI--------LVFFCVGMIagVFPWFLVAVgplVILFSVLHIVSRVL----IRELKRLDNITQSPFLSHITSSIQ 1059
Cdd:cd18555 114 ILSNQVIsliidlllLVIYLIYML--YYSPLLTLI---VLLLGLLIVLLLLLtrkkIKKLNQEEIVAQTKVQSYLTETLY 188
|
170 180
....*....|....*....|....
gi 767925452 1060 GLATIHAYNKGQEFLHRYQELLDD 1083
Cdd:cd18555 189 GIETIKSLGSEKNIYKKWENLFKK 212
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
576-753 |
8.64e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 8.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSL---ISAILGQMTLlEGSIAISG---TFAYV--AQQAWIL----------NA 637
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLmkvLSGVYPHGTY-EGEIIFEGeelQASNIrdTERAGIAiihqelalvkEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 638 TLRDNILFGKE--------YDE--ERYNSVLNscclRPDLAILPSsdlTEIGergaNLSGGQRQRISLARALYSDRSIYI 707
Cdd:PRK13549 98 SVLENIFLGNEitpggimdYDAmyLRAQKLLA----QLKLDINPA---TPVG----NLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767925452 708 LDDPLSALDAHVGNHIFNsaIRKHLKSKTV--LFVTHQLqylvdcDEV 753
Cdd:PRK13549 167 LDEPTASLTESETAVLLD--IIRDLKAHGIacIYISHKL------NEV 206
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
575-754 |
9.44e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 51.65 E-value: 9.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTF--AYVAQQAWiLNATLRDNIlfgkeydeE 652
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLriGYVPQKLY-LDTTLPLTV--------N 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 653 RYNSvlnsccLRPDLA---ILPSSDLTE----IGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD--AHVGNHI 723
Cdd:PRK09544 88 RFLR------LRPGTKkedILPALKRVQaghlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDvnGQVALYD 161
|
170 180 190
....*....|....*....|....*....|..
gi 767925452 724 FNSAIRKHLKSkTVLFVTHQLQY-LVDCDEVI 754
Cdd:PRK09544 162 LIDQLRRELDC-AVLMVSHDLHLvMAKTDEVL 192
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1193-1284 |
9.65e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.14 E-value: 9.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLPLV---LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI----SDIGLAD 1265
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100
....*....|....*....|.
gi 767925452 1266 LRSKLSIIPQ--EPVLFSGTV 1284
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTV 103
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
576-770 |
9.71e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.40 E-value: 9.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSID---LEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-FAYVAQQAWI----------------L 635
Cdd:PRK15079 32 KTLKAVDgvtLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdLLGMKDDEWRavrsdiqmifqdplasL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 636 NA--TLRDNIL---------FGKEYDEERYNSVLNSCCLRPDLailpssdlteIGERGANLSGGQRQRISLARALYSDRS 704
Cdd:PRK15079 112 NPrmTIGEIIAeplrtyhpkLSRQEVKDRVKAMMLKVGLLPNL----------INRYPHEFSGGQCQRIGIARALILEPK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 705 IYILDDPLSALDAHVGNHIFNsaIRKHLKSK---TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 770
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVVN--LLQQLQREmglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
561-768 |
1.09e-06 |
|
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: 50.60 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 561 EEEGKHIhlghlrlqrtLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQM--TLLEGSIAISGTFayvaqqawILNAT 638
Cdd:cd03217 9 SVGGKEI----------LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGED--------ITDLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 639 L----RDNILFGKEYDEErYNSVLNSCCLRpdlailpssdltEIGErgaNLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:cd03217 71 PeeraRLGIFLAFQYPPE-IPGVKNADFLR------------YVNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767925452 715 LDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYL--VDCDEVIFMKEGCITERGTHE 768
Cdd:cd03217 135 LDIDALRLVAEVINKLREEGKSVLIITHYQRLLdyIKPDRVHVLYDGRIVKSGDKE 190
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1193-1259 |
1.37e-06 |
|
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: 49.37 E-value: 1.37e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767925452 1193 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSL-GMALFRLVELSGGCIKIDGVRIS 1259
Cdd:cd03221 1 IELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTLlKLIAGELEPDEGIVTWGSTVKIG 66
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
578-762 |
1.76e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.34 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQ----QAWILNATL 639
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYIPEdrlgRGLVPDMSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 640 RDNILFGkEYDEERYNS--VLNSCCLRpDLA--------ILPSSDLTEIGergaNLSGGQRQRISLARALYSDRSIYILD 709
Cdd:COG3845 354 AENLILG-RYRRPPFSRggFLDRKAIR-AFAeelieefdVRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAA 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 710 DPLSALDahVGNhIfnSAIRKHL-----KSKTVLFVTHQLQYLVD-CDEVIFMKEGCIT 762
Cdd:COG3845 428 QPTRGLD--VGA-I--EFIHQRLlelrdAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
579-770 |
1.81e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.85 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 579 HSIDLEIQEGKLVGICGSVGSGKTSLISAILGQM----TLLEGSIAISGTFAYVAQQAWILNATLRDNilfgkeyDEERY 654
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPVAPCALRGRKIATIMQN-------PRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 655 NSVLN-------SCCLR---PDLAILPSSdLTEIG----ERGANL-----SGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:PRK10418 93 NPLHTmhthareTCLALgkpADDATLTAA-LEAVGlenaARVLKLypfemSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 716 DAHVGNHIFN---SAIRKHlkSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEEL 770
Cdd:PRK10418 172 DVVAQARILDlleSIVQKR--ALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETL 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
568-718 |
1.93e-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: 50.51 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 568 HLGHLRLQrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAIS---------------------GTFA 626
Cdd:COG4778 18 LQGGKRLP-VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdlaqaspreilalrrRTIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 627 YVAQqawILNATLRDNIL-----------FGKEYDEERYNSVLNSCCLRPDLAILPSsdlteigergANLSGGQRQRISL 695
Cdd:COG4778 97 YVSQ---FLRVIPRVSALdvvaepllergVDREEARARARELLARLNLPERLWDLPP----------ATFSGGEQQRVNI 163
|
170 180
....*....|....*....|...
