|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
103-953 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 806.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQM-TLLEGSIAISGTFAYVAQQAWILNATLRDNILFGKEYDEER 181
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELpPRSDASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPER 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 182 YNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKHLK 261
Cdd:PLN03130 710 YERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELR 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 262 SKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNlNGdyaTIFNNLLlGDTPPVE--INSKKETSGSQKKSQDKG 339
Cdd:PLN03130 790 GKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN-NG---PLFQKLM-ENAGKMEeyVEENGEEEDDQTSSKPVA 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 340 PKTGSVKKEKAV---KPEEGQ--LVQLEEKGQGSVPWSVYGVYIQAAGGplaFLVIMALFMLNVGSTAF---STWWLSYW 411
Cdd:PLN03130 865 NGNANNLKKDSSskkKSKEGKsvLIKQEERETGVVSWKVLERYKNALGG---AWVVMILFLCYVLTEVFrvsSSTWLSEW 941
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 412 IKQGSGNTTvtrgnetsvsdsmkdnpRMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFF 491
Cdd:PLN03130 942 TDQGTPKTH-----------------GPLFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFF 1004
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 492 DTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNV---ILVFFCVGMIAGVFPWflvAVGPLVILFSVLHIVSRVLIRELK 568
Cdd:PLN03130 1005 HTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIfqlLSTFVLIGIVSTISLW---AIMPLLVLFYGAYLYYQSTAREVK 1081
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 569 RLDNITQSPFLSHITSSIQGLATIHAYnKGQEFLHRYQELLDDNQAPFFLFT-CAMRWLAVRLDLISIALITTTGLMIVL 647
Cdd:PLN03130 1082 RLDSITRSPVYAQFGEALNGLSTIRAY-KAYDRMAEINGRSMDNNIRFTLVNmSSNRWLAIRLETLGGLMIWLTASFAVM 1160
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 648 MHGQI--PPAYA---GLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYIKtLSLEAPARIKNKAPSPDWPQEGEVT 722
Cdd:PLN03130 1161 QNGRAenQAAFAstmGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYID-LPSEAPLVIENNRPPPGWPSSGSIK 1239
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 723 FENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIP 802
Cdd:PLN03130 1240 FEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIP 1319
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 803 QEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILD 882
Cdd:PLN03130 1320 QAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLD 1399
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 883 EATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAM 953
Cdd:PLN03130 1400 EATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM 1470
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
80-953 |
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: 774.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 80 DSDERPSPEEEEGKHI--HLGHLRLQR----TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTF 153
Cdd:TIGR00957 622 DSIERRTIKPGEGNSItvHNATFTWARdlppTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 154 AYVAQQAWILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSI 233
Cdd:TIGR00957 702 AYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADI 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 234 YILDDPLSALDAHVGNHIFNSAI--RKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYAT---- 307
Cdd:TIGR00957 782 YLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEflrt 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 308 ---------------------------IFNNLLLGDTppVEINSKKETSGSQKKSQDKGPKTGSVKK-EKA-VKPEEGQL 358
Cdd:TIGR00957 862 yapdeqqghledswtalvsgegkeaklIENGMLVTDV--VGKQLQRQLSASSSDSGDQSRHHGSSAElQKAeAKEETWKL 939
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 359 VQLEEKGQGSVPWSVYGVYIQAAGGPLAFLVIMaLFMLNVGSTAFSTWWLSYWIKQGSGNTTvtrGNETSVsdsmkdnpR 438
Cdd:TIGR00957 940 MEADKAQTGQVELSVYWDYMKAIGLFITFLSIF-LFVCNHVSALASNYWLSLWTDDPMVNGT---QNNTSL--------R 1007
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 439 MQYYASIYALS-MAVMLILKAIRGvvfvkGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQ 517
Cdd:TIGR00957 1008 LSVYGALGILQgFAVFGYSMAVSI-----GGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPV 1082
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 518 AEMFIQNVILVFFCVGMIAGVFPWFLVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNK 597
Cdd:TIGR00957 1083 IKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEE 1162
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 598 GQEFLHRYQELLDDNQAPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRL 677
Cdd:TIGR00957 1163 QERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRM 1242
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 678 ASETEARFTSVERINHYIKTlSLEAPARIKNKAPSPDWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRT 757
Cdd:TIGR00957 1243 SSEMETNIVAVERLKEYSET-EKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRT 1321
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 758 GSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMK 837
Cdd:TIGR00957 1322 GAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLK 1401
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 838 ECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLH 917
Cdd:TIGR00957 1402 TFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLN 1481
|
890 900 910
....*....|....*....|....*....|....*.
gi 1622900610 918 TVLGSDRIMVLAQGQVVEFDTPSVLLSNdSSRFYAM 953
Cdd:TIGR00957 1482 TIMDYTRVIVLDKGEVAEFGAPSNLLQQ-RGIFYSM 1516
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
105-953 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 725.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 105 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLE-GSIAISGTFAYVAQQAWILNATLRDNILFGKEYDEERYN 183
Cdd:PLN03232 632 TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYW 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 184 SVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKHLKSK 263
Cdd:PLN03232 712 RAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGK 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 264 TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNlNGdyaTIFNNLLlgdtppvEINSKKETSGSQKKSQD----KG 339
Cdd:PLN03232 792 TRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSK-SG---SLFKKLM-------ENAGKMDATQEVNTNDEnilkLG 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 340 PK-TGSVKKEKAVKPEEGQ-----LVQLEEKGQGSVPWSVYGVYIQAAGGPLAFLVIMALFMLNVGSTAFSTWWLSYWIK 413
Cdd:PLN03232 861 PTvTIDVSERNLGSTKQGKrgrsvLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVCYLTTEVLRVSSSTWLSIWTD 940
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 414 QgsgnttvtrgnetsvsdSMKDNPRMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDT 493
Cdd:PLN03232 941 Q-----------------STPKSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHT 1003
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 494 TPTGRILNRFSKDMDEVDVRLPFQAEMFIQ---NVILVFFCVGMIAGVFPWflvAVGPLVILFSVLHIVSRVLIRELKRL 570
Cdd:PLN03232 1004 NPTGRVINRFSKDIGDIDRNVANLMNMFMNqlwQLLSTFALIGTVSTISLW---AIMPLLILFYAAYLYYQSTSREVRRL 1080
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 571 DNITQSPFLSHITSSIQGLATIHAYnKGQEFLHRYQELLDDNQAPFFLFTCAM-RWLAVRLDLISIALITTTGLMIVLMH 649
Cdd:PLN03232 1081 DSVTRSPIYAQFGEALNGLSSIRAY-KAYDRMAKINGKSMDNNIRFTLANTSSnRWLTIRLETLGGVMIWLTATFAVLRN 1159
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 650 GQIP-----PAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYIKtLSLEAPARIKNKAPSPDWPQEGEVTFE 724
Cdd:PLN03232 1160 GNAEnqagfASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYID-LPSEATAIIENNRPVSGWPSRGSIKFE 1238
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 725 NAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQE 804
Cdd:PLN03232 1239 DVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQS 1318
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 805 PVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEA 884
Cdd:PLN03232 1319 PVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 885 TAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAM 953
Cdd:PLN03232 1399 TASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRM 1467
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
83-962 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 632.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 83 ERPSPEEEEGKHIHLG----HLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQ 158
Cdd:PTZ00243 649 ATPTSERSAKTPKMKTddffELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQ 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 159 QAWILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDD 238
Cdd:PTZ00243 729 QAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 239 PLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNlNGDYATIFNNLLL---- 314
Cdd:PTZ00243 809 PLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR-TSLYATLAAELKEnkds 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 315 --GDTPP----VEINSKKETSGSQKKSQDKGPKTGSVKkeKAVKPEEGQLVQLEEKGQGSVPWSVYGVYIQAAGGPLAFL 388
Cdd:PTZ00243 888 keGDADAevaeVDAAPGGAVDHEPPVAKQEGNAEGGDG--AALDAAAGRLMTREEKASGSVPWSTYVAYLRFCGGLHAAG 965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 389 VIMALFMLNVGSTAFSTWWLSYWikqgsgnTTvtrgNETSVSDSMkdnprmqyYASIYALSMAVMLILKAIRGVVFVKGT 468
Cdd:PTZ00243 966 FVLATFAVTELVTVSSGVWLSMW-------ST----RSFKLSAAT--------YLYVYLGIVLLGTFSVPLRFFLSYEAM 1026
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 469 LRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPfqaeMFIQNVILVFF--CVGMIAGVF--PWFLV 544
Cdd:PTZ00243 1027 RRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLP----MSYLYLLQCLFsiCSSILVTSAsqPFVLV 1102
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 545 AVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKG----QEFLHRyqelLDDNQAPFFLFT 620
Cdd:PTZ00243 1103 ALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAhlvmQEALRR----LDVVYSCSYLEN 1178
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 621 CAMRWLAVRLDLIS------IALITTTGLMIVLMHGQIppAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 694
Cdd:PTZ00243 1179 VANRWLGVRVEFLSnivvtvIALIGVIGTMLRATSQEI--GLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYY 1256
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 695 IKTLSLEA----------------------------PARIKNKAPSPdwPQEGEVTFENAEMRYRENLPLVLKKVSFTIK 746
Cdd:PTZ00243 1257 TDEVPHEDmpeldeevdalerrtgmaadvtgtvviePASPTSAAPHP--VQAGSLVFEGVQMRYREGLPLVLRGVSFRIA 1334
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 747 PKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQ 826
Cdd:PTZ00243 1335 PREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAE 1414
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 827 IWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILIL-DEATAAMDTETDLLIQETIREAFA 905
Cdd:PTZ00243 1415 VWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFS 1494
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 906 DCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAENKVA 962
Cdd:PTZ00243 1495 AYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEALGRSEA 1551
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
383-695 |
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: 546.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 383 GPLAFLVIMALFMLNVGSTAFSTWWLSYWIKQGSGNTTVTRGNETSVSDSMKDNPRMQYYASIYALSMAVMLILKAIRGV 462
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDNSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 463 VFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWF 542
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 543 LVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCA 622
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 623 MRWLAVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 695
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
106-958 |
6.32e-141 |
|
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: 457.45 E-value: 6.32e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNATLRDNILFGKEYDEERYNSV 185
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSV 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 186 LNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKHLKSKTV 265
Cdd:TIGR01271 522 IKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTR 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 266 LFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIF-------------NNLLLGDT--------------- 317
Cdd:TIGR01271 602 ILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLlgleafdnfsaerRNSILTETlrrvsidgdstvfsg 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 318 ----------PPVEINSKKETS------------------------------------------------------GSQK 333
Cdd:TIGR01271 682 petikqsfkqPPPEFAEKRKQSiilnpiasarkfsfvqmgpqkaqattiedavrepserkfslvpedeqgeeslprGNQY 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 334 KSQ------------------DKGP-----KTGSVKKEKAVKPEEGQLVQL----------------------------- 361
Cdd:TIGR01271 762 HHGlqhqaqrrqsvlqlmthsNRGEnrreqLQTSFRKKSSITQQNELASELdiysrrlskdsvyeiseeineedlkecfa 841
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 362 --EEKGQGSVPWSVYGVYIqAAGGPLAFLVIMAL--FMLNVGSTAFSTWWLS---YWIKQGSGNTTVTRgNETSVSDSMK 434
Cdd:TIGR01271 842 deRENVFETTTWNTYLRYI-TTNRNLVFVLIFCLviFLAEVAASLLGLWLITdnpSAPNYVDQQHANAS-SPDVQKPVII 919
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 435 DNPRMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRL 514
Cdd:TIGR01271 920 TPTSAYYIFYIYVGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDML 999
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 515 PFQAEMFIQNVILVFFCVGMIAGVFPWFLVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHA 594
Cdd:TIGR01271 1000 PLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRA 1079
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 595 YNKGQEFLHRYQELLDDNQAPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHgQIPPAYAGLAISYAVQLTGLFQFT 674
Cdd:TIGR01271 1080 FGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTN-QDGEGEVGIILTLAMNILSTLQWA 1158
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 675 VRLASETEARFTSVERINHYI-------------KTLSLEAPARIKNKAPSPDWPQEGEVTFENAEMRYRENLPLVLKKV 741
Cdd:TIGR01271 1159 VNSSIDVDGLMRSVSRVFKFIdlpqeeprpsgggGKYQLSTVLVIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDL 1238
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 742 SFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGcIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQ 821
Cdd:TIGR01271 1239 SFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGE-IQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQ 1317
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 822 YTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIR 901
Cdd:TIGR01271 1318 WSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLK 1397
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 902 EAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLsNDSSRFYAMFAAAE 958
Cdd:TIGR01271 1398 QSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL-NETSLFKQAMSAAD 1453
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
719-939 |
1.97e-138 |
|
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: 412.66 E-value: 1.97e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 719 GEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 798
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 799 SIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKI 878
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 879 LILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTP 939
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
441-956 |
1.09e-120 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 379.89 E-value: 1.09e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 441 YYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 520
Cdd:COG1132 62 LLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 521 FIQNVILVFFCVGMIAGVFPWF-LVAVGPLVILFSVLHIVSRvLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQ 599
Cdd:COG1132 142 LVRSVVTLIGALVVLFVIDWRLaLIVLLVLPLLLLVLRLFGR-RLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 600 EFLHRYQELLDDNQAPFFLFTCAMRWLAVRLDLI---SIALITTTGLMIVLmHGQIPPAYAGLAISYAVQLTGLFQFTVR 676
Cdd:COG1132 221 RELERFREANEELRRANLRAARLSALFFPLMELLgnlGLALVLLVGGLLVL-SGSLTVGDLVAFILYLLRLFGPLRQLAN 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 677 LASETEARFTSVERINHYiktlsLEAPARIKNKA-PSPDWPQEGEVTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVG 755
Cdd:COG1132 300 VLNQLQRALASAERIFEL-----LDEPPEIPDPPgAVPLPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 756 RTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALE 832
Cdd:COG1132 374 PSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAK 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 833 RTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTI 912
Cdd:COG1132 452 AAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVI 531
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1622900610 913 AHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDsSRFYAMFAA 956
Cdd:COG1132 532 AHRLSTIRNADRILVLDDGRIVEQGTHEELLARG-GLYARLYRL 574
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
105-287 |
9.23e-112 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 342.53 E-value: 9.23e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 105 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNATLRDNILFGKEYDEERYNS 184
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGKPFDEERYEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 185 VLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKHLK-SK 263
Cdd:cd03250 100 VIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLnNK 179
|
170 180
....*....|....*....|....
gi 1622900610 264 TVLFVTHQLQYLVDCDEVIFMKEG 287
Cdd:cd03250 180 TRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
387-695 |
1.58e-108 |
|
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: 337.55 E-value: 1.58e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 387 FLVIMALFMLNVGSTAFSTWWLSYWIKQGSGNTTVTRGnetsvsdsmkdnprmQYYASIYALSMAVMLILKAIRGVVFVK 466
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSG---------------YYLGVYAALLVLASVLLVLLRWLLFVL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 467 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 546
Cdd:cd18580 66 AGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 547 GPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAMRWL 626
Cdd:cd18580 146 PPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 627 AVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 695
Cdd:cd18580 226 GLRLDLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
440-955 |
1.26e-101 |
|
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: 333.72 E-value: 1.26e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 440 QYYASIYALSMAVML------ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkDMDEVDVR 513
Cdd:COG2274 190 QDLSTLWVLAIGLLLallfegLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREF 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 514 LPFQAEMFIQNVILVFFCVGMIAGVFPWF----LVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSpflsHITSSIQGL 589
Cdd:COG2274 269 LTGSLLTALLDLLFVLIFLIVLFFYSPPLalvvLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQS----LLVETLRGI 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 590 ATIHAYNKGQEFLHRYQELLDDNQAPFFlftcAMRWLAVRLDLISIAL--ITTTGLMIV----LMHGQIPP-------AY 656
Cdd:COG2274 345 ETIKALGAESRFRRRWENLLAKYLNARF----KLRRLSNLLSTLSGLLqqLATVALLWLgaylVIDGQLTLgqliafnIL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 657 AGLAISYAVQLTGLFQftvRLAsetEARfTSVERINHYIKTLSLEAPARIKNKAPSPdwpqEGEVTFENAEMRYRENLPL 736
Cdd:COG2274 421 SGRFLAPVAQLIGLLQ---RFQ---DAK-IALERLDDILDLPPEREEGRSKLSLPRL----KGDIELENVSFRYPGDSPP 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL 816
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENI 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 817 ---DPfnQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETD 893
Cdd:COG2274 570 tlgDP--DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETE 647
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 894 LLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDsSRFYAMFA 955
Cdd:COG2274 648 AIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARK-GLYAELVQ 708
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
715-939 |
1.74e-99 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 310.50 E-value: 1.74e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 715 WPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADL 794
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 795 RSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALerthmkeciaqlplklesEVMENGDNFSVGERQLLCIARALLR 874
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 875 HCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTP 939
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
387-694 |
6.46e-90 |
|
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: 288.61 E-value: 6.46e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 387 FLVIMALFMLNVGSTAFSTWWLSYWIKQGSGNTTvtrgnetsvsdsmKDNPRMQYYASIYALSMAVMLILKAIRGVVFVK 466
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGT-------------QDTEQRDYRLGVYGALGLGQAIFVFLGSLALAL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 467 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 546
Cdd:cd18603 68 GCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 547 GPLVILFsvlHIVSRVLI---RELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAM 623
Cdd:cd18603 148 IPLAILY---FFIQRFYVatsRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSN 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 624 RWLAVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 694
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 ... |
387-694 |
5.90e-89 |
|
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: 285.52 E-value: 5.90e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 387 FLVIMALFMLNVGSTAFSTWWLSYWIKQGSGNTTvtrgnetsvsdsmkdnprmQYYASIYALSMAVMLILKAIRGVVFVK 466
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTEDFFGLSQ-------------------GFYIGIYAGLGVLQAIFLFLFGLLLAY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 467 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 546
Cdd:cd18606 62 LGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 547 GPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAMRWL 626
Cdd:cd18606 142 PPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWL 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 627 AVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 694
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; ... |
387-695 |
8.98e-86 |
|
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: 277.43 E-value: 8.98e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 387 FLVIMALFMLNVGSTAFSTWWLSYWikqGSGNTTVTRGNETSVSdsmkdnprMQYYASIYALSMAVMLILKAIRGVVFVK 466
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQSWWLGIW---ASAYETSSALPPSEVS--------VLYYLGIYALISLLSVLLGTLRYLLFFF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 467 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 546
Cdd:cd18604 70 GSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 547 GPLVILFSVlhiVSRVLI---RELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAM 623
Cdd:cd18604 150 VVLAALYVY---IGRLYLrasRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLN 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 624 RWLAVRLDLISIALITTTGLMIVLMHGqIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 695
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 ... |
387-695 |
3.45e-85 |
|
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: 275.95 E-value: 3.45e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 387 FLVIMALFMLNVGSTAFSTWWLSYWIkqgsgnttvtrgNETSVSDSMKDNPRMQYYASIYALSMAVMLILKAIRGVVFVK 466
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWV------------SHSNNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 467 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVilvFFCVGMIAGV---FPWFL 543
Cdd:cd18605 69 GGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQL---FGLLGYLVVIcyqLPWLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 544 VAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAM 623
Cdd:cd18605 146 LLLLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAAS 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 624 RWLAVRLDLISIALITTTGLMIVLMH---GQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 695
Cdd:cd18605 226 QWLSIRLQLLGVLIVTFVALTAVVQHffgLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
383-694 |
1.32e-82 |
|
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: 269.58 E-value: 1.32e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 383 GPLAFLVIMALFMLNVGSTAFSTWWLSYWiKQGSGNTTVTRGNETSVSDSMKDNPRMQ--YYASIYALSMAVMLILKAIR 460
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYW-ANLEEKLNDTTDRVQGENSTNVDIEDLDrdFNLGIYAGLTAATFVFGFLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 461 GVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFP 540
Cdd:cd18601 80 SLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 541 WFLVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFT 620
Cdd:cd18601 160 WVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 621 CAMRWLAVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 694
Cdd:cd18601 240 ATSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
719-950 |
1.11e-78 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 256.76 E-value: 1.11e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 719 GEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 798
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 799 SIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKI 878
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 879 LILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRF 950
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
387-694 |
4.73e-77 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 254.45 E-value: 4.73e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 387 FLVIMALFMLNVGSTAFSTWWLSYWIKQGSGNTTVTrgneTSVSDSMKDNPRMQYYASIYALSMAVMLILKAIRGVVFVK 466
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEANHDVASVV----FNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 467 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 546
Cdd:cd18602 77 AGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 547 GPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAMRWL 626
Cdd:cd18602 157 IPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 627 AVRLDLISiALITTTGLMIVL---MHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 694
Cdd:cd18602 237 GIRLDYLG-AVIVFLAALSSLtaaLAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
446-946 |
4.84e-77 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 262.77 E-value: 4.84e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 446 YALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDV---R-LP-- 515
Cdd:COG4988 60 LLGLLLAVLLLRALlawlRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGyfaRyLPql 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 516 FQAeMFIQNVILVF-FCVGMIAGVFpwfLVAVGPLVILFSVL-HIVSRVLIRelKRLDNITQspfLS-HITSSIQGLATI 592
Cdd:COG4988 140 FLA-ALVPLLILVAvFPLDWLSGLI---LLVTAPLIPLFMILvGKGAAKASR--RQWRALAR---LSgHFLDRLRGLTTL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 593 HAYNKGQEFLHRYQELLDDnqapfflFTCA-MRWLavRLDLISIA---LITTTGLMIV-------LMHGQIPPAyAGLAI 661
Cdd:COG4988 211 KLFGRAKAEAERIAEASED-------FRKRtMKVL--RVAFLSSAvleFFASLSIALVavyigfrLLGGSLTLF-AALFV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 662 syavqltgLFqftvrLASE---------------TEARfTSVERInhyIKTLSLEAPARIKNKAPSPdWPQEGEVTFENA 726
Cdd:COG4988 281 --------LL-----LAPEfflplrdlgsfyharANGI-AAAEKI---FALLDAPEPAAPAGTAPLP-AAGPPSIELEDV 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 727 EMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPV 806
Cdd:COG4988 343 SFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPY 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 807 LFSGTVRSNLDPFN-QYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEAT 885
Cdd:COG4988 422 LFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPT 501
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 886 AAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSND 946
Cdd:COG4988 502 AHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
468-955 |
6.12e-73 |
|
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: 251.61 E-value: 6.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 468 TLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD-----VRLPFqaemfIQNVILVFFCVGMIAGVFPWF 542
Cdd:COG4987 83 TLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDnlylrVLLPL-----LVALLVILAAVAFLAFFSPAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 543 --LVAVGPLVILFSVLHIVSRV---LIRELKRLdnitQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQApff 617
Cdd:COG4987 158 alVLALGLLLAGLLLPLLAARLgrrAGRRLAAA----RAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAA--- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 618 lftcAMRWLAvRLDLISIALIT-TTGLMIVLM---------HGQIPPAYAG------LAISYAVQ-LTGLFQFTVRLASe 680
Cdd:COG4987 231 ----AQRRLA-RLSALAQALLQlAAGLAVVAVlwlaaplvaAGALSGPLLAllvlaaLALFEALApLPAAAQHLGRVRA- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 681 tearftSVERINHyiktLSLEAPARIKNKAPSPDwPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSG 760
Cdd:COG4987 305 ------AARRLNE----LLDAPPAVTEPAEPAPA-PGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 761 KSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMK 837
Cdd:COG4987 374 KSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLG 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 838 ECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLH 917
Cdd:COG4987 452 DWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLA 531
|
490 500 510
....*....|....*....|....*....|....*...
gi 1622900610 918 TVLGSDRIMVLAQGQVVEFDTPSVLLSNDsSRFYAMFA 955
Cdd:COG4987 532 GLERMDRILVLEDGRIVEQGTHEELLAQN-GRYRQLYQ 568
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
719-943 |
5.69e-69 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 229.42 E-value: 5.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 719 GEVTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 798
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 799 SIIPQEPVLFSGTVRSNLDPFNQY-TEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 877
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900610 878 ILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLL 943
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
442-960 |
5.18e-64 |
|
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: 226.91 E-value: 5.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 442 YASIYALSMAVMLILKAIRGvvfvkgtlrassrlhdELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF 521
Cdd:TIGR02203 72 FVSTYLLSWVSNKVVRDIRV----------------RMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 522 IQNVILVFFCVGMIAgVFPWFLVAVgpLVILFSVLHIVSRVLIRELKRLDNITQSPF--LSHITS-SIQGLATIHAYNkG 598
Cdd:TIGR02203 136 VRETLTVIGLFIVLL-YYSWQLTLI--VVVMLPVLSILMRRVSKRLRRISKEIQNSMgqVTTVAEeTLQGYRVVKLFG-G 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 599 QEF-LHRYQELlddnqapfflfTCAMRWLAVRLD------------LISIALITTtgLMIVLMHGQIPPAYAGLAISYAV 665
Cdd:TIGR02203 212 QAYeTRRFDAV-----------SNRNRRLAMKMTsagsisspitqlIASLALAVV--LFIALFQAQAGSLTAGDFTAFIT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 666 QLTGLFQFTVRLA---SETEARFTSVERINHYIKT-LSLEAPARIKNKApspdwpqEGEVTFENAEMRYRENLPLVLKKV 741
Cdd:TIGR02203 279 AMIALIRPLKSLTnvnAPMQRGLAAAESLFTLLDSpPEKDTGTRAIERA-------RGDVEFRNVTFRYPGRDRPALDSI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 742 SFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DP 818
Cdd:TIGR02203 352 SLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 819 fNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQE 898
Cdd:TIGR02203 432 -EQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQA 510
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 899 TIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSsrFYAMFAAAENK 960
Cdd:TIGR02203 511 ALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNG--LYAQLHNMQFR 570
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
721-954 |
5.30e-63 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 213.25 E-value: 5.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 800
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 801 IPQEPVLFSGTVRSNLdpfnQY-----TEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRH 875
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 876 CKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLsNDSSRFYAMF 954
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEMW 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
721-932 |
1.18e-62 |
|
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: 209.55 E-value: 1.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 800
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 801 IPQEPVLFSGTVRSNLdpfnqytedqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKILI 880
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 881 LDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQ 932
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
721-953 |
1.70e-61 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 208.62 E-value: 1.70e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 800
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 801 IPQEPVLFSGTVRSNLdpfnQY-----TEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRH 875
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 876 CKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSsrFYAM 953
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGG--VYAK 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
446-935 |
2.18e-61 |
|
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: 220.08 E-value: 2.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 446 YALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTG---RILNRFSKDMDEVdVRlpfqaeMFI 522
Cdd:COG5265 84 YGLLRLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGglsRDIERGTKGIEFL-LR------FLL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 523 QNVILVFFCVGMIAGVF-----PWF----LVAVGpLVILFSVLHIVSRV-LIRELKRLDNITQSpflsHITSSIQGLATI 592
Cdd:COG5265 157 FNILPTLLEIALVAGILlvkydWWFalitLVTVV-LYIAFTVVVTEWRTkFRREMNEADSEANT----RAVDSLLNYETV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 593 HAYNkGQEF-LHRYQELLDDnqapfflFTCAMRWLAVRLDLISI--ALITTTGLMIVL-------MHGQIPPAYAGLAIS 662
Cdd:COG5265 232 KYFG-NEAReARRYDEALAR-------YERAAVKSQTSLALLNFgqALIIALGLTAMMlmaaqgvVAGTMTVGDFVLVNA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 663 YAVQLT---GLFQFTVRlasETEARFTSVERInhyiKTLsLEAPARIKNKAPSPDWP-QEGEVTFENAEMRYRENLPlVL 738
Cdd:COG5265 304 YLIQLYiplNFLGFVYR---EIRQALADMERM----FDL-LDQPPEVADAPDAPPLVvGGGEVRFENVSFGYDPERP-IL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 739 KKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLdp 818
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI-- 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 819 fnQY-----TEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETD 893
Cdd:COG5265 453 --AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTE 530
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1622900610 894 LLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVE 935
Cdd:COG5265 531 RAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
105-287 |
2.48e-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: 2.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 105 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAIS-----------------GTFAYVAQQAWILNATL 167
Cdd:cd03290 16 TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnknesepsfeatrsrnrYSVAYAAQKPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 168 RDNILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 247
Cdd:cd03290 96 EENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622900610 248 GNHIFNSAIRKHLK--SKTVLFVTHQLQYLVDCDEVIFMKEG 287
Cdd:cd03290 176 SDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
444-956 |
1.81e-58 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 211.10 E-value: 1.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 444 SIYALSMAVMLILKAIRGVVFVKGTL---RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 520
Cdd:TIGR02204 59 RYFAFLLVVALVLALGTAARFYLVTWlgeRVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSM 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 521 FIQNVILVFFCVGMIAGVFP---WFLVAVGPLVILFSVLhivsrvLIRELKRLDNITQSPFL---SHITSSIQGLATIHA 594
Cdd:TIGR02204 139 ALRNALMCIGGLIMMFITSPkltSLVLLAVPLVLLPILL------FGRRVRKLSRESQDRIAdagSYAGETLGAIRTVQA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 595 YNKGQEFLHRYQELLDDNqapfflFTCAMRWLAVRLDLISIAL-ITTTGLMIVL-------MHGQIPPAYAGLAISYAVQ 666
Cdd:TIGR02204 213 FGHEDAERSRFGGAVEKA------YEAARQRIRTRALLTAIVIvLVFGAIVGVLwvgahdvIAGKMSAGTLGQFVFYAVM 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 667 LTGLFQFTVRLASETEARFTSVERINHYIKTLS-LEAPARIKnkapSPDWPQEGEVTFENAEMRY--RENLPlVLKKVSF 743
Cdd:TIGR02204 287 VAGSIGTLSEVWGELQRAAGAAERLIELLQAEPdIKAPAHPK----TLPVPLRGEIEFEQVNFAYpaRPDQP-ALDGLNL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 744 TIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFN-QY 822
Cdd:TIGR02204 362 TVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRpDA 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 823 TEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIRE 902
Cdd:TIGR02204 442 TDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALET 521
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 903 AFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSndSSRFYAMFAA 956
Cdd:TIGR02204 522 LMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIA--KGGLYARLAR 573
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
103-303 |
1.95e-57 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 207.69 E-value: 1.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRD 169
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrrqIAWVPQNPYLFAGTIRE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 170 NILFGK-EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 248
Cdd:COG4988 430 NLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 249 NHIFNsAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNG 303
Cdd:COG4988 510 AEILQ-ALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
721-946 |
8.79e-56 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 193.14 E-value: 8.79e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRY--RENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 798
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 799 SIIPQEPVLFSGTVRSNL-----DPfnqyTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALL 873
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygkpDA----TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 874 RHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSND 946
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
105-310 |
1.68e-55 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 202.70 E-value: 1.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 105 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNI 171
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdirdltleslrrqIGVVPQDTFLFSGTIRENI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 172 LFGK-EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 250
Cdd:COG1132 435 RYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEAL 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 251 IFNsAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFN 310
Cdd:COG1132 515 IQE-ALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYR 573
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
444-945 |
1.79e-54 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 202.26 E-value: 1.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 444 SIYALSM--AVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF 521
Cdd:TIGR00958 203 AIFFMCLlsIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 522 IQNVILVFFCVGMIAGVFPWF----LVAVGPLVILFSVLHIVSRVLIRELKrlDNITQSPFLSHitSSIQGLATIHAY-N 596
Cdd:TIGR00958 283 LRNLVMLLGLLGFMLWLSPRLtmvtLINLPLVFLAEKVFGKRYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFaA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 597 KGQEfLHRYQELLDDnqapfflftcaMRWLAVRLDLISIALITTTGLM------IVL-------MHGQIPpayAGLAIS- 662
Cdd:TIGR00958 359 EEGE-ASRFKEALEE-----------TLQLNKRKALAYAGYLWTTSVLgmliqvLVLyyggqlvLTGKVS---SGNLVSf 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 663 --YAVQLTGLFQFTVRLASETEARFTSVERINHYI-KTLSLEAPARIknkAPSPDwpqEGEVTFENAEMRY--RENLPlV 737
Cdd:TIGR00958 424 llYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLdRKPNIPLTGTL---APLNL---EGLIEFQDVSFSYpnRPDVP-V 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLD 817
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIA 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 818 -PFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLI 896
Cdd:TIGR00958 577 yGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1622900610 897 QETirEAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSN 945
Cdd:TIGR00958 657 QES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMED 703
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
87-311 |
6.92e-54 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 200.45 E-value: 6.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 87 PEEEEGKH-IHL----GHLRLQR-----------TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAIS 150
Cdd:COG2274 456 PEREEGRSkLSLprlkGDIELENvsfrypgdsppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 151 GT-------------FAYVAQQAWILNATLRDNILFGKEY-DEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGG 216
Cdd:COG2274 536 GIdlrqidpaslrrqIGVVLQDVFLFSGTIRENITLGDPDaTDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 217 QRQRISLARALYSDRSIYILDDPLSALDAHvGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHE 296
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAE-TEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHE 694
|
250
....*....|....*
gi 1622900610 297 ELMNLNGDYATIFNN 311
Cdd:COG2274 695 ELLARKGLYAELVQQ 709
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
719-934 |
2.90e-53 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 185.10 E-value: 2.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 719 GEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 798
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 799 SIIPQEPVLFSGTVRSNLDPFNQYTEDQ-IWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 877
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDErILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 878 ILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVV 934
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
719-948 |
3.61e-52 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 184.29 E-value: 3.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 719 GEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGcIKIDGVRISDIGLADLRSKL 798
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGD-IQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 799 SIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKI 878
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 879 LILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSS 948
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSH 229
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
106-315 |
5.57e-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: 183.90 E-value: 5.57e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNATLRDNILFGKEYDEERYNSV 185
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 186 LNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKHLKSKTV 265
Cdd:cd03291 133 VKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTR 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622900610 266 LFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDyatiFNNLLLG 315
Cdd:cd03291 213 ILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPD----FSSKLMG 258
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
721-947 |
8.05e-51 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 178.83 E-value: 8.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 800
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 801 IPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 877
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 878 ILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDS 947
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
106-306 |
1.53e-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: 1.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 172
Cdd:COG4987 351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrdldeddlrrrIAVVPQRPHLFDTTLRENLR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 FGKEY-DEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI 251
Cdd:COG4987 431 LARPDaTDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 252 FNsAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 306
Cdd:COG4987 511 LA-DLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYR 564
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
383-928 |
1.15e-48 |
|
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: 181.72 E-value: 1.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 383 GPLAFLVIMALfmLNVGSTAFSTWWLSY----WIKQGSGNTTVTRgnetsvsdsmkdnprmqyYASIYALSMAVMLILKA 458
Cdd:TIGR02857 3 RALALLALLGV--LGALLIIAQAWLLARvvdgLISAGEPLAELLP------------------ALGALALVLLLRALLGW 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 459 IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDvrlPFQAEMFIQNVILVFFCVGMIAGV 538
Cdd:TIGR02857 63 LQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALD---GYFARYLPQLVLAVIVPLAILAAV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 539 FP--W----FLVAVGPLVILFSVL--HIVSRVLIRELKRLDNITqspflSHITSSIQGLATIHAYNKGqeflHRYQELLD 610
Cdd:TIGR02857 140 FPqdWisglILLLTAPLIPIFMILigWAAQAAARKQWAALSRLS-----GHFLDRLRGLPTLKLFGRA----KAQAAAIR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 611 DNQAPF-----------FLFTCAMRWLAVrldlISIALITTT-GLMivLMHGQIPPAYAGLAISYAVQltglFQFTVR-L 677
Cdd:TIGR02857 211 RSSEEYrertmrvlriaFLSSAVLELFAT----LSVALVAVYiGFR--LLAGDLDLATGLFVLLLAPE----FYLPLRqL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 678 ASETEARFTSVERINHyIKTLsLEAPARIK-NKAPSPdWPQEGEVTFENAEMRYrENLPLVLKKVSFTIKPKEKIGIVGR 756
Cdd:TIGR02857 281 GAQYHARADGVAAAEA-LFAV-LDAAPRPLaGKAPVT-AAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGP 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 757 TGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALER 833
Cdd:TIGR02857 357 SGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRP--DASDAEIREALER 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 834 THMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIA 913
Cdd:TIGR02857 435 AGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVT 514
|
570
....*....|....*
gi 1622900610 914 HRLHTVLGSDRIMVL 928
Cdd:TIGR02857 515 HRLALAALADRIVVL 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
478-956 |
4.17e-48 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 181.31 E-value: 4.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 478 ELFRRILRSPMKFFDTTPTGRILNRFSKDMDEV-DVRLPFQAEMFIQNVILVFFCVgmIAGVFPWFLVAVgpLVILFSVL 556
Cdd:PRK13657 94 EYFERIIQLPLAWHSQRGSGRALHTLLRGTDALfGLWLEFMREHLATLVALVVLLP--LALFMNWRLSLV--LVVLGIVY 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 557 HIVSRVLIRELKRLDNITQ---SPFLSHITSSIQGLATIHAYNKGQ---EFLHRYQELLDDNQAPfflftcAMRWLAVRL 630
Cdd:PRK13657 170 TLITTLVMRKTKDGQAAVEehyHDLFAHVSDAIGNVSVVQSYNRIEaetQALRDIADNLLAAQMP------VLSWWALAS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 631 DL------ISIALITTTGLMIVLmHGQIPP----AYAGLAISYAVQLTGLFQFTVRLasetearFTSVERINHYIKTLsl 700
Cdd:PRK13657 244 VLnraastITMLAILVLGAALVQ-KGQLRVgevvAFVGFATLLIGRLDQVVAFINQV-------FMAAPKLEEFFEVE-- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 701 EAPARIKNKAPSPDWPQ-EGEVTFENAEMRYrENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCI 779
Cdd:PRK13657 314 DAVPDVRDPPGAIDLGRvKGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 780 KIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL-----DPfnqyTEDQIWDALERTHMKECIAQLPLKLESEVMEN 854
Cdd:PRK13657 393 LIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAAAERAQAHDFIERKPDGYDTVVGER 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 855 GDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVV 934
Cdd:PRK13657 469 GRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
490 500
....*....|....*....|....*
gi 1622900610 935 E---FDTpsvlLSNDSSRFYAMFAA 956
Cdd:PRK13657 549 EsgsFDE----LVARGGRFAALLRA 569
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
479-946 |
8.24e-48 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 180.21 E-value: 8.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 479 LFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD----------VRlpfQAEMFIQNVILVFFcvgmiagvFPWFLVavgp 548
Cdd:PRK11176 104 LFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVAssssgalitvVR---EGASIIGLFIMMFY--------YSWQLS---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 549 lVILFSVLHIVSrVLIREL-KRLDNIT---QSPfLSHITSS----IQGLATIHAYNkGQEF-LHRYQELLDDnqapfflf 619
Cdd:PRK11176 169 -LILIVIAPIVS-IAIRVVsKRFRNISknmQNT-MGQVTTSaeqmLKGHKEVLIFG-GQEVeTKRFDKVSNR-------- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 620 tcaMRWLAVRL---DLIS---IALITTTGLMIVLMHGQIPPAYAGL-AISYAVQLTGLFQFTVRLASETE--ARFtsvER 690
Cdd:PRK11176 237 ---MRQQGMKMvsaSSISdpiIQLIASLALAFVLYAASFPSVMDTLtAGTITVVFSSMIALMRPLKSLTNvnAQF---QR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 691 INHYIKTL----SLEAPariKNKAPSPDWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGM 766
Cdd:PRK11176 311 GMAACQTLfailDLEQE---KDEGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIAN 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 767 ALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL--DPFNQYTEDQIWDALERTHMKECIAQLP 844
Cdd:PRK11176 388 LLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIayARTEQYSREQIEEAARMAYAMDFINKMD 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 845 LKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDR 924
Cdd:PRK11176 468 NGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADE 547
|
490 500
....*....|....*....|..
gi 1622900610 925 IMVLAQGQVVEFDTPSVLLSND 946
Cdd:PRK11176 548 ILVVEDGEIVERGTHAELLAQN 569
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
484-954 |
1.78e-46 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 176.45 E-value: 1.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 484 LRSPMKFFDTTPTGRILNRFSKDMdEVdVRlpfqaEMFIQNVILVFFCVGMIAGV------FPW--FLVAVG--PLVILF 553
Cdd:PRK10790 109 LRQPLSAFDTQPVGQLISRVTNDT-EV-IR-----DLYVTVVATVLRSAALIGAMlvamfsLDWrmALVAIMifPAVLVV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 554 SVLH------IVSRVlirelkrldnitqSPFLSHITS----SIQGLATIHAYNKGQEFLHRyqeLLDDNQAPFflftcAM 623
Cdd:PRK10790 182 MVIYqrystpIVRRV-------------RAYLADINDgfneVINGMSVIQQFRQQARFGER---MGEASRSHY-----MA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 624 RWLAVRLD------LISI--ALITTtGLMivLMHGQIPPAYAGLAISYA-VQLTG-----LFQFTVRLASETEArFTSVE 689
Cdd:PRK10790 241 RMQTLRLDgfllrpLLSLfsALILC-GLL--MLFGFSASGTIEVGVLYAfISYLGrlnepLIELTTQQSMLQQA-VVAGE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 690 RInhyiktlsLEAPARIKNKAPSPDWP-QEGEVTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMAL 768
Cdd:PRK10790 317 RV--------FELMDGPRQQYGNDDRPlQSGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 769 FRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLE 848
Cdd:PRK10790 388 MGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLY 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 849 SEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVL 928
Cdd:PRK10790 468 TPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVL 547
|
490 500
....*....|....*....|....*.
gi 1622900610 929 AQGQVVEFDTPSVLLSNdSSRFYAMF 954
Cdd:PRK10790 548 HRGQAVEQGTHQQLLAA-QGRYWQMY 572
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
718-933 |
2.93e-45 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 162.64 E-value: 2.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 718 EGEVTFENAEMRYReNLP--LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLR 795
Cdd:cd03248 9 KGIVKFQNVTFAYP-TRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 796 SKLSIIPQEPVLFSGTVRSNLD-PFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLR 874
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 875 HCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQV 933
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
468-916 |
7.29e-45 |
|
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: 170.62 E-value: 7.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 468 TLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD---VR--LPfqaemfiqnvILVFFCVGMIA-GVFPW 541
Cdd:TIGR02868 81 ALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQdlyVRviVP----------AGVALVVGAAAvAAIAV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 542 FLVAVGP-----LVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQEL------LD 610
Cdd:TIGR02868 151 LSVPAALilaagLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEAdreltrAE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 611 DNQApfflftcamRWLAVRLDLISIALITTTGLMIVL-----MHGQIPPAYagLAISYAVQLT---GLFQFTVRLASETE 682
Cdd:TIGR02868 231 RRAA---------AATALGAALTLLAAGLAVLGALWAggpavADGRLAPVT--LAVLVLLPLAafeAFAALPAAAQQLTR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 683 ARfTSVERINHYIKTLSLEAPARIKNKAPSPdwPQEGEVTFENAEMRYRENlPLVLKKVSFTIKPKEKIGIVGRTGSGKS 762
Cdd:TIGR02868 300 VR-AAAERIVEVLDAAGPVAEGSAPAAGAVG--LGKPTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 763 SLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMKEC 839
Cdd:TIGR02868 376 TLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRP--DATDEELWAALERVGLADW 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 840 IAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRL 916
Cdd:TIGR02868 454 LRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
738-956 |
4.33e-44 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 169.26 E-value: 4.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrLVELSG-----GCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTV 812
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSL------LNALLGflpyqGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 813 RSNL---DPfnQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMD 889
Cdd:PRK11174 440 RDNVllgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 890 TETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVE---FDTpsvlLSNDSSRFYAMFAA 956
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQqgdYAE----LSQAGGLFATLLAH 583
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
101-287 |
7.38e-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: 156.39 E-value: 7.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 101 RLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATL 167
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldleslrknIAYVPQDPFLFSGTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 168 RDNILfgkeydeerynsvlnscclrpdlailpssdlteigerganlSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 247
Cdd:cd03228 93 RENIL-----------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622900610 248 GNHIFNsAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEG 287
Cdd:cd03228 132 EALILE-ALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
470-944 |
8.09e-43 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 167.06 E-value: 8.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 470 RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKdMDEVDVRLpfqAEMFIQNVILVFFC----VGMIAGVFPWFLVA 545
Cdd:TIGR03797 206 RMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRIL---SGSTLTTLLSGIFAllnlGLMFYYSWKLALVA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 546 VGPLVILFSVLHIVSRVLIRELKRLDNItQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAMRW 625
Cdd:TIGR03797 282 VALALVAIAVTLVLGLLQVRKERRLLEL-SGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 626 LAVrldLISIALITTTGLMIVLMHGQIppAYAGLAISYAVQLTGLF-QFTVRLASETEARFTSVERINHYIKTLS-LEAP 703
Cdd:TIGR03797 361 LTV---FNAVLPVLTSAALFAAAISLL--GGAGLSLGSFLAFNTAFgSFSGAVTQLSNTLISILAVIPLWERAKPiLEAL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 704 ARIKNKAPSPDwPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLveLSG------G 777
Cdd:TIGR03797 436 PEVDEAKTDPG-KLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRL--LLGfetpesG 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 778 CIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDN 857
Cdd:TIGR03797 509 SVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGT 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 858 FSVGERQLLCIARALLRHCKILILDEATAAMDTETdlliQETIREAFA--DCTMLTIAHRLHTVLGSDRIMVLAQGQVVE 935
Cdd:TIGR03797 589 LSGGQRQRLLIARALVRKPRILLFDEATSALDNRT----QAIVSESLErlKVTRIVIAHRLSTIRNADRIYVLDAGRVVQ 664
|
....*....
gi 1622900610 936 FDTPSVLLS 944
Cdd:TIGR03797 665 QGTYDELMA 673
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
93-310 |
7.12e-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: 153.15 E-value: 7.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 93 KHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQ 159
Cdd:cd03253 4 ENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 160 AWILNATLRDNILFGKE--YDEERYNSVLnSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILD 237
Cdd:cd03253 84 TVLFNDTIGYNIRYGRPdaTDEEVIEAAK-AAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 238 DPLSALDAHVGNHIFNsAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFN 310
Cdd:cd03253 163 EATSALDTHTEREIQA-ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWK 234
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
371-695 |
3.35e-41 |
|
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: 154.19 E-value: 3.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 371 WSVYGVYIQAAGGPLAFLV-IMALFMLNVGSTAFSTWWLSYWIKQGSGNTTVTRGNETSVSDSMKDNprmQYYASIYALS 449
Cdd:cd18600 3 WNTYLRYITSHKSLIFVLIlCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSNTYAVIVTFTSS---YYVFYIYVGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 450 MAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVF 529
Cdd:cd18600 80 ADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 530 FCVGMIAGVFPWFLVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELL 609
Cdd:cd18600 160 GAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 610 DDNQAPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHGQiPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVE 689
Cdd:cd18600 240 NLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGD-GEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVS 318
|
....*.
gi 1622900610 690 RINHYI 695
Cdd:cd18600 319 RIFKFI 324
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
105-303 |
7.99e-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: 150.07 E-value: 7.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 105 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNI 171
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslrsmIGVVLQDTFLFSGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 172 LFGKEY-DEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 250
Cdd:cd03254 98 RLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 251 IfNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNG 303
Cdd:cd03254 178 I-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
106-306 |
8.10e-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: 150.07 E-value: 8.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 172
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 FGK-EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVGNHI 251
Cdd:cd03251 98 YGRpGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT-ESERL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 252 FNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 306
Cdd:cd03251 177 VQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
58-284 |
4.12e-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: 4.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 58 VRQLQRTEH---QAVLAEQKGHLLLDSDERPSPEEEEGKHIHLGHLRLQ----------RTLHSIDLEIQEGKLVGICGS 124
Cdd:TIGR02857 277 LRQLGAQYHaraDGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSgvsvaypgrrPALRPVSFTVPPGERVALVGP 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 125 VGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNILFGK-EYDEERYNSVLNSCC 190
Cdd:TIGR02857 357 SGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAENIRLARpDASDAEIREALERAG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 191 LRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKHLKSKTVLFVTH 270
Cdd:TIGR02857 437 LDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV-LEALRALAQGRTVLLVTH 515
|
250
....*....|....
gi 1622900610 271 QLQYLVDCDEVIFM 284
Cdd:TIGR02857 516 RLALAALADRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
686-953 |
1.59e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 155.37 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 686 TSVERINHYIktlslEAPARIKNKAPSPDWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLG 765
Cdd:PRK11160 309 ASARRINEIT-----EQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 766 MALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMkECIAQ 842
Cdd:PRK11160 384 QLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGL-EKLLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 843 LPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGS 922
Cdd:PRK11160 461 DDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF 540
|
250 260 270
....*....|....*....|....*....|.
gi 1622900610 923 DRIMVLAQGQVVEFDTPSVLLSNDsSRFYAM 953
Cdd:PRK11160 541 DRICVMDNGQIIEQGTHQELLAQQ-GRYYQL 570
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
481-952 |
2.43e-39 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 156.44 E-value: 2.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 481 RRILRSPMKFFDTTPTGRILNRFSKDMDEVDVrlpfqaemfIQNVIL-VFFCVGMIAGVfPWFLVAVGPLVILFSVLHIV 559
Cdd:TIGR01193 237 KHLFELPMSFFSTRRTGEIVSRFTDASSIIDA---------LASTILsLFLDMWILVIV-GLFLVRQNMLLFLLSLLSIP 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 560 SRVLI-----RELKRLDN---ITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCA---MRWLAV 628
Cdd:TIGR01193 307 VYAVIiilfkRTFNKLNHdamQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKAdqgQQAIKA 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 629 RLDLISIALITTTGLMIVLMH----GQIPpAYAGLaISYavqLTGLFQFTVRLASETEARFTSVERINHYIKTLSLEAPA 704
Cdd:TIGR01193 387 VTKLILNVVILWTGAYLVMRGkltlGQLI-TFNAL-LSY---FLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINK 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 705 RIKNKAPSPDwpqeGEVTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGV 784
Cdd:TIGR01193 462 KKRTELNNLN----GDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 785 RISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQ--YTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGE 862
Cdd:TIGR01193 537 SLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKenVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQ 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 863 RQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREaFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVL 942
Cdd:TIGR01193 617 KQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
490
....*....|
gi 1622900610 943 LsnDSSRFYA 952
Cdd:TIGR01193 696 L--DRNGFYA 703
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
729-933 |
3.53e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 144.57 E-value: 3.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 729 RYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLF 808
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 809 SGTVRSNLD-PFN----QYTEDQIWDALERthmkeciaqlpLKLESEVME-NGDNFSVGERQLLCIARALLRHCKILILD 882
Cdd:COG4619 87 GGTVRDNLPfPFQlrerKFDRERALELLER-----------LGLPPDILDkPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 883 EATAAMDTETDLLIQETIREAFADC--TMLTIAH------RLhtvlgSDRIMVLAQGQV 933
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEgrAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
105-289 |
6.74e-39 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 144.27 E-value: 6.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 105 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNI 171
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqldpadlrrnIGYVPQDVTLFYGTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 172 LFGKEY-DEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 250
Cdd:cd03245 99 TLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEER 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622900610 251 IFnSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCI 289
Cdd:cd03245 179 LK-ERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
109-311 |
9.84e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 153.08 E-value: 9.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 109 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLlEGSIAISGT-------------FAYVAQQAWILNATLRDNILFGK 175
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIelreldpeswrkhLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 176 -EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNS 254
Cdd:PRK11174 448 pDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV-MQ 526
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 255 AIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNN 311
Cdd:PRK11174 527 ALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
106-294 |
4.29e-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: 139.17 E-value: 4.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNIL 172
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISIIPQDPVLFSGTIRSNLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 FGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIf 252
Cdd:cd03244 100 PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALI- 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622900610 253 NSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGT 294
Cdd:cd03244 179 QKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
198-928 |
9.43e-37 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 150.56 E-value: 9.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 198 LPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDaHVGNHIFNSAIR--KHLKSKTVLFVTHQLQYL 275
Cdd:PTZ00265 565 LPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINnlKGNENRITIIIAHRLSTI 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 276 -------------------VDCDEVIFMKEGC----------------------------ITERGTHEELM-NLNGDYAT 307
Cdd:PTZ00265 644 ryantifvlsnrergstvdVDIIGEDPTKDNKennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMkNKNGIYYT 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 308 IFNNLllgdtppvEINSKKETSGSQKKSQDKgpKTGSVK-KEKAVKPEEGQLVQLEEKGQGSVPWSVYGVYIQA----AG 382
Cdd:PTZ00265 724 MINNQ--------KVSSKKSSNNDNDKDSDM--KSSAYKdSERGYDPDEMNGNSKHENESASNKKSCKMSDENAsennAG 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 383 GPLAFL----------------------------VIMALFMLNVGS--TAFSTWWLSYwikqgsgnttvtrgnetsVSdS 432
Cdd:PTZ00265 794 GKLPFLrnlfkrkpkapnnlrivyreifsykkdvTIIALSILVAGGlyPVFALLYAKY------------------VS-T 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 433 MKDNPRMQYYA---SIYALSMAV-MLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDT---TPtGRILNRFSK 505
Cdd:PTZ00265 855 LFDFANLEANSnkySLYILVIAIaMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINR 933
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 506 DMDEVDVRLPFQAEMFIQNVILvfFCVGMIAGVFPWFLVA---VGPLVILFSVLHIVSRVLIR---ELKRL--------- 570
Cdd:PTZ00265 934 DVHLLKTGLVNNIVIFTHFIVL--FLVSMVMSFYFCPIVAavlTGTYFIFMRVFAIRARLTANkdvEKKEInqpgtvfay 1011
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 571 ---DNITQSP-------FLSHITSSIQGL---------ATIHAYNKGQEFLHRYQELL--DDNQAPFFLFTCAMrWLAVR 629
Cdd:PTZ00265 1012 nsdDEIFKDPsfliqeaFYNMNTVIIYGLedyfcnlieKAIDYSNKGQKRKTLVNSMLwgFSQSAQLFINSFAY-WFGSF 1090
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 630 LdlISIALITTTGLMIVLMHGQIPPAYAGLAISyavqltglfqftvrLASETEARFTSVERINHYIKTLSL-----EAPA 704
Cdd:PTZ00265 1091 L--IRRGTILVDDFMKSLFTFLFTGSYAGKLMS--------------LKGDSENAKLSFEKYYPLIIRKSNidvrdNGGI 1154
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 705 RIKNKAPSpdwpqEGEVTFENAEMRY--RENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVEL-------- 774
Cdd:PTZ00265 1155 RIKNKNDI-----KGKIEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivf 1228
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 775 ----------------------------------------------SGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLF 808
Cdd:PTZ00265 1229 knehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLF 1308
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 809 SGTVRSNLDpFNQ--YTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATA 886
Cdd:PTZ00265 1309 NMSIYENIK-FGKedATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATS 1387
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 1622900610 887 AMDTETDLLIQETIREA--FADCTMLTIAHRLHTVLGSDRIMVL 928
Cdd:PTZ00265 1388 SLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVF 1431
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
737-936 |
3.42e-36 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 136.48 E-value: 3.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG---LADLRSKLSIIPQEPvlfsgtvR 813
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDP-------M 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 814 SNLDPfnQYT-EDQIWDALE--RTHMKECIAQLPLKLESEVMENGDN--------FSVGERQLLCIARALLRHCKILILD 882
Cdd:cd03257 93 SSLNP--RMTiGEQIAEPLRihGKLSKKEARKEAVLLLLVGVGLPEEvlnrypheLSGGQRQRVAIARALALNPKLLIAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 883 EATAAMDTET-----DLLIQetIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEF 936
Cdd:cd03257 171 EPTSALDVSVqaqilDLLKK--LQEEL-GLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
105-310 |
1.17e-35 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 143.70 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 105 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNI 171
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHdladytlaslrrqVALVSQDVVLFNDTIANNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 172 LFGK--EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 249
Cdd:TIGR02203 427 AYGRteQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESER 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 250 HIfNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFN 310
Cdd:TIGR02203 507 LV-QAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHN 566
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
106-306 |
2.92e-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: 134.20 E-value: 2.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 172
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 FGKEY--DEERyNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVgNH 250
Cdd:cd03249 99 YGKPDatDEEV-EEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES-EK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900610 251 IFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 306
Cdd:cd03249 177 LVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYA 232
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
106-305 |
3.41e-35 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 142.16 E-value: 3.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI-------------AISGTFAYVAQQAWILNATLRDNIL 172
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklqldSWRSRLAVVSQTPFLFSDTVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 FGK-EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI 251
Cdd:PRK10789 411 LGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 252 FNSaIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDY 305
Cdd:PRK10789 491 LHN-LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
738-886 |
6.31e-35 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 130.08 E-value: 6.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSG-TVRSNL 816
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 817 -------DPFNQYTEDQIWDALERthmkeciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATA 886
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEK-------LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
106-306 |
9.20e-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: 133.00 E-value: 9.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNIL 172
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 FGKE-YDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGNHI 251
Cdd:cd03252 98 LADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE-SEHA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 252 FNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 306
Cdd:cd03252 177 IMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
721-935 |
1.75e-34 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 130.13 E-value: 1.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGlADLRSKLSI 800
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 801 IPQEPVLFSGTVRSNLdpfnqytedqiwdalerthmkeciaqlplklesevmenGDNFSVGERQLLCIARALLRHCKILI 880
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 881 LDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVE 935
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
695-935 |
1.87e-34 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 139.85 E-value: 1.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 695 IKTLSLEAPARIKNKAPSPDwpQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVEL 774
Cdd:PRK10789 290 IRAMLAEAPVVKDGSEPVPE--GRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 775 SGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMKECIAQLPLKLESEV 851
Cdd:PRK10789 368 SEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTEV 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 852 MENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQG 931
Cdd:PRK10789 446 GERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHG 525
|
....
gi 1622900610 932 QVVE 935
Cdd:PRK10789 526 HIAQ 529
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
724-933 |
2.53e-34 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 129.26 E-value: 2.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 724 ENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQ 803
Cdd:cd03246 4 ENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 804 EPVLFSGTVRSNLdpfnqytedqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKILILDE 883
Cdd:cd03246 84 DDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 884 ATAAMDTETDLLIQETIREA-FADCTMLTIAHRLHTVLGSDRIMVLAQGQV 933
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
387-671 |
1.42e-33 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 130.46 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 387 FLVIMALFMLNVGSTAFSTWWLSYWIKqgsgntTVTRGNETSVSDSMKdnprmqyYASIYALSMAVMLILKAIRGVVFVK 466
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILD------VLLPDGDPETQALNV-------YSLALLLLGLAQFILSFLQSYLLNH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 467 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVIlVFFCVGMIAGVFPWFL--- 543
Cdd:pfam00664 68 TGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLA-TIVGGIIVMFYYGWKLtlv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 544 -VAVGPLVILFSVlhIVSRVLiRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCA 622
Cdd:pfam00664 147 lLAVLPLYILVSA--VFAKIL-RKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 623 MRWLAVRLDLI---SIALITTTGlMIVLMHGQIPPAYAGLAISYAVQLTGLF 671
Cdd:pfam00664 224 NGLSFGITQFIgylSYALALWFG-AYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
701-945 |
2.56e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 135.42 E-value: 2.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 701 EAPARIKNKAPSPDWPQEGE--VTFENAEMRYRENLP---LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS 775
Cdd:COG1123 239 AVPRLGAARGRAAPAAAAAEplLEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 776 GGCIKIDGVRISDIG---LADLRSKLSIIPQEPVlfsgtvrSNLDPFnqYT-EDQIWDALE------RTHMKECIAQLpL 845
Cdd:COG1123 319 SGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPY-------SSLNPR--MTvGDIIAEPLRlhgllsRAERRERVAEL-L 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 846 K---LESEVME-NGDNFSVGERQLLCIARALLRHCKILILDEATAAMdtetDLLIQETIREAFAD------CTMLTIAHR 915
Cdd:COG1123 389 ErvgLPPDLADrYPHELSGGQRQRVAIARALALEPKLLILDEPTSAL----DVSVQAQILNLLRDlqrelgLTYLFISHD 464
|
250 260 270
....*....|....*....|....*....|.
gi 1622900610 916 LHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 945
Cdd:COG1123 465 LAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
451-936 |
3.01e-33 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 136.03 E-value: 3.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 451 AVMLILKAIRGVVFVkgtlRASSRLHDEL----FRRILRSPMKFFDTTPTgRILNrfskDMDEVdvRlpfQaemFI-QNV 525
Cdd:COG4618 71 AVMGLLDAVRSRILV----RVGARLDRRLgprvFDAAFRAALRGGGGAAA-QALR----DLDTL--R---Q---FLtGPG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 526 ILVFF----CVGMIAGVF---PWF-LVAVGPLVILFSV---LHIVSRVLIRELKRLDNITQSpflsHITSSIQGLATIHA 594
Cdd:COG4618 134 LFALFdlpwAPIFLAVLFlfhPLLgLLALVGALVLVALallNERLTRKPLKEANEAAIRANA----FAEAALRNAEVIEA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 595 YNKGQEFLHRYQEL----LD------DNQAPFFLFTCAMR------------WLAVRLDLisialitTTGLMI---VLMh 649
Cdd:COG4618 210 MGMLPALRRRWQRAnaraLAlqarasDRAGGFSALSKFLRlllqsavlglgaYLVIQGEI-------TPGAMIaasILM- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 650 gqippayaGLAISYAVQLTGLFQFTVRlaseteARfTSVERINhyiKTLSLEAPARIKNKAPSPdwpqEGEVTFENAEMR 729
Cdd:COG4618 282 --------GRALAPIEQAIGGWKQFVS------AR-QAYRRLN---ELLAAVPAEPERMPLPRP----KGRLSVENLTVV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 730 YRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFS 809
Cdd:COG4618 340 PPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFD 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 810 GTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMD 889
Cdd:COG4618 420 GTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1622900610 890 TETDLLIQETIREAFAD-CTMLTIAHRLHTVLGSDRIMVLAQGQVVEF 936
Cdd:COG4618 500 DEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAF 547
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
721-945 |
2.23e-31 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 129.64 E-value: 2.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG---GCIKIDGVRISDIGLADLRSK 797
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 798 LSIIPQEPvlfsgtvRSNLDPFNqyTEDQIWDALE-----RTHMKECIAQL--PLKLESEVMENGDNFSVGERQLLCIAR 870
Cdd:COG1123 85 IGMVFQDP-------MTQLNPVT--VGDQIAEALEnlglsRAEARARVLELleAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 871 ALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 945
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
103-306 |
3.57e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 126.86 E-value: 3.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRD 169
Cdd:PRK11160 353 QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrqaISVVSQRVHLFSATLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 170 NILFGK-EYDEERYNSVLNscclRPDLAILPSSDL---TEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 245
Cdd:PRK11160 433 NLLLAApNASDEALIEVLQ----QVGLEKLLEDDKglnAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 246 HVGNHIFnSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 306
Cdd:PRK11160 509 ETERQIL-ELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYY 568
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
70-272 |
3.61e-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: 3.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 70 LAEQKGHLLLDSDERPSPEEEEG-----KHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLE 144
Cdd:TIGR02868 310 VLDAAGPVAEGSAPAAGAVGLGKptlelRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 145 GSIAISG-------------TFAYVAQQAWILNATLRDNILFGK-EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERG 210
Cdd:TIGR02868 390 GEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLRALPDGLDTVLGEGG 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 211 ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnSAIRKHLKSKTVLFVTHQL 272
Cdd:TIGR02868 470 ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELL-EDLLAALSGRTVVLITHHL 530
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
106-306 |
3.88e-30 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 126.67 E-value: 3.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 172
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdytlaslrnqVALVSQNVHLFNDTIANNIA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 FGKE--YDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGNH 250
Cdd:PRK11176 439 YARTeqYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE-SER 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900610 251 IFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 306
Cdd:PRK11176 518 AIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYA 573
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
106-306 |
1.02e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 126.76 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 172
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqydhhylhrqVALVGQEPVLFSGSVRENIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 FG-KEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI 251
Cdd:TIGR00958 577 YGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 252 FNSairKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 306
Cdd:TIGR00958 657 QES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
106-285 |
3.31e-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: 116.09 E-value: 3.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------FAYVAQQA---WILNATLRDNIL-- 172
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQRRsidRDFPISVRDVVLmg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 ------FGKEYDEERYNSVLnscclrpdlAILPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 245
Cdd:cd03235 95 lyghkgLFRRLSKADKAKVD---------EALERVGLSELADRQiGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622900610 246 HvGNHIFNSAIRK-HLKSKTVLFVTHQLQYLVD-CDEVIFMK 285
Cdd:cd03235 166 K-TQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLLN 206
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
106-306 |
3.36e-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: 3.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWI---LNATLRDNILFGKEYDEery 182
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLrrqMGVVLQENVLFSRSIRD--- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 183 nsvlNSCCLRPDLAI------------------LPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD 244
Cdd:TIGR01846 550 ----NIALCNPGAPFehvihaaklagahdfiseLPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALD 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 245 AHvGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 306
Cdd:TIGR01846 626 YE-SEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYA 686
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
722-932 |
3.91e-29 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 113.88 E-value: 3.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 722 TFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSII 801
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 802 PQepvlfsgtvrsnldpfnqytedqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKILIL 881
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 882 DEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTV-LGSDRIMVLAQGQ 932
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
103-306 |
4.60e-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: 4.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRD 169
Cdd:TIGR02204 353 QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVdlrqldpaelrarMALVPQDPVLFAASVME 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 170 NILFGK--EYDEERYNSVLNScclRPDLAI--LPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 245
Cdd:TIGR02204 433 NIRYGRpdATDEEVEAAARAA---HAHEFIsaLPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDA 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 246 HvGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 306
Cdd:TIGR02204 510 E-SEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYA 569
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
106-300 |
5.23e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 116.34 E-value: 5.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------FAYVAQQA---WILNATLRDNILFG 174
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVPQRAevdWDFPITVRDVVLMG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 175 --------KEYDEERYNSVLNScclrpdLAILpssDLTE-----IGErganLSGGQRQRISLARALYSDRSIYILDDPLS 241
Cdd:COG1121 102 rygrrglfRRPSRADREAVDEA------LERV---GLEDladrpIGE----LSGGQQQRVLLARALAQDPDLLLLDEPFA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 242 ALDAHVGNHIFnsAIRKHLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCITErGTHEELMN 300
Cdd:COG1121 169 GVDAATEEALY--ELLRELRRegKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLT 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
723-932 |
6.64e-29 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 115.26 E-value: 6.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 723 FENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIP 802
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 803 QEP--VLFSGTVRSNL--DPFN-QYTEDQIW----DALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALL 873
Cdd:cd03225 82 QNPddQFFGPTVEEEVafGLENlGLPEEEIEerveEALELVGLEGLRDRSPFTL-----------SGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 874 RHCKILILDEATAAMDTETDLLIQETIREaFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQ 932
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKK-LKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
93-293 |
6.94e-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: 113.95 E-value: 6.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 93 KHIHLGHL-RLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI------------AISGTFAYVAQQ 159
Cdd:cd03247 4 NNVSFSYPeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEItldgvpvsdlekALSSLISVLNQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 160 AWILNATLRDNIlfgkeydeerynsvlnscclrpdlailpssdlteigerGANLSGGQRQRISLARALYSDRSIYILDDP 239
Cdd:cd03247 84 PYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 240 LSALDAHVGNHIFnSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERG 293
Cdd:cd03247 126 TVGLDPITERQLL-SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
77-306 |
9.72e-29 |
|
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: 123.52 E-value: 9.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 77 LLLDSDERPSPEEEEGK---HIHL-----GHLRLQRTLHS-IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI 147
Cdd:TIGR03796 457 LLEEPEGSAATSEPPRRlsgYVELrnitfGYSPLEPPLIEnFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEI 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 148 AISG-------------TFAYVAQQAWILNATLRDNI-LFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANL 213
Cdd:TIGR03796 537 LFDGipreeiprevlanSVAMVDQDIFLFEGTVRDNLtLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANL 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 214 SGGQRQRISLARALYSDRSIYILDDPLSALDAHVgNHIFNSAIRKhlKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERG 293
Cdd:TIGR03796 617 SGGQRQRLEIARALVRNPSILILDEATSALDPET-EKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRG 693
|
250
....*....|...
gi 1622900610 294 THEELMNLNGDYA 306
Cdd:TIGR03796 694 THEELWAVGGAYA 706
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
106-306 |
1.13e-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: 122.62 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLI-----------SAIL--GQ----MTL--LEGSIAIsgtfayVAQQAWILNAT 166
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLArllfrfydvtsGRILidGQdirdVTQasLRAAIGI------VPQDTVLFNDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 167 LRDNILFGK-EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 245
Cdd:COG5265 448 IAYNIAYGRpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 246 HVGNHIfNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 306
Cdd:COG5265 528 RTERAI-QAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYA 587
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
106-311 |
1.45e-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: 122.93 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 172
Cdd:TIGR01193 490 LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFslkdidrhtlrqfINYLPQEPYIFSGSILENLL 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 FG--KEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 250
Cdd:TIGR01193 570 LGakENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKK 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 251 IFNSAIRkhLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNN 311
Cdd:TIGR01193 650 IVNNLLN--LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
721-932 |
1.47e-28 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 113.72 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRY---RENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlrsK 797
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 798 LSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 877
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 878 ILILDEATAAMDTET-DLLIQETIREAFADC-TMLTIAHRLHTVLGSDRIMVLAQGQ 932
Cdd:cd03250 148 IYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
91-300 |
3.67e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 114.13 E-value: 3.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 91 EGKHIHLGH---LRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FA 154
Cdd:COG1124 3 EVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrrrVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 155 YVAQQ-----------AWILNATLRdniLFGKEYDEERYNSVLNSCCLRPDLAilpssdlteiGERGANLSGGQRQRISL 223
Cdd:COG1124 83 MVFQDpyaslhprhtvDRILAEPLR---IHGLPDREERIAELLEQVGLPPSFL----------DRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 224 ARALYSDRSIYILDDPLSALDAHVGNHIFN--SAIRKHLKSkTVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEELM 299
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNllKDLREERGL-TYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVADLL 227
|
.
gi 1622900610 300 N 300
Cdd:COG1124 228 A 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
737-944 |
4.98e-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: 113.74 E-value: 4.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPvlfsgtvRSNL 816
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP-------YASL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 817 DPF---------------NQYTEDQIWDALERTHMKECIA-QLPLKLesevmengdnfSVGERQLLCIARALLRHCKILI 880
Cdd:COG1124 93 HPRhtvdrilaeplrihgLPDREERIAELLEQVGLPPSFLdRYPHQL-----------SGGQRQRVAIARALILEPELLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 881 LDEATAAMDTET-----DLLiqETIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 944
Cdd:COG1124 162 LDEPTSALDVSVqaeilNLL--KDLREER-GLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
103-287 |
5.08e-28 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 110.80 E-value: 5.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTfayvaQQAWILNATLRDNIlfgkeydeery 182
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-----DIAKLPLEELRRRI----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 183 nsvlnscclrpdlAILPSsdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGnHIFNSAIRKHLKS 262
Cdd:cd00267 76 -------------GYVPQ------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR-ERLLELLRELAEE 129
|
170 180
....*....|....*....|....*..
gi 1622900610 263 -KTVLFVTHQLQYLVD-CDEVIFMKEG 287
Cdd:cd00267 130 gRTVIIVTHDPELAELaADRVIVLKDG 156
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
106-306 |
4.89e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 117.37 E-value: 4.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 172
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvtraslrrnIAVVFQDAGLFNRSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 FGKE--YDEErynsvlnsccLRPDLAILPSSDL---------TEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLS 241
Cdd:PRK13657 431 VGRPdaTDEE----------MRAAAERAQAHDFierkpdgydTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 242 ALDAHVGNHIfNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 306
Cdd:PRK13657 501 ALDVETEAKV-KAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFA 564
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
91-309 |
7.26e-27 |
|
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: 116.91 E-value: 7.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 91 EGKHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVA 157
Cdd:TIGR01192 336 EFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIdintvtreslrksIATVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 158 QQAWILNATLRDNILFGKE--YDEERYNSVLNSCCLRPDLAILPSSDlTEIGERGANLSGGQRQRISLARALYSDRSIYI 235
Cdd:TIGR01192 416 QDAGLFNRSIRENIRLGREgaTDEEVYEAAKAAAAHDFILKRSNGYD-TLVGERGNRLSGGERQRLAIARAILKNAPILV 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 236 LDDPLSALDAHVGNHIFNsAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIF 309
Cdd:TIGR01192 495 LDEATSALDVETEARVKN-AIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL 567
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
106-300 |
7.29e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.15 E-value: 7.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------------FAYVAQQAWI-LNATLRDNIL 172
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrrrIGYVPQEPALyPDLTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 F-------GKEYDEERYNSVLNSCclrpdlailpssDLTE-IGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD 244
Cdd:COG1131 96 FfarlyglPRKEARERIDELLELF------------GLTDaADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 245 AhVGNHIFNSAIRKHLKS-KTVLFVTHQL---QYLvdCDEVIFMKEGCITERGTHEELMN 300
Cdd:COG1131 164 P-EARRELWELLRELAAEgKTVLLSTHYLeeaERL--CDRVAIIDKGRIVADGTPDELKA 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
721-946 |
7.63e-27 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 110.52 E-value: 7.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 800
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 801 IPQEPVL-FSGTVR--------SNLDPFNQYTED---QIWDALERTHMKEcIAQLPLklesevmengDNFSVGERQLLCI 868
Cdd:COG1120 80 VPQEPPApFGLTVRelvalgryPHLGLFGRPSAEdreAVEEALERTGLEH-LADRPV----------DELSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 869 ARALLRHCKILILDEATAAMDTETDLLIQETIRE--AFADCTMLTIAHRL-HTVLGSDRIMVLAQGQVVEFDTPSVLLSN 945
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVLTP 228
|
.
gi 1622900610 946 D 946
Cdd:COG1120 229 E 229
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
98-300 |
1.13e-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: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 98 GHLRLQR-----------TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------F 153
Cdd:COG4618 329 GRLSVENltvvppgskrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAdlsqwdreelgrhI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 154 AYVAQQAWILNATLRDNI-LFGKEYDEErynsVLNSCclrpDLA-----ILpssDL-----TEIGERGANLSGGQRQRIS 222
Cdd:COG4618 409 GYLPQDVELFDGTIAENIaRFGDADPEK----VVAAA----KLAgvhemIL---RLpdgydTRIGEGGARLSGGQRQRIG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 223 LARALYSDRSIYILDDPLSALDAhVGNHIFNSAIRkHLKS--KTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 300
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDD-EGEAALAAAIR-ALKArgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
106-300 |
3.45e-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: 108.59 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWI-LNATLRDNI 171
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaslsrrelarrIAYVPQEPPApFGLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 172 LFG-----------KEYDEERYNSVLNSCclrpdlailpssDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDP 239
Cdd:COG1120 97 ALGryphlglfgrpSAEDREAVEEALERT------------GLEHLADRPVDeLSGGERQRVLIARALAQEPPLLLLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 240 LSALDAHvgnHIFN--SAIRK--HLKSKTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEELMN 300
Cdd:COG1120 165 TSHLDLA---HQLEvlELLRRlaRERGRTVVMVLHDLnlaaRY---ADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
70-299 |
4.02e-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: 113.98 E-value: 4.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 70 LAEQKGHLLLDS-DERPSPEEeegkhihlghlrlQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIA 148
Cdd:TIGR01842 310 LPEPEGHLSVENvTIVPPGGK-------------KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 149 ISG-------------TFAYVAQQAWILNATLRDNIL-FGKEYDEErynSVLNSCCLRP--DLAI-LPSSDLTEIGERGA 211
Cdd:TIGR01842 377 LDGadlkqwdretfgkHIGYLPQDVELFPGTVAENIArFGENADPE---KIIEAAKLAGvhELILrLPDGYDTVIGPGGA 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 212 NLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVGNHIFNSAIrKHLKSK--TVLFVTHQLQYLVDCDEVIFMKEGCI 289
Cdd:TIGR01842 454 TLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE-EGEQALANAI-KALKARgiTVVVITHRPSLLGCVDKILVLQDGRI 531
|
250
....*....|
gi 1622900610 290 TERGTHEELM 299
Cdd:TIGR01842 532 ARFGERDEVL 541
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
723-946 |
5.51e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.54 E-value: 5.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 723 FENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIP 802
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 803 QEPvlfsgtvrsnlDpfNQY----TEDQIWDALE-----RTHMKECIAQLPLKLEsevMEN-----GDNFSVGERQLLCI 868
Cdd:PRK13632 90 QNP-----------D--NQFigatVEDDIAFGLEnkkvpPKKMKDIIDDLAKKVG---MEDyldkePQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 869 ARALLRHCKILILDEATAAMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSND 946
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
106-293 |
6.61e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 105.60 E-value: 6.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIaisgtfayvaqqawilnatlrdnILFGKEYDEerynsv 185
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI-----------------------LLDGKDLAS------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 186 LNSCCLRPDLAILPSS----DLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIR-KH 259
Cdd:cd03214 66 LSPKELARKIAYVPQAlellGLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRlAR 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622900610 260 LKSKTVLFVTHQL----QYlvdCDEVIFMKEGCITERG 293
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 ... |
106-289 |
8.85e-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: 104.99 E-value: 8.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 172
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSGSIAENIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 fgkeydeerynsvlnscclrpdlailpssdlteigerganlSGGQRQRISLARALYSDRSIYILDDPLSALDaHVGNHIF 252
Cdd:cd03246 98 -----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLD-VEGERAL 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622900610 253 NSAIRkHLKSK--TVLFVTHQLQYLVDCDEVIFMKEGCI 289
Cdd:cd03246 136 NQAIA-ALKAAgaTRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
92-293 |
1.09e-25 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 106.44 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 92 GKHIHLGHLRlQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAY 155
Cdd:cd03257 8 SVSFPTGGGS-VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkirrkeIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 156 VAQQA-----------WILNATLRdnILFGKEYDEERYNSVLNSCCLRPdlaiLPSSDLTEigeRGANLSGGQRQRISLA 224
Cdd:cd03257 87 VFQDPmsslnprmtigEQIAEPLR--IHGKLSKKEARKEAVLLLLVGVG----LPEEVLNR---YPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 225 RALYSDRSIYILDDPLSALDAHVGNHIFNsaIRKHLKSK---TVLFVTHQL---QYLvdCDEVIFMKEGCITERG 293
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILD--LLKKLQEElglTLLFITHDLgvvAKI--ADRVAVMYAGKIVEEG 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
95-289 |
1.72e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 105.28 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 95 IHLGHLRLQRT----LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVA 157
Cdd:COG4619 1 LELEGLSFRVGgkpiLSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppewrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 158 QQAWILNATLRDNILF-----GKEYDEERYNSVLNSCCLRPDLAilpssdlteigERGA-NLSGGQRQRISLARALYSDR 231
Cdd:COG4619 81 QEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPDIL-----------DKPVeRLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 232 SIYILDDPLSALDAHvgN-HIFNSAIRKHLKSK--TVLFVTH---QLQYLvdCDEVIFMKEGCI 289
Cdd:COG4619 150 DVLLLDEPTSALDPE--NtRRVEELLREYLAEEgrAVLWVSHdpeQIERV--ADRVLTLEAGRL 209
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
67-317 |
1.86e-25 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 112.50 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 67 QAVLAEQKGHLLLD-------SDERPSpeeeEGKHIHLGHLRL-----QRTLHSIDLEIQEGKLVGICGSVGSGKTSLIS 134
Cdd:PRK10790 310 QAVVAGERVFELMDgprqqygNDDRPL----QSGRIDIDNVSFayrddNLVLQNINLSVPSRGFVALVGHTGSGKSTLAS 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 135 AILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAILPSS 201
Cdd:PRK10790 386 LLMGYYPLTEGEIRLDGrplsslshsvlrqGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDG 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 202 DLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNS--AIRKHlksKTVLFVTHQLQYLVDCD 279
Cdd:PRK10790 466 LYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAlaAVREH---TTLVVIAHRLSTIVEAD 542
|
250 260 270
....*....|....*....|....*....|....*...
gi 1622900610 280 EVIFMKEGCITERGTHEELMNLNGDYATIFNNLLLGDT 317
Cdd:PRK10790 543 TILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEE 580
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
104-304 |
2.95e-25 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 105.71 E-value: 2.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGtFAYVAQQAWILNA--------------TLRD 169
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG-EDVRKEPREARRQigvlpderglydrlTVRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 170 NI-LFGKEYDEERYNsvlnsccLRPDLA-ILPSSDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSALDAh 246
Cdd:COG4555 94 NIrYFAELYGLFDEE-------LKKRIEeLIELLGLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 247 VGNHIFNSAIRKHLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMNLNGD 304
Cdd:COG4555 166 MARRLLREILRALKKEgKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
106-284 |
3.21e-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: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------FAYVAQQA----WilnATLRDNILF 173
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgpdRGVVFQEPallpW---LTVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 174 G-------KEYDEERYNSVLNSCCLRPDLAILPSsdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDA- 245
Cdd:COG1116 104 GlelrgvpKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDAl 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622900610 246 ---HVGNHIFNsaIRKHLKsKTVLFVTHqlqylvDCDEVIFM 284
Cdd:COG1116 173 treRLQDELLR--LWQETG-KTVLFVTH------DVDEAVFL 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
721-953 |
3.85e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 105.17 E-value: 3.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIsdiglADLRSKLSI 800
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 801 IPQE-------PVlfsgTVR----SNLDP----FNQYTE---DQIWDALERTHMKE----CIAQLplklesevmengdnf 858
Cdd:COG1121 80 VPQRaevdwdfPI----TVRdvvlMGRYGrrglFRRPSRadrEAVDEALERVGLEDladrPIGEL--------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 859 SVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEF 936
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLVAHG 220
|
250
....*....|....*..