gi 767925452 696 ARALYSDRSIYILDDPLSALDAH 718
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAA 186
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
923-1163 |
1.96e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 51.33 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 923 AVMLILKAIRGVVFV-------KGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdVRLPFQAEMFIQ 995
Cdd:cd18543 43 LLLLALGVAEAVLSFlrrylagRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLV-QRFLAFGPFLLG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 996 NVILVFFCVGMIAGVFPWF-LVAVGPLVILFsvlhIVSRVLIRELKRLDNITQS---PFLSHITSSIQGLATIHAYNKGQ 1071
Cdd:cd18543 122 NLLTLVVGLVVMLVLSPPLaLVALASLPPLV----LVARRFRRRYFPASRRAQDqagDLATVVEESVTGIRVVKAFGRER 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1072 EFLHRYQELLDDnqapffLFTCAMRwlAVRLDLISIALITT---TGLMIVL-------MHGQIPpayAG--LA-ISYAVQ 1138
Cdd:cd18543 198 RELDRFEAAARR------LRATRLR--AARLRARFWPLLEAlpeLGLAAVLalggwlvANGSLT---LGtlVAfSAYLTM 266
|
250 260
....*....|....*....|....*
gi 767925452 1139 LTGLFQFTVRLASETEARFTSVERI 1163
Cdd:cd18543 267 LVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1209-1288 |
1.96e-06 |
|
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: 50.21 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGLADLRSKLSIIPQEPVLFSG-TVRSN 1287
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIGMVFQDYALFPHlTVAEN 92
|
.
gi 767925452 1288 L 1288
Cdd:cd03259 93 I 93
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1209-1287 |
2.10e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 51.62 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSlgmaLFRLVEL----SGGCIKIDGVRISDI---GLADLRSKLSIIPQEPVLFS 1281
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKST----LIRCINLlerpTSGSVLVDGVDLTALserELRAARRKIGMIFQHFNLLS 95
|
....*..
gi 767925452 1282 G-TVRSN 1287
Cdd:COG1135 96 SrTVAEN 102
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1209-1282 |
2.61e-06 |
|
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: 49.45 E-value: 2.61e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMAL--FRLVELSGGCIKIDGVRISDIgLADLRSKLSII--PQEPVLFSG 1282
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDL-PPEERARLGIFlaFQYPPEIPG 91
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1209-1299 |
2.64e-06 |
|
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: 51.61 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS----GGCIKIDGVRISDIGLADLR----SKLSIIPQEPVlf 1280
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSERELRrirgNRIAMIFQEPM-- 102
|
90 100
....*....|....*....|
gi 767925452 1281 sgtvrSNLDPFnqYT-EDQI 1299
Cdd:COG4172 103 -----TSLNPL--HTiGKQI 115
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1209-1289 |
2.64e-06 |
|
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: 49.47 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMAL--FRLVELSGGCIKIDGVRISDIglaDLRSKLSIIPQEPVLFSG-TVR 1285
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKR---SFRKIIGYVPQDDILHPTlTVR 100
|
....
gi 767925452 1286 SNLD 1289
Cdd:cd03213 101 ETLM 104
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
581-741 |
3.00e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.85 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 581 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAwilnatlrdnilfgkeydeeRYNSVLNS 660
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS--------------------RFMAYLGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 661 C-CLRPDLAIL-----------------PSSDLTEIGERG------ANLSGGQRQRISLARALYSDRSIYILDDPLSALD 716
Cdd:PRK13543 90 LpGLKADLSTLenlhflcglhgrrakqmPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180
....*....|....*....|....*
gi 767925452 717 AHvGNHIFNSAIRKHLKSKTVLFVT 741
Cdd:PRK13543 170 LE-GITLVNRMISAHLRGGGAALVT 193
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
888-1083 |
3.09e-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: 50.74 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 888 SGNTTVTRGNETSVSDSM----KDNPHMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFF 963
Cdd:cd18558 31 NGGMTNITGNSSGLNSSAgpfeKLEEEMTLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 964 DTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVF--FCVGMIAGvfpW----FLVAVGPLVILFSVL--HIVSRVL 1035
Cdd:cd18558 111 DVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGtgFIIGFIRG---WkltlVILAISPVLGLSAVVwaKILSGFT 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767925452 1036 IRELKRLDNITQSPflshiTSSIQGLATIHAYNKGQEFLHRYQELLDD 1083
Cdd:cd18558 188 DKEKKAYAKAGAVA-----EEVLEAFRTVIAFGGQQKEETRYAQNLEI 230
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
578-784 |
3.60e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.43 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVA-------QQAWILNATLRdNILFG--KE 648
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAissglngQLTGIENIELK-GLMMGltKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 649 YDEErynsvlnscclrpdlaILPSS-DLTEIG----ERGANLSGGQRQRISLARALYSDRSIYILDDPLSaldahVGNHI 723
Cdd:PRK13545 119 KIKE----------------IIPEIiEFADIGkfiyQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS-----VGDQT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767925452 724 FNSAIRKHL-----KSKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNNL 784
Cdd:PRK13545 178 FTKKCLDKMnefkeQGKTIFFISHSLsQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNQM 244
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
573-759 |
3.94e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.77 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 573 RLQrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMT--LLEGSIAISG------TFAYVA---QQAWILN--ATL 639
Cdd:PLN03140 892 RLQ-LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGfpkkqeTFARISgycEQNDIHSpqVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 640 RDNILFG------KEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGanLSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:PLN03140 971 RESLIYSaflrlpKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTG--LSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767925452 714 ALDAHVGNhIFNSAIRKHLKS-KTVLFVTHQ--LQYLVDCDEVIFMKEG 759
Cdd:PLN03140 1049 GLDARAAA-IVMRTVRNTVDTgRTVVCTIHQpsIDIFEAFDELLLMKRG 1096
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1193-1288 |
4.31e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 49.99 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG-LADLRSKLS 1271
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90
....*....|....*....
gi 767925452 1272 IIPQEP-VLFSG-TVRSNL 1288
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDL 99
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1167-1310 |
4.91e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.74 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1167 IKTLSLEAP-ARIKNKAPSPDWPQegeVTFENAEMRYRENlPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE 1245
Cdd:PRK10522 299 LNKLALAPYkAEFPRPQAFPDWQT---LELRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQ 374
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767925452 1246 LSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTvrsnLDPFNQYTEDQIWDA-LERTHMKE 1310
Cdd:PRK10522 375 PQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMAH 436
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
575-743 |
5.25e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------------FAYVAQQAWI-LNATLRD 641
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlctyqkqLCFVGHRSGInPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 642 NILFGKEYDEEryNSVLNSCCLRPDLAILpssdlteIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 721
Cdd:PRK13540 94 NCLYDIHFSPG--AVGITELCRLFSLEHL-------IDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|...