gi 1622900610 937 DTPSVLLSNDSSRFYAM 953
Cdd:COG1121 221 PPEEVLTPENLSRAYGG 237
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
741-939 |
4.15e-25 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 107.06 E-value: 4.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 741 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE---LSGGCIKIDGVRISDIGLADLR----SKLSIIPQEPVlfsgtvr 813
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRkirgREIQMIFQDPM------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 814 SNLDPFnqYT-EDQIWDALeRTH-------MKECIAQLpLKL-----ESEVMengDN----FSVGERQLLCIARALLRHC 876
Cdd:COG0444 97 TSLNPV--MTvGDQIAEPL-RIHgglskaeARERAIEL-LERvglpdPERRL---DRypheLSGGMRQRVMIARALALEP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900610 877 KILILDEATAAMDTET-----DLLIQetIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE-------FDTP 939
Cdd:COG0444 170 KLLIADEPTTALDVTIqaqilNLLKD--LQREL-GLAILFITHDLGVVAEiADRVAVMYAGRIVEegpveelFENP 242
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
737-942 |
5.53e-25 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 104.18 E-value: 5.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGC-----IKIDGVRISDIGLAD--LRSKLSIIPQEPVLFS 809
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApdegeVLLDGKDIYDLDVDVleLRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 810 GTVRSNLDpfnqYTeDQIWDALERTHMKECIAQLpLK---LESEVME--NGDNFSVGERQLLCIARALLRHCKILILDEA 884
Cdd:cd03260 95 GSIYDNVA----YG-LRLHGIKLKEELDERVEEA-LRkaaLWDEVKDrlHALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 885 TAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVL 942
Cdd:cd03260 169 TSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
106-298 |
5.79e-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: 5.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGqmtlLE----GSIAISGT--F----------AYVAQQAwilnA---- 165
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAG----LEtpdsGRIVLNGRdlFtnlpprerrvGFVFQHY----Alfph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 166 -TLRDNILFG-------KEYDEERYNSVLnscclrpDLAilpssDLTEIGER-GANLSGGQRQRISLARALYSDRSIYIL 236
Cdd:COG1118 90 mTVAENIAFGlrvrppsKAEIRARVEELL-------ELV-----QLEGLADRyPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 237 DDPLSALDAHVgnhifnsaiRKHLKSK----------TVLFVTHQLQ--YLVdCDEVIFMKEGCITERGTHEEL 298
Cdd:COG1118 158 DEPFGALDAKV---------RKELRRWlrrlhdelggTTVFVTHDQEeaLEL-ADRVVVMNQGRIEQVGTPDEV 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
106-281 |
8.42e-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: 102.94 E-value: 8.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------------FAYVAQQ-AWILNATLRDNIL 172
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdaredyrrrLAYLGHAdGLKPELTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 F-----GKEYDEERYNSVLnscclrpdlAILpssDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDAH 246
Cdd:COG4133 98 FwaalyGLRADREAIDEAL---------EAV---GLAGLADLpVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622900610 247 vGNHIFNSAIRKHLKS-KTVLFVTHQLQYLVDCDEV 281
Cdd:COG4133 166 -GVALLAELIAAHLARgGAVLLTTHQPLELAAARVL 200
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
393-695 |
9.45e-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: 105.37 E-value: 9.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 393 LFMLNVGSTAFSTWWLSYWikqgsgntTVTRGNETSvsdsmkdnPRMQYYASIYALSMAVMLILKAIRGVVFVKGTLRAS 472
Cdd:cd18559 7 LVLCNHVFSGPSNLWLLLW--------FDDPVNGPQ--------EHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 473 SRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF---IQNVILVFFcvgMIAGVFPWFLVAVgPL 549
Cdd:cd18559 71 RAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWmgpLQNVIGLYL---LILLAGPMAAVGI-PL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 550 VILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRyQELLDDNQAPFFLFTCAMRWLAVR 629
Cdd:cd18559 147 GLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQ-VDAKRDNELAYLPSIVYLRALAVR 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900610 630 LDLISIALITTTGLMIVLMHGQIpPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 695
Cdd:cd18559 226 LWCVGPCIVLFASFFAYVSRHSL-AGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
106-289 |
1.33e-24 |
|
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: 101.32 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAIsgtfayvaqqawilnatlrdnilFGKEYDEERyNSV 185
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-----------------------LGKDIKKEP-EEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 186 LNSCCLRPDLAILPSsDLTeiGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVGNHIFNSAIRKHLKS-KT 264
Cdd:cd03230 72 KRRIGYLPEEPSLYE-NLT--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELLRELKKEgKT 147
|
170 180
....*....|....*....|....*.
gi 1622900610 265 VLFVTHQLQYLVD-CDEVIFMKEGCI 289
Cdd:cd03230 148 ILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
105-287 |
1.41e-24 |
|
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: 102.55 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 105 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAYVAQQawILNATL 167
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltklslkelrrkvglvFQNPDDQ--FFGPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 168 RDNILFGKE---YDEERYNSVLNSCCLRPDLAILPSSDLteigergANLSGGQRQRISLARALYSDRSIYILDDPLSALD 244
Cdd:cd03225 94 EEEVAFGLEnlgLPEEEIEERVEEALELVGLEGLRDRSP-------FTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622900610 245 AHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEG 287
Cdd:cd03225 167 PAGRRELLELLKKLKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
103-289 |
1.64e-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: 102.60 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQaWIL--NATLRD 169
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMVFQD-YALfpHLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 170 NILFG----KEYDEERYNSVLNScclrpdLAILpssDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALD 244
Cdd:cd03259 92 NIAFGlklrGVPKAEIRARVREL------LELV---GLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 245 AHVgnhifNSAIRKHLKS------KTVLFVTH-QLQYLVDCDEVIFMKEGCI 289
Cdd:cd03259 163 AKL-----REELREELKElqrelgITTIYVTHdQEEALALADRIAVMNEGRI 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
724-934 |
1.95e-24 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 101.36 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 724 ENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQ 803
Cdd:cd03214 3 ENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 804 epvlfsgtvrsnldpfnqytedqiwdALERT---HMKEC-IAQLplklesevmengdnfSVGERQLLCIARALLRHCKIL 879
Cdd:cd03214 81 --------------------------ALELLglaHLADRpFNEL---------------SGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 880 ILDEATAAMD----TETDLLIQETIREafADCTMLTIAHRL-HTVLGSDRIMVLAQGQVV 934
Cdd:cd03214 120 LLDEPTSHLDiahqIELLELLRRLARE--RGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
667-929 |
2.53e-24 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 110.50 E-value: 2.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 667 LTGLFQFTVRLASETEarftsverinhYIKtlSLEAPA---RIKNKAPSPDWPQEGE-------VTFENAEMRY--RENL 734
Cdd:PTZ00265 332 LISMFMLTIILPNITE-----------YMK--SLEATNslyEIINRKPLVENNDDGKklkdikkIQFKNVRFHYdtRKDV 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 735 PlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKI-DGVRISDIGLADLRSKLSIIPQEPVLFSGTVR 813
Cdd:PTZ00265 399 E-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIK 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 814 SNLDPF-----------NQYTED--------------------------QIWDALERTHMK------------------- 837
Cdd:PTZ00265 478 NNIKYSlyslkdlealsNYYNEDgndsqenknkrnscrakcagdlndmsNTTDSNELIEMRknyqtikdsevvdvskkvl 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 838 --ECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLT--IA 913
Cdd:PTZ00265 558 ihDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITiiIA 637
|
330
....*....|....*.
gi 1622900610 914 HRLHTVLGSDRIMVLA 929
Cdd:PTZ00265 638 HRLSTIRYANTIFVLS 653
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
106-284 |
2.90e-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: 102.16 E-value: 2.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------FAYVAQQA----WilnATLRDNILF 173
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQQDallpW---LTVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 174 GkeydeerynsvlnscclrPDLAILPSSDLTEIGER---------GAN-----LSGGQRQRISLARALYSDRSIYILDDP 239
Cdd:cd03293 97 G------------------LELQGVPKAEARERAEEllelvglsgFENayphqLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622900610 240 LSALDAHVGNHIFN--SAIRKHLKsKTVLFVTHqlqylvDCDEVIFM 284
Cdd:cd03293 159 FSALDALTREQLQEelLDIWRETG-KTVLLVTH------DIDEAVFL 198
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
102-294 |
4.38e-24 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 100.95 E-value: 4.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 102 LQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLR 168
Cdd:cd03369 20 LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 169 DNILFGKEYDEERYNSVLnscclrpdlailpssdltEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVg 248
Cdd:cd03369 100 SNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622900610 249 NHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGT 294
Cdd:cd03369 161 DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
724-940 |
4.79e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 103.17 E-value: 4.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 724 ENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQ 803
Cdd:PRK13635 9 EHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 804 EP-VLFSG-TVRSNLD--------PFNQYTEdQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALL 873
Cdd:PRK13635 89 NPdNQFVGaTVQDDVAfglenigvPREEMVE-RVDQALRQVGMEDFLNREPHRL-----------SGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 874 RHCKILILDEATAAMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPS 940
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
683-915 |
5.00e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.59 E-value: 5.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 683 ARFTS-VERINHYIKtlSLEAPARIKNKAPSPDWPQEGEVTFENAEMRYRENLPLVlKKVSFTIKPKEKIGIVGRTGSGK 761
Cdd:COG4178 326 AEWRAtVDRLAGFEE--ALEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLL-EDLSLSLKPGERLLITGPSGSGK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 762 SSLgmalFRLveLSG------GCIKI-DGVRISdigladlrsklsIIPQEPVLFSGTVRSNL---DPFNQYTEDQIWDAL 831
Cdd:COG4178 403 STL----LRA--IAGlwpygsGRIARpAGARVL------------FLPQRPYLPLGTLREALlypATAEAFSDAELREAL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 832 ERTHMKECIAQLplkleSEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLT 911
Cdd:COG4178 465 EAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVIS 539
|
....
gi 1622900610 912 IAHR 915
Cdd:COG4178 540 VGHR 543
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
106-300 |
5.02e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 107.30 E-value: 5.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYVAQ----QawiLNA 165
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdltklsrrslrelrrrVQMVFQdpysS---LNP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 166 --TLRDNILFG--------KEYDEERYNSVLNSCCLRPDLAilpssdlteiGERGANLSGGQRQRISLARALYSDRSIYI 235
Cdd:COG1123 358 rmTVGDIIAEPlrlhgllsRAERRERVAELLERVGLPPDLA----------DRYPHELSGGQRQRVAIARALALEPKLLI 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 236 LDDPLSALDAHVGNHIFN--SAIRKHLKsKTVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEELMN 300
Cdd:COG1123 428 LDEPTSALDVSVQAQILNllRDLQRELG-LTYLFISHDLA-VVRyiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
103-300 |
7.16e-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: 101.42 E-value: 7.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYVAQQAWILNA- 165
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSGALFDSl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 166 TLRDNILF--------GKEYDEERYNSVLNSCCLRPDLAILPssdlteigergANLSGGQRQRISLARALYSDRSIYILD 237
Cdd:cd03261 93 TVFENVAFplrehtrlSEEEIREIVLEKLEAVGLRGAEDLYP-----------AELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900610 238 DPLSALDAhVGNHIFNSAIRKHLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 300
Cdd:cd03261 162 EPTAGLDP-IASGVIDDLIRSLKKELglTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
106-241 |
1.19e-23 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 98.10 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNA-TLRDNI 171
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkeIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 172 LFG-------KEYDEERYNSVLNScclrpdLAILPSSDlTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLS 241
Cdd:pfam00005 81 RLGlllkglsKREKDARAEEALEK------LGLGDLAD-RPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
738-935 |
1.23e-23 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 106.31 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVElSGGCIKIDGVRISDIG---LADLRSKLSIIPQEPvlFSG---- 810
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FGSlspr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 811 -TV-----------RSNLDPfnQYTEDQIWDALERTHmkeciaqlplkLESEVM-----EngdnFSVGERQLLCIARALL 873
Cdd:COG4172 379 mTVgqiiaeglrvhGPGLSA--AERRARVAEALEEVG-----------LDPAARhryphE----FSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 874 RHCKILILDEATAAMdtetDLLIQETIREAFADC------TMLTIAHRLHTV--LgSDRIMVLAQGQVVE 935
Cdd:COG4172 442 LEPKLLVLDEPTSAL----DVSVQAQILDLLRDLqrehglAYLFISHDLAVVraL-AHRVMVMKDGKVVE 506
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
721-932 |
1.41e-23 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 98.80 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG--LADLRSKL 798
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 799 SIIPQEPVLFSG-TVRSNLdpfnqytedqiwdalerthmkeciaQLPLklesevmengdnfSVGERQLLCIARALLRHCK 877
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI-------------------------ALGL-------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 878 ILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQ 932
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
723-931 |
1.69e-23 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 99.53 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 723 FENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIsdiglADLRSKLSIIP 802
Cdd:cd03235 2 VEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 803 QE-------PVLFSGTVRSNLDP----FNQYTEDQ---IWDALERTHMKE----CIAQLplklesevmengdnfSVGERQ 864
Cdd:cd03235 75 QRrsidrdfPISVRDVVLMGLYGhkglFRRLSKADkakVDEALERVGLSEladrQIGEL---------------SGGQQQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 865 LLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLGS-DRIMVLAQG 931
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYfDRVLLLNRT 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
724-933 |
6.01e-23 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 96.70 E-value: 6.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 724 ENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGlADLRSKLSIIPQ 803
Cdd:cd03230 4 RNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 804 EPVLFSG-TVRSNLDpfnqytedqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKILILD 882
Cdd:cd03230 81 EPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 883 EATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQV 933
Cdd:cd03230 121 EPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
104-300 |
7.54e-23 |
|
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: 7.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFA-----------YVAQQ-AWILNATLRDNI 171
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAtdvpvqernvgFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 172 LFGKEYDEERYnsvlnscclRPDLA--------ILPSSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSA 242
Cdd:cd03296 96 AFGLRVKPRSE---------RPPEAeirakvheLLKLVQLDWLADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 243 LDAHVgnhifnsaiRKHLKS----------KTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEELMN 300
Cdd:cd03296 167 LDAKV---------RKELRRwlrrlhdelhVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
721-945 |
1.22e-22 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 97.65 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLVEL----SGGCIKIDGVRISDIGLADL 794
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGlerpTSGSVLVDGTDLTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 795 ---RSKLSIIPQEPVLFSG-TVRSNLD-PFnqytedQIWdALERTHMKECIAQLpLK---LESEVMENGDNFSVGERQLL 866
Cdd:cd03258 78 rkaRRRIGMIFQHFNLLSSrTVFENVAlPL------EIA-GVPKAEIEERVLEL-LElvgLEDKADAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 867 CIARALLRHCKILILDEATAAMDTET-----DLLIQetIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPS 940
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETtqsilALLRD--INREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVE 226
|
....*
gi 1622900610 941 VLLSN 945
Cdd:cd03258 227 EVFAN 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
741-935 |
1.64e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 99.81 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 741 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG---LADLRSKLSIIPQEPvlfsgtvRSNLD 817
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP-------YASLN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 818 PfnQYT-EDQIWDALE------RTHMKECIAQLPLK--LESEVM-----EngdnFSVGERQLLCIARALLRHCKILILDE 883
Cdd:COG4608 110 P--RMTvGDIIAEPLRihglasKAERRERVAELLELvgLRPEHAdryphE----FSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 884 ATAAMdtetDLLIQ-------ETIREAFaDCTMLTIAHRL----HTvlgSDRIMVLAQGQVVE 935
Cdd:COG4608 184 PVSAL----DVSIQaqvlnllEDLQDEL-GLTYLFISHDLsvvrHI---SDRVAVMYLGKIVE 238
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
100-293 |
5.12e-22 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 95.44 E-value: 5.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 100 LRLQRTLHSIDLEIQ---EGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAYVAQQ 159
Cdd:cd03297 4 VDIEKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlppqqrkIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 160 AWIL-NATLRDNILFGkeydeerynsvLNSCCLRPDL----AILPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSI 233
Cdd:cd03297 84 YALFpHLNVRENLAFG-----------LKRKRNREDRisvdELLDLLGLDHLLNRYpAQLSGGEKQRVALARALAAQPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 234 YILDDPLSALDAHVGNHIFN--SAIRKHLKsKTVLFVTH---QLQYLvdCDEVIFMKEGCITERG 293
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 ... |
93-287 |
6.12e-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: 95.25 E-value: 6.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 93 KHIHLGHLRLQrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAY 155
Cdd:cd03255 8 KTYGGGGEKVQ-ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrrrhIGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 156 VAQQAWILNA-TLRDNILFG-------KEYDEERYNSVLNSCCLRPDLAILPSsdlteigergaNLSGGQRQRISLARAL 227
Cdd:cd03255 87 VFQSFNLLPDlTALENVELPlllagvpKKERRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 228 YSDRSIYILDDPLSALDAHVGNHIFNsAIRK--HLKSKTVLFVTHQLQYLVDCDEVIFMKEG 287
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVME-LLRElnKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
106-299 |
6.40e-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: 95.48 E-value: 6.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG------TFAYVAQQAWIL---------NATLRDN 170
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkkNLRELRRKVGLVfqnpddqlfAPTVEED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 171 ILFG-------KEYDEERYNSVLNSCclrpdlailpssDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSA 242
Cdd:COG1122 97 VAFGpenlglpREEIRERVEEALELV------------GLEHLADRPpHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 243 LDAHVGNHIFNsAIRK-HLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 299
Cdd:COG1122 165 LDPRGRRELLE-LLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
104-298 |
1.02e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 97.84 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQaWIL--NATLRDN 170
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtdlppkdrnIAMVFQS-YALypHMTVYEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 171 ILFG----KEYDEERYNSVLNScclrpdLAILpssDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 245
Cdd:COG3839 96 IAFPlklrKVPKAEIDRRVREA------AELL---GLEDLLDRkPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 246 HVGNHifnsaIRKHLKS------KTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 298
Cdd:COG3839 167 KLRVE-----MRAEIKRlhrrlgTTTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
106-287 |
1.96e-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: 92.64 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT---------------FAYVAQQaWIL--NATLR 168
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdltdledelpplrrrIGMVFQD-FALfpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 169 DNILFGkeydeerynsvlnscclrpdlailpssdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAhvg 248
Cdd:cd03229 95 ENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDP--- 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622900610 249 nhIFNSAIRKHLKS------KTVLFVTHQLQYLVD-CDEVIFMKEG 287
Cdd:cd03229 134 --ITRREVRALLKSlqaqlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
737-949 |
2.06e-21 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 94.11 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI---SDIGLADLRSKLSIIPQEPVLFSG-TV 812
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRRMGMLFQSGALFDSlTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 813 RSNLD-PFNQYTEDQIWDALERThmKECIAQLPLKLESEVMEngDNFSVGERQLLCIARALLRHCKILILDEATAAMD-- 889
Cdd:cd03261 95 FENVAfPLREHTRLSEEEIREIV--LEKLEAVGLRGAEDLYP--AELSGGMKKRVALARALALDPELLLYDEPTAGLDpi 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 890 --TETDLLIQeTIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR 949
Cdd:cd03261 171 asGVIDDLIR-SLKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASDDPL 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
737-935 |
2.54e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.55 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--VRISDIGLAdLRSKLSIIPQEPVLFSG-TVR 813
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDA-QAAGIAIIHQELNLVPNlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 814 SNLdpF--NQYTEDQI--WDALERThMKECIAQL--PLKLESEVMEngdnFSVGERQLLCIARALLRHCKILILDEATAA 887
Cdd:COG1129 98 ENI--FlgREPRRGGLidWRAMRRR-ARELLARLglDIDPDTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 888 M-DTETDLLIqETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 935
Cdd:COG1129 171 LtEREVERLF-RIIRRLKAQgVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
737-934 |
2.65e-21 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 91.72 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlrsklsiipqEPVLFSGtvrsnl 816
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------------KEVSFAS------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 817 dpfnqytedqIWDALErtHMKECIAQLplklesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAM-DTETDLL 895
Cdd:cd03216 69 ----------PRDARR--AGIAMVYQL---------------SVGERQMVEIARALARNARLLILDEPTAALtPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622900610 896 IqETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 934
Cdd:cd03216 122 F-KVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
104-306 |
3.06e-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: 99.65 E-value: 3.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDN 170
Cdd:TIGR03797 467 LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGqdlagldvqavrrQLGVVLQNGRLMSGSIFEN 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 171 ILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD----AH 246
Cdd:TIGR03797 547 IAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDnrtqAI 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 247 VgnhifnSAIRKHLKSkTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 306
Cdd:TIGR03797 627 V------SESLERLKV-TRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFA 679
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
721-933 |
7.51e-21 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 92.17 E-value: 7.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLP--LVLKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVE-LSGGCIKIDGV---RISDIGLADL 794
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILGGLDrPTSGEVRVDGTdisKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 795 R-SKLSIIPQEPVLFSG-TVRSNLD-------PFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQL 865
Cdd:cd03255 80 RrRHIGFVFQSFNLLPDlTALENVElplllagVPKKERRERAEELLERVGLGDRLNHYPSEL-----------SGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 866 LCIARALLRHCKILILDEATAAMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLGSDRIMVLAQGQV 933
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
737-945 |
7.93e-21 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 92.11 E-value: 7.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLSIIPQEPVLFSG-TVRS 814
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 815 NL--------DPFNQYTEDQIWDALERthMKECIAQLplklesevmenGDNFSVGERQLLCIARALLRHCKILILDEATA 886
Cdd:cd03224 95 NLllgayarrRAKRKARLERVYELFPR--LKERRKQL-----------AGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 887 ----AMDTEtdllIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 945
Cdd:cd03224 162 glapKIVEE----IFEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
106-291 |
1.09e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 91.64 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISaILGqmTLL---EGSIAISGT-----------------FAYVAQQAWIL-N 164
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILG--GLDrptSGEVLIDGQdisslserelarlrrrhIGFVFQFFNLLpE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 165 ATLRDNILF-------GKEYDEERYNSVLnscclrpdlailpssDLTEIGERG----ANLSGGQRQRISLARALYSDRSI 233
Cdd:COG1136 101 LTALENVALplllagvSRKERRERARELL---------------ERVGLGDRLdhrpSQLSGGQQQRVAIARALVNRPKL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 234 YILDDPLSALDAHVGNHIFNsAIRKHLKS--KTVLFVTHQLQYLVDCDEVIFMKEGCITE 291
Cdd:COG1136 166 ILADEPTGNLDSKTGEEVLE-LLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
721-935 |
1.43e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 91.27 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENlPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSK 797
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 798 LSIIPQE-PVLFSGTVRSNL---------DPfnQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLC 867
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENValplrvtgkSR--KEIRRRVREVLDLVGLSDKAKALPHEL-----------SGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 868 IARALLRHCKILILDEATAAMDTET-----DLLiqETIREafADCTMLtIA-HRLHTVLGSD-RIMVLAQGQVVE 935
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETsweimELL--EEINR--RGTTVL-IAtHDLELVDRMPkRVLELEDGRLVR 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
104-300 |
1.84e-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: 96.13 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILG---QMTLLEGSIAISGT-------------FAYVAQQAWI-LN-A 165
Cdd:COG1123 20 PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRdllelsealrgrrIGMVFQDPMTqLNpV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 166 TLRDNILFGKEYD----EERYNSVLnscclrpdlAILPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPL 240
Cdd:COG1123 100 TVGDQIAEALENLglsrAEARARVL---------ELLEAVGLERRLDRYpHQLSGGQRQRVAIAMALALDPDLLIADEPT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 241 SALDAHVGNHIFnSAIRKHLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 300
Cdd:COG1123 171 TALDVTTQAEIL-DLLRELQRErgTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
106-298 |
1.86e-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: 91.49 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYVAQQAWILNA-TLR 168
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllsgkelrkarrrIGMIFQHFNLLSSrTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 169 DNILF-------GKEYDEERYNSVLNscclrpdlailpssdLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILD 237
Cdd:cd03258 101 ENVALpleiagvPKAEIEERVLELLE---------------LVGLEDKAdaypAQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 238 DPLSALDAHVGNHIFN--SAIRKHLKSkTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 298
Cdd:cd03258 166 EATSALDPETTQSILAllRDINRELGL-TIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
106-289 |
1.89e-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: 90.99 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNIL 172
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhsKVSLVGQEPVLFARSLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 FG-KEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGNHI 251
Cdd:cd03248 110 YGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SEQQ 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622900610 252 FNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCI 289
Cdd:cd03248 189 VQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
106-298 |
2.66e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.61 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQ-AWILNATLRDNILF 173
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 174 GKEYDEERYnsvlnscclRPDLAILPSS--------DLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALD 244
Cdd:PRK10851 98 GLTVLPRRE---------RPNAAAIKAKvtqllemvQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 245 AHVGNHIfNSAIRK-HLKSK-TVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 298
Cdd:PRK10851 169 AQVRKEL-RRWLRQlHEELKfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
106-298 |
2.73e-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: 93.62 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQAwilnA-----TLRD 169
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQDY----AlfphlTVAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 170 NILFG-------KEYDEERYNSVLnscclrpdlailpssDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILDD 238
Cdd:COG3842 97 NVAFGlrmrgvpKAEIRARVAELL---------------ELVGLEGLAdrypHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 239 PLSALDAHVGNHIfNSAIRKHLKS--KTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 298
Cdd:COG3842 162 PLSALDAKLREEM-REELRRLQRElgITFIYVTHdQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
103-298 |
4.32e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 90.58 E-value: 4.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAIlgqmTLLE---------GSIAISGTFAYVAQQAWILNatLRDNILF 173
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI----NLLEqpeagtirvGDITIDTARSLSQQKGLIRQ--LRQHVGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 174 -GKEYDEERYNSVLNSCCLRP--------DLAI-LPSSDLTEIGERGAN------LSGGQRQRISLARALYSDRSIYILD 237
Cdd:PRK11264 90 vFQNFNLFPHRTVLENIIEGPvivkgepkEEATaRARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 238 DPLSALDAHVGNHIFNSaIRKHLKSK-TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 298
Cdd:PRK11264 170 EPTSALDPELVGEVLNT-IRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
721-958 |
5.17e-20 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 90.44 E-value: 5.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLPLVlKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 800
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 801 IPQEPVLFSG-TVRSN--LDP-FNQYTEDQIwdaleRTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHC 876
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPkLLKWPKEKI-----RERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 877 KILILDEATAAMDTETDLLIQETIReafadctmltiahRLHTVLG----------------SDRIMVLAQGQVVEFDTPS 940
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFK-------------RLQQELGktivfvthdideafrlADRIAIMKNGEIVQVGTPD 221
|
250
....*....|....*...
gi 1622900610 941 VLLSNDSSRFYAMFAAAE 958
Cdd:cd03295 222 EILRSPANDFVAEFVGAD 239
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
95-304 |
5.58e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 89.81 E-value: 5.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 95 IHLGHLRLQrtlhsIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVAQ-------QAWILN 164
Cdd:COG3840 9 YRYGDFPLR-----FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdlTALPPAErpvsmlfQENNLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 165 A--TLRDNILFGkeydeerynsvlnsccLRPDL-----------AILPSSDLTEIGER-GANLSGGQRQRISLARALYSD 230
Cdd:COG3840 84 PhlTVAQNIGLG----------------LRPGLkltaeqraqveQALERVGLAGLLDRlPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 231 RSIYILDDPLSALDAhvgnhifnsAIRK---HLKSK-------TVLFVTHQLQylvD----CDEVIFMKEGCITERGTHE 296
Cdd:COG3840 148 RPILLLDEPFSALDP---------ALRQemlDLVDElcrerglTVLMVTHDPE---DaariADRVLLVADGRIAADGPTA 215
|
....*...
gi 1622900610 297 ELMNLNGD 304
Cdd:COG3840 216 ALLDGEPP 223
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
721-915 |
6.80e-20 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 87.59 E-value: 6.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLPLVlKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlRSKLSI 800
Cdd:cd03223 1 IELENLSLATPDGRVLL-KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 801 IPQEPVLFSGTVRsnldpfnqyteDQI---WDalerthmkeciaqlplklesevmengDNFSVGERQLLCIARALLRHCK 877
Cdd:cd03223 69 LPQRPYLPLGTLR-----------EQLiypWD--------------------------DVLSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622900610 878 ILILDEATAAMDTETDLLIQETIREAFAdcTMLTIAHR 915
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
58-303 |
8.65e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 95.81 E-value: 8.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 58 VRQLQRTEHQAVLAEQKGHLL--------LDSDERPSPEEEEGKHIHLG--HLR----LQRTLHSIDLEIQEGKLVGICG 123
Cdd:PLN03232 1190 LRQASKAENSLNSVERVGNYIdlpseataIIENNRPVSGWPSRGSIKFEdvHLRyrpgLPPVLHGLSFFVSPSEKVGVVG 1269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 124 SVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNILFGKEYDEERYNSVLNSCC 190
Cdd:PLN03232 1270 RTGAGKSSMLNALFRIVELEKGRIMIDDcdvakfgltdlrrVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAH 1349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 191 LRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVgNHIFNSAIRKHLKSKTVLFVTH 270
Cdd:PLN03232 1350 IKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT-DSLIQRTIREEFKSCTMLVIAH 1428
|
250 260 270
....*....|....*....|....*....|...
gi 1622900610 271 QLQYLVDCDEVIFMKEGCITERGTHEELMNLNG 303
Cdd:PLN03232 1429 RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
721-902 |
9.64e-20 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 88.30 E-value: 9.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGlADLRSKLSI 800
Cdd:COG4133 3 LEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 801 IPQEPVLFSG-TVRSNLDpF------NQYTEDQIWDALERTHMKECiAQLPLKlesevmengdNFSVGERQLLCIARALL 873
Cdd:COG4133 80 LGHADGLKPElTVRENLR-FwaalygLRADREAIDEALEAVGLAGL-ADLPVR----------QLSAGQKRRVALARLLL 147
|
170 180
....*....|....*....|....*....
gi 1622900610 874 RHCKILILDEATAAMDTETDLLIQETIRE 902
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
737-937 |
1.18e-19 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 88.35 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGLADLRSKLSIIPQEPVLFSG-TVRSN 815
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIGMVFQDYALFPHlTVAEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 816 LDpF--------NQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAA 887
Cdd:cd03259 93 IA-FglklrgvpKAEIRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 888 MDTETDLLIQETIREAFA--DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFD 937
Cdd:cd03259 161 LDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
106-298 |
2.56e-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: 88.01 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAI-----LGQMTLLEGSIAISG---------------TFAYVAQQAWILNA 165
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGkdiydldvdvlelrrRVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 166 TLRDNILFG--------KEYDEERYNSVLnscclrpDLAILPssdlTEIGER--GANLSGGQRQRISLARALYSDRSIYI 235
Cdd:cd03260 96 SIYDNVAYGlrlhgiklKEELDERVEEAL-------RKAALW----DEVKDRlhALGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 236 LDDPLSALDAhVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEEL 298
Cdd:cd03260 165 LDEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
106-287 |
2.85e-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: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTL--LEGSIAISGT----------FAYVAQQ-AWILNATLRDNIL 172
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRpldkrsfrkiIGYVPQDdILHPTLTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 FgkeydeerynsvlnSCCLRpdlailpssdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIF 252
Cdd:cd03213 105 F--------------AAKLR-------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622900610 253 nSAIRKHLKS-KTVLFVTHQLQYLV--DCDEVIFMKEG 287
Cdd:cd03213 152 -SLLRRLADTgRTIICSIHQPSSEIfeLFDKLLLLSQG 188
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
738-931 |
4.87e-19 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 87.00 E-value: 4.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSK----LSIIPQEPVLFSGTVR 813
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 814 SNL---DPFNQYTEDQIWDALErthMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDT 890
Cdd:cd03290 97 ENItfgSPFNKQRYKAVTDACS---LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622900610 891 E-TDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQG 931
Cdd:cd03290 174 HlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
737-946 |
5.45e-19 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 86.96 E-value: 5.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGL-ADLRSKLSI--IPQEPVLFSG-TV 812
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT--GLpPHRIARLGIgyVPEGRRIFPSlTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 813 RSNLD--PFNQYTEDQIWDALERTH-----MKECIAQLplklesevmenGDNFSVGERQLLCIARALLRHCKILILDEAT 885
Cdd:COG0410 96 EENLLlgAYARRDRAEVRADLERVYelfprLKERRRQR-----------AGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 886 AAmdtetdL--LIQETIREAFAD-----CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSND 946
Cdd:COG0410 165 LG------LapLIVEEIFEIIRRlnregVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLADP 227
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
378-883 |
6.51e-19 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 91.40 E-value: 6.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 378 IQAAGGPLAFLVIMALFmlnvgSTAFSTWWLSYwIkqgsgNTTVTRGNETSVSdsmkdnprmqyYASIYALSMAVMLILK 457
Cdd:COG4615 8 LRESRWLLLLALLLGLL-----SGLANAGLIAL-I-----NQALNATGAALAR-----------LLLLFAGLLVLLLLSR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 458 AIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMD---EVDVRLPFqaemFIQNVILVFFCVGM 534
Cdd:COG4615 66 LASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRtisQAFVRLPE----LLQSVALVLGCLAY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 535 IAgvfpW-----FLVAVGPLVILFSVLHIVSRVLIRELKRLDNiTQSPFLSHITSSIQGLA--TIHAyNKGQEFLHRY-- 605
Cdd:COG4615 142 LA----WlspplFLLTLVLLGLGVAGYRLLVRRARRHLRRARE-AEDRLFKHFRALLEGFKelKLNR-RRRRAFFDEDlq 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 606 ---QELLDDNQAPFFLFTCAMRWlavrldlISIALITTTGLmIVLMHGQIPPAYAGLAISYAvqLTGLF------QFTVR 676
Cdd:COG4615 216 ptaERYRDLRIRADTIFALANNW-------GNLLFFALIGL-ILFLLPALGWADPAVLSGFV--LVLLFlrgplsQLVGA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 677 LASETEARfTSVERINHYikTLSLEAPARIKNKAPSPDWPQE-GEVTFENAEMRYR---ENLPLVLKKVSFTIKPKEKIG 752
Cdd:COG4615 286 LPTLSRAN-VALRKIEEL--ELALAAAEPAAADAAAPPAPADfQTLELRGVTYRYPgedGDEGFTLGPIDLTIRRGELVF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 753 IVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFsgtvRSNLDPFNQYTEDQIWDALE 832
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADPARARELLE 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900610 833 RthmkeciaqlpLKLESEVMENGDNF-----SVGERQLLCIARALLRHCKILILDE 883
Cdd:COG4615 439 R-----------LELDHKVSVEDGRFsttdlSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
737-933 |
7.41e-19 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 86.04 E-value: 7.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD--IGLADLRSKLSIIPQEPVLFSG-TVR 813
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKVGMVFQQFNLFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 814 SNLdpfnqyTEDQIW--------------DALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKIL 879
Cdd:cd03262 95 ENI------TLAPIKvkgmskaeaeeralELLEKVGLADKADAYPAQL-----------SGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 880 ILDEATAAMDTEtdlLIQE---TIREAFAD-CTMLTIAHRlhtvLG-----SDRIMVLAQGQV 933
Cdd:cd03262 158 LFDEPTSALDPE---LVGEvldVMKDLAEEgMTMVVVTHE----MGfarevADRVIFMDDGRI 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
737-945 |
8.46e-19 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 86.72 E-value: 8.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLV----ELSGGCIKIDGVRISDIGlADLRSKLSIIP--QEPVLFSG 810
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLIsgflRPTSGSVLFDGEDITGLP-PHEIARLGIGRtfQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 811 -TVRSNL----------DPFNQYTEDQIWDALERTHmkECIAQLPLkleSEVM-ENGDNFSVGERQLLCIARALLRHCKI 878
Cdd:cd03219 90 lTVLENVmvaaqartgsGLLLARARREEREARERAE--ELLERVGL---ADLAdRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 879 LILDEATAAM-DTETDLLIqETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 945
Cdd:cd03219 165 LLLDEPAAGLnPEETEELA-ELIRElRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
721-944 |
8.47e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 87.86 E-value: 8.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLP-LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLS 799
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 800 IIPQepvlfsgtvrsnlDPFNQYT----EDQIWDALE-----RTHMKECIAQlplKLESEVMENGDN-----FSVGERQL 865
Cdd:PRK13650 85 MVFQ-------------NPDNQFVgatvEDDVAFGLEnkgipHEEMKERVNE---ALELVGMQDFKEreparLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 866 LCIARALLRHCKILILDEATAAMDTETDL-LIQ--ETIREAFaDCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVL 942
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLeLIKtiKGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
..
gi 1622900610 943 LS 944
Cdd:PRK13650 228 FS 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
82-271 |
1.07e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.02 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 82 DERPSPEEEEGKHIHLGHLRLQR-----TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGqmtlL----EGSIAI--S 150
Cdd:COG4178 350 EAASRIETSEDGALALEDLTLRTpdgrpLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG----LwpygSGRIARpaG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 151 GTFAYVAQQAWILNATLRDNILF---GKEYDEERYNSVLNSCCLrPDLAilpsSDLTEIGERGANLSGGQRQRISLARAL 227
Cdd:COG4178 426 ARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGL-GHLA----ERLDEEADWDQVLSLGEQQRLAFARLL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622900610 228 YSDRSIYILDDPLSALDAHVGNHIFnSAIRKHLKSKTVLFVTHQ 271
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALY-QLLREELPGTTVISVGHR 543
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
93-298 |
1.18e-18 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 86.47 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 93 KHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYV 156
Cdd:cd03256 4 ENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 157 AQQ-AWILNATLRDNILFGKE-------------YDEERYNSvlnscclrpdLAILPSSDLTE-IGERGANLSGGQRQRI 221
Cdd:cd03256 84 FQQfNLIERLSVLENVLSGRLgrrstwrslfglfPKEEKQRA----------LAALERVGLLDkAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 222 SLARALYSDRSIYILDDPLSALD---AHVGNHIFNSAIRKHlkSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEE 297
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDpasSRQVMDLLKRINREE--GITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAE 231
|
.
gi 1622900610 298 L 298
Cdd:cd03256 232 L 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
737-940 |
1.25e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.53 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVElSGGCIKIDGVRISDIG---LADLRSKLSIIPQEPvlfsgtvR 813
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP-------N 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 814 SNLDPfnQYTEDQIWDALERTHMKECIAQLPLKLESEVMEN-----------GDNFSVGERQLLCIARALLRHCKILILD 882
Cdd:PRK15134 373 SSLNP--RLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEvgldpetrhryPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 883 EATAAMDTETDLLI-------QETIREAFadctmLTIAHRLHTVLG-SDRIMVLAQGQVVE-------FDTPS 940
Cdd:PRK15134 451 EPTSSLDKTVQAQIlallkslQQKHQLAY-----LFISHDLHVVRAlCHQVIVLRQGEVVEqgdcervFAAPQ 518
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
737-945 |
1.38e-18 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 86.63 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLV----ELSGGCIKIDGVRISdiGL-ADLRSKLSI-----IPQepv 806
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTL----FNLItgfyRPTSGRILFDGRDIT--GLpPHRIARLGIartfqNPR--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 807 LFSG-TVRSN-----------------LDPFNQYTE-----DQIWDALERTHMKECIAQLPlklesevmengDNFSVGER 863
Cdd:COG0411 90 LFPElTVLENvlvaaharlgrgllaalLRLPRARREerearERAEELLERVGLADRADEPA-----------GNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 864 QLLCIARALLRHCKILILDEATAAM-DTETDLLIqETIRE--AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 939
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLnPEETEELA-ELIRRlrDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTP 237
|
....*.
gi 1622900610 940 SVLLSN 945
Cdd:COG0411 238 AEVRAD 243
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
721-953 |
1.41e-18 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 86.29 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSL-GMALFRLVELSGGCIKIDGVRISDIGLADLRSKLS 799
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLlSLITGDLPPTYGNDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 800 II---------PQEPVL------FSGTVrsnlDPFNQYTEDQI---WDALERTHMKECIAQLPLKLesevmengdnfSVG 861
Cdd:COG1119 82 LVspalqlrfpRDETVLdvvlsgFFDSI----GLYREPTDEQReraRELLELLGLAHLADRPFGTL-----------SQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 862 ERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGS-DRIMVLAQGQVVEF-D 937
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAgP 226
|
250
....*....|....*.
gi 1622900610 938 TPSVLLSNDSSRFYAM 953
Cdd:COG1119 227 KEEVLTSENLSEAFGL 242
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
94-299 |
1.46e-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: 88.62 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 94 HIHLGHLRLQrtlhsIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAYV 156
Cdd:COG4148 8 RLRRGGFTLD-----VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsargiflpphrrrIGYV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 157 AQQAwILNATL--RDNILFGkeydeeRYNSVLNSCCLRPDLAIlpssDLTEIG---ERG-ANLSGGQRQRISLARALYSD 230
Cdd:COG4148 83 FQEA-RLFPHLsvRGNLLYG------RKRAPRAERRISFDEVV----ELLGIGhllDRRpATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 231 RSIYILDDPLSALDAHvgnhifnsaiRKH--------LKSKT---VLFVTHQL---QYLvdCDEVIFMKEGCITERGTHE 296
Cdd:COG4148 152 PRLLLMDEPLAALDLA----------RKAeilpylerLRDELdipILYVSHSLdevARL--ADHVVLLEQGRVVASGPLA 219
|
...
gi 1622900610 297 ELM 299
Cdd:COG4148 220 EVL 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
445-935 |
1.54e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 91.58 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 445 IYALSMAVMLILKAIRGVVFVKGTLRASSRLHDEL----FRRILRSPMKFFDTTPTGRILNRFSKDMDEVDV-------- 512
Cdd:PLN03232 342 VYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLvaaiFHKSLRLTHEARKNFASGKVTNMITTDANALQQiaeqlhgl 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 513 -RLPFQaemFIQNVILVFFCVGmIAGVFpwflvavGPLVILfsVLHIVSRVLIRELKRL--DNITQSPFLSHITSSI-QG 588
Cdd:PLN03232 422 wSAPFR---IIVSMVLLYQQLG-VASLF-------GSLILF--LLIPLQTLIVRKMRKLtkEGLQWTDKRVGIINEIlAS 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 589 LATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLT 668
Cdd:PLN03232 489 MDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLR 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 669 GLFQFTVRLASETEARFTSVERINHYIktLSLEapaRIKNKAPsPDWPQEGEVTFENAEMRYRENLPL-VLKKVSFTIKP 747
Cdd:PLN03232 569 SPLNMLPNLLSQVVNANVSLQRIEELL--LSEE---RILAQNP-PLQPGAPAISIKNGYFSWDSKTSKpTLSDINLEIPV 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 748 KEKIGIVGRTGSGKSSLGMALfrLVELSGgcikidgvriSDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQI 827
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISAM--LGELSH----------AETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERY 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 828 WDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTE-TDLLIQETIREAFAD 906
Cdd:PLN03232 711 WRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKG 790
|
490 500
....*....|....*....|....*....
gi 1622900610 907 CTMLTIAHRLHTVLGSDRIMVLAQGQVVE 935
Cdd:PLN03232 791 KTRVLVTNQLHFLPLMDRIILVSEGMIKE 819
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
724-940 |
1.88e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 86.64 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 724 ENAEMRYRENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD--IGLADLRSKL 798
Cdd:PRK13637 6 ENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 799 SIIPQEP--VLFSGTVRSNLD--PFN-QYTEDQIWDALERThMKEciaqlpLKLESEVMENGDNF--SVGERQLLCIARA 871
Cdd:PRK13637 86 GLVFQYPeyQLFEETIEKDIAfgPINlGLSEEEIENRVKRA-MNI------VGLDYEDYKDKSPFelSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 872 LLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTI--AHRLHTVLG-SDRIMVLAQGQVVEFDTPS 940
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIIlvSHSMEDVAKlADRIIVMNKGKCELQGTPR 230
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
721-934 |
2.03e-18 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 85.11 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDiGLADLRSKL 798
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 799 SIIPQEPVLFSG-TVRSNLDPFNQYTedqiwdALERTHMKECIAQLPLKLE-SEVME-NGDNFSVGERQLLCIARALLRH 875
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAGLY------GLKGDELTARLEELADRLGmEELLDrRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 876 CKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 934
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
102-308 |
3.06e-18 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 85.73 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 102 LQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLR 168
Cdd:cd03288 33 LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIdisklplhtlrsrLSIILQDPILFSGSIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 169 DNILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 248
Cdd:cd03288 113 FNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 249 NhIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELM-NLNGDYATI 308
Cdd:cd03288 193 N-ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASL 252
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
93-284 |
5.22e-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: 5.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 93 KHIHL---GHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------FAYVAQQ-- 159
Cdd:COG4525 7 RHVSVrypGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVpvtgpgadRGVVFQKda 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 160 --AWiLNAtlRDNILFGKeydeeRYNSVLNSCCLRPDLAILPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYIL 236
Cdd:COG4525 87 llPW-LNV--LDNVAFGL-----RLRGVPKAERRARAEELLALVGLADFARRRiWQLSGGMRQRVGIARALAADPRFLLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 237 DDPLSALDA----HVGNHIFNSAIRKHlksKTVLFVTHqlqylvDCDEVIFM 284
Cdd:COG4525 159 DEPFGALDAltreQMQELLLDVWQRTG---KGVFLITH------SVEEALFL 201
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
722-956 |
5.48e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.04 E-value: 5.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 722 TFENAEMRYrENLPLvlkKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADlRsKLSII 801
Cdd:COG3840 3 RLDDLTYRY-GDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-R-PVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 802 PQEPVLFSG-TVRSN----LDPFNQYTEDQ---IWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALL 873
Cdd:COG3840 77 FQENNLFPHlTVAQNiglgLRPGLKLTAEQraqVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 874 RHCKILILDEATAAMD----TETDLLIQETIREAFAdcTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSS 948
Cdd:COG3840 146 RKRPILLLDEPFSALDpalrQEMLDLVDELCRERGL--TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEPP 223
|
....*...
gi 1622900610 949 rfyAMFAA 956
Cdd:COG3840 224 ---PALAA 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
105-293 |
6.00e-18 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 83.46 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 105 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-----------TFAYVAQQ-AWILNATLRDNIL 172
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 FG-------KEYDEERYNSVlnscclrpdlailpsSDLTEIGE----RGANLSGGQRQRISLARALYSDRSIYILDDPLS 241
Cdd:cd03301 95 FGlklrkvpKDEIDERVREV---------------AELLQIEHlldrKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 242 ALDAHVgnhifNSAIRKHLKS------KTVLFVTH-QLQYLVDCDEVIFMKEGCITERG 293
Cdd:cd03301 160 NLDAKL-----RVQMRAELKRlqqrlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
106-282 |
6.55e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 82.67 E-value: 6.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG--TFAYVAQQ---AWILNATLRDNI---LFGKEY 177
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVamgRWARRG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 178 DEERYN----SVLNSCCLRPDLAILPSSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN 253
Cdd:NF040873 88 LWRRLTrddrAAVDDALERVGLADLAGRQLGE-------LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180
....*....|....*....|....*....
gi 1622900610 254 SAIRKHLKSKTVLFVTHQLQYLVDCDEVI 282
Cdd:NF040873 161 LLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
108-300 |
8.38e-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: 83.89 E-value: 8.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 108 SIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWIL-NATLRDNI-- 171
Cdd:cd03295 19 NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFpHMTVEENIal 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 172 ---LFG--KEYDEERYNSVLNSCCLRPdlailpssdlTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 245
Cdd:cd03295 99 vpkLLKwpKEKIRERADELLALVGLDP----------AEFADRyPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 246 hvgnhIFNSAIR---KHLKS---KTVLFVTHQLQ-YLVDCDEVIFMKEGCITERGTHEELMN 300
Cdd:cd03295 169 -----ITRDQLQeefKRLQQelgKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
108-323 |
1.14e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 85.54 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 108 SIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVAQ-------QAWIL--NATLRDNILFG- 174
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvTHRSIQQrdicmvfQSYALfpHMSLGENVGYGl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 175 ---KEYDEERYNSVlnscclRPDLAILpssDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDAHvgnh 250
Cdd:PRK11432 104 kmlGVPKEERKQRV------KEALELV---DLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDAN---- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 251 ifnsaIRKHLKSK----------TVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL---------MNLNGDyATIFN 310
Cdd:PRK11432 171 -----LRRSMREKirelqqqfniTSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELyrqpasrfmASFMGD-ANIFP 244
|
250
....*....|...
gi 1622900610 311 NLLLGDTppVEIN 323
Cdd:PRK11432 245 ATLSGDY--VDIY 255
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
106-300 |
1.69e-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: 83.46 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAYVAQQ-AWILNATL 167
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaamsrkelrelrrkkISMVFQSfALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 168 RDNILFG-------KEYDEERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDRSIYILDDPL 240
Cdd:cd03294 120 LENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 241 SALDahvgnhifnSAIRKHLKS----------KTVLFVTHqlqylvDCDEVI-------FMKEGCITERGTHEELMN 300
Cdd:cd03294 189 SALD---------PLIRREMQDellrlqaelqKTIVFITH------DLDEALrlgdriaIMKDGRLVQVGTPEEILT 250
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
716-955 |
1.79e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.22 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 716 PQEGEVTFENAEMRYRENL--PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLV----ELSGGCIKIDGVRISDI 789
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGggVTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLIagleKPTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 790 GladlrSKLSIIPQEPVLFs-gTVRSN---------LDPfnQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfS 859
Cdd:COG1116 79 G-----PDRGVVFQEPALLpwlTVLDNvalglelrgVPK--AERRERARELLELVGLAGFEDAYPHQL-----------S 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 860 VGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAH------RLhtvlgSDRIMVLAQ- 930
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtgKTVLFVTHdvdeavFL-----ADRVVVLSAr 215
|
250 260 270
....*....|....*....|....*....|.
gi 1622900610 931 -GQV-----VEFDTPSVLLSNDSSRFYAMFA 955
Cdd:COG1116 216 pGRIveeidVDLPRPRDRELRTSPEFAALRA 246
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
109-299 |
2.07e-17 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 84.78 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 109 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAYVAQQAWIL-NATLRDN 170
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiflppekrrIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 171 ILFGK-----EYDEERYNSVLNSCCLRPDLAILPssdlteigergANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 245
Cdd:TIGR02142 96 LRYGMkrarpSERRISFERVIELLGIGHLLGRLP-----------GRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 246 HVGNHI--FNSAIRKHLKSKtVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 299
Cdd:TIGR02142 165 PRKYEIlpYLERLHAEFGIP-ILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVW 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
91-290 |
2.27e-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: 81.53 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 91 EGKHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG----------TFAYVAQQA 160
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 161 wilnatlrDNILFGkeydeeryNSVLNSCCLRPDLA---------ILPSSDLTEIGERG-ANLSGGQRQRISLARALYSD 230
Cdd:cd03226 81 --------DYQLFT--------DSVREELLLGLKELdagneqaetVLKDLDLYALKERHpLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 231 RSIYILDDPLSALDAH----VGNHIfnsairKHLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCIT 290
Cdd:cd03226 145 KDLLIFDEPTSGLDYKnmerVGELI------RELAAqgKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
738-935 |
3.04e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.45 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI---SDIGLADLRSKLSIIPQEPVlfsgtvrS 814
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPY-------A 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 815 NLDPfNQYTEDQIWDALeRTH-----------MKECIAQLPLKLEsEVMENGDNFSVGERQLLCIARALLRHCKILILDE 883
Cdd:PRK10261 413 SLDP-RQTVGDSIMEPL-RVHgllpgkaaaarVAWLLERVGLLPE-HAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 884 ATAAMDTET-----DLL--IQETIREAFadctmLTIAHRLHTVLG-SDRIMVLAQGQVVE 935
Cdd:PRK10261 490 AVSALDVSIrgqiiNLLldLQRDFGIAY-----LFISHDMAVVERiSHRVAVMYLGQIVE 544
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
106-300 |
5.85e-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: 81.23 E-value: 5.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQ-AWILNATLRDNILF 173
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 174 G----KEYDEERYNSVLNsccLRPDLAIlpssdlTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVg 248
Cdd:cd03299 95 GlkkrKVDKKEIERKVLE---IAEMLGI------DHLLNRKpETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 249 nhifNSAIRKHLK------SKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELMN 300
Cdd:cd03299 165 ----KEKLREELKkirkefGVTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
100-293 |
7.18e-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: 80.23 E-value: 7.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 100 LRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVAQQAwiLNATLRDNILFGKE 176
Cdd:cd03298 8 FSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvTAAPPADRP--VSMLFQENNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 177 YDEERYnsvlnscclrpDLAILPSSDLTEIgERGA-------------------NLSGGQRQRISLARALYSDRSIYILD 237
Cdd:cd03298 86 TVEQNV-----------GLGLSPGLKLTAE-DRQAievalarvglaglekrlpgELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 238 DPLSALDAHVGNHIFNSAIRKHLKSK-TVLFVTHQLQYLVDCDE-VIFMKEGCITERG 293
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLHAETKmTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
106-300 |
7.92e-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: 80.79 E-value: 7.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYVAQQAwilnA---- 165
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQditglsekelyelrrrIGMLFQGG----Alfds 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 166 -TLRDNILFG-KEYD-------EERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDRSIYIL 236
Cdd:COG1127 97 lTVFENVAFPlREHTdlseaeiRELVLEKLELVGLPGAADKMPSE-----------LSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 237 DDPLSALDAHVGNHIFN--SAIRKHLKSkTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 300
Cdd:COG1127 166 DEPTAGLDPITSAVIDEliRELRDELGL-TSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
738-934 |
1.60e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.54 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLgM-ALFRLVELSGGCIKIDG--VRISDIGLAdLRSKLSIIPQEPVLFSG-TVR 813
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTL-MkILYGLYQPDSGEILIDGkpVRIRSPRDA-IALGIGMVHQHFMLVPNlTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 814 SNL----DPFNQYTEDqiWDALeRTHMKECIAQLPLKL--ESEVmengDNFSVGERQLLCIARALLRHCKILILDEATAA 887
Cdd:COG3845 99 ENIvlglEPTKGGRLD--RKAA-RARIRELSERYGLDVdpDAKV----EDLSVGEQQRVEILKALYRGARILILDEPTAV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 888 M-DTETDLLIqETIREaFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 934
Cdd:COG3845 172 LtPQEADELF-EILRR-LAAegKSIIFITHKLREVMAiADRVTVLRRGKVV 220
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
737-945 |
2.41e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 80.08 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGC-----IKIDGVRI--SDIGLADLRSKLSIIPQEPVLFS 809
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDIydPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 810 GTV---------------RSNLDpfnqytedqiwDALERThmkeciaqlpLK---LESEV----MENGDNFSVGERQLLC 867
Cdd:COG1117 106 KSIydnvayglrlhgiksKSELD-----------EIVEES----------LRkaaLWDEVkdrlKKSALGLSGGQQQRLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 868 IARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAH------RLhtvlgSDRIMVLAQGQVVEFDTPSV 941
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRV-----SDYTAFFYLGELVEFGPTEQ 239
|
....
gi 1622900610 942 LLSN 945
Cdd:COG1117 240 IFTN 243
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
721-948 |
3.21e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 79.80 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLPLVLKKVSFTIkPKEK-IGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLS 799
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNI-PKGQwTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 800 IIPQEPV-LFSGT-----VRSNLDPFNQYTEDqiwdalerthMKECIAQLpLKlESEVMENGDN----FSVGERQLLCIA 869
Cdd:PRK13648 87 IVFQNPDnQFVGSivkydVAFGLENHAVPYDE----------MHRRVSEA-LK-QVDMLERADYepnaLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 870 RALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDS 947
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhnITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
.
gi 1622900610 948 S 948
Cdd:PRK13648 235 E 235
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
737-965 |
3.22e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 84.06 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIkPKEKIGIV-GRTGSGKSSLGMALFRLVELSGGCIkidgvrisdigLADlRSkLSIIPQEPVLFSGTVRSN 815
Cdd:PTZ00243 675 LLRDVSVSV-PRGKLTVVlGATGSGKSTLLQSLLSQFEISEGRV-----------WAE-RS-IAYVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 816 LDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTET-DL 894
Cdd:PTZ00243 741 ILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgER 820
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 895 LIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQvVEFdtpsvllSNDSSRF-----YAMFAA--AENKVAVKG 965
Cdd:PTZ00243 821 VVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGR-VEF-------SGSSADFmrtslYATLAAelKENKDSKEG 890
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
721-935 |
3.40e-16 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 78.67 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLP--LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGladlrSKL 798
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 799 SIIPQEPVLFS-GTVRSN--LDPfnqytEDQIWDALE-RTHMKECIAQLPLKlesevmENGDNF----SVGERQLLCIAR 870
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvaLGL-----ELQGVPKAEaRERAEELLELVGLS------GFENAYphqlSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 871 ALLRHCKILILDEATAAMDTETDLLIQETIREAFADC--TMLTIAHRLH-TVLGSDRIMVLAQ--GQVVE 935
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
737-934 |
3.63e-16 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 77.98 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMAL--FRLVELSGGCIKIDGVRISDIglaDLRSKLSIIPQEPVLFSG-TVR 813
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKR---SFRKIIGYVPQDDILHPTlTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 814 SNLdpfnQYTedqiwdalerthmkeciAQLplklesevmengDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETD 893
Cdd:cd03213 101 ETL----MFA-----------------AKL------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622900610 894 LLIQETIRE-AFADCTMLTIAHRLHTVLGS--DRIMVLAQGQVV 934
Cdd:cd03213 148 LQVMSLLRRlADTGRTIICSIHQPSSEIFElfDKLLLLSQGRVI 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
737-934 |
4.14e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.41 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAdLRSKLSI--IPQEPVLFSG-TVR 813
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 814 SNLD---PFNQytedqiwDALERthMKECIAQLPLKLESEVmeNGDNFSVGERQLLCIARALLRHCKILILDEATAAMD- 889
Cdd:PRK15439 105 ENILfglPKRQ-------ASMQK--MKQLLAALGCQLDLDS--SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTp 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622900610 890 TETDLLIQEtIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 934
Cdd:PRK15439 174 AETERLFSR-IRELLAqGVGIVFISHKLPEIRQlADRISVMRDGTIA 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
103-291 |
4.37e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 79.35 E-value: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG----------------TFAYVAQQA------ 160
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplaklnraqrkafrrDIQMVFQDSisavnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 161 -----WILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAilpssdlteiGERGANLSGGQRQRISLARALYSDRSIYI 235
Cdd:PRK10419 105 rktvrEIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVL----------DKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 236 LDDPLSALDAHVGNHIFnsAIRKHLKSKT---VLFVTHQLQyLVD--CDEVIFMKEGCITE 291
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVI--RLLKKLQQQFgtaCLFITHDLR-LVErfCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
721-953 |
4.86e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.26 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG-LADLRSKLS 799
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 800 IIPQEP-VLFSG-TVRSNLdPFNqyTEDQIWDALE-RTHMKECIAQlpLKLESEVMENGDNFSVGERQLLCIARALLRHC 876
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDL-AFG--PENLCLPPIEiRKRVDRALAE--IGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 877 KILILDEATAAMDTETDLLIQETIREAFADC-TMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAM 953
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGL 233
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
106-300 |
7.16e-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: 79.13 E-value: 7.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILgQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNI- 171
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGVIPQKVFIFSGTFRKNLd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 172 LFGKEYDEERYNsVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhvgnhI 251
Cdd:cd03289 99 PYGKWSDEEIWK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-----I 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 252 FNSAIRKHLKSK----TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 300
Cdd:cd03289 173 TYQVIRKTLKQAfadcTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
93-300 |
7.42e-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: 77.47 E-value: 7.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 93 KHIHLGHLRLQrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQ 158
Cdd:cd03224 4 ENLNAGYGKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 159 -QAWILNATLRDNILFG-----KEYDEERYNSVLNsccLRPDLAilpssdlTEIGERGANLSGGQRQRISLARALYSDRS 232
Cdd:cd03224 83 gRRIFPELTVEENLLLGayarrRAKRKARLERVYE---LFPRLK-------ERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 233 IYILDDPLSALDAHVGNHIFNsAIRKhLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 300
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFE-AIRE-LRDEgvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
106-289 |
7.76e-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: 77.18 E-value: 7.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWilnATLRDNI--LFgkeydeERYN 183
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNI---NELRQKVgmVF------QQFN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 184 -----SVLNSCCLRPDLAI-LPSSDLTEIGER-----G---------ANLSGGQRQRISLARALYSDRSIYILDDPLSAL 243
Cdd:cd03262 87 lfphlTVLENITLAPIKVKgMSKAEAEERALEllekvGladkadaypAQLSGGQQQRVAIARALAMNPKVMLFDEPTSAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622900610 244 DAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCI 289
Cdd:cd03262 167 DPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
103-300 |
8.08e-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: 77.66 E-value: 8.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQ-AWILNATLRDN 170
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlpphkrpVNTVFQNyALFPHLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 171 ILFG-------KEYDEERYNSVLnscclrpDLAilpssDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSA 242
Cdd:cd03300 93 IAFGlrlkklpKAEIKERVAEAL-------DLV-----QLEGYANRKpSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 243 LDAHvgnhifnsaIRKHLKSK----------TVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEELMN 300
Cdd:cd03300 161 LDLK---------LRKDMQLElkrlqkelgiTFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
434-691 |
9.32e-16 |
|
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: 78.75 E-value: 9.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 434 KDNPRMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVR 513
Cdd:cd07346 33 GDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 514 LPFQAEMFIQNVILVFFCVGMIAgVFPW--FLVAVGPLVILFSVLHIVSRvLIRELKRLDNITQSPFLSHITSSIQGLAT 591
Cdd:cd07346 113 VSSGLLQLLSDVLTLIGALVILF-YLNWklTLVALLLLPLYVLILRYFRR-RIRKASREVRESLAELSAFLQESLSGIRV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 592 IHAYNKGQEFLHRYQELLDDNqapFFLFTCAMRWLAvrLDLISIALITTTGLMIVL-------MHGQIPPAYAGLAISYA 664
Cdd:cd07346 191 VKAFAAEEREIERFREANRDL---RDANLRAARLSA--LFSPLIGLLTALGTALVLlyggylvLQGSLTIGELVAFLAYL 265
|
250 260
....*....|....*....|....*..
gi 1622900610 665 VQLTGLFQFTVRLASETEARFTSVERI 691
Cdd:cd07346 266 GMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
434-674 |
1.59e-15 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 78.20 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 434 KDNPRMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvr 513
Cdd:cd18544 35 GDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEAL--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 514 lpfqAEMFIQNVILVFFCVGMIAGVF----------PWFLVAVGPLVILFSVLH-IVSRVLIRELKRLdnitqspfLSHI 582
Cdd:cd18544 112 ----NELFTSGLVTLIGDLLLLIGILiamfllnwrlALISLLVLPLLLLATYLFrKKSRKAYREVREK--------LSRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 583 TS----SIQGLATIHAYNKGQEFLHRYQELlddNQApffLFTCAMRwlAVRLDLI---SIALITTTGLMIVLMHGqippa 655
Cdd:cd18544 180 NAflqeSISGMSVIQLFNREKREFEEFDEI---NQE---YRKANLK--SIKLFALfrpLVELLSSLALALVLWYG----- 246
|
250
....*....|....*....
gi 1622900610 656 yAGLAISYAVQLTGLFQFT 674
Cdd:cd18544 247 -GGQVLSGAVTLGVLYAFI 264
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
106-300 |
1.92e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.72 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYVAQQAWILNATLRD 169
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsklqgirklvgIVFQNPETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 170 NILFGKEydeerynsvlnSCCLRP-DLAILPSSDLTEIG------ERGANLSGGQRQRISLARALYSDRSIYILDDPLSA 242
Cdd:PRK13644 98 DLAFGPE-----------NLCLPPiEIRKRVDRALAEIGlekyrhRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 243 LDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 300
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
103-291 |
2.67e-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: 77.15 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG----------------TFAYVAQQA------ 160
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqldrkqrrafrrDVQLVFQDSpsavnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 161 -----WILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAilpssdlteiGERGANLSGGQRQRISLARALYSDRSIYI 235
Cdd:TIGR02769 104 rmtvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDA----------DKLPRQLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 236 LDDPLSALDAHVGNHIFnsAIRKHLKSK---TVLFVTHQLQyLVD--CDEVIFMKEGCITE 291
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVIL--ELLRKLQQAfgtAYLFITHDLR-LVQsfCQRVAVMDKGQIVE 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
103-299 |
3.02e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.12 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI-------------AISGTFAYVAQQAWI-LNATLR 168
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVlvagddvealsarAASRRVASVPQDTSLsFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 169 DNILFGKEYDEERYN-------SVLNSCCLRPDLAILPSSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLS 241
Cdd:PRK09536 96 QVVEMGRTPHRSRFDtwtetdrAAVERAMERTGVAQFADRPVTS-------LSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 242 ALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 299
Cdd:PRK09536 169 SLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
109-271 |
3.40e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.30 E-value: 3.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 109 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVAQQAWIL---NA-----TLRDNILFGKEy 177
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiDDPDVAEACHYLghrNAmkpalTVAENLEFWAA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 178 deerynsVLNSCCLRPD--LAILPSSDLTEIgeRGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGNHIFNSA 255
Cdd:PRK13539 100 -------FLGGEELDIAaaLEAVGLAPLAHL--PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFAEL 169
|
170
....*....|....*..
gi 1622900610 256 IRKHLKSK-TVLFVTHQ 271
Cdd:PRK13539 170 IRAHLAQGgIVIAATHI 186
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
724-959 |
4.42e-15 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 75.84 E-value: 4.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 724 ENAEMRYREnlpLVLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrlVELSGGCIKIDGVRIS----DI-GLADLRSKL 798
Cdd:cd03299 4 ENLSKDWKE---FKLKNVSLEVERGDYFVILGPTGSGKSVL-------LETIAGFIKPDSGKILlngkDItNLPPEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 799 SIIPQEPVLFSgtvrsnldpfNQYTEDQIWDALE-RTHMKEciaqlplKLESEVME-------------NGDNFSVGERQ 864
Cdd:cd03299 74 SYVPQNYALFP----------HMTVYKNIAYGLKkRKVDKK-------EIERKVLEiaemlgidhllnrKPETLSGGEQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 865 LLCIARALLRHCKILILDEATAAMDTET-DLLIQE--TIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPS 940
Cdd:cd03299 137 RVAIARALVVNPKILLLDEPFSALDVRTkEKLREElkKIRKEF-GVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPE 215
|
250
....*....|....*....
gi 1622900610 941 VLLSNDSSRFYAMFAAAEN 959
Cdd:cd03299 216 EVFKKPKNEFVAEFLGFNN 234
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
106-298 |
5.68e-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: 75.42 E-value: 5.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAIlgqmTLLE----GSIAISGTfaYVAQQAWILNAtLRDNI--LFgkeyde 179
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCI----NLLEepdsGTITVDGE--DLTDSKKDINK-LRRKVgmVF------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 180 ERYN-----SVLNSCCLRPdlaI----LPSSDLTEIGER-----G---------ANLSGGQRQRISLARALYSDRSIYIL 236
Cdd:COG1126 84 QQFNlfphlTVLENVTLAP---IkvkkMSKAEAEERAMEllervGladkadaypAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 237 DDPLSALD----AHVGNHIfnsairKHLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 298
Cdd:COG1126 161 DEPTSALDpelvGEVLDVM------RDLAKEgmTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
737-941 |
5.77e-15 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 75.16 E-value: 5.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRS-KLSIIPQ--------- 803
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARLRArHVGFVFQsfqllptlt 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 804 --EPVLFSGTVRSNLDPFNQYTEdqiwdALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILIL 881
Cdd:COG4181 107 alENVMLPLELAGRRDARARARA-----LLERVGLGHRLDHYPAQL-----------SGGEQQRVALARAFATEPAILFA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 882 DEATAAMDTET-----DLLIQETiREAFAdcTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSV 941
Cdd:COG4181 171 DEPTGNLDAATgeqiiDLLFELN-RERGT--TLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
109-271 |
6.11e-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: 74.32 E-value: 6.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 109 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------------FAYVAQQAWILNA-TLRDNILFgk 175
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdephenILYLGHLPGLKPElSALENLHF-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 176 eydeerYNSVLNSCCLRPDLAiLPSSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGNHIFNS 254
Cdd:TIGR01189 97 ------WAAIHGGAQRTIEDA-LAAVGLTGFEDLPAAqLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVALLAG 168
|
170
....*....|....*...
gi 1622900610 255 AIRKHL-KSKTVLFVTHQ 271
Cdd:TIGR01189 169 LLRAHLaRGGIVLLTTHQ 186
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
721-945 |
6.39e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 76.38 E-value: 6.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLV---ELSGGCIKIDGVRISDIGLADLRSK 797
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 798 LSIIPQepvlfsgtvrsnlDPFNQY----TEDQIWDALE-----RTHMKECIAQLplkLESEVMEN-----GDNFSVGER 863
Cdd:PRK13640 86 VGIVFQ-------------NPDNQFvgatVGDDVAFGLEnravpRPEMIKIVRDV---LADVGMLDyidsePANLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 864 QLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSV 941
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE 229
|
....
gi 1622900610 942 LLSN 945
Cdd:PRK13640 230 IFSK 233
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
687-964 |
6.59e-15 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 79.60 E-value: 6.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 687 SVERINHYIKTLSLEaPARIKNKAPSPDwpQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGM 766
Cdd:TIGR00957 606 SLKRLRIFLSHEELE-PDSIERRTIKPG--EGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLS 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 767 ALFRLVELSGGCIKIDGvrisdigladlrsKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLK 846
Cdd:TIGR00957 683 ALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSG 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 847 LESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETI---REAFADCTMLTIAHRLHTVLGSD 923
Cdd:TIGR00957 750 DRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVD 829
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1622900610 924 RIMVLAQGQVVEFDTPSVLLSNDSS--RFYAMFAAAENKVAVK 964
Cdd:TIGR00957 830 VIIVMSGGKISEMGSYQELLQRDGAfaEFLRTYAPDEQQGHLE 872
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
106-298 |
6.77e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 77.04 E-value: 6.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAIlgqmTLLE----GSIAISGT--------------------FayvaQQAW 161
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI----NLLErptsGSVLVDGVdltalserelraarrkigmiF----QHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 162 ILNA-TLRDNILF-------GKEYDEERYNSVLnscclrpdlailpssDLTEIGERG----ANLSGGQRQRISLARALYS 229
Cdd:COG1135 93 LLSSrTVAENVALpleiagvPKAEIRKRVAELL---------------ELVGLSDKAdaypSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900610 230 DRSIYILDDPLSALDAHVGNHIFN--SAIRKHLKsKTVLFVTHQLqylvD-----CDEVIFMKEGCITERGTHEEL 298
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDllKDINRELG-LTIVLITHEM----DvvrriCDRVAVLENGRIVEQGPVLDV 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
737-946 |
8.12e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.58 E-value: 8.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVL-FSGTVRS- 814
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 815 ---NLDPFNQ-YTEDQ--IWDALERThmkECIA-------QLplklesevmengdnfSVGERQLLCIARAL--LRHC--- 876
Cdd:PRK13548 97 vamGRAPHGLsRAEDDalVAAALAQV---DLAHlagrdypQL---------------SGGEQQRVQLARVLaqLWEPdgp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 877 -KILILDEATAAMdtetDLLIQETIreafadctmLTIAHR------------LH----TVLGSDRIMVLAQGQVVEFDTP 939
Cdd:PRK13548 159 pRWLLLDEPTSAL----DLAHQHHV---------LRLARQlaherglavivvLHdlnlAARYADRIVLLHQGRLVADGTP 225
|
....*..
gi 1622900610 940 SVLLSND 946
Cdd:PRK13548 226 AEVLTPE 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
106-287 |
8.88e-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: 72.85 E-value: 8.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTfayvaqqawilnatlrdnilfgkeydEERYNSv 185
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--------------------------EVSFAS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 186 lnscclrPDLAIlpssdlteigERGAN----LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNsAIRKhLK 261
Cdd:cd03216 69 -------PRDAR----------RAGIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK-VIRR-LR 129
|
170 180
....*....|....*....|....*....
gi 1622900610 262 S--KTVLFVTHQLQYLVD-CDEVIFMKEG 287
Cdd:cd03216 130 AqgVAVIFISHRLDEVFEiADRVTVLRDG 158
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
106-301 |
9.28e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 77.29 E-value: 9.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-TFAYVAQQAWILNA-----------TLRDNILF 173
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqDITHVPAENRHVNTvfqsyalfphmTVFENVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 174 G----KEYDEERYNSVLNScclrpdlaiLPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 248
Cdd:PRK09452 110 GlrmqKTPAAEITPRVMEA---------LRMVQLEEFAQRKpHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLR 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 249 NHIFNSAirKHLKSK---TVLFVTH-QLQYLVDCDEVIFMKEGCITERGT----HEELMNL 301
Cdd:PRK09452 181 KQMQNEL--KALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTpreiYEEPKNL 239
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
724-944 |
1.13e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.51 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 724 ENAEMRY-RENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIP 802
Cdd:PRK13642 8 ENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 803 QEP-VLFSGTVRSNLDPFNQytEDQiwdALERTHMKECI--AQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKIL 879
Cdd:PRK13642 88 QNPdNQFVGATVEDDVAFGM--ENQ---GIPREEMIKRVdeALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 880 ILDEATAAMD----TETDLLIQEtIREAFaDCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLS 944
Cdd:PRK13642 163 ILDESTSMLDptgrQEIMRVIHE-IKEKY-QLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
737-960 |
1.30e-14 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 78.80 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlrsKLSIIPQEPVLFSGTVRSNL 816
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 817 DPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDlli 896
Cdd:TIGR01271 508 IFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE--- 584
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 897 qetiREAFADCTMLTIAHRlhtvlgsDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAENK 960
Cdd:TIGR01271 585 ----KEIFESCLCKLMSNK-------TRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAK 637
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
99-287 |
1.56e-14 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 72.85 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 99 HLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVA----QQA 160
Cdd:cd03215 9 GLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrkREG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 161 WILNATLRDNILfgkeydeerynsvlnscclrpdLAILpssdlteigerganLSGGQRQRISLARALYSDRSIYILDDPL 240
Cdd:cd03215 89 LVLDLSVAENIA----------------------LSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622900610 241 SALDahVG--NHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEG 287
Cdd:cd03215 133 RGVD--VGakAEIYRLIRELADAGKAVLLISSELDELLGlCDRILVMYEG 180
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
737-935 |
1.69e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 74.84 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSKLSIIPQE-PVLFSG-- 810
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDsPSAVNPrm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 811 TVRSNL-DPFNQYTEdqiwdaLERTHMKECIAQL--PLKLESEVMEN-GDNFSVGERQLLCIARALLRHCKILILDEATA 886
Cdd:TIGR02769 106 TVRQIIgEPLRHLTS------LDESEQKARIAELldMVGLRSEDADKlPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 887 AMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 935
Cdd:TIGR02769 180 NLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
737-932 |
1.70e-14 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 74.01 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCI-------KIDGVRISDIGLADLRSK--------LSII 801
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggWVDLAQASPREILALRRRtigyvsqfLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 802 PQ--------EPVLFSGTVRsnldpfnQYTEDQIWDALERTHMKECIAQLPLKlesevmengdNFSVGERQLLCIARALL 873
Cdd:COG4778 106 PRvsaldvvaEPLLERGVDR-------EEARARARELLARLNLPERLWDLPPA----------TFSGGEQQRVNIARGFI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 874 RHCKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQ 932
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRAVVVELIEEAKARgTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
121-298 |
1.80e-14 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 75.61 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 121 ICGSVGSGKTSLISAILGQMTLLEGSIAISGT-FAYVAQ---------QAWIL--NATLRDNILFG----KEYDEERYNS 184
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEdVTNVPPhlrhinmvfQSYALfpHMTVEENVAFGlkmrKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 185 VLnscclrpdlAILPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKHLK-S 262
Cdd:TIGR01187 81 VL---------EALRLVQLEEFADRKpHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlG 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622900610 263 KTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 298
Cdd:TIGR01187 152 ITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
106-300 |
1.99e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 74.64 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKtSLISAIL-GQMTLLEGSIAISG------TFAYVAQQAWI---------LNATLRD 169
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGK-STISKILtGLLKPQSGEIKIDGitiskeNLKEIRKKIGIifqnpdnqfIGATVED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 170 NILFGKEydeerynsvlNSCCLRPDLA--ILPSSDLTEIGE----RGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 243
Cdd:PRK13632 104 DIAFGLE----------NKKVPPKKMKdiIDDLAKKVGMEDyldkEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 244 DAHVGNHI--FNSAIRKHlKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 300
Cdd:PRK13632 174 DPKGKREIkkIMVDLRKT-RKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
106-298 |
2.13e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.39 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILG-QMTLLE--GSIAISGT----------FAYVAQQAWILNA-TLRDNI 171
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrSPKGVKgsGSVLLNGMpidakemraiSAYVQQDDLFIPTlTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 172 LF----------GKEYDEERYNSVLNscclrpDLAILPSSDlTEIGERGA--NLSGGQRQRISLARALYSDRSIYILDDP 239
Cdd:TIGR00955 121 MFqahlrmprrvTKKEKRERVDEVLQ------ALGLRKCAN-TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 240 LSALDAHVGNHIFnsAIRKHL--KSKTVLFVTHQLQYLVDC--DEVIFMKEGCITERGTHEEL 298
Cdd:TIGR00955 194 TSGLDSFMAYSVV--QVLKGLaqKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQA 254
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
103-293 |
2.15e-14 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 73.02 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTF------------AYVAQQAWILNATLRDN 170
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSyqkniealrrigALIEAPGFYPNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 171 I-LFGKEYD--EERYNSVLNSCCLRpdlailpssdlTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhV 247
Cdd:cd03268 93 LrLLARLLGirKKRIDEVLDVVGLK-----------DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP-D 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622900610 248 GNHIFNSAIRKHLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 293
Cdd:cd03268 161 GIKELRELILSLRDQgITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
104-305 |
2.37e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.28 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMT----------LLEGSIAISGTFA-----------YVAQQAWI 162
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksagshieLLGRTVQREGRLArdirksrantgYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 163 LNA-TLRDNILFGKEYDEERYNSvlnscCLR---PDLAILPSSDLTEIG------ERGANLSGGQRQRISLARALYSDRS 232
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTPFWRT-----CFSwftREQKQRALQALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900610 233 IYILDDPLSALDAHVGnHIFNSAIR--KHLKSKTVLFVTHQLQY-LVDCDEVIFMKEGCITERGTHEELMNLNGDY 305
Cdd:PRK09984 173 VILADEPIASLDPESA-RIVMDTLRdiNQNDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQFDNERFDH 247
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
109-287 |
2.83e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 70.94 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 109 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--FAYVAQqawilnatlrdnilfgkeydeerynsvl 186
Cdd:cd03221 19 ISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTvkIGYFEQ---------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 187 nscclrpdlailpssdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDahvgnhIFN-SAIRKHLKS--K 263
Cdd:cd03221 71 --------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD------LESiEALEEALKEypG 118
|
170 180
....*....|....*....|....*.
gi 1622900610 264 TVLFVTHQlQYLVD--CDEVIFMKEG 287
Cdd:cd03221 119 TVILVSHD-RYFLDqvATKIIELEDG 143
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
737-935 |
3.61e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.41 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS-----GGCIKIDGVRISDIGLADLRSKLSIIPQEP------ 805
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpipnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 806 VLFS----GTVRSNLDPFNQYTEDQIWDALERthmkeciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILIL 881
Cdd:PRK14247 98 SIFEnvalGLKLNRLVKSKKELQERVRWALEK-------AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 882 DEATAAMDTETDLLIQETIREAFADCTMLTIAH-RLHTVLGSDRIMVLAQGQVVE 935
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVE 225
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
731-954 |
3.93e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.45 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 731 RENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRS----KLSIIPQEPV 806
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 807 LFSG-TVRSNldpfNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEAT 885
Cdd:PRK10070 117 LMPHmTVLDN----TAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 886 AAMDTETDLLIQETI--REAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMF 954
Cdd:PRK10070 193 SALDPLIRTEMQDELvkLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
106-287 |
4.33e-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: 72.31 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---------TFAYVAQQAWI-LNATLRDNILF-- 173
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLPEERGLyPKMKVIDQLVYla 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 174 -----GKEYDEERYNSVLNscclRPDLAILPSSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVG 248
Cdd:cd03269 96 qlkglKKEEARRRIDEWLE----RLELSEYANKRVEE-------LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622900610 249 NHIFNSAIRKHL-KSKTVLFVTHQLQyLVD--CDEVIFMKEG 287
Cdd:cd03269 164 VELLKDVIRELArAGKTVILSTHQME-LVEelCDRVLLLNKG 204
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
733-959 |
4.53e-14 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 73.74 E-value: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 733 NLPL----VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlrsKLSIIPQEPVLF 808
Cdd:cd03291 44 NLCLvgapVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 809 SGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAM 888
Cdd:cd03291 111 PGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 889 DTETDlliqetiREAFADCTMLTIAHRlhtvlgsDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAEN 959
Cdd:cd03291 191 DVFTE-------KEIFESCVCKLMANK-------TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQS 247
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
740-934 |
4.59e-14 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 72.33 E-value: 4.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 740 KVSFTIkPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD----IGLADLRSKLSIIPQEPVLFSG-TVRS 814
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 815 NL--------DPFNQYTEDQIWDALERTHMKEciaQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATA 886
Cdd:cd03297 95 NLafglkrkrNREDRISVDELLDLLGLDHLLN---RYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 887 AMDTETDLLIQETIREAFAD--CTMLTIAHRLHTV-LGSDRIMVLAQGQVV 934
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
110-293 |
4.59e-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: 72.20 E-value: 4.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 110 DLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQAWIL-NATLRDNILFG--- 174
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQshtglapyqrpVSMLFQENNLFaHLTVRQNIGLGlhp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 175 ----KEYDEERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 250
Cdd:TIGR01277 98 glklNAEQQEKVVDAAQQVGIADYLDRLPEQ-----------LSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622900610 251 IFnsAIRKHL---KSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 293
Cdd:TIGR01277 167 ML--ALVKQLcseRQRTLLMVTHHLSDARAiASQIAVVSQGKIKVVS 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
735-945 |
4.64e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.58 E-value: 4.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 735 PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG-LADLRSKLSIIPQEP-------- 805
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqivati 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 806 ----VLFSgtvRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILIL 881
Cdd:PRK13633 103 veedVAFG---PENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLL-----------SGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900610 882 DEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSN 945
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELNKKygITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
106-301 |
4.95e-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: 4.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFayvaqqAWIL--------NATLRDNILFG--- 174
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV------SALLelgagfhpELTGRENIYLNgrl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 175 -----KEYDeERYNSVLnscclrpdlailpssDLTEIGE------RgaNLSGGQRQRISLARALYSDRSIYILDDPLSAL 243
Cdd:COG1134 116 lglsrKEID-EKFDEIV---------------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVG 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 244 DAHvgnhiFN----SAIRKHLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMNL 301
Cdd:COG1134 178 DAA-----FQkkclARIRELRESgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
96-300 |
5.53e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.43 E-value: 5.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 96 HLGHLRLqrtLHSIDLEIQEGKLVGICGSVGSGKTSLISAI--LGQMT---LLEGSIAISGTFA----------YVAQQA 160
Cdd:PRK09493 10 HFGPTQV---LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITsgdLIVDGLKVNDPKVderlirqeagMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 161 WIL-NATLRDNILFG--------KEYDEERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDR 231
Cdd:PRK09493 87 YLFpHLTALENVMFGplrvrgasKEEAEKQARELLAKVGLAERAHHYPSE-----------LSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 232 SIYILDDPLSALDAHVGNHIFNsaIRKHLKSK--TVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELMN 300
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLK--VMQDLAEEgmTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
106-300 |
5.69e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 72.95 E-value: 5.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------FAYVAQQ------------------AW 161
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdYKYRCKHirmifqdpntslnprlniGQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 162 ILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLteigerganlSGGQRQRISLARALYSDRSIYILDDPLS 241
Cdd:COG4167 109 ILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHML----------SSGQKQRVALARALILQPKIIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 242 ALDAHVGNHIFNsaIRKHLKSK---TVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEELMN 300
Cdd:COG4167 179 ALDMSVRSQIIN--LMLELQEKlgiSYIYVSQHLG-IVKhiSDKVLVMHQGEVVEYGKTAEVFA 239
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
737-935 |
6.38e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 73.96 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSlgmaLFRLVEL----SGGCIKIDGVRISDI---GLADLRSKLSIIPQEPVLFS 809
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKST----LIRCINLlerpTSGSVLVDGVDLTALserELRAARRKIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 810 G-TVRSNldpfnqytedqiwdalerthmkecIAqLPLKL--------ESEVME---------NGDNF----SVGERQLLC 867
Cdd:COG1135 96 SrTVAEN------------------------VA-LPLEIagvpkaeiRKRVAEllelvglsdKADAYpsqlSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 868 IARALLRHCKILILDEATAAMDTET-----DLLiqETIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 935
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETtrsilDLL--KDINREL-GLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
103-304 |
9.21e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 72.74 E-value: 9.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGtFAYVAQQAW----------------ILNAT 166
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSEETVWdvrrqvgmvfqnpdnqFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 167 LRDNILFGKE-----YDE--ERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDRSIYILDDP 239
Cdd:PRK13635 99 VQDDVAFGLEnigvpREEmvERVDQALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 240 LSALDAhVGNHIFNSAIRkHLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGD 304
Cdd:PRK13635 168 TSMLDP-RGRREVLETVR-QLKEQkgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
721-954 |
1.06e-13 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 71.50 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGladlrsklsi 800
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 801 IPQEPVlfsGTVRSNLDPFNQYT-EDQIWDALERTHMKECI------AQLPL-KLESEVMENGDNFSVGERQLLCIARAL 872
Cdd:cd03300 69 PHKRPV---NTVFQNYALFPHLTvFENIAFGLRLKKLPKAEikervaEALDLvQLEGYANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 873 LRHCKILILDEATAAMDTETDLLIQETIReafadctmltiahRLHTVLG----------------SDRIMVLAQGQVVEF 936
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELK-------------RLQKELGitfvfvthdqeealtmSDRIAVMNKGKIQQI 212
|
250
....*....|....*...