gi 767925452 722 HIFnSAIRKH-LKSKTVLFVTHQ 743
Cdd:PRK13540 165 TII-TKIQEHrAKGGAVLLTSHQ 186
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
575-754 |
5.30e-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: 49.18 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRTLHSIDLEIQEGKLVGICGSVGSGKTSL----------------ISA----ILGQM-----TLLEG-SIAIS------ 622
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAyarqFLGQMdkpdvDSIEGlSPAIAidqktt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 623 -----GTFAYVAQqawiLNATLRdnILFGKEYDEERYNSvlnscclrpdlailpssdLTEIG------ERGAN-LSGGQR 690
Cdd:cd03270 88 srnprSTVGTVTE----IYDYLR--LLFARVGIRERLGF------------------LVDVGlgyltlSRSAPtLSGGEA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767925452 691 QRISLARALYSDRS--IYILDDPLSALDAHvGNHIFNSAIrKHLKSK--TVLFVTHQLQYLVDCDEVI 754
Cdd:cd03270 144 QRIRLATQIGSGLTgvLYVLDEPSIGLHPR-DNDRLIETL-KRLRDLgnTVLVVEHDEDTIRAADHVI 209
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
585-749 |
6.09e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 585 IQEGKLVGICGSVGSGKTSLISAILGQMT------------------------------LLEGSIAISGTFAYVAQQAWI 634
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIpnlgdyeeepswdevlkrfrgtelqnyfkkLYNGEIKVVHKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 635 LNATLRDnILfgKEYDE----ERYNSVLNscclrpdlailpssdLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILD 709
Cdd:PRK13409 176 FKGKVRE-LL--KKVDErgklDEVVERLG---------------LENILDRDiSELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767925452 710 DPLSALDahVGNHIfNSA--IRKHLKSKTVLFVTHQ---LQYLVD 749
Cdd:PRK13409 238 EPTSYLD--IRQRL-NVArlIRELAEGKYVLVVEHDlavLDYLAD 279
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
576-776 |
6.27e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.29 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNA---------------TLR 640
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAgvaiiyqelhlvpemTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 641 DNILFGK------EYDEERYNSVLNSCCLRPDLAILPSSDLteigergANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:PRK11288 98 ENLYLGQlphkggIVNRRLLNYEAREQLEHLGVDIDPDTPL-------KYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 715 LDAHVGNHIFnSAIRKhLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCITErgTHEELMNLNGD 776
Cdd:PRK11288 171 LSAREIEQLF-RVIRE-LRAegRVILYVSHRMEEIFAlCDAITVFKDGRYVA--TFDDMAQVDRD 231
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
578-773 |
6.93e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.17 E-value: 6.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQ--------MTLLEG--------SIAISGTFAYVA----QQAWILNA 637
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRsygrnisgTVFKDGkevdvstvSDAIDAGLAYVTedrkGYGLNLID 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 638 TLRDNI----LFG----------KEYDE-ERYnsvlnscclRPDLAILPSSDLTEIGergaNLSGGQRQRISLARALYSD 702
Cdd:NF040905 356 DIKRNItlanLGKvsrrgvidenEEIKVaEEY---------RKKMNIKTPSVFQKVG----NLSGGNQQKVVLSKWLFTD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 703 RSIYILDDPLSALDahVGN--HIFnSAIRKHLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCIT-----ERGTHEELMNL 773
Cdd:NF040905 423 PDVLILDEPTRGID--VGAkyEIY-TIINELAAEgKGVIVISSELPELLGmCDRIYVMNEGRITgelprEEASQERIMRL 499
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1192-1284 |
7.46e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 49.25 E-value: 7.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1192 EVTFENAEMRYRENLP---LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIdGVRISDIG-----L 1263
Cdd:PRK13634 2 DITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkL 80
|
90 100
....*....|....*....|...
gi 767925452 1264 ADLRSKLSIIPQ--EPVLFSGTV 1284
Cdd:PRK13634 81 KPLRKKVGIVFQfpEHQLFEETV 103
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
572-770 |
9.03e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 48.76 E-value: 9.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 572 LRLQ----RTLHSIDLEIQEGKLVGICGSVGSGKTSLISaILGQMTLLEGSIAISGTFAYVAQQAW-------------- 633
Cdd:PRK14247 9 LKVSfgqvEVLDGVNLEIPDNTITALMGPSGSGKSTLLR-VFNRLIELYPEARVSGEVYLDGQDIFkmdvielrrrvqmv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 634 ------ILNATLRDNILFG---------KEYDEERYNSVLNSCCLRPDLAilpssdlTEIGERGANLSGGQRQRISLARA 698
Cdd:PRK14247 88 fqipnpIPNLSIFENVALGlklnrlvksKKELQERVRWALEKAQLWDEVK-------DRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767925452 699 LYSDRSIYILDDPLSALDAHvgnhifNSAIRKHL-----KSKTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPE------NTAKIESLflelkKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1202-1288 |
9.09e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 48.56 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1202 YRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFS 1281
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
....*..
gi 767925452 1282 GTVRSNL 1288
Cdd:PRK10247 95 DTVYDNL 101
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
680-755 |
9.24e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.01 E-value: 9.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 680 ERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhvgnhIFNSAIR---KHLKSK-TVLFVTHQLQ---------- 745
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDP-----ISTLRIEelmHELKEQyTIIIVTHNMQqaarvsdmta 221
|
90 100
....*....|....*....|....*.
gi 767925452 746 --------------YLVDCD--EVIF 755
Cdd:PRK14243 222 ffnveltegggrygYLVEFDrtEKIF 247
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1196-1277 |
9.44e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.94 E-value: 9.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1196 ENAEMRY-RENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIP 1274
Cdd:PRK13642 8 ENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
...
gi 767925452 1275 QEP 1277
Cdd:PRK13642 88 QNP 90
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1160-1273 |
9.58e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 50.06 E-value: 9.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1160 VERINHYIKtLSLEAPARIKNKApspdwpqegeVTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSlgma 1239
Cdd:COG0488 294 PPRRDKTVE-IRFPPPERLGKKV----------LELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKST---- 356
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 767925452 1240 LFRL----VELSGGCIKI-DGVRIS--DIGLADLRSKLSII 1273
Cdd:COG0488 357 LLKLlageLEPDSGTVKLgETVKIGyfDQHQEELDPDKTVL 397
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
685-770 |
9.74e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.85 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 685 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN-SAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCIT 762
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQlIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAV 248
|
....*...
gi 767925452 763 ERGTHEEL 770
Cdd:PRK10261 249 ETGSVEQI 256
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
576-759 |
1.29e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQA-WILNATLR 640
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQELnLVLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 641 DNILFGkeydeeRYNS----VLNSCCLRPDLAILPSSDL-TEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:PRK10982 92 DNMWLG------RYPTkgmfVDQDKMYRDTKAIFDELDIdIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767925452 716 DAHVGNHIFnSAIRKhLKSK--TVLFVTHQLQYLVD-CDEVIFMKEG 759
Cdd:PRK10982 166 TEKEVNHLF-TIIRK-LKERgcGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1209-1288 |
1.36e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 49.25 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--VRISDIGLAdLRSKLSIIPQEPVLFSG-TVR 1285
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDA-QAAGIAIIHQELNLVPNlSVA 97
|
...
gi 767925452 1286 SNL 1288
Cdd:COG1129 98 ENI 100
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1209-1320 |
1.40e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 48.23 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVL-FSGTVRS- 1286
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEv 96
|
90 100 110
....*....|....*....|....*....|....*..
gi 767925452 1287 ---NLDPFNQYTEDQiwDALERTHMKECDSSHLKNKF 1320
Cdd:PRK13548 97 vamGRAPHGLSRAED--DALVAAALAQVDLAHLAGRD 131
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1193-1352 |
1.42e-05 |
|
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: 48.16 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSL-GMALFRLVELSGGCIKIDGVRISDIGLADLRSKLS 1271
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLlSLITGDLPPTYGNDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1272 II---------PQEPVL------FSGTVrsnlDPFNQYTEDQI---WDALERTHMkecdsSHLKNK-FCSL---Qkmfhr 1329
Cdd:COG1119 82 LVspalqlrfpRDETVLdvvlsgFFDSI----GLYREPTDEQReraRELLELLGL-----AHLADRpFGTLsqgE----- 147
|
170 180
....*....|....*....|...
gi 767925452 1330 hgptaldfRRRVLfltilfpIAR 1352
Cdd:COG1119 148 --------QRRVL-------IAR 155
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
686-770 |
1.45e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.95 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 686 SGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI----------FNSAIrkhlksktvLFVTHQLQYLVD-CDEVI 754
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQImtllnelkreFNTAI---------IMITHDLGVVAGiCDKVL 233
|
90
....*....|....*.
gi 767925452 755 FMKEGCITERGTHEEL 770
Cdd:PRK09473 234 VMYAGRTMEYGNARDV 249
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
584-749 |
1.45e-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: 47.18 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 584 EIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-TFAYVAQQAwilnatlrdnilfgkeydeerynsvlnscc 662
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQYI------------------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 663 lrpdlailpssdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKHLK--SKTVLFV 740
Cdd:cd03222 71 ---------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNA-ARAIRRLSEegKKTALVV 128
|
170
....*....|..
gi 767925452 741 THQL---QYLVD 749
Cdd:cd03222 129 EHDLavlDYLSD 140
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
566-716 |
1.71e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 566 HIHLGHLRLQ--RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISgtFAYVA-----QQAWILNAT 638
Cdd:PRK10938 5 QISQGTFRLSdtKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ--FSHITrlsfeQLQKLVSDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 639 LRDN---ILFGKEYDEERYNSVL-------NSCCLRpdLA-ILPSSDLteIGERGANLSGGQRQRISLARALYSDRSIYI 707
Cdd:PRK10938 83 WQRNntdMLSPGEDDTGRTTAEIiqdevkdPARCEQ--LAqQFGITAL--LDRRFKYLSTGETRKTLLCQALMSEPDLLI 158
|
....*....
gi 767925452 708 LDDPLSALD 716
Cdd:PRK10938 159 LDEPFDGLD 167
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
581-744 |
1.73e-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: 49.63 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 581 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-----TFAYVAQ------QAWIL--NATLRDNILF-- 645
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietNLDAVRQslgmcpQHNILfhHLTVAEHILFya 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 646 ---GKEYDEERYNSVlnscclrpdlAILPSSDLT-EIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 721
Cdd:TIGR01257 1029 qlkGRSWEEAQLEME----------AMLEDTGLHhKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180
....*....|....*....|...
gi 767925452 722 HIFNsAIRKHLKSKTVLFVTHQL 744
Cdd:TIGR01257 1099 SIWD-LLLKYRSGRTIIMSTHHM 1120
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
685-772 |
2.04e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.78 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 685 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKHLKSKTVLFVTHQL-QYLVDCDEVIFMKEGCITE 763
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVE 242
|
....*....
gi 767925452 764 RGTHEELMN 772
Cdd:PRK14271 243 EGPTEQLFS 251
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
566-718 |
2.10e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.90 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 566 HIHLGHlRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMT--------LLEGSIAISGT--FAYVAQQAWIL 635
Cdd:PRK13547 6 HLHVAR-RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEplAAIDAPRLARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 636 NATL------------RDNILFGKeYDEERYNSVLN-------SCCL-RPDLAILPSSDLTeigergaNLSGGQRQRISL 695
Cdd:PRK13547 85 RAVLpqaaqpafafsaREIVLLGR-YPHARRAGALThrdgeiaWQALaLAGATALVGRDVT-------TLSGGELARVQF 156
|
170 180 190
....*....|....*....|....*....|...
gi 767925452 696 ARAL---------YSDRSIYILDDPLSALD-AH 718
Cdd:PRK13547 157 ARVLaqlwpphdaAQPPRYLLLDEPTAALDlAH 189
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
685-772 |
2.14e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.93 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 685 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnsAIRKHLKSK---TVLFVTHQLQYLVD-CDEVIFMKEGC 760
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQIL--QLLRELQQElnmGLLFITHNLSIVRKlADRVAVMQNGR 234
|
90
....*....|..
gi 767925452 761 ITERGTHEELMN 772
Cdd:PRK15134 235 CVEQNRAATLFS 246
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
563-770 |
2.29e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 47.92 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 563 EGKHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-FAYVAQQawILNatLRD 641
Cdd:PRK13636 7 KVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpIDYSRKG--LMK--LRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 642 NI-LFGKEYDEERYN-SVLNSCCLRPDLAILPSSDLTEIGERGAN--------------LSGGQRQRISLARALYSDRSI 705
Cdd:PRK13636 83 SVgMVFQDPDNQLFSaSVYQDVSFGAVNLKLPEDEVRKRVDNALKrtgiehlkdkpthcLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 706 YILDDPLSALDAhVGnhifNSAIRKHLKSK------TVLFVTHQLQYL-VDCDEVIFMKEGCITERGTHEEL 770
Cdd:PRK13636 163 LVLDEPTAGLDP-MG----VSEIMKLLVEMqkelglTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
576-766 |
2.49e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 47.82 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 576 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT---------------------FAYVAQQawI 634
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstsknkdikqirkkvglvFQFPESQ--L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 635 LNATLRDNILFG-------KEYDEERynsvlnsccLRPDLAILPSSDltEIGERGA-NLSGGQRQRISLARALYSDRSIY 706
Cdd:PRK13649 99 FEETVLKDVAFGpqnfgvsQEEAEAL---------AREKLALVGISE--SLFEKNPfELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 707 ILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGT 766
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
578-770 |
2.57e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 47.76 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-TFAYVAQQawILNATLRDNILFGKEYDEERYNS 656
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGePIKYDKKS--LLEVRKTVGIVFQNPDDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 657 VLNSCCLRPDLAILPSSD--------LTEIGERG------ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 722
Cdd:PRK13639 96 VEEDVAFGPLNLGLSKEEvekrvkeaLKAVGMEGfenkppHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767925452 723 IFNSAIRKHLKSKTVLFVTHQLQYL-VDCDEVIFMKEGCITERGTHEEL 770
Cdd:PRK13639 176 IMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
931-1042 |
2.66e-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: 47.69 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 931 IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVF-FCVGMIag 1009
Cdd:cd18784 55 IRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIgVIVFMF-- 132
|
90 100 110
....*....|....*....|....*....|...