gi 1622900610 937 DTPSVLLSNDSSRFYAMF 954
Cdd:cd03300 213 GTPEEIYEEPANRFVADF 230
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
106-300 |
1.08e-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: 72.04 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEG-SIAISGT-------------FAYV--AQQAWIL-NATLR 168
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGErrggedvwelrkrIGLVspALQLRFPrDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 169 DNILFG--------KEYDEERYNSVLnscclrpdlAILPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDP 239
Cdd:COG1119 99 DVVLSGffdsiglyREPTDEQRERAR---------ELLELLGLAHLADRPfGTLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 240 LSALDAHvGNHIFNSAIRK--HLKSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELMN 300
Cdd:COG1119 170 TAGLDLG-ARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLT 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
103-284 |
1.08e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.04 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI-----AISGTFA---YVAQQAWILN-ATLRDNILF 173
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSItldgkPVEGPGAergVVFQNEGLLPwRNVQDNVAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 174 GKEY----DEERYNSVLnscclrpdlAILPSSDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 248
Cdd:PRK11248 94 GLQLagveKMQRLEIAH---------QMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622900610 249 NHIFNSAIRK-HLKSKTVLFVTHqlqylvDCDEVIFM 284
Cdd:PRK11248 165 EQMQTLLLKLwQETGKQVLLITH------DIEEAVFM 195
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
99-301 |
1.28e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.67 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 99 HLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYV----AQQA 160
Cdd:COG1129 261 GLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVpedrKGEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 161 WILNATLRDNILFGkeydeeRYNSVLNSCCLRP------------DLAILPSSDLTEIGergaNLSGGQRQRISLARALY 228
Cdd:COG1129 341 LVLDLSIRENITLA------SLDRLSRGGLLDRrreralaeeyikRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 229 SDRSIYILDDPLSALDahVGNH--IFNsAIRKhLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCIT-----ERGTHEEL 298
Cdd:COG1129 411 TDPKVLILDEPTRGID--VGAKaeIYR-LIRE-LAAegKAVIVISSELPELLGlSDRILVMREGRIVgeldrEEATEEAI 486
|
...
gi 1622900610 299 MNL 301
Cdd:COG1129 487 MAA 489
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
111-289 |
1.40e-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: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 111 LEIQEGKLVGICGSVGSGKTSLISAILGQM---TLLEGSIAISG----------TFAYVAQQ-AWILNATLRDNILF--- 173
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGqprkpdqfqkCVAYVRQDdILLPGLTVRETLTYtai 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 174 ---GKEYDEERYNSVLNSCCLRpDLAILPSSdlteiGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 250
Cdd:cd03234 108 lrlPRKSSDAIRKKRVEDVLLR-DLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622900610 251 IFnsAIRKHL--KSKTVLFVTHQ-----LQYLvdcDEVIFMKEGCI 289
Cdd:cd03234 182 LV--STLSQLarRNRIVILTIHQprsdlFRLF---DRILLLSSGEI 222
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
153-300 |
1.47e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.45 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 153 FAYVAQQAWILNATLRDNILFGKE-YDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDR 231
Cdd:PTZ00265 1298 FSIVSQEPMLFNMSIYENIKFGKEdATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREP 1377
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 232 SIYILDDPLSALDAHVGNHIFNSAIR-KHLKSKTVLFVTHQLQYLVDCDEVIFM----KEGCITE-RGTHEELMN 300
Cdd:PTZ00265 1378 KILLLDEATSSLDSNSEKLIEKTIVDiKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLS 1452
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
738-937 |
1.48e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 71.73 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS-----GGCIKIDGVRI--SDIGLADLRSKLSIIPQEPVLFSG 810
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 811 TVRSNLD---PFNQYTEDQIWDALERTHMKEciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAA 887
Cdd:PRK14239 101 SIYENVVyglRLKGIKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 888 MDTETDLLIQETIREAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFD 937
Cdd:PRK14239 179 LDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYN 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
106-293 |
1.53e-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: 70.86 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAY-----VAQQAWILNA--------TLRDNIL 172
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVkepaeARRRLGFVSDstglydrlTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 -FGKEYDEERYNsvlnsccLRPDLAILpsSDLTEIGE----RGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhV 247
Cdd:cd03266 101 yFAGLYGLKGDE-------LTARLEEL--ADRLGMEElldrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV-M 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622900610 248 GNHIFNSAIRkHLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 293
Cdd:cd03266 171 ATRALREFIR-QLRAlgKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
724-949 |
1.76e-13 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 71.03 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 724 ENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLaDLRSKLSII-- 801
Cdd:cd03218 4 ENLSKRYGKRK--VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIGyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 802 PQEPVLFSG-TVRSNLDPFNQYTEDQIWDALERThmKECIAQLplKLESEVMENGDNFSVGERQLLCIARALLRHCKILI 880
Cdd:cd03218 81 PQEASIFRKlTVEENILAVLEIRGLSKKEREEKL--EELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 881 LDEATAAMDTETDLLIQETIREaFADCTM--LTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR 949
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKI-LKDRGIgvLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
106-282 |
1.95e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.51 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 172
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 F-----GKEYDEERynsvlnsccLRPDLAI--LPSSDLTEigeRGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 245
Cdd:PRK10247 103 FpwqirNQQPDPAI---------FLDDLERfaLPDTILTK---NIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622900610 246 HvGNHIFNSAIRKHLKSK--TVLFVTHQLQYLVDCDEVI 282
Cdd:PRK10247 171 S-NKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVI 208
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
732-933 |
2.05e-13 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 69.38 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 732 ENL--PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--VRISDIGLAdLRSKLSIIPqepvl 807
Cdd:cd03215 8 RGLsvKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkpVTRRSPRDA-IRAGIAYVP----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 808 fsgtvrsnldpfnqytEDqiwdaleRTHMKeciaqlpLKLESEVMEN---GDNFSVGERQLLCIARALLRHCKILILDEA 884
Cdd:cd03215 82 ----------------ED-------RKREG-------LVLDLSVAENialSSLLSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 885 TAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQV 933
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
737-936 |
2.57e-13 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 69.91 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIkPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAdLRSKLSIIPQEPVLFSG-TVRSN 815
Cdd:cd03264 15 ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLPQEFGVYPNfTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 816 LDPFNqytedqiwdALERTHMKECIAQLPLKLESEVMENGDN-----FSVGERQLLCIARALLRHCKILILDEATAAMDT 890
Cdd:cd03264 93 LDYIA---------WLKGIPSKEVKARVDEVLELVNLGDRAKkkigsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622900610 891 ETDLLIQETIREAFADCTMLTIAHRLHTVLGS-DRIMVLAQGQVVEF 936
Cdd:cd03264 164 EERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFE 210
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
94-300 |
2.96e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 70.91 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 94 HIHLGHLRLqrtLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---------------------- 151
Cdd:COG4559 8 SVRLGGRTL---LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarrravlpqhs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 152 --TFAYVAQQ-------AWILNATLRDNILfgkeydeerynsvlnscclrpdLAILPSSDLTEIGERG-ANLSGGQRQRI 221
Cdd:COG4559 85 slAFPFTVEEvvalgraPHGSSAAQDRQIV----------------------REALALVGLAHLAGRSyQTLSGGEQQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 222 SLARAL-------YSDRSIYILDDPLSALD-AHVgNHIFNSAirKHLKSK--TVLFVTHQL----QYlvdCDEVIFMKEG 287
Cdd:COG4559 143 QLARVLaqlwepvDGGPRWLFLDEPTSALDlAHQ-HAVLRLA--RQLARRggGVVAVLHDLnlaaQY---ADRILLLHQG 216
|
250
....*....|...
gi 1622900610 288 CITERGTHEELMN 300
Cdd:COG4559 217 RLVAQGTPEEVLT 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
741-945 |
3.23e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.05 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 741 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG---VRISDIGLADLRSKLSIIPQEPvLFSGTVRSNL- 816
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdlLGMKDDEWRAVRSDIQMIFQDP-LASLNPRMTIg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 817 ----DPFNQYTEDqiwdaLERTHMKECIAQLPLK---LESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMD 889
Cdd:PRK15079 119 eiiaEPLRTYHPK-----LSRQEVKDRVKAMMLKvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 890 TETDL----LIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 945
Cdd:PRK15079 194 VSIQAqvvnLLQQLQRE--MGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
738-954 |
4.80e-13 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 70.37 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRS----KLSIIPQEPVLFSG-TV 812
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 813 RSNLdPF--------NQYTEDQIWDALERTHMKECIAQLPlklesevmengDNFSVGERQLLCIARALLRHCKILILDEA 884
Cdd:cd03294 120 LENV-AFglevqgvpRAEREERAAEALELVGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 885 TAAMDTetdlLIQETIREAFADC------TMLTIAHRLHTV--LGsDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMF 954
Cdd:cd03294 188 FSALDP----LIRREMQDELLRLqaelqkTIVFITHDLDEAlrLG-DRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
106-271 |
6.43e-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: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAI---SGTFaYVAQQAWILNATLRDNIlfgkeydeery 182
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpegEDLL-FLPQRPYLPLGTLREQL----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 183 nsvlnscclrpdlaILPSSDlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnSAIRKHLks 262
Cdd:cd03223 85 --------------IYPWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY-QLLKELG-- 138
|
....*....
gi 1622900610 263 KTVLFVTHQ 271
Cdd:cd03223 139 ITVISVGHR 147
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
737-935 |
6.72e-13 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 72.41 E-value: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS----GGCIKIDGVRISDIGLADLR----SKLSIIPQEPVlf 808
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSERELRrirgNRIAMIFQEPM-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 809 sgtvrSNLDPFnqYT-EDQIW-------------------DALERTHMKE---CIAQLPLKLesevmengdnfSVGERQL 865
Cdd:COG4172 103 -----TSLNPL--HTiGKQIAevlrlhrglsgaaararalELLERVGIPDperRLDAYPHQL-----------SGGQRQR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 866 LCIARALLRHCKILILDEATAAMDTET-----DLL--IQETIREAfadctMLTIAHRLHTVLG-SDRIMVLAQGQVVE 935
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVTVqaqilDLLkdLQRELGMA-----LLLITHDLGVVRRfADRVAVMRQGEIVE 237
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
95-271 |
8.97e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.29 E-value: 8.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 95 IHLGHLRLQRTL-HSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------FAYVAQQAWI--LNA 165
Cdd:PRK13538 5 RNLACERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpirrqrDEYHQDLLYLghQPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 166 -----TLRDNILF----GKEYDEERYNSVLNSCCL--RPDLAIlpssdlteigergANLSGGQRQRISLARALYSDRSIY 234
Cdd:PRK13538 85 iktelTALENLRFyqrlHGPGDDEALWEALAQVGLagFEDVPV-------------RQLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622900610 235 ILDDPLSALDAHvGNHIFNSAIRKHLKSK-TVLFVTHQ 271
Cdd:PRK13538 152 ILDEPFTAIDKQ-GVARLEALLAQHAEQGgMVILTTHQ 188
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
109-298 |
9.01e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.83 E-value: 9.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 109 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQ-AWILNATLRDNILFG-- 174
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvppaergVGMVFQSyALYPHLSVAENMSFGlk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 175 -----KEYDEERYNSVLnscclrpdlAILPSSDLTEigERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA--HV 247
Cdd:PRK11000 102 lagakKEEINQRVNQVA---------EVLQLAHLLD--RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 248 GNHIFNSAIRKHLKSkTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 298
Cdd:PRK11000 171 QMRIEISRLHKRLGR-TMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
732-937 |
9.42e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.59 E-value: 9.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 732 ENL--PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--VRISDI------GLA----DlRSK 797
Cdd:COG1129 260 EGLsvGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPrdairaGIAyvpeD-RKG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 798 LSIIPQEPVLFSGTVrSNLDPFNQYTedQIWDALERTHMKECIAQLPLK---LESEVMengdNFSVGERQLLCIARALLR 874
Cdd:COG1129 339 EGLVLDLSIRENITL-ASLDRLSRGG--LLDRRRERALAEEYIKRLRIKtpsPEQPVG----NLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 875 HCKILILDEATAAMD----TEtdllIQETIREaFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV-EFD 937
Cdd:COG1129 412 DPKVLILDEPTRGIDvgakAE----IYRLIRE-LAAegKAVIVISSELPELLGlSDRILVMREGRIVgELD 477
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
721-935 |
1.04e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.60 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLVEL----SGGCIKIDGVRI---SDIGL 791
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTL----IRCINLlerpTSGRVLVDGQDLtalSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 792 ADLRSKLSIIPQEPVLFSG-TVRSNldpfnqytedqiwdalerthmkecIAqLPLKL--------ESEVMENGD------ 856
Cdd:PRK11153 78 RKARRQIGMIFQHFNLLSSrTVFDN------------------------VA-LPLELagtpkaeiKARVTELLElvglsd 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 857 -------NFSVGERQLLCIARALLRHCKILILDEATAAMDTET-----DLL--IQETIreafaDCTMLTIAHRLHTVLG- 921
Cdd:PRK11153 133 kadrypaQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATtrsilELLkdINREL-----GLTIVLITHEMDVVKRi 207
|
250
....*....|....
gi 1622900610 922 SDRIMVLAQGQVVE 935
Cdd:PRK11153 208 CDRVAVIDAGRLVE 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
721-945 |
1.15e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 69.47 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLPLV---LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI----SDIGLAD 793
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 794 LRSKLSIIPQ--EPVLFSGTVRSNLD--PFN-QYTEDQiwdalERTHMKECIAQLPLkleSEVMENGDNF--SVGERQLL 866
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEfgPKNfGFSEDE-----AKEKALKWLKKVGL---SEDLISKSPFelSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 867 CIARALLRHCKILILDEATAAMDTETdlliQETIREAFADC-----TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPS 940
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFKDYqkaghTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPK 230
|
....*
gi 1622900610 941 VLLSN 945
Cdd:PRK13641 231 EIFSD 235
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
106-293 |
1.16e-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: 68.33 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGtfayvaQQAWIL--------NATLRDNILFG--- 174
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSLLglgggfnpELTGRENIYLNgrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 175 ----KEYDEERYNSVLnscclrpdlailpssDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAH 246
Cdd:cd03220 112 lglsRKEIDEKIDEII---------------EFSELGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 247 vgnhiF----NSAIRKHLK-SKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 293
Cdd:cd03220 177 -----FqekcQRRLRELLKqGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
721-948 |
1.24e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.58 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDiGLADLRsklsI 800
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDER----L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 801 IPQEpvlfSGTVRSNLDPFNQYTedqiwdALE---------RTHMKECIAQLPLKLESEV--MENGDNF----SVGERQL 865
Cdd:PRK09493 75 IRQE----AGMVFQQFYLFPHLT------ALEnvmfgplrvRGASKEEAEKQARELLAKVglAERAHHYpselSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 866 LCIARALLRHCKILILDEATAAMDTEtdlLIQETIR--EAFAD--CTMLTIAHRL---HTVlGSdRIMVLAQGQVVEFDT 938
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPE---LRHEVLKvmQDLAEegMTMVIVTHEIgfaEKV-AS-RLIFIDKGRIAEDGD 219
|
250
....*....|
gi 1622900610 939 PSVLLSNDSS 948
Cdd:PRK09493 220 PQVLIKNPPS 229
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
97-297 |
1.25e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 70.29 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 97 LGHLRLQrtlhsIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAYVAQQ 159
Cdd:PRK11144 10 LGDLCLT-----VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppekrrIGYVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 160 AWIL-NATLRDNILFG-KEYDEERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDRSIYILD 237
Cdd:PRK11144 85 ARLFpHYKVRGNLRYGmAKSMVAQFDKIVALLGIEPLLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 238 DPLSALDAHvgnhifnsaiRKH-----LK--SKTV----LFVTHQLQYLVD-CDEVIFMKEGCITERGTHEE 297
Cdd:PRK11144 154 EPLASLDLP----------RKRellpyLErlAREInipiLYVSHSLDEILRlADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
695-935 |
1.38e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.54 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 695 IKTLSLEAP-ARIKNKAPSPDWPQegeVTFENAEMRYRENlPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE 773
Cdd:PRK10522 299 LNKLALAPYkAEFPRPQAFPDWQT---LELRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQ 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 774 LSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTvrsnLDPFNQYTEDQIWDA-LERTHMKEciaqlplKLEsevM 852
Cdd:PRK10522 375 PQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMAH-------KLE---L 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 853 ENGD----NFSVGERQLLCIARALLRHCKILILDEATAAMDTE------TDLL--IQETIREAFAdctmltIAHRLHTVL 920
Cdd:PRK10522 441 EDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfrrefyQVLLplLQEMGKTIFA------ISHDDHYFI 514
|
250
....*....|....*
gi 1622900610 921 GSDRIMVLAQGQVVE 935
Cdd:PRK10522 515 HADRLLEMRNGQLSE 529
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
737-943 |
1.48e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.86 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI-SDIGLAdlRSKLSIIPQEPVL-FSGTVRS 814
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLA--RARIGVVPQFDNLdLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 815 NLDPFNQYTedqiwdaleRTHMKECIAQLPLKLESEVMENGDNFSV-----GERQLLCIARALLRHCKILILDEATAAMD 889
Cdd:PRK13536 134 NLLVFGRYF---------GMSTREIEAVIPSLLEFARLESKADARVsdlsgGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 890 TETDLLIQETIREAFA--DCTMLTI-----AHRLhtvlgSDRIMVLAQGQVVEFDTPSVLL 943
Cdd:PRK13536 205 PHARHLIWERLRSLLArgKTILLTThfmeeAERL-----CDRLCVLEAGRKIAEGRPHALI 260
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
106-270 |
1.50e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.25 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG--TFAYVAQQAWIL-NATLRDNIL--FGKEYD-E 179
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDdDLTVLDTVLdgDAELRAlE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 180 ERYNSVLNSCCLRPDLAILPSSDLTEIGERGA--------------------------NLSGGQRQRISLARALYSDRSI 233
Cdd:COG0488 94 AELEELEAKLAEPDEDLERLAELQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARALLSEPDL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622900610 234 YILDDPLSALDAHvgnhifnsAIR---KHLKS--KTVLFVTH 270
Cdd:COG0488 174 LLLDEPTNHLDLE--------SIEwleEFLKNypGTVLVVSH 207
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
738-940 |
1.71e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.11 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--VRISDIGLADLRSKLSIIPQEP--VLFSGTVR 813
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQDPdnQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 814 SNLD--PFN-QYTEDQIWDALERTHMKECIAQLPLKLESEVmengdnfSVGERQLLCIARALLRHCKILILDEATAAMD- 889
Cdd:PRK13636 102 QDVSfgAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCL-------SFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDp 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 890 ---TETDLLIQETIREafADCTMLTIAHRLHTV-LGSDRIMVLAQGQVVEFDTPS 940
Cdd:PRK13636 175 mgvSEIMKLLVEMQKE--LGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPK 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
104-298 |
1.88e-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: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG------------TFAYVAQQAWILNA-TLRDN 170
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 171 I-LFGKEYD---EERYNSVLNscclrpdlaILPSSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 245
Cdd:cd03265 94 LyIHARLYGvpgAERRERIDE---------LLDFVGLLEAADRlVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 246 HVGNHIFnSAIRKHLKSK--TVLFVTHqlqYLVD----CDEVIFMKEGCITERGTHEEL 298
Cdd:cd03265 165 QTRAHVW-EYIEKLKEEFgmTILLTTH---YMEEaeqlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
721-892 |
1.90e-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: 67.43 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSK 797
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 798 LSIIPQEPVLFSG-TVRSNLDPFNQYTEDQIWDALERthMKECIAQLPLKLESEVMENGdnFSVGERQLLCIARALLRHC 876
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENVAFALEVTGVPPREIRKR--VPAALELVGLSHKHRALPAE--LSGGEQQRVAIARAIVNSP 155
|
170
....*....|....*.
gi 1622900610 877 KILILDEATAAMDTET 892
Cdd:cd03292 156 TILIADEPTGNLDPDT 171
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
213-300 |
2.06e-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: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 213 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNsaIRKHLKSK---TVLFVTHQLQ---YLvdCDEVIFMKE 286
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILD--LLRDLQREhglAYLFISHDLAvvrAL--AHRVMVMKD 501
|
90
....*....|....
gi 1622900610 287 GCITERGTHEELMN 300
Cdd:COG4172 502 GKVVEQGPTEQVFD 515
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
109-287 |
2.14e-12 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 67.53 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 109 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG----TFAYVAQQA-----------WILnaTLRDNILF 173
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirTDRKAARQSlgycpqfdalfDEL--TVREHLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 174 -----GKEYDEERYNSvlnscclrpdLAILPSSDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 247
Cdd:cd03263 99 yarlkGLPKSEIKEEV----------ELLLRVLGLTDKANKRArTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622900610 248 GNHIFNsAIRKHLKSKTVLFVTHQLQ---YLvdCDEVIFMKEG 287
Cdd:cd03263 169 RRAIWD-LILEVRKGRSIILTTHSMDeaeAL--CDRIAIMSDG 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
106-298 |
2.38e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 68.60 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFayvaqqawiLNATLRDNIlfGkeY-DEERyns 184
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP---------LDPEDRRRI--G--YlPEER--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 185 vlnscCLRPDLAI------------LPSSDLT----------EIGERGA----NLSGGQRQRISLARALYSDRSIYILDD 238
Cdd:COG4152 81 -----GLYPKMKVgeqlvylarlkgLSKAEAKrradewlerlGLGDRANkkveELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 239 PLSALDAhVGNHIFNSAIRKHLKS-KTVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEEL 298
Cdd:COG4152 156 PFSGLDP-VNVELLKDVIRELAAKgTTVIFSSHQME-LVEelCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
737-945 |
2.47e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.15 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKID------GVRISDIGLADLRSKLSIIPQEPVLFSG 810
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 811 -TVRSNLD-PFNQYTedqIWDALE-RTHMKECIAQLPL--KLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEAT 885
Cdd:PRK14246 105 lSIYDNIAyPLKSHG---IKEKREiKKIVEECLRKVGLwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 886 AAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 945
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
106-300 |
2.51e-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: 67.57 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTF--------------AYVAQQAWIL-NATLRDN 170
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhkrarlgiGYLPQEASIFrKLTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 171 IL-------FGKEYDEERYNSVLNscclrpDLAILPSSDlteigERGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 243
Cdd:cd03218 96 ILavleirgLSKKEREEKLEELLE------EFHITHLRK-----SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 244 DAHVGNHIfnSAIRKHLKSKT--VLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 300
Cdd:cd03218 165 DPIAVQDI--QKIIKILKDRGigVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
737-945 |
2.58e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.14 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG-----GCIKIDGVRISD--IGLADLRSKLSIIPQEPVLFS 809
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVNLNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 810 GTVRSNLdpfnQYTEDQI-W------DALERTHMKEciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILD 882
Cdd:PRK14258 102 MSVYDNV----AYGVKIVgWrpkleiDDIVESALKD--ADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900610 883 EATAAMDTETDLLIQETIREAF--ADCTMLTIAHRLHTVL-----------GSDRImvlaqGQVVEFDTPSVLLSN 945
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSrlsdftaffkgNENRI-----GQLVEFGLTKKIFNS 246
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
737-949 |
2.66e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.87 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVL-FSGTVR-- 813
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRqv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 814 ---------SNLDPFNQYTEDQIWDALERTHMKECIAQlPLklesevmengDNFSVGERQLLCIARALLRHCKILILDEA 884
Cdd:PRK09536 98 vemgrtphrSRFDTWTETDRAAVERAMERTGVAQFADR-PV----------TSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 885 TAAMDTETDLLIQETIRE-------AFADCTMLTIAHRLhtvlgSDRIMVLAQGQVVEFDTPSVLLSNDSSR 949
Cdd:PRK09536 167 TASLDINHQVRTLELVRRlvddgktAVAAIHDLDLAARY-----CDELVLLADGRVRAAGPPADVLTADTLR 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
737-944 |
2.73e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.50 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRL-----VELSGGCIKIDGVRISDIGLADLR----SKLSIIPQEPVL 807
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 808 fsgtvrsNLDPFNQyTEDQIWDALE----------RTHMKECIAQLPLKLESEVMEN-GDNFSVGERQLLCIARALLRHC 876
Cdd:PRK15134 104 -------SLNPLHT-LEKQLYEVLSlhrgmrreaaRGEILNCLDRVGIRQAAKRLTDyPHQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 877 KILILDEATAAMDTETDLLIQETIREAFADCTM--LTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 944
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLRELQQELNMglLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
741-959 |
2.82e-12 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 69.36 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 741 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD----IGLADLRSKLSIIPQEPVLFSG-TVRSN 815
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargIFLPPHRRRIGYVFQEARLFPHlSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 816 LdpfnQYTEDQIWDALERTHMKECIAQL---PLkLESEVmengDNFSVGERQLLCIARALLRHCKILILDEATAAMDTET 892
Cdd:COG4148 98 L----LYGRKRAPRAERRISFDEVVELLgigHL-LDRRP----ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 893 -----DLLiqETIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAEN 959
Cdd:COG4148 169 kaeilPYL--ERLRDEL-DIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGS 238
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
721-934 |
2.95e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.30 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYrENLPLvlkKVSFTIKPKEKIGIVGRTGSGKSSLG--MALFRLVElsGGCIKIDGVRISDIGLAdlRSKL 798
Cdd:PRK10771 2 LKLTDITWLY-HHLPM---RFDLTVERGERVAILGPSGAGKSTLLnlIAGFLTPA--SGSLTLNGQDHTTTPPS--RRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 799 SIIPQEPVLFSG-TVRSN----LDP---FNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIAR 870
Cdd:PRK10771 74 SMLFQENNLFSHlTVAQNiglgLNPglkLNAAQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALAR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 871 ALLRHCKILILDEATAAMD----TETDLLIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 934
Cdd:PRK10771 143 CLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQE--RQLTLLMVSHSLEDAARiAPRSLVVADGRIA 209
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
737-949 |
3.66e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.21 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLSIIPQEPVLFSG-TVRS 814
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 815 NLDPFNQYTEDQIWdaleRTHMKECIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDL 894
Cdd:PRK11614 100 NLAMGGFFAERDQF----QERIKWVYELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 895 LIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR 949
Cdd:PRK11614 175 QIFDTIEQLREQgMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALLANEAVR 231
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
103-300 |
4.11e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 67.42 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------FAYVAQQAWIL---NA-----TLR 168
Cdd:COG4604 14 KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvattpSRELAKRLAILrqeNHinsrlTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 169 DNILFG---------KEYDEERYNSVLNSCclrpdlailpssDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDD 238
Cdd:COG4604 94 ELVAFGrfpyskgrlTAEDREIIDEAIAYL------------DLEDLADRYLDeLSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 239 PLSALDahvgnhIFNS-AIRKHLKS------KTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEELMN 300
Cdd:COG4604 162 PLNNLD------MKHSvQMMKLLRRladelgKTVVIVLHDInfasCY---ADHIVAMKDGRVVAQGTPEEIIT 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
106-300 |
4.77e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 67.30 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAY----------VAQQAWILNATLRDNILFgK 175
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLRLLRTRLTMVF-Q 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 176 EYDEERYNSVLNSCCLRPDLAI-LPSSDLTE----------IGERG-----ANLSGGQRQRISLARALYSDRSIYILDDP 239
Cdd:PRK10619 100 HFNLWSHMTVLENVMEAPIQVLgLSKQEAREravkylakvgIDERAqgkypVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 240 LSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELMN 300
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
103-289 |
4.89e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.01 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRT-LHSIDLEIQEGKLVGICGSVGSGKTSLISAILG-----QMTLLEGSIAIsgtfayvaqqawilnATLRDNILFgkE 176
Cdd:PRK11247 24 ERTvLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGletpsAGELLAGTAPL---------------AEAREDTRL--M 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 177 YDEER---YNSVLNSCCL------RPD-LAILPSSDLTE-IGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 245
Cdd:PRK11247 87 FQDARllpWKKVIDNVGLglkgqwRDAaLQALAAVGLADrANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622900610 246 HVG---NHIFNSAIRKHlkSKTVLFVTHQLQYLVD-CDEVIFMKEGCI 289
Cdd:PRK11247 167 LTRiemQDLIESLWQQH--GFTVLLVTHDVSEAVAmADRVLLIEEGKI 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
106-270 |
4.94e-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: 66.28 E-value: 4.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT---------FAYVAQQ--------AWILNATLR 168
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraIPYLRRKigvvfqdfRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 169 DNILFGKEYDE-------ERYNSVLNSCCLRPDLAILPssdlteigergANLSGGQRQRISLARALYSDRSIYILDDPLS 241
Cdd:cd03292 97 ENVAFALEVTGvppreirKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180
....*....|....*....|....*....
gi 1622900610 242 ALDAHVGNHIFNSAIRKHLKSKTVLFVTH 270
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
104-300 |
5.04e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 67.77 E-value: 5.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------------TFAYVAQQawILN 164
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkkvglVFQYPEYQ--LFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 165 ATLRDNILFGK----EYDEERYNSVLNSCclrpDLAILPSSDLTEigERGANLSGGQRQRISLARALYSDRSIYILDDPL 240
Cdd:PRK13637 99 ETIEKDIAFGPinlgLSEEEIENRVKRAM----NIVGLDYEDYKD--KSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 241 SALDAHVGNHIFNSAIRKHLKSK-TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 300
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFK 234
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
737-937 |
5.56e-12 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 66.40 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvRIS---DIGLAdLRSKLSIIpqEPVLFSGTVR 813
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSsllGLGGG-FNPELTGR--ENIYLNGRLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 814 SNLDPFNQYTEDQIWDALErthMKECIaQLPLKlesevmengdNFSVGERQLLCIARALLRHCKILILDEATAAMDTETD 893
Cdd:cd03220 113 GLSRKEIDEKIDEIIEFSE---LGDFI-DLPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622900610 894 LLIQETIREAFADCTMLTIA-HRLHTVLG-SDRIMVLAQGQVVEFD 937
Cdd:cd03220 179 EKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
106-300 |
5.82e-12 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 66.54 E-value: 5.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQAWIL-NATLRDN 170
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIFpSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 171 ILFG------KEYDEERYNSVLNsccLRPDLAilpssdlteigER----GANLSGGQRQRISLARALYSDRSIYILDDPL 240
Cdd:COG0410 99 LLLGayarrdRAEVRADLERVYE---LFPRLK-----------ERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 241 SALDAHVGNHIFNsAIRKhLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 300
Cdd:COG0410 165 LGLAPLIVEEIFE-IIRR-LNREgvTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
106-308 |
5.92e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.43 E-value: 5.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTfAYVAQQAWILN----------------ATLRD 169
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWNLRrkigmvfqnpdnqfvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 170 NILFGKEYDEERYNSVLNscclRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 249
Cdd:PRK13642 102 DVAFGMENQGIPREEMIK----RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 250 HIFNsaIRKHLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATI 308
Cdd:PRK13642 178 EIMR--VIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEI 237
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
712-935 |
6.54e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 6.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 712 SPDWPQEGEVTFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG------ 783
Cdd:PRK10261 4 SDELDARDVLAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 784 ----VRISDIGLADLR----SKLSIIPQEPVlfsgtvrSNLDPFNQYTEdQIWDALeRTHM----KECIAQLPLKL---- 847
Cdd:PRK10261 84 srqvIELSEQSAAQMRhvrgADMAMIFQEPM-------TSLNPVFTVGE-QIAESI-RLHQgasrEEAMVEAKRMLdqvr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 848 --ESEVM--ENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTM--LTIAHRLHTVLG 921
Cdd:PRK10261 155 ipEAQTIlsRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgvIFITHDMGVVAE 234
|
250
....*....|....*
gi 1622900610 922 -SDRIMVLAQGQVVE 935
Cdd:PRK10261 235 iADRVLVMYQGEAVE 249
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
724-942 |
6.80e-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: 65.85 E-value: 6.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 724 ENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG---VRISDiglaDLRSKLSI 800
Cdd:cd03265 4 ENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvVREPR----EVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 801 IPQEPVLFSG-TVRSNLdpfnqYTEDQIWdALERTHMKECIAQLpLKLeSEVMENGD----NFSVGERQLLCIARALLRH 875
Cdd:cd03265 78 VFQDLSVDDElTGWENL-----YIHARLY-GVPGAERRERIDEL-LDF-VGLLEAADrlvkTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 876 CKILILDEATAAMDTETDLLIQETIR---EAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVL 942
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEklkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
741-933 |
7.30e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.80 E-value: 7.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 741 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE-LSGGCIKIDG--VRIS------DIGLADL---RSKLSIIPQEPVLF 808
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRnpqqaiAQGIAMVpedRKRDGIVPVMGVGK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 809 SGTVrSNLDPFNQYTedQIWDALERTHMKECIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILDEATAAM 888
Cdd:PRK13549 361 NITL-AALDRFTGGS--RIDDAAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622900610 889 DT----ETDLLIQETIREAFAdctMLTIAHRLHTVLG-SDRIMVLAQGQV 933
Cdd:PRK13549 437 DVgakyEIYKLINQLVQQGVA---IIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
736-945 |
7.33e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.73 E-value: 7.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 736 LVLKKVSFTIkPKEKI-GIVGRTGSGKSSLGMALFRLVELSGGCiKIDGVRI--------SDIGLADLRSKLSIIPQEPV 806
Cdd:PRK14243 24 LAVKNVWLDI-PKNQItAFIGPSGCGKSTILRCFNRLNDLIPGF-RVEGKVTfhgknlyaPDVDPVEVRRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 807 LFSGTVRSNLD---PFNQYTEDQiwDALERTHMKEciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDE 883
Cdd:PRK14243 102 PFPKSIYDNIAygaRINGYKGDM--DELVERSLRQ--AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 884 ATAAMDTETDLLIQETIREAFADCTMLTIAHRLH---------------TVLGSDRimvlaQGQVVEFDTPSVLLSN 945
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMQqaarvsdmtaffnveLTEGGGR-----YGYLVEFDRTEKIFNS 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
738-932 |
7.76e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.80 E-value: 7.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLgMALfrlveLSG--------GCIKIDGVRISDIGLADL-RSKLSIIPQEPVLF 808
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTL-MKV-----LSGvyphgtyeGEIIFEGEELQASNIRDTeRAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 809 SG-TVRSNLDPFNQYTEDQI--WDALERtHMKECIAQLPLKL--ESEVMENGdnfsVGERQLLCIARALLRHCKILILDE 883
Cdd:PRK13549 95 KElSVLENIFLGNEITPGGImdYDAMYL-RAQKLLAQLKLDInpATPVGNLG----LGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 884 ATAAM-DTETDLLIqETIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQ 932
Cdd:PRK13549 170 PTASLtESETAVLL-DIIRDLKAhGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
106-300 |
8.57e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.42 E-value: 8.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI-------------------------------------A 148
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvleklviqktrfkkikkikE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 149 ISGTFAYVAQQA--WILNATLRDNILFG-------KEYDEERYNSVLNSCCLrpDLAILPSSDLteigergaNLSGGQRQ 219
Cdd:PRK13651 103 IRRRVGVVFQFAeyQLFEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESYLQRSPF--------ELSGGQKR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 220 RISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG-THEE 297
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEwTKRTIFFKDGKIIKDGdTYDI 252
|
...
gi 1622900610 298 LMN 300
Cdd:PRK13651 253 LSD 255
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
106-277 |
9.41e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 65.46 E-value: 9.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYVAQQAWIL-NATLR 168
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlkrreipylrrrIGVVFQDFRLLpDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 169 DNILF-----GKEYDE--ERYNSVLnscclrpdlailpssDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILD 237
Cdd:COG2884 98 ENVALplrvtGKSRKEirRRVREVL---------------DLVGLSDKAkalpHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622900610 238 DPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQyLVD 277
Cdd:COG2884 163 EPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE-LVD 201
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
95-270 |
9.76e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 65.20 E-value: 9.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 95 IHLGHLRLqrtLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQmtlLEGSIAISGtfayvaqQAWI-------LNATL 167
Cdd:COG4136 9 ITLGGRPL---LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGT---LSPAFSASG-------EVLLngrrltaLPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 168 R------------------DNILFG---KEYDEERYNSVLNScclrpdlaiLPSSDLTEIGERG-ANLSGGQRQRISLAR 225
Cdd:COG4136 76 RrigilfqddllfphlsvgENLAFAlppTIGRAQRRARVEQA---------LEEAGLAGFADRDpATLSGGQRARVALLR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622900610 226 ALYSDRSIYILDDPLSALDAH----VGNHIFNSAIRKHLkskTVLFVTH 270
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAAlraqFREFVFEQIRQRGI---PALLVTH 192
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
113-296 |
1.00e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.55 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 113 IQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGtfAYVAQQAWILNA---------------TLRDNIL-FGKE 176
Cdd:PRK13536 64 VASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLARArigvvpqfdnldlefTVRENLLvFGRY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 177 YdeeRYNSvlnscclRPDLAILPSsdLTEIGE-------RGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGN 249
Cdd:PRK13536 142 F---GMST-------REIEAVIPS--LLEFARleskadaRVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-AR 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622900610 250 HIFNSAIRKHL-KSKTVLFVTHQLQYLVD-CDEVIFMKEGC-ITERGTHE 296
Cdd:PRK13536 209 HLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGRkIAEGRPHA 258
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
737-952 |
1.02e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.66 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVElsggciKIDGVRIS-DIGLA-----------DLRSKLSIIPQE 804
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMND------KVSGYRYSgDVLLGgrsifnyrdvlEFRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 805 PVLFSGTVRSN---------LDPFNQY--------TEDQIWDALerthmKECIAQLPLKLesevmengdnfSVGERQLLC 867
Cdd:PRK14271 110 PNPFPMSIMDNvlagvrahkLVPRKEFrgvaqarlTEVGLWDAV-----KDRLSDSPFRL-----------SGGQQQLLC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 868 IARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRL-HTVLGSDRIMVLAQGQVVEFDTPSVLLSN- 945
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSSp 253
|
250
....*....|
gi 1622900610 946 ---DSSRFYA 952
Cdd:PRK14271 254 khaETARYVA 263
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
104-300 |
1.19e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.57 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGqMTLLEGSIAISGTFAYVAQ---------------------QAWI 162
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNG-LIISETGQTIVGDYAIPANlkkikevkrlrkeiglvfqfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 163 LNATLRDNILFGK----EYDEERYNSVlnscclrPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDD 238
Cdd:PRK13645 104 FQETIEKDIAFGPvnlgENKQEAYKKV-------PELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 239 PLSALDAHVGNHIFNSAIR-KHLKSKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELMN 300
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERlNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
103-272 |
1.54e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.83 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAiLGQMTLLEGSIAISGTFAYVAQQAWILNATL------------RDN 170
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYERRVNLnrlrrqvsmvhpKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 171 ILFGKEYDEERYNSVLNSccLRPDLAI-------LPSSDL-----TEIGERGANLSGGQRQRISLARALYSDRSIYILDD 238
Cdd:PRK14258 99 LFPMSVYDNVAYGVKIVG--WRPKLEIddivesaLKDADLwdeikHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622900610 239 PLSALDA----HVGNHIFNSAIRKHLkskTVLFVTHQL 272
Cdd:PRK14258 177 PCFGLDPiasmKVESLIQSLRLRSEL---TMVIVSHNL 211
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
106-298 |
1.58e-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: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQ-AWILNATLRDNILF 173
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelepadrdIAMVFQNyALYPHMSVRENMAY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 174 G-------KEYDEERynsvlnscclrpdlaILPSSDLTEIGE----RGANLSGGQRQRISLARALYSDRSIYILDDPLSA 242
Cdd:PRK11650 100 GlkirgmpKAEIEER---------------VAEAARILELEPlldrKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 243 LDAHVGNHIfNSAIRK-HLKSKTV-LFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 298
Cdd:PRK11650 165 LDAKLRVQM-RLEIQRlHRRLKTTsLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
741-944 |
1.61e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.91 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 741 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGG--CIKI--DGVRISDIGLaDLRSK----LSIIPQEPVLFsgTV 812
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVgdEWVDMTKPGP-DGRGRakryIGILHQEYDLY--PH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 813 RSNLDPFNQYTEDQIWDALERthMKECIAQLPLKLESEVMEN-----GDNFSVGERQLLCIARALLRHCKILILDEATAA 887
Cdd:TIGR03269 380 RTVLDNLTEAIGLELPDELAR--MKAVITLKMVGFDEEKAEEildkyPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 888 MDTETDLLIQETIREAFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 944
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
106-289 |
1.84e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.83 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISaILGQMtllegSIAISGTFAYVAQQAWILN----ATLRDN----------- 170
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCL-----DKPTSGTYRVAGQDVATLDadalAQLRREhfgfifqryhl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 171 --------------ILFGKEYDEERYNSVlnscclrpdlAILPSSDLTE-IGERGANLSGGQRQRISLARALYSDRSIYI 235
Cdd:PRK10535 98 lshltaaqnvevpaVYAGLERKQRLLRAQ----------ELLQRLGLEDrVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900610 236 LDDPLSALDAHVGNHIFnsAIRKHLKSK--TVLFVTHQLQYLVDCDEVIFMKEGCI 289
Cdd:PRK10535 168 ADEPTGALDSHSGEEVM--AILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
103-299 |
2.10e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 65.42 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNA-TLR 168
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlarrLALLPQHHLTPEGiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 169 DNILFGK-----------EYDEERYNSVLNScclrpdlailpsSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYIL 236
Cdd:PRK11231 95 ELVAYGRspwlslwgrlsAEDNARVNQAMEQ------------TRINHLADRRlTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 237 DDPLSALDAhvgNHIFN--SAIRK-HLKSKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELM 299
Cdd:PRK11231 163 DEPTTYLDI---NHQVElmRLMRElNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
109-300 |
2.12e-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: 64.77 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 109 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIA-----ISG-------------TFayvaQQAWIL-NATLRD 169
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgedITGlppheiarlgigrTF----QIPRLFpELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 170 NILFGKEYDEERYNSVLNSCCLRPDL-----AILpssDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILDDPL 240
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREEREAreraeELL---ERVGLADLAdrpaGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 241 SALD----AHVGNHIfnSAIRKHlkSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 300
Cdd:cd03219 172 AGLNpeetEELAELI--RELRER--GITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
736-921 |
2.25e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.12 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 736 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvriSDIGLADLRSKLSII----PQEPVLfsgT 811
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLghrnAMKPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 812 VRSNLD---PFNQYTEDQIWDALERTHMKEcIAQLPLKlesevmengdNFSVGERQLLCIARALLRHCKILILDEATAAM 888
Cdd:PRK13539 90 VAENLEfwaAFLGGEELDIAAALEAVGLAP-LAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190
....*....|....*....|....*....|...