gi 767925452 1010 VFPWFLVAVgpLVILFSVLHIVSRVLIRELKRL 1042
Cdd:cd18784 133 KLSWQLSLV--TLIGLPLIAIVSKVYGDYYKKL 163
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
578-753 |
2.94e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.48 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFA--YVAQQAWI--------L--NATLRDN 642
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpvRIRspRDAIALGIgmvhqhfmLvpNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 643 ILFGKEydeerynsvlNSCCLRPDLAILpSSDLTEIGER-G---------ANLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:COG3845 101 IVLGLE----------PTKGGRLDRKAA-RARIRELSERyGldvdpdakvEDLSVGEQQRVEILKALYRGARILILDEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767925452 713 SALDAHVGNHIFnsAIRKHLKS--KTVLFVTHQLqylvdcDEV 753
Cdd:COG3845 170 AVLTPQEADELF--EILRRLAAegKSIIFITHKL------REV 204
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1210-1277 |
3.20e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.09 E-value: 3.20e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767925452 1210 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdIGLADLRS-KLSIIPQEP 1277
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSqRIRMIFQDP 96
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1209-1259 |
3.43e-05 |
|
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: 46.76 E-value: 3.43e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvRIS 1259
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVS 86
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
581-763 |
4.91e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 581 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGtfAYVAQQAW-----ILNATLRDNILF-------GKE 648
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG--KPVTAEQPedyrkLFSAVFTDFHLFdqllgpeGKP 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 649 YDEERYNSVLNSCCLRpdlailpsSDLTEIGERGAN--LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVgNHIFNS 726
Cdd:PRK10522 420 ANPALVEKWLERLKMA--------HKLELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFYQ 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 767925452 727 AIRKHLKS--KTVLFVTHQLQYLVDCDEVIFMKEGCITE 763
Cdd:PRK10522 491 VLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1210-1319 |
5.26e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 46.76 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1210 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--VRISDIGLADLRSKLSIIPQEP--VLFSGTVR 1285
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQDPdnQLFSASVY 101
|
90 100 110
....*....|....*....|....*....|....*..
gi 767925452 1286 SNLD--PFN-QYTEDQIWDALERThMKECDSSHLKNK 1319
Cdd:PRK13636 102 QDVSfgAVNlKLPEDEVRKRVDNA-LKRTGIEHLKDK 137
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1196-1284 |
6.22e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 46.27 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1196 ENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQ 1275
Cdd:PRK13647 8 EDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQ 86
|
90
....*....|.
gi 767925452 1276 EP--VLFSGTV 1284
Cdd:PRK13647 87 DPddQVFSSTV 97
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
575-759 |
6.39e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.57 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 575 QRT-LHSIDLEIQEGKLVGICGSVGSGKTSLISAILG--QMTLLEGSIAISG---------TFAYVAQQAWIL-NATLRD 641
Cdd:PLN03211 80 ERTiLNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNrkptkqilkRTGFVTQDDILYpHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 642 NILF------GKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGanLSGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:PLN03211 160 TLVFcsllrlPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRG--ISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767925452 716 DAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLV--DCDEVIFMKEG 759
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVyqMFDSVLVLSEG 283
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
919-1120 |
6.42e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 46.42 E-value: 6.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 919 ALSMAVML--ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFsKDMDEVDVRLPFQAEMFIQN 996
Cdd:cd18566 47 GVVIAILLesLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLTGQALLALLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 997 VILVFFCVGMIAgVFPWFLVAVgPLVIL--FSV----LHIVSRVLIRELKRLDNITQspflSHITSSIQGLATIHAYNKG 1070
Cdd:cd18566 126 LPFVLIFLGLIW-YLGGKLVLV-PLVLLglFVLvailLGPILRRALKERSRADERRQ----NFLIETLTGIHTIKAMAME 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767925452 1071 QEFLHRYQELLDDnqapfflftCAMRWLAVRlDLISIALITTTGLMIVLM 1120
Cdd:cd18566 200 PQMLRRYERLQAN---------AAYAGFKVA-KINAVAQTLGQLFSQVSM 239
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1155-1305 |
7.39e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 47.11 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1155 ARFTS-VERINHYIKtlSLEAPARIKNKAPSPDWPQEGEVTFENAEMRYRENLPLVlKKVSFTIKPKEKIGIVGRTGSGK 1233
Cdd:COG4178 326 AEWRAtVDRLAGFEE--ALEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLL-EDLSLSLKPGERLLITGPSGSGK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1234 SSlgmaLFRLveLSG------GCIKI-DGVRIsdigladlrsklSIIPQEPVLFSGTVRSNL---DPFNQYTEDQIWDAL 1303
Cdd:COG4178 403 ST----LLRA--IAGlwpygsGRIARpAGARV------------LFLPQRPYLPLGTLREALlypATAEAFSDAELREAL 464
|
..
gi 767925452 1304 ER 1305
Cdd:COG4178 465 EA 466
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1209-1288 |
8.73e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.97 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAdLRSKLSI--IPQEPVLFSG-TVR 1285
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFPNlSVK 104
|
...
gi 767925452 1286 SNL 1288
Cdd:PRK15439 105 ENI 107
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1184-1278 |
9.57e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.77 E-value: 9.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1184 SPDWPQEGEVTFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG------ 1255
Cdd:PRK10261 4 SDELDARDVLAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrr 83
|
90 100 110
....*....|....*....|....*....|.
gi 767925452 1256 ----VRISDIGLADLR----SKLSIIPQEPV 1278
Cdd:PRK10261 84 srqvIELSEQSAAQMRhvrgADMAMIFQEPM 114
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
578-759 |
1.00e-04 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 44.95 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 578 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQmtlLEGSIAISGTFAYVAQQAWILNATLRDNILFGKEydEERYNSV 657
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSE--EDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 658 LN-------SCCLRPDLAIlpssdlteigeRGanLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSaIR- 729
Cdd:cd03233 98 LTvretldfALRCKGNEFV-----------RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKC-IRt 163
|
170 180 190
....*....|....*....|....*....|...
gi 767925452 730 --KHLKSKTVLFVTHQLQYLVDC-DEVIFMKEG 759
Cdd:cd03233 164 maDVLKTTTFVSLYQASDEIYDLfDKVLVLYEG 196
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1205-1288 |
1.07e-04 |
|
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: 45.62 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1205 NLPL----VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlrsKLSIIPQEPVLF 1280
Cdd:cd03291 44 NLCLvgapVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIM 110
|
....*...
gi 767925452 1281 SGTVRSNL 1288
Cdd:cd03291 111 PGTIKENI 118
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1193-1288 |
1.27e-04 |
|
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: 44.07 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLPLVlKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlRSKLSI 1272
Cdd:cd03223 1 IELENLSLATPDGRVLL-KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLF 68
|
90
....*....|....*.
gi 767925452 1273 IPQEPVLFSGTVRSNL 1288
Cdd:cd03223 69 LPQRPYLPLGTLREQL 84
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1209-1278 |
1.29e-04 |
|
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: 43.96 E-value: 1.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLSIIPQEPV 1278
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQLSV 85
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1193-1277 |
1.44e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 45.49 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLP-LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLS 1271
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
....*.
gi 767925452 1272 IIPQEP 1277
Cdd:PRK13650 85 MVFQNP 90
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1193-1276 |
1.58e-04 |
|
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: 44.71 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSK 1269
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
....*..
gi 767925452 1270 LSIIPQE 1276
Cdd:cd03292 80 IGVVFQD 86
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1210-1267 |
1.74e-04 |
|
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: 44.94 E-value: 1.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 767925452 1210 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLR 1267
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELR 97
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1193-1277 |
2.00e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 44.79 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLV---ELSGGCIKIDGVRISDIGLADLRSK 1269
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
....*...
gi 767925452 1270 LSIIPQEP 1277
Cdd:PRK13640 86 VGIVFQNP 93
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1193-1291 |
2.01e-04 |
|
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: 44.28 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDiGLADLRSKL 1270
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100
....*....|....*....|..
gi 767925452 1271 SIIPQEPVLFSG-TVRSNLDPF 1291
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYF 102
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
932-1083 |
2.15e-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: 45.02 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 932 RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILvffCVGMIAgvf 1011
Cdd:cd18590 56 RGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVK---TLGMLG--- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1012 pwFLVAVGPLVILFSVLHIVSRVLI--------RELKR--LDNITQSPFLshITSSIQGLATIHAYNKGQEFLHRYQELL 1081
Cdd:cd18590 130 --FMLSLSWQLTLLTLIEMPLTAIAqkvyntyhQKLSQavQDSIAKAGEL--AREAVSSIRTVRSFKAEEEEACRYSEAL 205
|
..
gi 767925452 1082 DD 1083
Cdd:cd18590 206 ER 207
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1204-1278 |
2.36e-04 |
|
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: 43.57 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1204 ENL--PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIS--------DIGLA----DlRSK 1269
Cdd:cd03215 8 RGLsvKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrsprdaiRAGIAyvpeD-RKR 86
|
....*....
gi 767925452 1270 LSIIPQEPV 1278
Cdd:cd03215 87 EGLVLDLSV 95
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1213-1277 |
2.66e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 44.70 E-value: 2.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767925452 1213 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG---VRISDIGLADLRSKLSIIPQEP 1277
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdlLGMKDDEWRAVRSDIQMIFQDP 107
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
591-770 |
2.76e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 44.41 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 591 VGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQA--WILNATLRDNILFG-------KE 648
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkenirevrkFVGLVFQNPddQIFSPTVEQDIAFGpinlgldEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 649 YDEERYNSVLNSCCLRPDLAILPSsdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIF---N 725
Cdd:PRK13652 113 TVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIdflN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767925452 726 SAIRKHlkSKTVLFVTHQLQYLVDCDEVIF-MKEGCITERGTHEEL 770
Cdd:PRK13652 182 DLPETY--GMTVIFSTHQLDLVPEMADYIYvMDKGRIVAYGTVEEI 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
581-769 |
2.76e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.29 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 581 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVA---------------QQAWILNATLRDN 642
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpiDIRSPRdairagimlcpedrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 643 ILFGKeydeeRYNSVLNSCCLRP------------DLAILPSSDLTEIGergaNLSGGQRQRISLARALYSDRSIYILDD 710
Cdd:PRK11288 352 INISA-----RRHHLRAGCLINNrweaenadrfirSLNIKTPSREQLIM----NLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767925452 711 PLSALDahVG------NHIFNSAIRKhlksKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEE 769
Cdd:PRK11288 423 PTRGID--VGakheiyNVIYELAAQG----VAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
919-1079 |
2.90e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 44.43 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 919 ALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVrlpFQAEMFI 994
Cdd:cd18564 57 AAALVGIALLRGLasyaGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQD---LLVSGVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 995 QNVILVFFCVGMIAGVFpWF-----LVAVGPL-VILFSVLHIVSRvlIRELKRldniTQSPFLSHITS----SIQGLATI 1064
Cdd:cd18564 134 PLLTNLLTLVGMLGVMF-WLdwqlaLIALAVApLLLLAARRFSRR--IKEASR----EQRRREGALASvaqeSLSAIRVV 206
|
170
....*....|....*
gi 767925452 1065 HAYNKGQEFLHRYQE 1079
Cdd:cd18564 207 QAFGREEHEERRFAR 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1204-1261 |
3.30e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.01 E-value: 3.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 1204 ENL--PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--VRISDI 1261
Cdd:COG1129 260 EGLsvGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSP 321
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1209-1308 |
3.36e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 44.30 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI--SDIGLADLRSKLSIIPQEP--VLFSGTV 1284
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVGIVFQNPddQLFAPTV 96
|
90 100 110
....*....|....*....|....*....|.