gi 1622900610 889 DTETDLLIQETIREAFADCTMLTIAhrLHTVLG 921
Cdd:PRK13539 159 DAAAVALFAELIRAHLAQGGIVIAA--THIPLG 189
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
742-934 |
2.31e-11 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 64.44 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 742 SFTIKPKEKIGIVGRTGSGKSSLgMALFRLVEL-SGGCIKIDGVrisDIGLADL-RSKLSIIPQEPVLFSG-TVRSNLD- 817
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTL-LNLIAGFETpQSGRVLINGV---DVTAAPPaDRPVSMLFQENNLFAHlTVEQNVGl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 818 ---PFNQYTEDQ---IWDALERTHMKECIAQLPlklesevmengDNFSVGERQLLCIARALLRHCKILILDEATAAMD-- 889
Cdd:cd03298 94 glsPGLKLTAEDrqaIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVRDKPVLLLDEPFAALDpa 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622900610 890 --TETDLLIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 934
Cdd:cd03298 163 lrAEMLDLVLDLHAE--TKMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
97-271 |
2.66e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 64.05 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 97 LGHLRLQRTLHS-IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------------FAYVAQQAWIL 163
Cdd:cd03231 6 LTCERDGRALFSgLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiargLLYLGHAPGIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 164 NA-TLRDNILFgkeydeerynsvlnSCCLRPDLAI---LPSSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDD 238
Cdd:cd03231 86 TTlSVLENLRF--------------WHADHSDEQVeeaLARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|....
gi 1622900610 239 PLSALDAHvGNHIFNSAIRKHL-KSKTVLFVTHQ 271
Cdd:cd03231 152 PTTALDKA-GVARFAEAMAGHCaRGGMVVLTTHQ 184
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
730-900 |
2.79e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.35 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 730 YRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFS 809
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 810 GTVRSNLD-PFnqytedQIW-DALERTHMKECIAQLPLKlESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAA 887
Cdd:PRK10247 95 DTVYDNLIfPW------QIRnQQPDPAIFLDDLERFALP-DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170
....*....|...
gi 1622900610 888 MDTETDLLIQETI 900
Cdd:PRK10247 168 LDESNKHNVNEII 180
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
744-927 |
2.88e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 64.74 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 744 TIKPKEKIGIVGRTGSGKSSLgmalfrlVELSGGCIKIDGVrisDIGLAdlRSKLSIIPQE-PVLFSGTVRSNLdpfnqy 822
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTF-------IKMLAGVLKPDEG---DIEIE--LDTVSYKPQYiKADYEGTVRDLL------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 823 tEDQIWDALERTHMKECIAQlPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIRE 902
Cdd:cd03237 83 -SSITKDFYTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180
....*....|....*....|....*....
gi 1622900610 903 aFA---DCTMLTIAHRLHTV-LGSDRIMV 927
Cdd:cd03237 161 -FAennEKTAFVVEHDIIMIdYLADRLIV 188
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
443-608 |
3.27e-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: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 443 ASIYALSMAVMLILkairGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvrlpfqAEMFI 522
Cdd:cd18547 52 LGLYLLSALFSYLQ----NRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNI-------SQALS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 523 QNVILVFFCVGMIAGVF-------PWF-LVAVGPLVILFSVLHIV---SRVLIREL-KRLDNITqspflSHITSSIQGLA 590
Cdd:cd18547 121 QSLTQLISSILTIVGTLimmlyisPLLtLIVLVTVPLSLLVTKFIakrSQKYFRKQqKALGELN-----GYIEEMISGQK 195
|
170
....*....|....*...
gi 1622900610 591 TIHAYNKGQEFLHRYQEL 608
Cdd:cd18547 196 VVKAFNREEEAIEEFDEI 213
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
106-291 |
3.28e-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: 64.38 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--FAyvaqqawiLN----ATLR-DNILFgkeyd 178
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlFA--------LDedarARLRaRHVGF----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 179 eerynsVLNSCCLRPDL-AI----LPssdLTEIGERGA----------------------NLSGGQRQRISLARALYSDR 231
Cdd:COG4181 95 ------VFQSFQLLPTLtALenvmLP---LELAGRRDArararallervglghrldhypaQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 232 SIYILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLF-VTHQLQYLVDCDEVIFMKEGCITE 291
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVlVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
106-300 |
3.49e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 65.21 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTS---LISAILGQMTLLEGSIAISGTfAYVAQQAW----------------ILNAT 166
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGI-TLTAKTVWdirekvgivfqnpdnqFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 167 LRDNILFGKEydeerynsvlNSCCLRPDLAILPSSDLTEIG------ERGANLSGGQRQRISLARALYSDRSIYILDDPL 240
Cdd:PRK13640 102 VGDDVAFGLE----------NRAVPRPEMIKIVRDVLADVGmldyidSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 241 SALDAHVGNHIFnSAIRKHLKSK--TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 300
Cdd:PRK13640 172 SMLDPAGKEQIL-KLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
106-285 |
3.59e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.90 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------FAYVAQQA---WILNATLRDNIL 172
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQSEevdWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 173 FG-----------KEYDEERYNSVLNscclRPDLAILPSSdltEIGErganLSGGQRQRISLARALYSDRSIYILDDPLS 241
Cdd:PRK15056 103 MGryghmgwlrraKKRDRQIVTAALA----RVDMVEFRHR---QIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622900610 242 ALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMK 285
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEfCDYTVMVK 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
737-946 |
3.81e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.14 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGL-ADLRSKLSIIPQEPVLFSG-TVRS 814
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 815 NLDPFNQYTEDqiwdaLERTHMKECIAQLPLKLESEVMEN--GDNFSVGERQLLCIARALLRHCKILILDEATAAMDTET 892
Cdd:PRK10895 98 NLMAVLQIRDD-----LSAEQREDRANELMEEFHIEHLRDsmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 893 DLLIQETIrEAFADCTM--LTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSND 946
Cdd:PRK10895 173 VIDIKRII-EHLRDSGLgvLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
103-300 |
4.48e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.41 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAIlGQMTLLEGSIAISGTFAY---------------------VAQQAW 161
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 162 ILNATLRDNILFGKEYDEERYNSVLNSCCLRpdlAILPSSDLTEIGER----GANLSGGQRQRISLARALYSDRSIYILD 237
Cdd:PRK14239 97 PFPMSIYENVVYGLRLKGIKDKQVLDEAVEK---SLKGASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900610 238 DPLSALDAHVGNHIFNSAIRkhLKSK-TVLFVTHQLQYLVD-CDEVIFMKEGCITERG-THEELMN 300
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLG--LKDDyTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNdTKQMFMN 237
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
741-935 |
4.60e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 65.37 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 741 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG---VRISDIGLADLRSKLSIIPQEPVlfsgtvrSNLD 817
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdlLKADPEAQKLLRQKIQIVFQNPY-------GSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 818 PfNQYTEDQIWDALE----------RTHMKECIAQLPLKLESEV----MengdnFSVGERQLLCIARALLRHCKILILDE 883
Cdd:PRK11308 107 P-RKKVGQILEEPLLintslsaaerREKALAMMAKVGLRPEHYDryphM-----FSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 884 ATAAMDTEtdllIQETIREAFAD------CTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 935
Cdd:PRK11308 181 PVSALDVS----VQAQVLNLMMDlqqelgLSYVFISHDLSVVEHiADEVMVMYLGRCVE 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
103-298 |
4.77e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 64.66 E-value: 4.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAI------SGT---------------FAYVAQQaw 161
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKknkklkplrkkvgivFQFPEHQ-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 162 ILNATLRDNILFG-------KEYDEERYNSVLNSCCLRPDLaiLPSSDLteigergaNLSGGQRQRISLARALYSDRSIY 234
Cdd:PRK13634 98 LFEETVEKDICFGpmnfgvsEEDAKQKAREMIELVGLPEEL--LARSPF--------ELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 235 ILDDPLSALDAHVGNHIFNSAIRKHL-KSKTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEEL 298
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMedaaRY---ADQIVVMHKGTVFLQGTPREI 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
723-937 |
5.68e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.24 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 723 FENAEMRYreNLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSlgmaLFRLV----ELSGGCIKID-GVRIsdigladlrsk 797
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKST----LLKILagelEPDSGEVSIPkGLRI----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 798 lSIIPQEPVLFSG-TVRSN-LDPFNQYteDQIWDALERTHMKECIAQLPLKLESEVME-----NG--------------- 855
Cdd:COG0488 64 -GYLPQEPPLDDDlTVLDTvLDGDAEL--RALEAELEELEAKLAEPDEDLERLAELQEefealGGweaearaeeilsglg 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 856 ----------DNFSVGERQLLCIARALLRHCKILILDEATAAMDTET-----DLLIQEtireafaDCTMLTIAH-R--LH 917
Cdd:COG0488 141 fpeedldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKNY-------PGTVLVVSHdRyfLD 213
|
250 260
....*....|....*....|
gi 1622900610 918 TVlgSDRIMVLAQGQVVEFD 937
Cdd:COG0488 214 RV--ATRILELDRGKLTLYP 231
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
738-944 |
6.20e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.04 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdIGLADLRS-KLSIIPQEPV---------- 806
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSqRIRMIFQDPStslnprqris 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 807 -LFSGTVRSNLDPFNQYTEDQIWDALERTHM-KECIAQLPLKLESevmengdnfsvGERQLLCIARALLRHCKILILDEA 884
Cdd:PRK15112 108 qILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAP-----------GQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 885 TAAMDTETD-------LLIQETIREAFADCTMlTIAHRLHTvlgSDRIMVLAQGQVVEF-DTPSVLLS 944
Cdd:PRK15112 177 LASLDMSMRsqlinlmLELQEKQGISYIYVTQ-HLGMMKHI---SDQVLVMHQGEVVERgSTADVLAS 240
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
103-293 |
6.34e-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: 62.98 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGkLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG------------TFAYVAQQAwilnaTLRDN 170
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQEF-----GVYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 171 IlfgKEYDEERYNSVLNSC----CLRPDLAILPSSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDa 245
Cdd:cd03264 87 F---TVREFLDYIAWLKGIpskeVKARVDEVLELVNLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622900610 246 hVGNHI-FNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 293
Cdd:cd03264 163 -PEERIrFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
111-343 |
7.07e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.44 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 111 LEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNATLRDNILFGKEYDEERYNSVLNSCC 190
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 191 LRPDLAILPSSD--------LTEIG-ERGAN-----LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAI 256
Cdd:PRK10070 129 FGMELAGINAEErrekaldaLRQVGlENYAHsypdeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 257 RKHLK-SKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELMN--LNGDYATIFNNLLLGDTPPVEINSKKETSGSQ 332
Cdd:PRK10070 209 KLQAKhQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNnpANDYVRTFFRGVDISQVFSAKDIARRTPNGLI 288
|
250
....*....|.
gi 1622900610 333 KKSQDKGPKTG 343
Cdd:PRK10070 289 RKTPGFGPRSA 299
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
740-938 |
8.01e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 64.75 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 740 KVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG---GCIKIDGVRISDI---GLADLRS-KLSIIPQEPVlfsgtv 812
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLpekELNKLRAeQISMIFQDPM------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 813 rSNLDPFNQYTEdQIWDAL-------------ERTHMKECIaQLPLKLESEVMENGDnFSVGERQLLCIARALLRHCKIL 879
Cdd:PRK09473 108 -TSLNPYMRVGE-QLMEVLmlhkgmskaeafeESVRMLDAV-KMPEARKRMKMYPHE-FSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 880 ILDEATAAMDTETD----LLIQETIREaFaDCTMLTIAHRLHTVLGS-DRIMVLAQGQVVEFDT 938
Cdd:PRK09473 184 IADEPTTALDVTVQaqimTLLNELKRE-F-NTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYGN 245
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
433-555 |
8.32e-11 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 64.10 E-value: 8.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 433 MKDNPRMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDV 512
Cdd:cd18572 29 DGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSD 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1622900610 513 RLPFQAEMFIQNVILVFFCVGMIAGVfPWFL-----VAVGPLVILFSV 555
Cdd:cd18572 109 PLSTNLNVFLRNLVQLVGGLAFMFSL-SWRLtllafITVPVIALITKV 155
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
737-944 |
9.28e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.49 E-value: 9.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSG-TVRSN 815
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 816 L----DPFNQY-----TEDQ--IWDALERTHMKEcIAQLPLklesevmengDNFSVGERQLLCIARALLRHCKILILDEA 884
Cdd:PRK11231 97 VaygrSPWLSLwgrlsAEDNarVNQAMEQTRINH-LADRRL----------TDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 885 TAAMDTETDLLIQETIREAFADC-TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 944
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQGkTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
110-308 |
1.01e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 62.68 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 110 DLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVAQQ-AWIL--------NATLRDNILFGkey 177
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhTTTPPSRRpVSMLfqennlfsHLTVAQNIGLG--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 178 deerynsvlnsccLRPDL-----------AILPSSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 245
Cdd:PRK10771 96 -------------LNPGLklnaaqreklhAIARQMGIEDLLARlPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 246 HVGNHIFN----SAIRKHLkskTVLFVTHQLQylvDCDEV----IFMKEGCITERGTHEELMNLNGDYATI 308
Cdd:PRK10771 163 ALRQEMLTlvsqVCQERQL---TLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELLSGKASASAL 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
105-300 |
1.04e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 63.62 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 105 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI-----AISG-TFAYVAQQAWIL---------NATLRD 169
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDdNFEKLRKHIGIVfqnpdnqfvGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 170 NILFGKE-----YDE--ERYNSVLNscclrpDLAILPSSDlteigERGANLSGGQRQRISLARALYSDRSIYILDDPLSA 242
Cdd:PRK13648 104 DVAFGLEnhavpYDEmhRRVSEALK------QVDMLERAD-----YEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 243 LDAHVGNHIFNsaIRKHLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 300
Cdd:PRK13648 173 LDPDARQNLLD--LVRKVKSEhniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
104-300 |
1.17e-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: 65.21 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILG--QMTLLEGSI----AISGTFAYVAQQA----------------- 160
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvALCEKCGYVERPSkvgepcpvcggtlepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 161 ---WILNATLRDNI-------------LFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTE---IGER----GANLSGGQ 217
Cdd:TIGR03269 94 vdfWNLSDKLRRRIrkriaimlqrtfaLYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEmvqLSHRithiARDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 218 RQRISLARALYSDRSIYILDDPLSALDAHVGNhIFNSAIRKHLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGT 294
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASgiSMVLTSHWPEVIEDlSDKAIWLENGEIKEEGT 252
|
....*.
gi 1622900610 295 HEELMN 300
Cdd:TIGR03269 253 PDEVVA 258
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
724-946 |
1.24e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.22 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 724 ENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQ 803
Cdd:PRK13647 8 EDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 804 EP--VLFSGTVRSNL--DPFNQ-----YTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLR 874
Cdd:PRK13647 87 DPddQVFSSTVWDDVafGPVNMgldkdEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 875 HCKILILDEATAAMDTETdlliQETIREAFADC-----TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSND 946
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRG----QETLMEILDRLhnqgkTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
741-933 |
1.27e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.85 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 741 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS-GGCIKIDGVRISDIGLAD-LRSKLSIIPQE-------PVLFSG- 810
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQaIRAGIAMVPEDrkrhgivPILGVGk 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 811 -TVRSNLDPFNQYTedQIWDALERTHMKECIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILDEATAAMD 889
Cdd:TIGR02633 359 nITLSVLKSFCFKM--RIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622900610 890 T----ETDLLIQETIREAFAdctMLTIAHRLHTVLG-SDRIMVLAQGQV 933
Cdd:TIGR02633 436 VgakyEIYKLINQLAQEGVA---IIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
83-293 |
1.59e-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: 62.35 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 83 ERPSPEEEEGKHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG----------- 151
Cdd:cd03267 14 SKEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwkrrkkfl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 152 -----TFAYVAQQAWILNAtlRDNILFGKE-YD--EERYNSVLNSCClrpdlailpssDLTEIGE------RgaNLSGGQ 217
Cdd:cd03267 94 rrigvVFGQKTQLWWDLPV--IDSFYLLAAiYDlpPARFKKRLDELS-----------ELLDLEElldtpvR--QLSLGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 218 RQRISLARALYSDRSIYILDDPLSALDAHVGNhifnsAIRKHLKS------KTVLFVTHqlqYLVD----CDEVIFMKEG 287
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQE-----NIRNFLKEynrergTTVLLTSH---YMKDiealARRVLVIDKG 230
|
....*.
gi 1622900610 288 CITERG 293
Cdd:cd03267 231 RLLYDG 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
737-935 |
1.70e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 61.39 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMAL--FRLVELSGGCIKIDGVRISDIgLADLRSKLSII--PQEPVLFSGtv 812
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDL-PPEERARLGIFlaFQYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 813 rsnldpfnqytedqiwdalerthmkeciaqlpLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTET 892
Cdd:cd03217 92 --------------------------------VKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622900610 893 DLLIQETIRE-AFADCTMLTIAH--RLHTVLGSDRIMVLAQGQVVE 935
Cdd:cd03217 140 LRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
737-935 |
1.73e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.78 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSKLSIIPQEP---VLFSG 810
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSisaVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 811 TVRSNLD-PFNQYT----EDQIWDALERTHMKECIAQLPLKLESEVmengdnfSVGERQLLCIARALLRHCKILILDEAT 885
Cdd:PRK10419 107 TVREIIRePLRHLLsldkAERLARASEMLRAVDLDDSVLDKRPPQL-------SGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 886 AAMdtetDLLIQ-------ETIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 935
Cdd:PRK10419 180 SNL----DLVLQagvirllKKLQQQF-GTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
738-939 |
1.86e-10 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 62.10 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGladlrsklsiiPQEPVLFSG------- 810
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG-----------PDRMVVFQNysllpwl 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 811 TVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEvmENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDT 890
Cdd:TIGR01184 70 TVRENIALAVDRVLPDLSKSERRAIVEEHIALVGLTEAAD--KRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 891 ETDLLIQETIREAFAD--CTMLTIAHRL-HTVLGSDRIMVLAQ------GQVVEFDTP 939
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEhrVTVLMVTHDVdEALLLSDRVVMLTNgpaaniGQILEVPFP 205
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
108-299 |
1.91e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.50 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 108 SIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAIS------GTFAYVAQQ------------------AWIL 163
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfGDYSYRSQRirmifqdpstslnprqriSQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 164 NATLRDNILFGKEYDEERYNSVLNSCCLRPDLA-ILPSSdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSA 242
Cdd:PRK15112 111 DFPLRLNTDLEPEQREKQIIETLRQVGLLPDHAsYYPHM-----------LAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 243 LDAHVGNHIFNSAIrkHLKSK---TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 299
Cdd:PRK15112 180 LDMSMRSQLINLML--ELQEKqgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
741-959 |
1.97e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 63.70 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 741 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIglADLRSKLSIIPQEPVLFSG-TVRSNLD-- 817
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALFPHmTVEQNIAfg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 818 ------PFNQYTeDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMDTE 891
Cdd:PRK11607 116 lkqdklPKAEIA-SRVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 892 ----TDLLIQETIREAFADCTMLTiaH---RLHTVLGsdRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAEN 959
Cdd:PRK11607 184 lrdrMQLEVVDILERVGVTCVMVT--HdqeEAMTMAG--RIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVN 254
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
737-954 |
1.98e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.44 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKID-GVRISDIgladlRSKLSIIPQEPVLFSGTVRsn 815
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNgKLRIGYV-----PQKLYLDTTLPLTVNRFLR-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 816 LDPFNQytEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMDTETDL- 894
Cdd:PRK09544 92 LRPGTK--KEDILPALKRVQAGHLIDAPMQKL-----------SGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVa 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 895 ---LIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQgQVVEFDTPSVLLSNdsSRFYAMF 954
Cdd:PRK09544 159 lydLIDQLRRE--LDCAVLMVSHDLHLVMAkTDEVLCLNH-HICCSGTPEVVSLH--PEFISMF 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
688-937 |
1.99e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.32 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 688 VERINHYIKtLSLEAPARIKNKApspdwpqegeVTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSlgma 767
Cdd:COG0488 294 PPRRDKTVE-IRFPPPERLGKKV----------LELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKST---- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 768 LFRL----VELSGGCIKIdGVRIsdigladlrsKLSIIPQEpvlfsgtvRSNLDPfnqytEDQIWDALERTHmkeciaql 843
Cdd:COG0488 357 LLKLlageLEPDSGTVKL-GETV----------KIGYFDQH--------QEELDP-----DKTVLDELRDGA-------- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 844 PLKLESEVME-------NGD-------NFSVGERQLLCIARALLRHCKILILDEATAAMDTETdlliqetiREAFADC-- 907
Cdd:COG0488 405 PGGTEQEVRGylgrflfSGDdafkpvgVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET--------LEALEEAld 476
|
250 260 270
....*....|....*....|....*....|....*..
gi 1622900610 908 ----TMLTIAH-R--LHTVlgSDRIMVLAQGQVVEFD 937
Cdd:COG0488 477 dfpgTVLLVSHdRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
744-927 |
2.12e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 744 TIKPKEKIGIVGRTGSGKSSLGMALfrlvelsGGCIKIDGvrisdiGLADLRSKLSIIPQE-PVLFSGTVRSNLDpfnqy 822
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLL-------AGVLKPDE------GEVDPELKISYKPQYiKPDYDGTVEDLLR----- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 823 tedQIWDALERTHMKECIAQlPLKLEsEVME-NGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIR 901
Cdd:PRK13409 423 ---SITDDLGSSYYKSEIIK-PLQLE-RLLDkNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 497
|
170 180 190
....*....|....*....|....*....|
gi 1622900610 902 EaFA---DCTMLTIAHRLHTV-LGSDRIMV 927
Cdd:PRK13409 498 R-IAeerEATALVVDHDIYMIdYISDRLMV 526
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
721-934 |
2.22e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 61.53 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiglADLRSKLSI 800
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 801 IPQEPVLFSG-TVRSNLDPFNQ-------YTEDQIWDALERTHMKEciaqlplKLESEVMEngdnFSVGERQLLCIARAL 872
Cdd:cd03269 75 LPEERGLYPKmKVIDQLVYLAQlkglkkeEARRRIDEWLERLELSE-------YANKRVEE----LSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 873 LRHCKILILDEATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 934
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
435-648 |
2.25e-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: 62.85 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 435 DNPRMQYYASIYALSM----AVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTP--TGRILNRFSKDMD 508
Cdd:cd18578 43 DDDELRSEANFWALMFlvlaIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDAS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 509 EV----DVRLPfqaeMFIQNVILVFFCVGmIAGVFPWFL----VAVGPLVILFSVLHIvsRVLIR-ELKRLDNITQSpfl 579
Cdd:cd18578 123 DVrglvGDRLG----LILQAIVTLVAGLI-IAFVYGWKLalvgLATVPLLLLAGYLRM--RLLSGfEEKNKKAYEES--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 580 SHITS-SIQGLATIHAYNKGQEFLHRYQELLDDNQ-------------------APFFLFTCAMRWLAVrldLISIALIT 639
Cdd:cd18578 193 SKIASeAVSNIRTVASLTLEDYFLEKYEEALEEPLkkglrralisglgfglsqsLTFFAYALAFWYGGR---LVANGEYT 269
|
....*....
gi 1622900610 640 TTGLMIVLM 648
Cdd:cd18578 270 FEQFFIVFM 278
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
721-946 |
2.59e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.90 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGLADL-RSKLS 799
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP--SRARHaRQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 800 IIPQ----EPVLfsgTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMEngdnFSVGERQLLCIARALLRH 875
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 876 CKILILDEATAAMDTETDLLIQETIREAFADC-TMLTIAH------RLhtvlgSDRIMVLAQGQVVEFDTPSVLLSND 946
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
109-271 |
2.75e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.51 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 109 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISgtfayVAQQAWILNATLRDNILFGKEYDEERYnsVLNS 188
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLIDAIGRKGDFKDAVE--LLNA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 189 CCLrpdlailpsSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD---AHVGNHIFNSAIRKHlkSKTV 265
Cdd:COG2401 122 VGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQKLARRA--GITL 190
|
....*.
gi 1622900610 266 LFVTHQ 271
Cdd:COG2401 191 VVATHH 196
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
211-300 |
2.87e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 211 ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnsAIRKHLKSK---TVLFVTHQLQYLVD-CDEVIFMKE 286
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL--ALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQ 501
|
90
....*....|....
gi 1622900610 287 GCITERGTHEELMN 300
Cdd:PRK15134 502 GEVVEQGDCERVFA 515
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
737-935 |
2.91e-10 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 61.39 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGlADLRSKLSI--IPQEPVLFSG-TVR 813
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLP-PHERARAGIayVPQGREIFPRlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 814 SNLdpfnqytedQI-WDALERTHMK--ECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDT 890
Cdd:TIGR03410 94 ENL---------LTgLAALPRRSRKipDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622900610 891 ETDLLIQETIRE--AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 935
Cdd:TIGR03410 165 SIIKDIGRVIRRlrAEGGMAILLVEQYLDFARElADRYYVMERGRVVA 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
106-300 |
3.04e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.10 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-----------------TFAYVAQ--QAWILNAT 166
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 167 LRDNILFG--------KEYDEERYNSVLNSCCLRPDLAILPssdlteigergANLSGGQRQRISLARALYSDRSIYILDD 238
Cdd:PRK13646 103 VEREIIFGpknfkmnlDEVKNYAHRLLMDLGFSRDVMSQSP-----------FQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 239 PLSALDAHVGNHIFNSAIRKHLK-SKTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEELMN 300
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMnevaRY---ADEVIVMKEGSIVSQTSPKELFK 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
720-939 |
3.14e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 62.34 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 720 EVTFENAEMRYRENLP---LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIdGVRISDIG-----L 791
Cdd:PRK13634 2 DITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 792 ADLRSKLSIIPQ--EPVLFSGTVRSNL--DPFNQYTEDQiwDALERThmKECIAQlpLKLESEVMENGD-NFSVGERQLL 866
Cdd:PRK13634 81 KPLRKKVGIVFQfpEHQLFEETVEKDIcfGPMNFGVSEE--DAKQKA--REMIEL--VGLPEELLARSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 867 CIARALLRHCKILILDEATAAMDTETdlliQETIREAFA------DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 939
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFYklhkekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
744-927 |
3.27e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.04 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 744 TIKPKEKIGIVGRTGSGKSSLgmalfrlVELSGGCIKIDGvrisdiGLADLRSKLSIIPQEPV-LFSGTVRSNLdpfnqy 822
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTF-------AKILAGVLKPDE------GEVDEDLKISYKPQYISpDYDGTVEEFL------ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 823 tEDQIWDALERTHMKECIAQlPLKLEsEVME-NGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIR 901
Cdd:COG1245 423 -RSANTDDFGSSYYKTEIIK-PLGLE-KLLDkNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
170 180 190
....*....|....*....|....*....|
gi 1622900610 902 EaFA---DCTMLTIAHRLHTV-LGSDRIMV 927
Cdd:COG1245 500 R-FAenrGKTAMVVDHDIYLIdYISDRLMV 528
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
105-298 |
3.45e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.06 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 105 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTfAYVAQQAW----------------ILNATLR 168
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdirhkigmvfqnpdnqFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 169 DNILFGKE-----YDE--ERYNSVLNscclrpdlaILPSSDLTEigERGANLSGGQRQRISLARALYSDRSIYILDDPLS 241
Cdd:PRK13650 101 DDVAFGLEnkgipHEEmkERVNEALE---------LVGMQDFKE--REPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 242 ALDAHVGNHIFNS--AIRKHLKsKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEEL 298
Cdd:PRK13650 170 MLDPEGRLELIKTikGIRDDYQ-MTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
737-945 |
5.08e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 61.63 E-value: 5.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI--SDIGLADLRSKLSIIPQEP--VLFSGTV 812
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVGIVFQNPddQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 813 RSNL--DPFN-----QYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEAT 885
Cdd:PRK13639 97 EEDVafGPLNlglskEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 886 AAMD----TETDLLIQETIREAfadctmLTIAHRLHTV----LGSDRIMVLAQGQVVEFDTPSVLLSN 945
Cdd:PRK13639 166 SGLDpmgaSQIMKLLYDLNKEG------ITIIISTHDVdlvpVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
106-294 |
5.62e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.60 E-value: 5.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTfaYVAQQAWILNATLRDNILfGKEYDEER---- 181
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ--PMSKLSSAAKAELRNQKL-GFIYQFHHllpd 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 182 YNSVLNSCC------LRPDLAILPSSD-LTEIG------ERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 248
Cdd:PRK11629 102 FTALENVAMplligkKKPAEINSRALEmLAAVGlehranHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622900610 249 NHIFNSAIRKHLKSKTV-LFVTHQLQYLVDCDEVIFMKEGCITERGT 294
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAfLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
94-285 |
5.85e-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: 58.91 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 94 HIHLGHLRLQRTlhSIDLEIQEGKLVGICGSVGSGKTSLISAIlgqmtllegsiaisgtfayvaqqawILNATLRDNILF 173
Cdd:cd03227 1 KIVLGRFPSYFV--PNDVTFGEGSLTIITGPNGSGKSTILDAI-------------------------GLALGGAQSATR 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 174 GKEYDEERYNSvlnsCCLRPDLAILPSSdlteigerganLSGGQRQRISLARAL----YSDRSIYILDDPLSALDAHVGN 249
Cdd:cd03227 54 RRSGVKAGCIV----AAVSAELIFTRLQ-----------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQ 118
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622900610 250 HIFNsAIRKHLKSK-TVLFVTHQLQYLVDCDEVIFMK 285
Cdd:cd03227 119 ALAE-AILEHLVKGaQVIVITHLPELAELADKLIHIK 154
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
106-294 |
6.57e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 61.74 E-value: 6.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAIlgqmTLLE----GSIAISGT----------------FAYVAQQAWILNA 165
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCI----NLLErptsGRVLVDGQdltalsekelrkarrqIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 166 -TLRDNILF-------GKEYDEERYNSVLnscclrpdlailpssDLTEIGERG----ANLSGGQRQRISLARALYSDRSI 233
Cdd:PRK11153 97 rTVFDNVALplelagtPKAEIKARVTELL---------------ELVGLSDKAdrypAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 234 YILDDPLSALDAHVGNHIFN--SAIRKHLKSkTVLFVTHQLQyLVD--CDEVIFMKEGCITERGT 294
Cdd:PRK11153 162 LLCDEATSALDPATTRSILEllKDINRELGL-TIVLITHEMD-VVKriCDRVAVIDAGRLVEQGT 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
737-940 |
7.07e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.51 E-value: 7.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVE----LSGGCI--------------------------------K 780
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDqyepTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 781 IDGVRISDIGLADLRSKLSIIPQEPVLFSG--TVRSN----LDPFNQYTEDQIWDALERTHMkeciaqlpLKLESEVMEN 854
Cdd:TIGR03269 94 VDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNvleaLEEIGYEGKEAVGRAVDLIEM--------VQLSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 855 GDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAF--ADCTMLTIAHRLHTVLG-SDRIMVLAQG 931
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIEDlSDKAIWLENG 245
|
....*....
gi 1622900610 932 QVVEFDTPS 940
Cdd:TIGR03269 246 EIKEEGTPD 254
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
106-291 |
8.10e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.39 E-value: 8.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--FAYVAQQAWIL--NATLRDNILFGKEYDEER 181
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETvkIGYFDQHQEELdpDKTVLDELRDGAPGGTEQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 182 Y-NSVLNSCCLRPDLAilpssdLTEIGergaNLSGGQRQRISLARALYSDRSIYILDDPlsaldahvGNH-------IFN 253
Cdd:COG0488 411 EvRGYLGRFLFSGDDA------FKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEP--------TNHldietleALE 472
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622900610 254 SAIRKHlkSKTVLFVTHQlQYLVD--CDEVIFMKEGCITE 291
Cdd:COG0488 473 EALDDF--PGTVLLVSHD-RYFLDrvATRILEFEDGGVRE 509
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
109-298 |
8.52e-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: 61.22 E-value: 8.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 109 IDLEIQEGKLVGICGSVGSGKTSLISAILGqmtLLE------GSIAISGT-----------------FAYVAQQA----- 160
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILG---LLPppgitsGEILFDGEdllklsekelrkirgreIQMIFQDPmtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 161 ------WILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAIL---PSsdlteigergaNLSGGQRQRISLARALYSDR 231
Cdd:COG0444 101 pvmtvgDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLdryPH-----------ELSGGMRQRVMIARALALEP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 232 SIYILDDPLSALDAHVGNHIFN--SAIRKHLKSkTVLFVTHQL---QYLvdCDEVIFMKEGCITERGTHEEL 298
Cdd:COG0444 170 KLLIADEPTTALDVTIQAQILNllKDLQRELGL-AILFITHDLgvvAEI--ADRVAVMYAGRIVEEGPVEEL 238
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
425-611 |
8.91e-10 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 60.95 E-value: 8.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 425 NETSVSDSMKDnprMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFS 504
Cdd:cd18577 35 GESSPDEFLDD---VNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 505 KDMDEVdvrlpfQ---AE---MFIQNVILVF--FCVGMIAGvfpW----FLVAVGPLVILfsVLHIVSRVLIR-ELKRLD 571
Cdd:cd18577 112 SDTNLI------QdgiGEklgLLIQSLSTFIagFIIAFIYS---WkltlVLLATLPLIAI--VGGIMGKLLSKyTKKEQE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622900610 572 NITQSpfLSHITSSIQGLATIHAYNKGQEFLHRYQELLDD 611
Cdd:cd18577 181 AYAKA--GSIAEEALSSIRTVKAFGGEEKEIKRYSKALEK 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
94-300 |
8.98e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 60.56 E-value: 8.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 94 HIHLGHLRLqrtLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQA 160
Cdd:PRK13548 9 SVRLGGRTL---LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 161 WILNA-TLRDNILFG-------KEYDEERYNSVLNSCclrpDLAILPSSDLTEigerganLSGGQRQRISLARAL----- 227
Cdd:PRK13548 86 SLSFPfTVEEVVAMGraphglsRAEDDALVAAALAQV----DLAHLAGRDYPQ-------LSGGEQQRVQLARVLaqlwe 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 228 -YSDRSIYILDDPLSALD-AH---VGNHIFNSAIRKHLkskTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEEL 298
Cdd:PRK13548 155 pDGPPRWLLLDEPTSALDlAHqhhVLRLARQLAHERGL---AVIVVLHDLnlaaRY---ADRIVLLHQGRLVADGTPAEV 228
|
..
gi 1622900610 299 MN 300
Cdd:PRK13548 229 LT 230
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
737-934 |
9.24e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.48 E-value: 9.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGLADL-RSKL-SIIPQEPVL---FSGT 811
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT--KLPEYkRAKYiGRVFQDPMMgtaPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 812 VRSNLdpfnqytedqiwdAL-----------------ERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLR 874
Cdd:COG1101 99 IEENL-------------ALayrrgkrrglrrgltkkRRELFRELLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 875 HCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVL--GsDRIMVLAQGQVV 934
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLELTEKIVEEnnLTTLMVTHNMEQALdyG-NRLIMMHEGRII 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
106-296 |
9.67e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 60.03 E-value: 9.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAilgqMTLLEgsIAISGTFAyVAQQAWILNAT--------LRDNI--LFgk 175
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRV----LNLLE--MPRSGTLN-IAGNHFDFSKTpsdkaireLRRNVgmVF-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 176 eydeERYN-----SVLNSCCLRP--------------DLAILPSSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYI 235
Cdd:PRK11124 89 ----QQYNlwphlTVQQNLIEAPcrvlglskdqalarAEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 236 LDDPLSALDAHVGNHIFNsaIRKHLKSK--TVLFVTHQlqylVD-----CDEVIFMKEGCITERGTHE 296
Cdd:PRK11124 165 FDEPTAALDPEITAQIVS--IIRELAETgiTQVIVTHE----VEvarktASRVVYMENGHIVEQGDAS 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
721-914 |
1.15e-09 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 57.46 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrlvelsggcikidgvrisdigladlrskLSI 800
Cdd:cd03221 1 IELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 801 IPQEPVLFSGTVrsnldpfnqytedqiwdaleRTHMKECIAQLPlklesevmengdNFSVGERQLLCIARALLRHCKILI 880
Cdd:cd03221 46 IAGELEPDEGIV--------------------TWGSTVKIGYFE------------QLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....
gi 1622900610 881 LDEATAAMDTETDLLIQETIREaFaDCTMLTIAH 914
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKE-Y-PGTVILVSH 125
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
109-299 |
1.19e-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: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 109 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-FAYVAQQAW-------------------------- 161
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQdITGLSGRELrplrrrmqmvfqdpyaslnprmtvgd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 162 ILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAilpssdlteigERGAN-LSGGQRQRISLARALYSDRSIYILDDPL 240
Cdd:COG4608 117 IIAEPLRIHGLASKAERRERVAELLELVGLRPEHA-----------DRYPHeFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 241 SALDAHVGNHIFNsaIRKHLKSK---TVLFVTHQL---QYLvdCDEVIFMKEGCITERGTHEELM 299
Cdd:COG4608 186 SALDVSIQAQVLN--LLEDLQDElglTYLFISHDLsvvRHI--SDRVAVMYLGKIVEIAPRDELY 246
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
104-294 |
1.41e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.13 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILG-----QMTLLEGSIAISGTfayvAQQAWILNATLRDNILFGKEYD 178
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSST----SKQKEIKPVRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 179 EERYNSVLNSCCLRP--------DLAILPSSDLTEIG------ERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSAL 243
Cdd:PRK13643 96 QLFEETVLKDVAFGPqnfgipkeKAEKIAAEKLEMVGladefwEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 244 DAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGT 294
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
434-650 |
1.42e-09 |
|
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: 60.17 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 434 KDNPRMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvr 513
Cdd:cd18545 34 GDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSL--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 514 lpfqAEMF---IQNVILVFFCVGMIAGVFPWF-----LVAVGPLVILFSVLhIVSRVLIRELKRLDNITQSPFLSHITSS 585
Cdd:cd18545 111 ----SDLLsngLINLIPDLLTLVGIVIIMFSLnvrlaLVTLAVLPLLVLVV-FLLRRRARKAWQRVRKKISNLNAYLHES 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 586 IQGLATIHAYNKGQEFLHRYQELLDDNQAPFflftcaMRwlAVRL-DLI--SIALITTTGLMIVLMHG 650
Cdd:cd18545 186 ISGIRVIQSFAREDENEEIFDELNRENRKAN------MR--AVRLnALFwpLVELISALGTALVYWYG 245
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
109-293 |
1.47e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 60.59 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 109 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG----TFAYVAQQAWIL---------NATLRDNIL-FG 174
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpSRARHARQRVGVvpqfdnldpDFTVRENLLvFG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 175 keydeeRYNSVLNSCC--LRPDL---AILPSSDLTEIGErganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGN 249
Cdd:PRK13537 106 ------RYFGLSAAAAraLVPPLlefAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-AR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 250 HIFNSAIRKHLKS-KTVLFVTHqlqylvdcdeviFMKEG-------CITERG 293
Cdd:PRK13537 175 HLMWERLRSLLARgKTILLTTH------------FMEEAerlcdrlCVIEEG 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
103-300 |
1.54e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.52 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQAWILNA-TL 167
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararrgIGYLPQEASIFRRlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 168 RDNIL--------FGKEYDEERYNSVL---NSCCLRPDLailpssdlteigerGANLSGGQRQRISLARALYSDRSIYIL 236
Cdd:PRK10895 96 YDNLMavlqirddLSAEQREDRANELMeefHIEHLRDSM--------------GQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 237 DDPLSALDAHVGNHIfnSAIRKHLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 300
Cdd:PRK10895 162 DEPFAGVDPISVIDI--KRIIEHLRDSglGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
737-939 |
1.60e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 59.32 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvRIS---DIGLA---DL--RsklsiipqEPVLF 808
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSallELGAGfhpELtgR--------ENIYL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 809 SGTVrsnldpfNQYTEDQIwdaleRTHMKECIA--------QLPLKlesevmengdNFSVGERQLLCIARALLRHCKILI 880
Cdd:COG1134 112 NGRL-------LGLSRKEI-----DEKFDEIVEfaelgdfiDQPVK----------TYSSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 881 LDEATAAMDTE-----TDlLIQETIREAfadCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 939
Cdd:COG1134 170 VDEVLAVGDAAfqkkcLA-RIRELRESG---RTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDP 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
738-934 |
1.73e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.34 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLSIIPQE-PVLFSGTVRSN 815
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaAQLGIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 816 LdPFNQYTEDQIW--DALERTHMKECIAQLPLK--LESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAM-DT 890
Cdd:PRK09700 101 L-YIGRHLTKKVCgvNIIDWREMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtNK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622900610 891 ETD---LLIQETIREAFAdctMLTIAHRLHTVLG-SDRIMVLAQGQVV 934
Cdd:PRK09700 180 EVDylfLIMNQLRKEGTA---IVYISHKLAEIRRiCDRYTVMKDGSSV 224
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
108-271 |
1.86e-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: 61.69 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 108 SIDLEIQEGKLVGICGSVGSGKTSLISaILGQMTLLEG---SIAISGTFAYVAQQAWILNATLRDNILFGKEYDEERYNS 184
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRG 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 185 VLNScclrpDL-AILPSSDLTEIGERGAN----------LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN 253
Cdd:TIGR00954 549 LSDK-----DLeQILDNVQLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYR 623
|
170
....*....|....*...