gi 767925452 1285 RSNL--DPFN-----QYTEDQIWDALERTHM 1308
Cdd:PRK13639 97 EEDVafGPLNlglskEEVEKRVKEALKAVGM 127
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1203-1267 |
3.62e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 44.64 E-value: 3.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767925452 1203 RENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLR 1267
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELR 101
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
942-982 |
4.33e-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: 44.07 E-value: 4.33e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 767925452 942 RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEV 982
Cdd:cd18574 72 RVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEF 112
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
586-749 |
4.54e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.39 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 586 QEGKLVGICGSVGSGKTSLISAILGQMT------------------------------LLEGSIAISGTFAYVAQQAWIL 635
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKpnlgdydeepswdevlkrfrgtelqdyfkkLANGEIKVAHKPQYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 636 NATLRDnILfgKEYDEErynSVLNSccLRPDLAILPSSDlTEIGErganLSGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:COG1245 177 KGTVRE-LL--EKVDER---GKLDE--LAEKLGLENILD-RDISE----LSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767925452 716 DahVGNHIfNSA--IRKHLKS-KTVLFVTHQ---LQYLVD 749
Cdd:COG1245 244 D--IYQRL-NVArlIRELAEEgKYVLVVEHDlaiLDYLAD 280
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1209-1289 |
4.84e-04 |
|
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: 42.95 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1209 VLKKVSFTIkPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAdLRSKLSIIPQEPVLFSG-TVRSN 1287
Cdd:cd03264 15 ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLPQEFGVYPNfTVREF 92
|
..
gi 767925452 1288 LD 1289
Cdd:cd03264 93 LD 94
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1208-1260 |
6.11e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 42.55 E-value: 6.11e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 767925452 1208 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD 1260
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDD 68
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
919-1086 |
6.28e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 43.25 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 919 ALSMAVMLILKAIRGVVFVKGTLRASSR-LHD---ELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVrlpfqaemFI 994
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERlLYDlrlRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSE--------LL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 995 QN-----VILVFFCVGMIAGVF----PWFLVAVGPLVILFsvlhIVSRVLIRELKRL-----DNITQSpfLSHITSSIQG 1060
Cdd:cd18546 114 QTglvqlVVSLLTLVGIAVVLLvldpRLALVALAALPPLA----LATRWFRRRSSRAyrrarERIAAV--NADLQETLAG 187
|
170 180
....*....|....*....|....*.
gi 767925452 1061 LATIHAYNKGQEFLHRYQELLDDNQA 1086
Cdd:cd18546 188 IRVVQAFRRERRNAERFAELSDDYRD 213
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
680-777 |
6.30e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 680 ERGAN-LSGGQRQRISLARALYSDRS--IYILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFM 756
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDI 562
|
90 100 110
....*....|....*....|....*....|.
gi 767925452 757 KE------GCITERGTHEELMN----LNGDY 777
Cdd:TIGR00630 563 GPgagehgGEVVASGTPEEILAnpdsLTGQY 593
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
270-466 |
6.40e-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: 43.31 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 270 EKSLGELINICSNDgqrmfeAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLG---SAVFILFYPAMMFASRltaYFRRK 346
Cdd:cd07346 92 RNRTGDLMSRLTSD------VDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNwklTLVALLLLPLYVLILR---YFRRR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 347 CVAATDERVQKM-------NEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFS 419
Cdd:cd07346 163 IRKASREVRESLaelsaflQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLL 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767925452 420 V--HMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 466
Cdd:cd07346 243 YggYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLER 291
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
947-1145 |
6.84e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 43.29 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 947 LHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNViLVFFCVGMIAGVFPWFLVAVG----PLV 1022
Cdd:cd18778 75 LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNV-LTLVGVAIILFSINPKLALLTlipiPFL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1023 ILFSVLH-IVSRVLIRELKRldnitqspFLSHITS----SIQGLATIHAYNKGQEFLHRYQELLDDnqapffLFTCAMRw 1097
Cdd:cd18778 154 ALGAWLYsKKVRPRYRKVRE--------ALGELNAllqdNLSGIREIQAFGREEEEAKRFEALSRR------YRKAQLR- 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767925452 1098 lAVRLDLI---SIALITTTGLMIVLMHGqippayAGLAISYAVQLTGLFQF 1145
Cdd:cd18778 219 -AMKLWAIfhpLMEFLTSLGTVLVLGFG------GRLVLAGELTIGDLVAF 262
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
686-725 |
8.48e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.69 E-value: 8.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 767925452 686 SGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN 725
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIIN 504
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1209-1310 |
9.58e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 42.69 E-value: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSG-TVRSN 1287
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVREL 96
|
90 100 110
....*....|....*....|....*....|....
gi 767925452 1288 L----DPFNQY-----TEDQ--IWDALERTHMKE 1310
Cdd:PRK11231 97 VaygrSPWLSLwgrlsAEDNarVNQAMEQTRINH 130
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
567-713 |
9.70e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 567 IHLGHLRL----QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAIL-------GQMTLLEGSIAISGTFAYVAQQ-AWI 634
Cdd:NF033858 2 ARLEGVSHrygkTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgarkiqqGRVEVLGGDMADARHRRAVCPRiAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 635 -------LNATL--RDNI-----LFGKEYDEERYnsvlnscclRPDlAILPSSDLTEIGERGA-NLSGGQRQRISLARAL 699
Cdd:NF033858 82 pqglgknLYPTLsvFENLdffgrLFGQDAAERRR---------RID-ELLRATGLAPFADRPAgKLSGGMKQKLGLCCAL 151
|
170 180
....*....|....*....|
gi 767925452 700 YSDRSIYILD------DPLS 713
Cdd:NF033858 152 IHDPDLLILDepttgvDPLS 171
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1209-1277 |
9.89e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 42.59 E-value: 9.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS-----GGCIKIDGVRISDIGLADLRSKLSIIPQEP 1277
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQIP 91
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1213-1277 |
1.25e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 42.64 E-value: 1.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767925452 1213 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG---VRISDIGLADLRSKLSIIPQEP 1277
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdlLKADPEAQKLLRQKIQIVFQNP 101
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1209-1267 |
1.34e-03 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 43.17 E-value: 1.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG---LADLR 1267
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadaLAQLR 84
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
678-770 |
1.37e-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: 43.08 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 678 IGERGANLSGGQRQRISLARALY---SDRSIYILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVI 754
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYII 902
|
90 100
....*....|....*....|..
gi 767925452 755 FM------KEGCITERGTHEEL 770
Cdd:TIGR00630 903 DLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
930-978 |
1.40e-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: 42.24 E-value: 1.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767925452 930 AIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKD 978
Cdd:cd18780 60 FLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSD 108
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1193-1276 |
1.41e-03 |
|
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: 41.50 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiglADLRSKLSI 1272
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGY 74
|
....
gi 767925452 1273 IPQE 1276
Cdd:cd03269 75 LPEE 78
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1193-1304 |
1.41e-03 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 42.00 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1193 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDiGLADLRsklsI 1272
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDER----L 74
|
90 100 110
....*....|....*....|....*....|..
gi 767925452 1273 IPQEpvlfSGTVRSNLDPFNQYTedqiwdALE 1304
Cdd:PRK09493 75 IRQE----AGMVFQQFYLFPHLT------ALE 96
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
683-749 |
1.79e-03 |
|
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: 42.61 E-value: 1.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 683 ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAH-VgnhifnSAIRKHLK--SKTVLFVTHQlQYLVD 749
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAEsV------AWLERHLQeyPGTVVAVTHD-RYFLD 222
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
674-749 |
2.08e-03 |
|
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: 41.58 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 674 DLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDahVGNHIfNSA--IRKHLK-SKTVLFVTHQ---LQY 746
Cdd:cd03236 128 ELRHVLDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD--IKQRL-NAArlIRELAEdDNYVLVVEHDlavLDY 204
|
...
gi 767925452 747 LVD 749
Cdd:cd03236 205 LSD 207
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
568-770 |
2.41e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.03 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 568 HLGHLRlqrTLHSIDLEIQEGKLVGICGSVGSG--KTSLISAILGQ---------MTLLEGSIAISGTFAY--VAQQAWI 634
Cdd:NF000106 22 HFGEVK---AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPdagrrpwrf*TWCANRRALRRTIG*hrPVR*GRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 635 LNATLRDNI-LFGKEYDEERYNSVLnscclRPDlAILPSSDLTEI-GERGANLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:NF000106 99 ESFSGRENLyMIGR*LDLSRKDARA-----RAD-ELLERFSLTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925452 713 SALDAHVGNHIFNSAIRKHLKSKTVLFVThqlQYLVDCD----EVIFMKEGCITERGTHEEL 770
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMVRDGATVLLTT---QYMEEAEqlahELTVIDRGRVIADGKVDEL 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1209-1280 |
2.51e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 41.19 E-value: 2.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKID------GVRISDIGLADLRSKLSIIPQEPVLF 1280
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVFQQPNPF 102
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1201-1275 |
2.52e-03 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 40.95 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1201 RYREN--LPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGV---RISDIGLADLRS-KLSIIP 1274
Cdd:PRK11629 14 RYQEGsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsKLSSAAKAELRNqKLGFIY 93
|
.
gi 767925452 1275 Q 1275
Cdd:PRK11629 94 Q 94
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1193-1265 |
2.57e-03 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 40.70 E-value: 2.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925452 1193 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD 1265
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD 71
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1209-1294 |
2.60e-03 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 41.74 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1209 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI-SDIGLAdlRSKLSIIPQEPVL-FSGTVRS 1286
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLA--RARIGVVPQFDNLdLEFTVRE 133
|
....*...
gi 767925452 1287 NLDPFNQY 1294
Cdd:PRK13536 134 NLLVFGRY 141
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
918-1072 |
3.14e-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: 41.24 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 918 YALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD---VR-LP-- 987
Cdd:cd18584 39 LLLLLLAALLLRALlawaQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTEGVDALDgyfARyLPql 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 988 FQAeMFIQNVILVF-FCVGMIAGVfpwFLVAVGPLVILFSVL-----HIVSRVLIRELKRLDNitqspflsHITSSIQGL 1061
Cdd:cd18584 119 VLA-AIVPLLILVAvFPLDWVSAL---ILLVTAPLIPLFMILigkaaQAASRRQWAALSRLSG--------HFLDRLRGL 186
|
170
....*....|.
gi 767925452 1062 ATIHAYNKGQE 1072
Cdd:cd18584 187 PTLKLFGRARA 197
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1208-1277 |
3.73e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 41.55 E-value: 3.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925452 1208 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLR-SKLSIIPQEP 1277
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrLGVAYIPEDR 342
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
926-1081 |
3.74e-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: 41.01 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 926 LILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDmDEVDVRLPFQAEMFIQNVILVFFCVG 1005
Cdd:cd18568 56 ILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQEN-QKIRRFLTRSALTTILDLLMVFIYLG 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767925452 1006 MIAgVFPWFL--VAVGpLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELL 1081
Cdd:cd18568 135 LMF-YYNLQLtlIVLA-FIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKF 210
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
685-774 |
4.68e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 685 LSGGQRQRISLARALYS---DRSIYILDDPLSAL---DAHVGNHIFNSAIRkhlKSKTVLFVTHQLQYLVDCDEVIFM-- 756
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhthDIKALIYVLQSLTH---QGHTVVIIEHNMHVVKVADYVLELgp 886
|
90 100
....*....|....*....|..
gi 767925452 757 ----KEGCITERGTHEELMNLN 774
Cdd:PRK00635 887 eggnLGGYLLASCSPEELIHLH 908
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1214-1305 |
6.48e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 39.40 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 1214 SFTIKPKEKIGIVGRTGSGKSSlgmaLFRLveLSG------GCIKIDGVRISDIGlADLRSKLsiipqepvLFSG----- 1282
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTS----LLRI--LAGlarpdaGEVLWQGEPIRRQR-DEYHQDL--------LYLGhqpgi 85
|
90 100 110
....*....|....*....|....*....|..
gi 767925452 1283 ----TVRSNLDpFNQ-----YTEDQIWDALER 1305
Cdd:PRK13538 86 ktelTALENLR-FYQrlhgpGDDEALWEALAQ 116
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
651-718 |
7.05e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 7.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767925452 651 EERYNSVLNSCCLRPDLAIlpssdlteigERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAH 718
Cdd:PLN03073 321 EARAASILAGLSFTPEMQV----------KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLH 378
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
912-1066 |
7.33e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 40.19 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 912 QYYASIYALSMAVML------ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRIlnrfSKDMDEVD-V 984
Cdd:cd18783 36 QSYSTLYVLTIGVVIallfegILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVL----TKHMQQIErI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925452 985 RlpfqaeMFI-QNVILVFFCVGMIAGVFP---WFLVAVGPLVILFSVL-----HIVSRVLIRELKRLDNITQSPfLSHIT 1055
Cdd:cd18783 112 R------QFLtGQLFGTLLDATSLLVFLPvlfFYSPTLALVVLAFSALialiiLAFLPPFRRRLQALYRAEGER-QAFLV 184
|
170
....*....|.
gi 767925452 1056 SSIQGLATIHA 1066
Cdd:cd18783 185 ETVHGIRTVKS 195
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
946-1068 |
9.94e-03 |
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Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 39.72 E-value: 9.94e-03
10 20 30 40 50 60 70 80
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gi 767925452 946 RLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAgVFPWFLVAVgpLVILF 1025
Cdd:cd18551 70 DLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMF-LLDWVLTLV--TLAVV 146
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90 100 110 120
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gi 767925452 1026 SVLHIVSRVLIRELKRLDNITQ---SPFLSHITSSIQGLATIHAYN 1068
Cdd:cd18551 147 PLAFLIILPLGRRIRKASKRAQdalGELSAALERALSAIRTVKASN 192
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