gi 1622900610 254 SAIRKHLkskTVLFVTHQ 271
Cdd:TIGR00954 624 LCREFGI---TLFSVSHR 638
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
104-299 |
2.23e-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: 60.97 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGqmtLLEGSiaiSGTFAYVAQQAWIL----------NATLRDNILF 173
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAG---VLEPT---SGEVNVRVGDEWVDmtkpgpdgrgRAKRYIGILH 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 174 gKEYDEERYNSVLN------SCCLRPDLA------ILPSSDLTE-----IGERGAN-LSGGQRQRISLARALYSDRSIYI 235
Cdd:TIGR03269 372 -QEYDLYPHRTVLDnlteaiGLELPDELArmkaviTLKMVGFDEekaeeILDKYPDeLSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 236 LDDPLSALD----AHVGNHIFNSaiRKHLkSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 299
Cdd:TIGR03269 451 LDEPTGTMDpitkVDVTHSILKA--REEM-EQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
104-300 |
2.25e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 59.36 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILN---------------ATLR 168
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSkvglvfqdpddqvfsSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 169 DNILFGKEYDEERYNSVLNscclRPDLAiLPSSDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 247
Cdd:PRK13647 99 DDVAFGPVNMGLDKDEVER----RVEEA-LKAVRMWDFRDKPPyHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 248 GNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 300
Cdd:PRK13647 174 QETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
738-946 |
2.45e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 59.26 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRL----------VELSGGCIKIDGVRISDIGLA-----------DLRS 796
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagshIELLGRTVQREGRLARDIRKSrantgyifqqfNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 797 KLSIIpqEPVLFS--GTV---RSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARA 871
Cdd:PRK09984 100 RLSVL--ENVLIGalGSTpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTL-----------SGGQQQRVAIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 872 LLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVeFDTPSVLLSND 946
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRyCERIVALRQGHVF-YDGSSQQFDNE 243
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
455-609 |
2.56e-09 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 59.53 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 455 ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkDMDEVDVRLPFQAEMFIQNVILVFFCVGM 534
Cdd:cd18782 57 VLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTALTTLLDVLFSVIYIAV 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 535 IAgVFPWFL----VAVGPLVILFSVLhiVSRVLIRELKRLdNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELL 609
Cdd:cd18782 136 LF-SYSPLLtlvvLATVPLQLLLTFL--FGPILRRQIRRR-AEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRY 210
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
724-935 |
2.68e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.09 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 724 ENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG-----GCIKIDGVRI--SDIGLADLRS 796
Cdd:PRK14267 8 VNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIEVRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 797 KLSIIPQEPVLFSG-TVRSN----------LDPFNQYTEDQIWdALERthmkeciAQLPLKLESEVMENGDNFSVGERQL 865
Cdd:PRK14267 86 EVGMVFQYPNPFPHlTIYDNvaigvklnglVKSKKELDERVEW-ALKK-------AALWDEVKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 866 LCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHR-LHTVLGSDRIMVLAQGQVVE 935
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIE 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
738-934 |
2.77e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.61 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVELSG---GCIKIDGVRISDIGLADLRSK-LSIIPQEPVLFSG-TV 812
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTL-MKILSGVYPHGtwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 813 RSNLDPFNQYTE--DQIWDALERTHMKECIAQLPLKLESEVMENGDnFSVGERQLLCIARALLRHCKILILDEATAAM-D 889
Cdd:TIGR02633 96 AENIFLGNEITLpgGRMAYNAMYLRAKNLLRELQLDADNVTRPVGD-YGGGQQQLVEIAKALNKQARLLILDEPSSSLtE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622900610 890 TETDLLIqETIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 934
Cdd:TIGR02633 175 KETEILL-DIIRDLKAhGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
737-934 |
3.99e-09 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 58.11 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAdLRSKLSIIpqepvlfsgtvrsnl 816
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKK-FLRRIGVV--------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 817 dpFNQYTEdQIWD--ALERTHMKECIAQLP-------LKLESEVMENGD-------NFSVGERQLLCIARALLRHCKILI 880
Cdd:cd03267 100 --FGQKTQ-LWWDlpVIDSFYLLAAIYDLPparfkkrLDELSELLDLEElldtpvrQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 881 LDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 934
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
106-289 |
4.14e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 58.56 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVAQQA-WIL------------NATLRD 169
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvTKLPEYKRAkYIGrvfqdpmmgtapSMTIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 170 NILF----GKEY---------DEERYnsvlnscclRPDLAILpssDL-------TEIGergaNLSGGQRQRISLARALYS 229
Cdd:COG1101 102 NLALayrrGKRRglrrgltkkRRELF---------RELLATL---GLglenrldTKVG----LLSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 230 DRSIYILDDPLSALD---AHVGNHIFNSAIR-KHLkskTVLFVTHQLQYLVDC-DEVIFMKEGCI 289
Cdd:COG1101 166 KPKLLLLDEHTAALDpktAALVLELTEKIVEeNNL---TTLMVTHNMEQALDYgNRLIMMHEGRI 227
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
447-611 |
4.23e-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: 58.73 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 447 ALSMAVMLILKAIrgVVFVKGTL------RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 520
Cdd:cd18557 39 ALILLAIYLLQSV--FTFVRYYLfniageRIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 521 FIQNVILVFFCVGMIA----GVFPWFLVAVGPLVILFSVLHIVSRVLIREL-KRLDNITQspflsHITSSIQGLATIHAY 595
Cdd:cd18557 117 LLRNILQVIGGLIILFilswKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVqDALAKAGQ-----VAEESLSNIRTVRSF 191
|
170
....*....|....*.
gi 1622900610 596 NKGQEFLHRYQELLDD 611
Cdd:cd18557 192 SAEEKEIRRYSEALDR 207
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
447-691 |
7.96e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 57.90 E-value: 7.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 447 ALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVI 526
Cdd:cd18563 50 AGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNIL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 527 LVFFCVGMIAGVFPWF-LVAVG--PLVILFSVLH--IVSRVLIRELKRLDNITqspflSHITSSIQGLATIHAYnkGQE- 600
Cdd:cd18563 130 MIIGIGVVLFSLNWKLaLLVLIpvPLVVWGSYFFwkKIRRLFHRQWRRWSRLN-----SVLNDTLPGIRVVKAF--GQEk 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 601 -----FLHRYQELLDDNqapfflftcamrwlaVRLDLIS------IALITTTGLMIV-------LMHGQIPP----AYag 658
Cdd:cd18563 203 reikrFDEANQELLDAN---------------IRAEKLWatffplLTFLTSLGTLIVwyfggrqVLSGTMTLgtlvAF-- 265
|
250 260 270
....*....|....*....|....*....|...
gi 1622900610 659 laISYAVQLTGLFQFTVRLASETEARFTSVERI 691
Cdd:cd18563 266 --LSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
106-311 |
8.43e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 57.35 E-value: 8.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAiLGQMTLL------EGSIAISGTFAY---------------VAQQAWILN 164
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRC-LNRMNDLipgarvEGEILLDGEDIYdpdvdvvelrrrvgmVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 165 ATLRDNILFGkeydeerynsvlnsccLRpDLAILPSSDLTEIGER------------------GANLSGGQRQRISLARA 226
Cdd:COG1117 106 KSIYDNVAYG----------------LR-LHGIKSKSELDEIVEEslrkaalwdevkdrlkksALGLSGGQQQRLCIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 227 LYSDRSIYILDDPLSALD----AHVGNHIFNsairkhLKSK-TVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEElmn 300
Cdd:COG1117 169 LAVEPEVLLMDEPTSALDpistAKIEELILE------LKKDyTIVIVTHNMQQAARVsDYTAFFYLGELVEFGPTEQ--- 239
|
250
....*....|.
gi 1622900610 301 lngdyatIFNN 311
Cdd:COG1117 240 -------IFTN 243
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
214-327 |
8.47e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.44 E-value: 8.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 214 SGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN--SAIRKHLKSKTVlFVTHQLQyLVD--CDEVIFMKEGCI 289
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNlmMDLQQELGLSYV-FISHDLS-VVEhiADEVMVMYLGRC 233
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1622900610 290 TERGTHEelmnlngdyaTIFNN-------LLLGDTPPVEINSKKE 327
Cdd:PRK11308 234 VEKGTKE----------QIFNNprhpytqALLSATPRLNPDDRRE 268
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
721-947 |
9.54e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.87 E-value: 9.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIS----DIGLAD 793
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 794 LRSKLSIIPQ--EPVLFSGTVRSNL----DPFNQYTEDqiwdalerthMKECIAQLPLKL--ESEVMENGD-NFSVGERQ 864
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIifgpKNFKMNLDE----------VKNYAHRLLMDLgfSRDVMSQSPfQMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 865 LLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSV 941
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKE 232
|
....*.
gi 1622900610 942 LLSNDS 947
Cdd:PRK13646 233 LFKDKK 238
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
729-917 |
9.71e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.13 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 729 RYREN--LPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGV---RISDIGLADLRS-KLSIIP 802
Cdd:PRK11629 14 RYQEGsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsKLSSAAKAELRNqKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 803 QepvlfsgtvrsnldpFNQYTEDqiWDALERTHMKECIAQLPLK--------------LESEVMENGDNFSVGERQLLCI 868
Cdd:PRK11629 94 Q---------------FHHLLPD--FTALENVAMPLLIGKKKPAeinsralemlaavgLEHRANHRPSELSGGERQRVAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 869 ARALLRHCKILILDEATAAMDTET-----DLLIQETIRE--AFADCTM-LTIAHRLH 917
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNadsifQLLGELNRLQgtAFLVVTHdLQLAKRMS 213
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
441-650 |
9.98e-09 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 57.82 E-value: 9.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 441 YYASIYALSMAVMLILKAIRgvvfvkgtlrassrlhDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 520
Cdd:cd18552 56 SYLQTYLMAYVGQRVVRDLR----------------NDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 521 FIQNVILVFFCVG-MIagVFPWFL----VAVGPLVILfsvlhiVSRVLIRELKRLDNITQSpFLSHITS----SIQGLAT 591
Cdd:cd18552 120 LVRDPLTVIGLLGvLF--YLDWKLtliaLVVLPLAAL------PIRRIGKRLRKISRRSQE-SMGDLTSvlqeTLSGIRV 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 592 IHAYNKGQEFLHRYQELLDDNqapfflFTCAMRWLAVRlDLIS--IALITTTGLMIVLMHG 650
Cdd:cd18552 191 VKAFGAEDYEIKRFRKANERL------RRLSMKIARAR-ALSSplMELLGAIAIALVLWYG 244
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
445-613 |
1.03e-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: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 445 IYALSMAVMLILKA----IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkdmdevDVrlpfqaeM 520
Cdd:cd18570 43 IISIGLILLYLFQSllsyIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN------DA-------N 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 521 FIQNVI-----------LVFFCVGMIAGVFPW--FLVAVGPLVILFSVLHIVSRVLIRELKRLdNITQSPFLSHITSSIQ 587
Cdd:cd18570 110 KIREAIssttislfldlLMVIISGIILFFYNWklFLITLLIIPLYILIILLFNKPFKKKNREV-MESNAELNSYLIESLK 188
|
170 180
....*....|....*....|....*.
gi 1622900610 588 GLATIHAYNKGQEFLHRYQELLDDNQ 613
Cdd:cd18570 189 GIETIKSLNAEEQFLKKIEKKFSKLL 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
106-298 |
1.18e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 57.40 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAW----------------ILNATLRD 169
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdirnkagmvfqnpdnqIVATIVEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 170 NILFGKEydeerynsvlnscclrpDLAILPSsdltEIGERGAN-----------------LSGGQRQRISLARALYSDRS 232
Cdd:PRK13633 106 DVAFGPE-----------------NLGIPPE----EIRERVDEslkkvgmyeyrrhaphlLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 233 IYILDDPLSALDAHVGNHIFNSAirKHLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEEL 298
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTI--KELNKKygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
87-298 |
1.18e-08 |
|
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: 58.66 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 87 PEEEEGKHIHLGhlrlqrtlhSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGtfAYVAQQAWilnAT 166
Cdd:COG4615 338 PGEDGDEGFTLG---------PIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG--QPVTADNR---EA 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 167 LRDNI--------LFGKEY------DEERynsvlnsccLRPDLAILPSSDLTEIgERGA----NLSGGQRQRISLARALY 228
Cdd:COG4615 404 YRQLFsavfsdfhLFDRLLgldgeaDPAR---------ARELLERLELDHKVSV-EDGRfsttDLSQGQRKRLALLVALL 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 229 SDRSIYILD------DPlsaldahVGNHIFNSAIRKHLKS--KTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEEL 298
Cdd:COG4615 474 EDRPILVFDewaadqDP-------EFRRVFYTELLPELKArgKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAAL 544
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
740-944 |
1.26e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.89 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 740 KVSFTIKPKEKIGIVGRTGSGKSSLGMALFRlVELSGGCIKIDGVRISDIGLADL----RSKL-----SIIPQEPvlfsg 810
Cdd:PRK15093 25 RVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRMRFDDIDLLRLspreRRKLvghnvSMIFQEP----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 811 tvRSNLDPfNQYTEDQIWDAL----------ERTHMK-----ECIAQLPLKLESEVMENGD-NFSVGERQLLCIARALLR 874
Cdd:PRK15093 99 --QSCLDP-SERVGRQLMQNIpgwtykgrwwQRFGWRkrraiELLHRVGIKDHKDAMRSFPyELTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 875 HCKILILDEATAAMDTETdlliQETIREAFA------DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 944
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTT----QAQIFRLLTrlnqnnNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVT 248
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
446-650 |
1.38e-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: 57.11 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 446 YALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF 521
Cdd:cd18576 38 IALLLLGLFLLQAVfsffRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 522 IQNVILVFFCVGMIAGVFP---WFLVAVGPLVILFSVlhIVSRVlIREL--KRLDNITQSpfLSHITSSIQGLATIHAYN 596
Cdd:cd18576 118 LRQILTLIGGVVLLFFISWkltLLMLATVPVVVLVAV--LFGRR-IRKLskKVQDELAEA--NTIVEETLQGIRVVKAFT 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 597 KGQEFLHRYQELLDDnqapffLFTCAMRWLAVRLDLIS-IALITTTGLMIVLMHG 650
Cdd:cd18576 193 REDYEIERYRKALER------VVKLALKRARIRALFSSfIIFLLFGAIVAVLWYG 241
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
109-299 |
1.46e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.26 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 109 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQ----AWILNATLRDN 170
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgMAYITESrrdnGFFPNFSIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 171 ILFGK---------------EYDEERYNSVLnscclRPDLAILPSSDLTEIGErganLSGGQRQRISLARALYSDRSIYI 235
Cdd:PRK09700 362 MAISRslkdggykgamglfhEVDEQRTAENQ-----RELLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 236 LDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQL-QYLVDCDEVIFMKEGCITE------RGTHEELM 299
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELpEIITVCDRIAVFCEGRLTQiltnrdDMSEEEIM 503
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
451-556 |
1.46e-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: 57.06 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 451 AVMLILKAIRGVV-FVKGTL------RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQ 523
Cdd:cd18542 43 LLILGVALLRGVFrYLQGYLaekasqKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVR 122
|
90 100 110
....*....|....*....|....*....|....*.
gi 1622900610 524 NVILVFFCVGMIAGVFP---WFLVAVGPLVILFSVL 556
Cdd:cd18542 123 AVLLFIGALIIMFSINWkltLISLAIIPFIALFSYV 158
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
739-933 |
1.73e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.14 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 739 KKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLSIIP---QEPVLF------ 808
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYldapla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 809 --SGTVRSNLDPFNQYT--EDQIwdaLERTHmkeciAQLPLKLeSEVMENGDNFSVGERQLLCIARALLRHCKILILDEA 884
Cdd:PRK15439 360 wnVCALTHNRRGFWIKParENAV---LERYR-----RALNIKF-NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 885 TAAMDTETDLLIQETIREAFADCT-MLTIAHRLHTVLG-SDRIMVLAQGQV 933
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
737-951 |
1.97e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 56.19 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFR----LVELSGGCIKIDGVRISDIGLaDLRSKLSI--IPQEPVLFSG 810
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTT----FYmivgLVKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASIFRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 811 -TVRSNLDPFNQYTEdqiwdaLERTHMKECIAQLplkLE----SEVMEN-GDNFSVGERQLLCIARALLRHCKILILDEA 884
Cdd:COG1137 93 lTVEDNILAVLELRK------LSKKEREERLEEL---LEefgiTHLRKSkAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 885 TAAMD--TETDllIQETIREafadctmLT---IA-----HRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR-FY 951
Cdd:COG1137 164 FAGVDpiAVAD--IQKIIRH-------LKergIGvlitdHNVRETLGiCDRAYIISEGKVLAEGTPEEILNNPLVRkVY 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
727-948 |
2.11e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.52 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 727 EMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG-----VRISD--IGLAD------ 793
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlVRDKDgqLKVADknqlrl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 794 LRSKLSIIPQEPVLFSG-TVRSNLdpfnQYTEDQIWdALERTHMKECIAQLPLKL---ESEVMENGDNFSVGERQLLCIA 869
Cdd:PRK10619 90 LRTRLTMVFQHFNLWSHmTVLENV----MEAPIQVL-GLSKQEARERAVKYLAKVgidERAQGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 870 RALLRHCKILILDEATAAMDTEtdlLIQETIR--EAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 944
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPE---LVGEVLRimQQLAEegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
....
gi 1622900610 945 NDSS 948
Cdd:PRK10619 242 NPQS 245
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
106-298 |
2.25e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.21 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNA-------------------- 165
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiklrkevgmvfqqpnpfphl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 166 TLRDNILFGKEY----DEERYNSVLNSCCLRPDLailpssdLTEIGER----GANLSGGQRQRISLARALYSDRSIYILD 237
Cdd:PRK14246 106 SIYDNIAYPLKShgikEKREIKKIVEECLRKVGL-------WKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 238 DPLSALDAhVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 298
Cdd:PRK14246 179 EPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
721-937 |
2.28e-08 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 55.34 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADlrSKLSI 800
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 801 IPQEPVLFSG-TVRSNLD---PFNQYTEDQIwdaLERTHMkecIAQLpLKLESEVMENGDNFSVGERQLLCIARALLRHC 876
Cdd:cd03301 77 VFQNYALYPHmTVYDNIAfglKLRKVPKDEI---DERVRE---VAEL-LQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 877 KILILDEATAAMDTEtdlliqetIREAfadctMLTIAHRLHTVLG----------------SDRIMVLAQGQVVEFD 937
Cdd:cd03301 150 KVFLMDEPLSNLDAK--------LRVQ-----MRAELKRLQQRLGtttiyvthdqveamtmADRIAVMNDGQIQQIG 213
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
112-277 |
2.88e-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: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 112 EIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-TFAYVAQQAWILNATLRDNILFGKE---YDEERYNS-VL 186
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKADYEGTVRDLLSSITkdfYTHPYFKTeIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 187 NSCCLRPdlaiLPSSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKHL--KSKT 264
Cdd:cd03237 101 KPLQIEQ----ILDREVPE-------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA-SKVIRRFAenNEKT 168
|
170
....*....|....*.
gi 1622900610 265 VLFVTHQL---QYLVD 277
Cdd:cd03237 169 AFVVEHDIimiDYLAD 184
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
736-934 |
3.25e-08 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 55.35 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 736 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE---LSGGCIKIDGVRISDiglADLRSKLSIIPQEPVLFSG-T 811
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKP---DQFQKCVAYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 812 VRSNLdpfnQYTedqiwdALERTHmkECIAQLPLKLESEVMENGD------------NFSVGERQLLCIARALLRHCKIL 879
Cdd:cd03234 98 VRETL----TYT------AILRLP--RKSSDAIRKKRVEDVLLRDlaltriggnlvkGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 880 ILDEATAAMDTETDLLIQETIREafadctmltIAHRLHTVLGS------------DRIMVLAQGQVV 934
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQ---------LARRNRIVILTihqprsdlfrlfDRILLLSSGEIV 223
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
104-268 |
3.75e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.27 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNA---------------TLR 168
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREavaivpegrrvfsrmTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 169 DNILFG-----KEYDEERYNSVLNsccLRPDLailpssdLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 243
Cdd:PRK11614 99 ENLAMGgffaeRDQFQERIKWVYE---LFPRL-------HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180
....*....|....*....|....*
gi 1622900610 244 DAHVGNHIFNSAIRKHLKSKTVLFV 268
Cdd:PRK11614 169 APIIIQQIFDTIEQLREQGMTIFLV 193
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
106-342 |
3.84e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.40 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAI----------SGTFAYVAQQAWILNA---------- 165
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELITNPYSKKIKNFkelrrrvsmv 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 166 -----------TLRDNILFG-------KEYDEERYNSVLNSCCLRPDLAilpssdlteigERGA-NLSGGQRQRISLARA 226
Cdd:PRK13631 122 fqfpeyqlfkdTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSYL-----------ERSPfGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 227 LYSDRSIYILDDPLSALDAHvGNHIFNSAIRKHLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTheelmnlngD 304
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAKANnKTVFVITHTMEHVLEvADEVIVMDKGKILKTGT---------P 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1622900610 305 YATIFNNLLLGDT----PPV--EINSKKETSGSQKKSQDKGPKT 342
Cdd:PRK13631 261 YEIFTDQHIINSTsiqvPRViqVINDLIKKDPKYKKLYQKQPRT 304
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
104-287 |
4.00e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.14 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILG--QMTLLEGSIAISGT--------------FAYVAQQ-AWILNAT 166
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSplkasnirdteragIVIIHQElTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 167 LRDNILFGKEYDEE----RYNSVLNSC-CLRPDLAILPSSDLTEIGERGanlsGGQRQRISLARALYSDRSIYILDDPLS 241
Cdd:TIGR02633 95 VAENIFLGNEITLPggrmAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622900610 242 ALDAHVGNHIFNsaIRKHLKSKTV--LFVTHQLQYL-VDCDEVIFMKEG 287
Cdd:TIGR02633 171 SLTEKETEILLD--IIRDLKAHGVacVYISHKLNEVkAVCDTICVIRDG 217
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
103-284 |
4.18e-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: 53.87 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQmtllEGSIAISGTFAYVAQQAWILNATLRDNILFGKEYdeery 182
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFLPKFSRNKLIFIDQLQFLIDVGLGY----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 183 nsvlnscclrpdlailpssdLTeIGERGANLSGGQRQRISLARALYSD--RSIYILDDPLSALDAHVGNHIFNSAIRKHL 260
Cdd:cd03238 79 --------------------LT-LGQKLSTLSGGELQRVKLASELFSEppGTLFILDEPSTGLHQQDINQLLEVIKGLID 137
|
170 180
....*....|....*....|....
gi 1622900610 261 KSKTVLFVTHQLQYLVDCDEVIFM 284
Cdd:cd03238 138 LGNTVILIEHNLDVLSSADWIIDF 161
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
104-298 |
4.20e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQAWIL-NATLR 168
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLFpNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 169 DNILFG---KEYDEERYNSVLN--SCCLRPDLAilpssdlteigerGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 243
Cdd:PRK15439 105 ENILFGlpkRQASMQKMKQLLAalGCQLDLDSS-------------AGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 244 DAHVGNHIFnSAIRKhLKSKTV--LFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 298
Cdd:PRK15439 172 TPAETERLF-SRIRE-LLAQGVgiVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
721-940 |
4.61e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.51 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLPLV---LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG----LAD 793
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 794 LRSKLSIIPQEP--VLFSGTVRSNL----DPFNQYTEDQIWDALERTHM----KECIAQLPLKLesevmengdnfSVGER 863
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVafgpQNFGIPKEKAEKIAAEKLEMvglaDEFWEKSPFEL-----------SGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 864 QLLCIARALLRHCKILILDEATAAMDTETDLLIQ---ETIREAFAdcTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 939
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMqlfESIHQSGQ--TVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
.
gi 1622900610 940 S 940
Cdd:PRK13643 229 S 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
737-945 |
4.71e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.14 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI-SDIGLADLRSKLSIIPQEpvlfSGTVRSN 815
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLIRQLRQH----VGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 816 LDPFNQYTedqiwdALE---------RTHMKECIAQLPLKLESEVMENGDN------FSVGERQLLCIARALLRHCKILI 880
Cdd:PRK11264 94 FNLFPHRT------VLEniiegpvivKGEPKEEATARARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 881 LDEATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 945
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
83-277 |
4.89e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 83 ERPSPEEEEGKHIHLGHLRLQRTLHSIDL-----EIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVA 157
Cdd:PRK13409 327 EERPPRDESERETLVEYPDLTKKLGDFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 158 Q----------QAWILNATlrdnilfgKEYDEERYNSVLnsccLRP-DLAILPSSDLTEigerganLSGGQRQRISLARA 226
Cdd:PRK13409 407 QyikpdydgtvEDLLRSIT--------DDLGSSYYKSEI----IKPlQLERLLDKNVKD-------LSGGELQRVAIAAC 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 227 LYSDRSIYILDDPLSALDAH----VGnhifnSAIRKHL--KSKTVLFVTHQLqYLVD 277
Cdd:PRK13409 468 LSRDADLYLLDEPSAHLDVEqrlaVA-----KAIRRIAeeREATALVVDHDI-YMID 518
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
106-298 |
4.99e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.57 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYV--AQQAWI------LN----ATLRDN 170
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvRFRSPrdAQAAGIaiihqeLNlvpnLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 171 ILFGKEY------D----EERYNSVLNscclRPDLAILPSsdlTEIGErganLSGGQRQRISLARALYSDRSIYILDDPL 240
Cdd:COG1129 100 IFLGREPrrggliDwramRRRARELLA----RLGLDIDPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 241 SALDAHVGNHIFNsAIRKhLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 298
Cdd:COG1129 169 ASLTEREVERLFR-IIRR-LKAQgvAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
104-300 |
5.70e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.18 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTL-HSIDLEIQEGKLVGICGSVGSGKTSLI------------SAILGQMTLLE-GSIAISGTFAYVAQQawiLNA---- 165
Cdd:PRK10575 24 RTLlHPLSLTFPAGKVTGLIGHNGSGKSTLLkmlgrhqppsegEILLDAQPLESwSSKAFARKVAYLPQQ---LPAaegm 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 166 TLRDNILFGK-----------EYDEERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDRSIY 234
Cdd:PRK10575 101 TVRELVAIGRypwhgalgrfgAADREKVEEAISLVGLKPLAHRLVDS-----------LSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 235 ILDDPLSALD-AHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 300
Cdd:PRK10575 170 LLDEPTSALDiAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
385-650 |
5.76e-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: 350019 [Multi-domain] Cd Length: 289 Bit Score: 55.18 E-value: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 385 LAFLVIMALFMLNVGSTafstwwLSYWIKQGSGNttvtrGNETSVSdsmkdnprmQYYASIYALSmAVMLILKAIRgVVF 464
Cdd:cd18575 2 LIALLIAAAATLALGQG------LRLLIDQGFAA-----GNTALLN---------RAFLLLLAVA-LVLALASALR-FYL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 465 VkGTL--RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAgVFPWF 542
Cdd:cd18575 60 V-SWLgeRVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLF-ITSPK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 543 LVAVGPLVILFSVLHIVsrVLIRELKRLDNITQSPFL---SHITSSIQGLATIHAYNKGQEFLHRYQELLDDNqapfflF 619
Cdd:cd18575 138 LTLLVLLVIPLVVLPII--LFGRRVRRLSRASQDRLAdlsAFAEETLSAIKTVQAFTREDAERQRFATAVEAA------F 209
|
250 260 270
....*....|....*....|....*....|..
gi 1622900610 620 TCAMRWLAVRLDLISIA-LITTTGLMIVLMHG 650
Cdd:cd18575 210 AAALRRIRARALLTALViFLVFGAIVFVLWLG 241
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
737-940 |
6.95e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.27 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG---LADLRSK-LSIIPQEPVLFSG-T 811
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadaLAQLRREhFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 812 VRSNLD-PfnqytedQIWDALERTHMKECIAQL--PLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAM 888
Cdd:PRK10535 103 AAQNVEvP-------AVYAGLERKQRLLRAQELlqRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 889 DT---ETDLLIQETIREafADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEfDTPS 940
Cdd:PRK10535 176 DShsgEEVMAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEIVR-NPPA 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
738-938 |
7.32e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 7.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrLVELSG------GCIKIDG--VRISDIGLAdLRSKLSIIPQE----P 805
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTL------LKILSGnyqpdaGSILIDGqeMRFASTTAA-LAAGVAIIYQElhlvP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 806 VLfsgTVRSNLdpfnqytedqiwdalerthmkeCIAQLPLK--------LESEVMEN----GDNF---------SVGERQ 864
Cdd:PRK11288 93 EM---TVAENL----------------------YLGQLPHKggivnrrlLNYEAREQlehlGVDIdpdtplkylSIGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 865 LLCIARALLRHCKILILDEATAAMDT-ETDLLIQeTIREAFADCT-MLTIAHRLHTVLG-SDRIMVLAQGQVVE-FDT 938
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSArEIEQLFR-VIRELRAEGRvILYVSHRMEEIFAlCDAITVFKDGRYVAtFDD 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
714-946 |
8.44e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.41 E-value: 8.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 714 DWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD 793
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 794 LRSKLSIIPQE-PVLFSGTVRSnLDPFNQYTedqiWD-------ALERTHMKECIAQLPLK-LESEVMengDNFSVGERQ 864
Cdd:PRK10575 83 FARKVAYLPQQlPAAEGMTVRE-LVAIGRYP----WHgalgrfgAADREKVEEAISLVGLKpLAHRLV---DSLSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 865 LLCIARALLRHCKILILDEATAAMD----TETDLLIQETIREafadcTMLTIAHRLHTVLGS----DRIMVLAQGQVVEF 936
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLALVHRLSQE-----RGLTVIAVLHDINMAarycDYLVALRGGEMIAQ 229
|
250
....*....|
gi 1622900610 937 DTPSVLLSND 946
Cdd:PRK10575 230 GTPAELMRGE 239
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
441-652 |
8.88e-08 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 54.72 E-value: 8.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 441 YYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 520
Cdd:cd18541 41 RYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 521 FIQNVILVFFCVGMIAGVFPWF-LVAVGPLVILFsvlhIVSRVLIRELKRLDNITQSPFlSHITSSIQ----GLATIHAY 595
Cdd:cd18541 121 LVDALFLGVLVLVMMFTISPKLtLIALLPLPLLA----LLVYRLGKKIHKRFRKVQEAF-SDLSDRVQesfsGIRVIKAF 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 596 NKGQEFLHRYQELLDDNQApfflftcamRWLA-VRLD---LISIALITTTGLMIVL-------MHGQI 652
Cdd:cd18541 196 VQEEAEIERFDKLNEEYVE---------KNLRlARVDalfFPLIGLLIGLSFLIVLwyggrlvIRGTI 254
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
737-939 |
8.89e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 55.24 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKpKEKI-GIVGRTGSGKSSLgmalfrlVELSGGCIKidgVRISDIGLADLRSKLSIIPQEPVLFSGT---- 811
Cdd:PRK13631 41 ALNNISYTFE-KNKIyFIIGNSGSGKSTL-------VTHFNGLIK---SKYGTIQVGDIYIGDKKNNHELITNPYSkkik 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 812 ----VRSNLDPFNQYTEDQIW-DALERTHMKECIAQLPLKLES--------EVMENGDNF--------SVGERQLLCIAR 870
Cdd:PRK13631 110 nfkeLRRRVSMVFQFPEYQLFkDTIEKDIMFGPVALGVKKSEAkklakfylNKMGLDDSYlerspfglSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 871 ALLRHCKILILDEATAAMDTETDLLIQETIREAFADC-TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 939
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNkTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP 260
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
103-244 |
1.37e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 54.84 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-FAYVAQ---------QAWIL--NATLRDN 170
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdLSHVPPyqrpinmmfQSYALfpHMTVEQN 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 171 ILFGKEYDEERYNSVLNSCClrpdlAILPSSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALD 244
Cdd:PRK11607 112 IAFGLKQDKLPKAEIASRVN-----EMLGLVHMQEFAKRKPHqLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
720-954 |
1.54e-07 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 53.50 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 720 EVTFENAEMRYrENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADlrSKLS 799
Cdd:cd03296 2 SIEVRNVSKRF-GDFV-ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 800 IIPQEPVLFSG-TVRSNL-----------DPFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLC 867
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVafglrvkprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 868 IARALLRHCKILILDEATAAMDTETDLLIQETIREAFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 944
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYD 226
|
250
....*....|
gi 1622900610 945 NDSSRFYAMF 954
Cdd:cd03296 227 HPASPFVYSF 236
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
428-611 |
1.55e-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: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 428 SVSDSMKDNPRMQYYASIYALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRF 503
Cdd:cd18573 25 VASKESGDIEIFGLSLKTFALALLGVFVVGAAanfgRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 504 SKDMDEVdvrlpfqAEMFIQNV-------ILVFFCVGMIAGVFP---WFLVAVGPLVILFSVlhivsrVLIRELKRLDNI 573
Cdd:cd18573 105 SSDTSVV-------GKSLTQNLsdglrslVSGVGGIGMMLYISPkltLVMLLVVPPIAVGAV------FYGRYVRKLSKQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622900610 574 TQSPfLSHITSS----IQGLATIHAYNKGQEFLHRYQELLDD 611
Cdd:cd18573 172 VQDA-LADATKVaeerLSNIRTVRAFAAERKEVERYAKKVDE 212
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
666-915 |
1.62e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 55.14 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 666 QLTGlfqFTVRLASetearFTSV-ERIN--HYIKTLSLEAPARIKNKAPSPDWPQEGEVTFENAEMRYrENLPLV----- 737
Cdd:TIGR00954 395 RLAG---FTARVDT-----LLQVlDDVKsgNFKRPRVEEIESGREGGRNSNLVPGRGIVEYQDNGIKF-ENIPLVtpngd 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 --LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLVelsGGCIKIDGVRISdiglADLRSKLSIIPQEPVLFSGTVRsn 815
Cdd:TIGR00954 466 vlIESLSFEVPSGNNLLICGPNGCGKSSL----FRIL---GELWPVYGGRLT----KPAKGKLFYVPQRPYMTLGTLR-- 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 816 ldpfnqyteDQIW--DALERTHMK-------ECIAQLpLKLESEVMENG---------DNFSVGERQLLCIARALLRHCK 877
Cdd:TIGR00954 533 ---------DQIIypDSSEDMKRRglsdkdlEQILDN-VQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQ 602
|
250 260 270
....*....|....*....|....*....|....*...
gi 1622900610 878 ILILDEATAAMDTETDLLIQETIREafADCTMLTIAHR 915
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
106-300 |
1.87e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 53.11 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQAWIL-NATLRDN 170
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIFrKLTVEDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 171 IL-------FGKEYDEERYNSVLNscclrpDLailpssDLTEIGE-RGANLSGGQRQRISLARALYSDRSIYILD----- 237
Cdd:COG1137 99 ILavlelrkLSKKEREERLEELLE------EF------GITHLRKsKAYSLSGGERRRVEIARALATNPKFILLDepfag 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 238 -DPLSALDahvgnhifnsaIRK---HLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 300
Cdd:COG1137 167 vDPIAVAD-----------IQKiirHLKERgiGVLITDHNVRETLGiCDRAYIISEGKVLAEGTPEEILN 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
719-960 |
1.94e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.86 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 719 GEVTFENAEMRYRENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSL------------GMALFRLVELSGGCIKIDG 783
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMiqltngliisetGQTIVGDYAIPANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 784 VRisdiglaDLRSKLSIIPQEP--VLFSGTVRSNL--DPFNQYTEDQiwDALERTHMKECIAQLPlklESEVMENGDNFS 859
Cdd:PRK13645 85 VK-------RLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENKQ--EAYKKVPELLKLVQLP---EDYVKRSPFELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 860 VGERQLLCIARALLRHCKILILDEATAAMDT--ETDL--LIQETIREAFADCTMLTiaHRLHTVLG-SDRIMVLAQGQVV 934
Cdd:PRK13645 153 GGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgEEDFinLFERLNKEYKKRIIMVT--HNMDQVLRiADEVIVMHEGKVI 230
|
250 260 270
....*....|....*....|....*....|....*
gi 1622900610 935 EFDTPSVLLSN---------DSSRFYAMFAAAENK 960
Cdd:PRK13645 231 SIGSPFEIFSNqelltkieiDPPKLYQLMYKLKNK 265
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
98-287 |
2.75e-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: 51.86 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 98 GHLRLqrtLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMT--LLEGSIAISG-----TFA----YVAQQ-AWILNA 165
Cdd:cd03232 18 GKRQL---LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGrpldkNFQrstgYVEQQdVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 166 TLRDNILFgkeydeerynsvlnSCCLRpdlailpssdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDA 245
Cdd:cd03232 95 TVREALRF--------------SALLR-------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622900610 246 HVGNHIFNsAIRKHLKS-KTVLFVTHQ-----LQYLvdcDEVIFMKEG 287
Cdd:cd03232 142 QAAYNIVR-FLKKLADSgQAILCTIHQpsasiFEKF---DRLLLLKRG 185
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
735-935 |
3.09e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.78 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 735 PLVlKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRL----VELSGGCIKIDGVRISdigLADLRSKL-SIIPQEPvlfs 809
Cdd:PRK10418 17 PLV-HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVA---PCALRGRKiATIMQNP---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 810 gtvRSNLDPFNQYtedqiwdaleRTHMKECI---------AQLPLKLESEVMENGD--------NFSVGERQLLCIARAL 872
Cdd:PRK10418 89 ---RSAFNPLHTM----------HTHARETClalgkpaddATLTAALEAVGLENAArvlklypfEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 873 LRHCKILILDEATaamdTETDLLIQETIREAFADCT------MLTIAHRLHTVLG-SDRIMVLAQGQVVE 935
Cdd:PRK10418 156 LCEAPFIIADEPT----TDLDVVAQARILDLLESIVqkralgMLLVTHDMGVVARlADDVAVMSHGRIVE 221
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
738-953 |
3.65e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.24 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGcIKIDGVRISDIGLADL---RSKLSiiPQEPVLFsgtvrs 814
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGS-IQFAGQPLEAWSAAELarhRAYLS--QQQTPPF------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 815 NLDPFnQY---------TEDQIWDALERthmkecIAQLpLKLESEVMENGDNFSVGERQ-------LLCIARALLRHCKI 878
Cdd:PRK03695 83 AMPVF-QYltlhqpdktRTEAVASALNE------VAEA-LGLDDKLGRSVNQLSGGEWQrvrlaavVLQVWPDINPAGQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 879 LILDEATAAMD----TETDLLIQETIREAFAdctMLTIAHRL-HTVLGSDRIMVLAQGQVVEFDTP-SVLLSNDSSRFYA 952
Cdd:PRK03695 155 LLLDEPMNSLDvaqqAALDRLLSELCQQGIA---VVMSSHDLnHTLRHADRVWLLKQGKLLASGRRdEVLTPENLAQVFG 231
|
.
gi 1622900610 953 M 953
Cdd:PRK03695 232 V 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
93-291 |
3.89e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.09 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 93 KHIHLGHLRLQrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGqmtLLEGSiaiSGTFAYVAQQAWILN----ATLR 168
Cdd:PRK10584 14 KSVGQGEHELS-ILTGVELVVKRGETIALIGESGSGKSTLLAILAG---LDDGS---SGEVSLVGQPLHQMDeearAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 169 -DNILFgkeydeerynsVLNSCCLRPDLAILPSSDLTEI----------------------GER----GANLSGGQRQRI 221
Cdd:PRK10584 87 aKHVGF-----------VFQSFMLIPTLNALENVELPALlrgessrqsrngakalleqlglGKRldhlPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 222 SLARALYSDRSIYILDDPLSALDAHVGNHIFN---SAIRKHlkSKTVLFVTHQLQYLVDCDEVIFMKEGCITE 291
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADllfSLNREH--GTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
213-298 |
4.05e-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: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 213 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnsAIRKHLKSKT---VLFVTHQLQyLVD--CDEVIFMKEG 287
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQIL--DLLKDLQRELgmaLLLITHDLG-VVRrfADRVAVMRQG 233
|
90
....*....|.
gi 1622900610 288 CITERGTHEEL 298
Cdd:COG4172 234 EIVEQGPTAEL 244
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
106-282 |
4.16e-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: 52.23 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQ--MTLLEGSIAISGTFAYVAQQAWI----------LNATLRDN--- 170
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPalARRLHLKKEQPGNHDRIEGLEHIdkvividqspIGRTPRSNpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 171 ---------ILF-----GKEYDEE----RYNS-----VLNSCC------------LRPDLAILPSSDLTEI--GERGANL 213
Cdd:cd03271 91 ytgvfdeirELFcevckGKRYNREtlevRYKGksiadVLDMTVeealeffenipkIARKLQTLCDVGLGYIklGQPATTL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 214 SGGQRQRISLARALY---SDRSIYILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVI 282
Cdd:cd03271 171 SGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWII 242
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
741-934 |
4.52e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 741 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLSIIP----QEPVLFSGTVRSN 815
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaIRAGIMLCPedrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 816 LD--------PFNQYTeDQIWdalERTHMKECIAQLPLK---LESEVMengdNFSVGERQLLCIARALLRHCKILILDEA 884
Cdd:PRK11288 352 INisarrhhlRAGCLI-NNRW---EAENADRFIRSLNIKtpsREQLIM----NLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 885 TAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 934
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIA 475
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
106-298 |
4.63e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.15 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAI-----LGQMTLLEGSIAISGTFAY--------VAQQAWIL--------N 164
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYspdvdpieVRREVGMVfqypnpfpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 165 ATLRDNILFG----------KEYDEerynsvlnscclRPDLAILPSSDLTEIGER----GANLSGGQRQRISLARALYSD 230
Cdd:PRK14267 100 LTIYDNVAIGvklnglvkskKELDE------------RVEWALKKAALWDEVKDRlndyPSNLSGGQRQRLVIARALAMK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 231 RSIYILDDPLSALDAhVGNHIFNSAIRKHLKSKTVLFVTHQ-LQYLVDCDEVIFMKEGCITERGTHEEL 298
Cdd:PRK14267 168 PKILLMDEPTANIDP-VGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
736-945 |
4.89e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 52.30 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 736 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGLadlrsklsiiPQEPVLFSGTVRS- 814
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE--GL----------PGHQIARMGVVRTf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 815 -NLDPFNQYTedqiwdALE------RTHMKECIAQLPLKL------ESEVMENG-----------------DNFSVGERQ 864
Cdd:PRK11300 87 qHVRLFREMT------VIEnllvaqHQQLKTGLFSGLLKTpafrraESEALDRAatwlervgllehanrqaGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 865 LLCIARALLRHCKILILDEATAAMD-TETDLLiQETI---REAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 939
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNpKETKEL-DELIaelRNEH-NVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTP 238
|
....*.
gi 1622900610 940 SVLLSN 945
Cdd:PRK11300 239 EEIRNN 244
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
444-611 |
5.10e-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: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 444 SIYALSMAVMLILKA----IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkdmDEVDVRlpfqaE 519
Cdd:cd18555 42 NVLGIGILILFLLYGlfsfLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRAN---SNVYIR-----Q 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 520 MFIQNVI--------LVFFCVGMIagVFPWFLVAVgplVILFSVLHIVSRVL----IRELKRLDNITQSPFLSHITSSIQ 587
Cdd:cd18555 114 ILSNQVIsliidlllLVIYLIYML--YYSPLLTLI---VLLLGLLIVLLLLLtrkkIKKLNQEEIVAQTKVQSYLTETLY 188
|
170 180
....*....|....*....|....
gi 1622900610 588 GLATIHAYNKGQEFLHRYQELLDD 611
Cdd:cd18555 189 GIETIKSLGSEKNIYKKWENLFKK 212
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
104-287 |
5.45e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.25 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQAWILNA-TLR 168
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqlgIGIIYQELSVIDElTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 169 DNILFGK------------EYDEERynSVLNSCCLRPDLAIlpssdltEIGERGANLSGGQRQRISLARALYSDRSIYIL 236
Cdd:PRK09700 99 ENLYIGRhltkkvcgvniiDWREMR--VRAAMMLLRVGLKV-------DLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 237 DDPLSALDAHVGNHIFnsAIRKHLKS--KTVLFVTHQLQYLVD-CDEVIFMKEG 287
Cdd:PRK09700 170 DEPTSSLTNKEVDYLF--LIMNQLRKegTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
104-298 |
6.45e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.40 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSID---LEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-FAYVAQQAWI----------------L 163
Cdd:PRK15079 32 KTLKAVDgvtLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdLLGMKDDEWRavrsdiqmifqdplasL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 164 NA--TLRDNIL---------FGKEYDEERYNSVLNSCCLRPDLailpssdlteIGERGANLSGGQRQRISLARALYSDRS 232
Cdd:PRK15079 112 NPrmTIGEIIAeplrtyhpkLSRQEVKDRVKAMMLKVGLLPNL----------INRYPHEFSGGQCQRIGIARALILEPK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 233 IYILDDPLSALDAHVGNHIFNsaIRKHLKSK---TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 298
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVVN--LLQQLQREmglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
112-277 |
6.81e-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: 53.25 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 112 EIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQqaWILN-------ATLRDNIlfGKEYDEERYNS 184
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQ--YISPdydgtveEFLRSAN--TDDFGSSYYKT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 185 VLnsccLRPdLAI--LPSSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDA----HVGnhifnSAIRK 258
Cdd:COG1245 438 EI----IKP-LGLekLLDKNVKD-------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVA-----KAIRR 500
|
170 180
....*....|....*....|.
gi 1622900610 259 HLKS--KTVLFVTHQLqYLVD 277
Cdd:COG1245 501 FAENrgKTAMVVDHDI-YLID 520
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
451-691 |
7.04e-07 |
|
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: 52.10 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 451 AVMLILKAIRGVVFV-------KGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdVRLPFQAEMFIQ 523
Cdd:cd18543 43 LLLLALGVAEAVLSFlrrylagRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLV-QRFLAFGPFLLG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 524 NVILVFFCVGMIAGVFPWF-LVAVGPLVILFsvlhIVSRVLIRELKRLDNITQS---PFLSHITSSIQGLATIHAYNKGQ 599
Cdd:cd18543 122 NLLTLVVGLVVMLVLSPPLaLVALASLPPLV----LVARRFRRRYFPASRRAQDqagDLATVVEESVTGIRVVKAFGRER 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 600 EFLHRYQELLDDnqapffLFTCAMRwlAVRLDLISIALITT---TGLMIVL-------MHGQIPpayAG--LA-ISYAVQ 666
Cdd:cd18543 198 RELDRFEAAARR------LRATRLR--AARLRARFWPLLEAlpeLGLAAVLalggwlvANGSLT---LGtlVAfSAYLTM 266
|
250 260
....*....|....*....|....*
gi 1622900610 667 LTGLFQFTVRLASETEARFTSVERI 691
Cdd:cd18543 267 LVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
103-282 |
9.14e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 51.27 E-value: 9.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTF--AYVAQQAWiLNATLRDNIlfgkeydeE 180
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLriGYVPQKLY-LDTTLPLTV--------N 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 181 RYNSvlnsccLRPDLA---ILPSSDLTE----IGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD--AHVGNHI 251
Cdd:PRK09544 88 RFLR------LRPGTKkedILPALKRVQaghlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDvnGQVALYD 161
|
170 180 190
....*....|....*....|....*....|..
gi 1622900610 252 FNSAIRKHLKSkTVLFVTHQLQY-LVDCDEVI 282
Cdd:PRK09544 162 LIDQLRRELDC-AVLMVSHDLHLvMAKTDEVL 192
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
737-892 |
1.07e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.63 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrlvelsggcIKI-DGVRISDIGLADLRS--KLSIIPQEPVL-FSGTV 812
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTL--------------LRImAGVDKDFNGEARPQPgiKVGYLPQEPQLdPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 813 RSN-----------LDPFNQ----YTE-DQIWDAL--ERTHMKECIAQLPL-KLESEV---ME-----NGD----NFSVG 861
Cdd:TIGR03719 86 RENveegvaeikdaLDRFNEisakYAEpDADFDKLaaEQAELQEIIDAADAwDLDSQLeiaMDalrcpPWDadvtKLSGG 165
|
170 180 190
....*....|....*....|....*....|.
gi 1622900610 862 ERQLLCIARALLRHCKILILDEATAAMDTET 892
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
104-281 |
1.34e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.24 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSL---ISAILGQMTLlEGSIAISG---TFAYV--AQQAWIL----------NA 165
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLmkvLSGVYPHGTY-EGEIIFEGeelQASNIrdTERAGIAiihqelalvkEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 166 TLRDNILFGKE--------YDE--ERYNSVLNscclRPDLAILPSsdlTEIGergaNLSGGQRQRISLARALYSDRSIYI 235
Cdd:PRK13549 98 SVLENIFLGNEitpggimdYDAmyLRAQKLLA----QLKLDINPA---TPVG----NLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622900610 236 LDDPLSALDAHVGNHIFNsaIRKHLKSKTV--LFVTHQLqylvdcDEV 281
Cdd:PRK13549 167 LDEPTASLTESETAVLLD--IIRDLKAHGIacIYISHKL------NEV 206
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
96-246 |
1.42e-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: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 96 HLGHLRLQrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAIS---------------------GTFA 154
Cdd:COG4778 18 LQGGKRLP-VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdlaqaspreilalrrRTIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 155 YVAQqawILNATLRDNIL-----------FGKEYDEERYNSVLNSCCLRPDLAILPSsdlteigergANLSGGQRQRISL 223
Cdd:COG4778 97 YVSQ---FLRVIPRVSALdvvaepllergVDREEARARARELLARLNLPERLWDLPP----------ATFSGGEQQRVNI 163
|
170 180
....*....|....*....|...
gi 1622900610 224 ARALYSDRSIYILDDPLSALDAH 246
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAA 186
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
107-298 |
1.73e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.47 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 107 HSIDLEIQEGKLVGICGSVGSGKTSLISAILGQM----TLLEGSIAISGTFAYVAQQAWILNATLRDNilfgkeyDEERY 182
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPVAPCALRGRKIATIMQN-------PRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 183 NSVLN-------SCCLR---PDLAILPSSdLTEIG----ERGANL-----SGGQRQRISLARALYSDRSIYILDDPLSAL 243
Cdd:PRK10418 93 NPLHTmhthareTCLALgkpADDATLTAA-LEAVGlenaARVLKLypfemSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 244 DAHVGNHIFN---SAIRKHlkSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEEL 298
Cdd:PRK10418 172 DVVAQARILDlleSIVQKR--ALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETL 228
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
416-611 |
1.74e-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: 51.12 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 416 SGNTTVTRGNETSVSDSM----KDNPRMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFF 491
Cdd:cd18558 31 NGGMTNITGNSSGLNSSAgpfeKLEEEMTLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 492 DTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVF--FCVGMIAGvfpW----FLVAVGPLVILFSVL--HIVSRVL 563
Cdd:cd18558 111 DVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGtgFIIGFIRG---WkltlVILAISPVLGLSAVVwaKILSGFT 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622900610 564 IRELKRLDNITQSPflshiTSSIQGLATIHAYNKGQEFLHRYQELLDD 611
Cdd:cd18558 188 DKEKKAYAKAGAVA-----EEVLEAFRTVIAFGGQQKEETRYAQNLEI 230
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
101-287 |
1.81e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.16 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 101 RLQrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMT--LLEGSIAISG------TFAYVA---QQAWILN--ATL 167
Cdd:PLN03140 892 RLQ-LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGfpkkqeTFARISgycEQNDIHSpqVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 168 RDNILFG------KEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGanLSGGQRQRISLARALYSDRSIYILDDPLS 241
Cdd:PLN03140 971 RESLIYSaflrlpKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTG--LSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622900610 242 ALDAHVGNhIFNSAIRKHLKS-KTVLFVTHQ--LQYLVDCDEVIFMKEG 287
Cdd:PLN03140 1049 GLDARAAA-IVMRTVRNTVDTgRTVVCTIHQpsIDIFEAFDELLLMKRG 1096
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
89-296 |
1.88e-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: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 89 EEEGKHIhlghlrlqrtLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQM--TLLEGSIAISGTFayvaqqawILNAT 166
Cdd:cd03217 9 SVGGKEI----------LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGED--------ITDLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 167 L----RDNILFGKEYDEErYNSVLNSCCLRpdlailpssdltEIGErgaNLSGGQRQRISLARALYSDRSIYILDDPLSA 242
Cdd:cd03217 71 PeeraRLGIFLAFQYPPE-IPGVKNADFLR------------YVNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900610 243 LDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYL--VDCDEVIFMKEGCITERGTHE 296
Cdd:cd03217 135 LDIDALRLVAEVINKLREEGKSVLIITHYQRLLdyIKPDRVHVLYDGRIVKSGDKE 190
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
738-935 |
1.92e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.71 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLgMALfrlveLSG--------GCIKIDG--VRISDIGLADlRSKLSIIPQE--- 804
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTL-MKV-----LSGvyphgsyeGEILFDGevCRFKDIRDSE-ALGIVIIHQElal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 805 -PVLfsgTVRSNLDPFNQYTEDQI--WDALERtHMKECIAQLPLKlesevmENGD----NFSVGERQLLCIARALLRHCK 877
Cdd:NF040905 90 iPYL---SIAENIFLGNERAKRGVidWNETNR-RARELLAKVGLD------ESPDtlvtDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 878 ILILDEATAAMDtETD---LLiqETIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 935
Cdd:NF040905 160 LLILDEPTAALN-EEDsaaLL--DLLLELKAqGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
106-290 |
1.93e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQ----QAWILNATL 167
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYIPEdrlgRGLVPDMSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 168 RDNILFGkEYDEERYNS--VLNSCCLRpDLA--------ILPSSDLTEIGergaNLSGGQRQRISLARALYSDRSIYILD 237
Cdd:COG3845 354 AENLILG-RYRRPPFSRggFLDRKAIR-AFAeelieefdVRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAA 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 238 DPLSALDahVGNhIfnSAIRKHL-----KSKTVLFVTHQLQYLVD-CDEVIFMKEGCIT 290
Cdd:COG3845 428 QPTRGLD--VGA-I--EFIHQRLlelrdAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
737-946 |
2.20e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.57 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEP--VLFSGTVRS 814
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 815 NL--DPFN-----QYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAA 887
Cdd:PRK13652 99 DIafGPINlgldeETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 888 MDTETdllIQETIR--EAFADCTMLTIAHRLHTV----LGSDRIMVLAQGQVVEFDTPSVLLSND 946
Cdd:PRK13652 168 LDPQG---VKELIDflNDLPETYGMTVIFSTHQLdlvpEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
737-902 |
2.24e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 50.01 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVEL-SGGCIKIDG------VRISDIGLADLRSKLSIIPQE----P 805
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSL-LRVLNLLEMpRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQynlwP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 806 VLfsgTVRSNL--DPFN------QYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCK 877
Cdd:PRK11124 96 HL---TVQQNLieAPCRvlglskDQALARAEKLLERLRLKPYADRFPLHL-----------SGGQQQRVAIARALMMEPQ 161
|
170 180
....*....|....*....|....*
gi 1622900610 878 ILILDEATAAMDTETDLLIQETIRE 902
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRE 186
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
109-269 |
2.26e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.46 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 109 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAwilnatlrdnilfgkeydeeRYNSVLNS 188
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS--------------------RFMAYLGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 189 C-CLRPDLAIL-----------------PSSDLTEIGERG------ANLSGGQRQRISLARALYSDRSIYILDDPLSALD 244
Cdd:PRK13543 90 LpGLKADLSTLenlhflcglhgrrakqmPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180
....*....|....*....|....*
gi 1622900610 245 AHvGNHIFNSAIRKHLKSKTVLFVT 269
Cdd:PRK13543 170 LE-GITLVNRMISAHLRGGGAALVT 193
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
738-932 |
2.30e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.16 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIS--------DIGLADLRSKLSIIPQEPV--- 806
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqEAGIGIIHQELNLIPQLTIaen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 807 LFSGtvRSNLDPFNQYTEDQIW---DALerthmkecIAQLPLKLESEVMENgdNFSVGERQLLCIARALLRHCKILILDE 883
Cdd:PRK10762 100 IFLG--REFVNRFGRIDWKKMYaeaDKL--------LARLNLRFSSDKLVG--ELSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 884 ATAAM-DTETDLLIQeTIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQ 932
Cdd:PRK10762 168 PTDALtDTETESLFR-VIRELKSqGRGIVYISHRLKEIFEiCDDVTVFRDGQ 218
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
741-935 |
2.76e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.92 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 741 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADL---------RSKLSIIPQEP------ 805
Cdd:PRK11701 25 VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHPrdglrm 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 806 -VLFSGTVRSNLDPF--NQYTE--DQIWDALERTHMKEC-IAQLPlklesevmengDNFSVGERQLLCIARALLRHCKIL 879
Cdd:PRK11701 105 qVSAGGNIGERLMAVgaRHYGDirATAGDWLERVEIDAArIDDLP-----------TTFSGGMQQRLQIARNLVTHPRLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 880 ILDEATAAMDTET-----DLLiQETIREafADCTMLTIAHRLHTV-LGSDRIMVLAQGQVVE 935
Cdd:PRK11701 174 FMDEPTGGLDVSVqarllDLL-RGLVRE--LGLAVVIVTHDLAVArLLAHRLLVMKQGRVVE 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
737-935 |
3.56e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.01 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSK--------LSIIP--- 802
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKhvgfvfqsFMLIPtln 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 803 -QEPVLFSGTVRSNLDpfnQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILIL 881
Cdd:PRK10584 105 aLENVELPALLRGESS---RQSRNGAKALLEQLGLGKRLDHLPAQL-----------SGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900610 882 DEATAAMDTET-----DLLIQETIREAfadCTMLTIAHRLHTVLGSDRIMVLAQGQVVE 935
Cdd:PRK10584 171 DEPTGNLDRQTgdkiaDLLFSLNREHG---TTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
103-271 |
3.57e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------------FAYVAQQAWI-LNATLRD 169
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlctyqkqLCFVGHRSGInPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 170 NILFGKEYDEEryNSVLNSCCLRPDLAILpssdlteIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 249
Cdd:PRK13540 94 NCLYDIHFSPG--AVGITELCRLFSLEHL-------IDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|...
gi 1622900610 250 HIFnSAIRKH-LKSKTVLFVTHQ 271
Cdd:PRK13540 165 TII-TKIQEHrAKGGAVLLTSHQ 186
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
106-312 |
3.64e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 50.66 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVA-------QQAWILNATLRdNILFG--KE 176
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAissglngQLTGIENIELK-GLMMGltKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 177 YDEErynsvlnscclrpdlaILPSS-DLTEIG----ERGANLSGGQRQRISLARALYSDRSIYILDDPLSaldahVGNHI 251
Cdd:PRK13545 119 KIKE----------------IIPEIiEFADIGkfiyQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS-----VGDQT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900610 252 FNSAIRKHL-----KSKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNNL 312
Cdd:PRK13545 178 FTKKCLDKMnefkeQGKTIFFISHSLsQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNQM 244
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
738-933 |
4.14e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI--------GLA---DLRSKLSIIPQEPV 806
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHnaneainhGFAlvtEERRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 807 LFSGTVrSNLDPFNQYtedqiWDALERTHMKE----CIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILD 882
Cdd:PRK10982 344 GFNSLI-SNIRNYKNK-----VGLLDNSRMKSdtqwVIDSMRVKTPGHRTQIG-SLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 883 EATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQV 933
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
740-951 |
4.90e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.78 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 740 KVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIsDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPF 819
Cdd:TIGR01257 948 RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHILF 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 820 NQYTEDQIWD--ALERTHMKECIAqlplkLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQ 897
Cdd:TIGR01257 1027 YAQLKGRSWEeaQLEMEAMLEDTG-----LHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900610 898 ETIREAFADCTMLTIAHRLHT--VLGsDRIMVLAQGQVVEFDTPSVLLSNDSSRFY 951
Cdd:TIGR01257 1102 DLLLKYRSGRTIIMSTHHMDEadLLG-DRIAIISQGRLYCSGTPLFLKNCFGTGFY 1156
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
113-287 |
5.19e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 113 IQEGKLVGICGSVGSGKTSLISAILGQMT------------------------------LLEGSIAISGTFAYVAQQAWI 162
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIpnlgdyeeepswdevlkrfrgtelqnyfkkLYNGEIKVVHKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 163 LNATLRDnILfgKEYDE----ERYNSVLNscclrpdlailpssdLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILD 237
Cdd:PRK13409 176 FKGKVRE-LL--KKVDErgklDEVVERLG---------------LENILDRDiSELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 238 DPLSALDahVGNHIfNSA--IRKHLKSKTVLFVTHQ---LQYLVDCDEVIFMKEG 287
Cdd:PRK13409 238 EPTSYLD--IRQRL-NVArlIRELAEGKYVLVVEHDlavLDYLADNVHIAYGEPG 289
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
753-937 |
5.44e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.49 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 753 IVGRTGSGKSSLGMALFRLVELSGGCIKIDGvRIsdigLADLRSKLSIIP---------QEPVLFSG-TVRSNL----DP 818
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNG-RV----LFDAEKGICLPPekrrigyvfQDARLFPHyKVRGNLrygmAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 819 FNQYTEDQIWDALERTHMkecIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMDT--ETDLL- 895
Cdd:PRK11144 104 SMVAQFDKIVALLGIEPL---LDRYPGSL-----------SGGEKQRVAIGRALLTAPELLLMDEPLASLDLprKRELLp 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622900610 896 -IQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFD 937
Cdd:PRK11144 170 yLERLARE--INIPILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
104-304 |
6.15e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.91 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNA---------------TLR 168
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAgvaiiyqelhlvpemTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 169 DNILFGK------EYDEERYNSVLNSCCLRPDLAILPSSDLteigergANLSGGQRQRISLARALYSDRSIYILDDPLSA 242
Cdd:PRK11288 98 ENLYLGQlphkggIVNRRLLNYEAREQLEHLGVDIDPDTPL-------KYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900610 243 LDAHVGNHIFnSAIRKhLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCITErgTHEELMNLNGD 304
Cdd:PRK11288 171 LSAREIEQLF-RVIRE-LRAegRVILYVSHRMEEIFAlCDAITVFKDGRYVA--TFDDMAQVDRD 231
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
208-283 |
6.21e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.01 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 208 ERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhvgnhIFNSAIR---KHLKSK-TVLFVTHQLQ---------- 273
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDP-----ISTLRIEelmHELKEQyTIIIVTHNMQqaarvsdmta 221
|
90 100
....*....|....*....|....*.
gi 1622900610 274 --------------YLVDCD--EVIF 283
Cdd:PRK14243 222 ffnveltegggrygYLVEFDrtEKIF 247
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
103-282 |
6.71e-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: 48.41 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRTLHSIDLEIQEGKLVGICGSVGSGKTSL----------------ISA----ILGQM-----TLLEG-SIAIS------ 150
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAyarqFLGQMdkpdvDSIEGlSPAIAidqktt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 151 -----GTFAYVAQqawiLNATLRdnILFGKEYDEERYNSvlnscclrpdlailpssdLTEIG------ERGAN-LSGGQR 218
Cdd:cd03270 88 srnprSTVGTVTE----IYDYLR--LLFARVGIRERLGF------------------LVDVGlgyltlSRSAPtLSGGEA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 219 QRISLARALYSDRS--IYILDDPLSALDAHvGNHIFNSAIrKHLKSK--TVLFVTHQLQYLVDCDEVI 282
Cdd:cd03270 144 QRIRLATQIGSGLTgvLYVLDEPSIGLHPR-DNDRLIETL-KRLRDLgnTVLVVEHDEDTIRAADHVI 209
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
717-934 |
7.09e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 48.73 E-value: 7.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 717 QEGEVTFENAEMRYReNLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDiglADLRS 796
Cdd:PRK15056 3 QQAGIVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 797 KLSIIPQE-------PVLFSGTVRSN-------LDPFNQYTEDQIWDALERTHMkeciaqlplkLESEVMENGDnFSVGE 862
Cdd:PRK15056 79 LVAYVPQSeevdwsfPVLVEDVVMMGryghmgwLRRAKKRDRQIVTAALARVDM----------VEFRHRQIGE-LSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 863 RQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLGSDRIMVLAQGQVV 934
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVL 220
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
100-298 |
7.24e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 48.37 E-value: 7.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 100 LRLQ----RTLHSIDLEIQEGKLVGICGSVGSGKTSLISaILGQMTLLEGSIAISGTFAYVAQQAW-------------- 161
Cdd:PRK14247 9 LKVSfgqvEVLDGVNLEIPDNTITALMGPSGSGKSTLLR-VFNRLIELYPEARVSGEVYLDGQDIFkmdvielrrrvqmv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 162 ------ILNATLRDNILFG---------KEYDEERYNSVLNSCCLRPDLAilpssdlTEIGERGANLSGGQRQRISLARA 226
Cdd:PRK14247 88 fqipnpIPNLSIFENVALGlklnrlvksKKELQERVRWALEKAQLWDEVK-------DRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 227 LYSDRSIYILDDPLSALDAHvgnhifNSAIRKHL-----KSKTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 298
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPE------NTAKIESLflelkKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
213-298 |
7.31e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.85 E-value: 7.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 213 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN-SAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCIT 290
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQlIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAV 248
|
....*...
gi 1622900610 291 ERGTHEEL 298
Cdd:PRK10261 249 ETGSVEQI 256
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
106-301 |
9.51e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.40 E-value: 9.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQ--------MTLLEG--------SIAISGTFAYVA----QQAWILNA 165
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRsygrnisgTVFKDGkevdvstvSDAIDAGLAYVTedrkGYGLNLID 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 166 TLRDNI----LFG----------KEYDE-ERYnsvlnscclRPDLAILPSSDLTEIGergaNLSGGQRQRISLARALYSD 230
Cdd:NF040905 356 DIKRNItlanLGKvsrrgvidenEEIKVaEEY---------RKKMNIKTPSVFQKVG----NLSGGNQQKVVLSKWLFTD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 231 RSIYILDDPLSALDahVGN--HIFnSAIRKHLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCIT-----ERGTHEELMNL 301
Cdd:NF040905 423 PDVLILDEPTRGID--VGAkyEIY-TIINELAAEgKGVIVISSELPELLGmCDRIYVMNEGRITgelprEEASQERIMRL 499
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
214-298 |
9.65e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.95 E-value: 9.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 214 SGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI----------FNSAIrkhlksktvLFVTHQLQYLVD-CDEVI 282
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQImtllnelkreFNTAI---------IMITHDLGVVAGiCDKVL 233
|
90
....*....|....*.
gi 1622900610 283 FMKEGCITERGTHEEL 298
Cdd:PRK09473 234 VMYAGRTMEYGNARDV 249
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
736-941 |
1.05e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.25 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 736 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLR-SKLSIIPQEP-----VLfS 809
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrLGVAYIPEDRlgrglVP-D 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 810 GTVRSNLDpFNQYTEDQI-------WDALeRTHMKECIAQLPLK---LESEVmengDNFSVGERQLLCIARALLRHCKIL 879
Cdd:COG3845 351 MSVAENLI-LGRYRRPPFsrggfldRKAI-RAFAEELIEEFDVRtpgPDTPA----RSLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 880 I-------LDEATAAMdtetdllIQETIREAfAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV-EFDTPSV 941
Cdd:COG3845 425 IaaqptrgLDVGAIEF-------IHQRLLEL-RDagAAVLLISEDLDEILAlSDRIAVMYEGRIVgEVPAAEA 489
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
109-272 |
1.14e-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: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 109 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-----TFAYVAQ------QAWIL--NATLRDNILF-- 173
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietNLDAVRQslgmcpQHNILfhHLTVAEHILFya 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 174 ---GKEYDEERYNSVlnscclrpdlAILPSSDLT-EIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 249
Cdd:TIGR01257 1029 qlkGRSWEEAQLEME----------AMLEDTGLHhKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180
....*....|....*....|...
gi 1622900610 250 HIFNsAIRKHLKSKTVLFVTHQL 272
Cdd:TIGR01257 1099 SIWD-LLLKYRSGRTIIMSTHHM 1120
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
106-298 |
1.25e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 48.29 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------------TFAYVAQQAWILNAT 166
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkkvSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 167 LRDNILFG-------KEYDEERYNSVLNSCCLRPDLailpssdlteIGERGANLSGGQRQRISLARALYSDRSIYILDDP 239
Cdd:PRK13641 103 VLKDVEFGpknfgfsEDEAKEKALKWLKKVGLSEDL----------ISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 240 LSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 298
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEI 232
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
112-277 |
1.34e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.80 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 112 EIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-TFAYVAQQAwilnatlrdnilfgkeydeerynsvlnscc 190
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQYI------------------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 191 lrpdlailpssdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKHLK--SKTVLFV 268
Cdd:cd03222 71 ---------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNA-ARAIRRLSEegKKTALVV 128
|
170
....*....|..
gi 1622900610 269 THQL---QYLVD 277
Cdd:cd03222 129 EHDLavlDYLSD 140
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
213-300 |
1.37e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.78 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 213 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKHLKSKTVLFVTHQL-QYLVDCDEVIFMKEGCITE 291
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVE 242
|
....*....
gi 1622900610 292 RGTHEELMN 300
Cdd:PRK14271 243 EGPTEQLFS 251
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
94-246 |
1.41e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.90 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 94 HIHLGHlRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMT--------LLEGSIAISGT--FAYVAQQAWIL 163
Cdd:PRK13547 6 HLHVAR-RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEplAAIDAPRLARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 164 NATL------------RDNILFGKeYDEERYNSVLN-------SCCL-RPDLAILPSSDLTeigergaNLSGGQRQRISL 223
Cdd:PRK13547 85 RAVLpqaaqpafafsaREIVLLGR-YPHARRAGALThrdgeiaWQALaLAGATALVGRDVT-------TLSGGELARVQF 156
|
170 180 190
....*....|....*....|....*....|...
gi 1622900610 224 ARAL---------YSDRSIYILDDPLSALD-AH 246
Cdd:PRK13547 157 ARVLaqlwpphdaAQPPRYLLLDEPTAALDlAH 189
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
104-287 |
1.42e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQA-WILNATLR 168
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQELnLVLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 169 DNILFGkeydeeRYNS----VLNSCCLRPDLAILPSSDL-TEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 243
Cdd:PRK10982 92 DNMWLG------RYPTkgmfVDQDKMYRDTKAIFDELDIdIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622900610 244 DAHVGNHIFnSAIRKhLKSK--TVLFVTHQLQYLVD-CDEVIFMKEG 287
Cdd:PRK10982 166 TEKEVNHLF-TIIRK-LKERgcGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
459-570 |
1.43e-05 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 48.08 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 459 IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVF-FCVGMIag 537
Cdd:cd18784 55 IRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIgVIVFMF-- 132
|
90 100 110
....*....|....*....|....*....|...
gi 1622900610 538 VFPWFLVAVgpLVILFSVLHIVSRVLIRELKRL 570
Cdd:cd18784 133 KLSWQLSLV--TLIGLPLIAIVSKVYGDYYKKL 163
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
94-244 |
1.57e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 94 HIHLGHLRLQ--RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISgtFAYVA-----QQAWILNAT 166
Cdd:PRK10938 5 QISQGTFRLSdtKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ--FSHITrlsfeQLQKLVSDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 167 LRDN---ILFGKEYDEERYNSVL-------NSCCLRpdLA-ILPSSDLteIGERGANLSGGQRQRISLARALYSDRSIYI 235
Cdd:PRK10938 83 WQRNntdMLSPGEDDTGRTTAEIiqdevkdPARCEQ--LAqQFGITAL--LDRRFKYLSTGETRKTLLCQALMSEPDLLI 158
|
....*....
gi 1622900610 236 LDDPLSALD 244
Cdd:PRK10938 159 LDEPFDGLD 167
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
213-300 |
1.70e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.55 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 213 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnsAIRKHLKSK---TVLFVTHQLQYLVD-CDEVIFMKEGC 288
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQIL--QLLRELQQElnmGLLFITHNLSIVRKlADRVAVMQNGR 234
|
90
....*....|..
gi 1622900610 289 ITERGTHEELMN 300
Cdd:PRK15134 235 CVEQNRAATLFS 246
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
701-933 |
2.57e-05 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 46.98 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 701 EAPARIKNKAPspdwpqegeVTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGcik 780
Cdd:PRK11247 2 MNTARLNQGTP---------LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 781 idGVRISDIGLADLRSKLSIIPQEPVLF-------------SGTVRsnldpfnqyteDQIWDALERTHMKECIAQLPLKL 847
Cdd:PRK11247 68 --ELLAGTAPLAEAREDTRLMFQDARLLpwkkvidnvglglKGQWR-----------DAALQALAAVGLADRANEWPAAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 848 esevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETI-----REAFadcTMLTIAHRL-HTVLG 921
Cdd:PRK11247 135 -----------SGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIeslwqQHGF---TVLLVTHDVsEAVAM 200
|
250
....*....|..
gi 1622900610 922 SDRIMVLAQGQV 933
Cdd:PRK11247 201 ADRVLLIEEGKI 212
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
104-294 |
2.64e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 47.05 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 104 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT---------------------FAYVAQQawI 162
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstsknkdikqirkkvglvFQFPESQ--L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 163 LNATLRDNILFG-------KEYDEERynsvlnsccLRPDLAILPSSDltEIGERGA-NLSGGQRQRISLARALYSDRSIY 234
Cdd:PRK13649 99 FEETVLKDVAFGpqnfgvsQEEAEAL---------AREKLALVGISE--SLFEKNPfELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 235 ILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGT 294
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
91-298 |
2.75e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 47.15 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 91 EGKHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-FAYVAQQawILNatLRD 169
Cdd:PRK13636 7 KVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpIDYSRKG--LMK--LRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 170 NI-LFGKEYDEERYN-SVLNSCCLRPDLAILPSSDLTEIGERGAN--------------LSGGQRQRISLARALYSDRSI 233
Cdd:PRK13636 83 SVgMVFQDPDNQLFSaSVYQDVSFGAVNLKLPEDEVRKRVDNALKrtgiehlkdkpthcLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 234 YILDDPLSALDAhVGnhifNSAIRKHLKSK------TVLFVTHQLQYL-VDCDEVIFMKEGCITERGTHEEL 298
Cdd:PRK13636 163 LVLDEPTAGLDP-MG----VSEIMKLLVEMqkelglTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
741-937 |
3.06e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.69 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 741 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLSIIPQEP----VLFSGTVRSN 815
Cdd:PRK10762 271 VSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRkrdgLVLGMSVKEN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 816 -----LDPFNqYTEDQIWDALERTHMKECIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILDEATAAMDT 890
Cdd:PRK10762 351 msltaLRYFS-RAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIG-LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622900610 891 ETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVV-EFD 937
Cdd:PRK10762 429 GAKKEIYQLINQFKAEgLSIILVSSEMPEVLGmSDRILVMHEGRISgEFT 478
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
103-287 |
3.20e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.95 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 103 QRT-LHSIDLEIQEGKLVGICGSVGSGKTSLISAILG--QMTLLEGSIAISG---------TFAYVAQQAWIL-NATLRD 169
Cdd:PLN03211 80 ERTiLNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNrkptkqilkRTGFVTQDDILYpHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 170 NILF------GKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGanLSGGQRQRISLARALYSDRSIYILDDPLSAL 243
Cdd:PLN03211 160 TLVFcsllrlPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRG--ISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622900610 244 DAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLV--DCDEVIFMKEG 287
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVyqMFDSVLVLSEG 283
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
106-298 |
3.20e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 46.61 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-TFAYVAQQawILNATLRDNILFGKEYDEERYNS 184
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGePIKYDKKS--LLEVRKTVGIVFQNPDDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 185 VLNSCCLRPDLAILPSSD--------LTEIGERG------ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 250
Cdd:PRK13639 96 VEEDVAFGPLNLGLSKEEvekrvkeaLKAVGMEGfenkppHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622900610 251 IFNSAIRKHLKSKTVLFVTHQLQYL-VDCDEVIFMKEGCITERGTHEEL 298
Cdd:PRK13639 176 IMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
109-291 |
3.40e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 109 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGtfAYVAQQAW-----ILNATLRDNILF-------GKE 176
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG--KPVTAEQPedyrkLFSAVFTDFHLFdqllgpeGKP 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 177 YDEERYNSVLNSCCLRpdlailpsSDLTEIGERGAN--LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVgNHIFNS 254
Cdd:PRK10522 420 ANPALVEKWLERLKMA--------HKLELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFYQ 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622900610 255 AIRKHLKS--KTVLFVTHQLQYLVDCDEVIFMKEGCITE 291
Cdd:PRK10522 491 VLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
856-954 |
3.47e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 47.02 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 856 DNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIRE---AFaDCTMLTIAHRLHTVLG-SDRIMVLAQG 931
Cdd:PRK11432 135 DQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRElqqQF-NITSLYVTHDQSEAFAvSDTVIVMNKG 213
|
90 100
....*....|....*....|...
gi 1622900610 932 QVVEFDTPSVLLSNDSSRFYAMF 954
Cdd:PRK11432 214 KIMQIGSPQELYRQPASRFMASF 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
106-281 |
3.62e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.33 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFA--YVAQQAWI--------L--NATLRDN 170
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpvRIRspRDAIALGIgmvhqhfmLvpNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 171 ILFGKEydeerynsvlNSCCLRPDLAILpSSDLTEIGER-G---------ANLSGGQRQRISLARALYSDRSIYILDDPL 240
Cdd:COG3845 101 IVLGLE----------PTKGGRLDRKAA-RARIRELSERyGldvdpdakvEDLSVGEQQRVEILKALYRGARILILDEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622900610 241 SALDAHVGNHIFnsAIRKHLKS--KTVLFVTHQLqylvdcDEV 281
Cdd:COG3845 170 AVLTPQEADELF--EILRRLAAegKSIIFITHKL------REV 204
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
447-648 |
3.64e-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: 46.81 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 447 ALSMAVML--ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFsKDMDEVDVRLPFQAEMFIQN 524
Cdd:cd18566 47 GVVIAILLesLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLTGQALLALLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 525 VILVFFCVGMIAgVFPWFLVAVgPLVIL--FSV----LHIVSRVLIRELKRLDNITQspflSHITSSIQGLATIHAYNKG 598
Cdd:cd18566 126 LPFVLIFLGLIW-YLGGKLVLV-PLVLLglFVLvailLGPILRRALKERSRADERRQ----NFLIETLTGIHTIKAMAME 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622900610 599 QEFLHRYQELLDDnqapfflftCAMRWLAVRlDLISIALITTTGLMIVLM 648
Cdd:cd18566 200 PQMLRRYERLQAN---------AAYAGFKVA-KINAVAQTLGQLFSQVSM 239
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
737-892 |
4.22e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLG--MAlfrlvelsgGCIK-IDG-VRISDiGLadlrsKLSIIPQEPVL-FSGT 811
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLriMA---------GVDKeFEGeARPAP-GI-----KVGYLPQEPQLdPEKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 812 VRSN-----------LDPFNQ----YTE-DQIWDAL--ERTHMKECIAQLPL-KLESEV---ME-----NGD----NFSV 860
Cdd:PRK11819 87 VRENveegvaevkaaLDRFNEiyaaYAEpDADFDALaaEQGELQEIIDAADAwDLDSQLeiaMDalrcpPWDakvtKLSG 166
|
170 180 190
....*....|....*....|....*....|..
gi 1622900610 861 GERQLLCIARALLRHCKILILDEATAAMDTET 892
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
742-891 |
5.15e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.18 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 742 SFTIKPKEKIGIVGRTGSGKSSlgmaLFRLveLSG------GCIKIDGVRISDIGlADLRSKLsiipqepvLFSG----- 810
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTS----LLRI--LAGlarpdaGEVLWQGEPIRRQR-DEYHQDL--------LYLGhqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 811 ----TVRSNLDpFNQ-----YTEDQIWDALERTHMKEcIAQLPLKlesevmengdNFSVGERQLLCIARALLRHCKILIL 881
Cdd:PRK13538 86 ktelTALENLR-FYQrlhgpGDDEALWEALAQVGLAG-FEDVPVR----------QLSAGQQRRVALARLWLTRAPLWIL 153
|
170
....*....|
gi 1622900610 882 DEATAAMDTE 891
Cdd:PRK13538 154 DEPFTAIDKQ 163
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
737-892 |
6.86e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 45.33 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDgVRISDIGladlrSKLSIIPQEPVlfsgtvrsnL 816
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-VPDNQFG-----REASLIDAIGR---------K 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900610 817 DPFNQYTEdqiwdALERTHMKEciAQLPLKLESEvmengdnFSVGERQLLCIARALLRHCKILILDEATAAMDTET 892
Cdd:COG2401 110 GDFKDAVE-----LLNAVGLSD--AVLWLRRFKE-------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
106-287 |
6.88e-05 |
|
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: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 106 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQmtlLEGSIAISGTFAYVAQQAWILNATLRDNILFGKEydEERYNSV 185
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSE--EDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 186 LN-------SCCLRPDLAIlpssdlteigeRGanLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSaIR- 257
Cdd:cd03233 98 LTvretldfALRCKGNEFV-----------RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKC-IRt 163
|
170 180 190
....*....|....*....|....*....|...
gi 1622900610 258 --KHLKSKTVLFVTHQLQYLVDC-DEVIFMKEG 287
Cdd:cd03233 164 maDVLKTTTFVSLYQASDEIYDLfDKVLVLYEG 196
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
737-889 |
8.10e-05 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 44.79 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL 816
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 817 DPFNQY-TEDQIWDALERTHMK----ECIAQLplklesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMD 889
Cdd:cd03231 95 RFWHADhSDEQVEEALARVGLNgfedRPVAQL---------------SAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
460-611 |
1.06e-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: 45.41 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 460 RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILvffCVGMIAgvf 539
Cdd:cd18590 56 RGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVK---TLGMLG--- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 540 pwFLVAVGPLVILFSVLHIVSRVLI--------RELKR--LDNITQSPFLshITSSIQGLATIHAYNKGQEFLHRYQELL 609
Cdd:cd18590 130 --FMLSLSWQLTLLTLIEMPLTAIAqkvyntyhQKLSQavQDSIAKAGEL--AREAVSSIRTVRSFKAEEEEACRYSEAL 205
|
..
gi 1622900610 610 DD 611
Cdd:cd18590 206 ER 207
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
737-953 |
1.17e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 44.98 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL 816
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 817 DPFNQYTEDQI---W-----DALERTHMKECIAQLPLklesevmENGDNFSVGERQLLCIARALLRHCKILILDEATAAM 888
Cdd:PRK10253 102 VARGRYPHQPLftrWrkedeEAVTKAMQATGITHLAD-------QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 889 DT--ETDL--LIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSND-SSRFYAM 953
Cdd:PRK10253 175 DIshQIDLleLLSELNRE--KGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVTAElIERIYGL 243
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
447-607 |
1.28e-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: 45.20 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 447 ALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVrlpFQAEMFI 522
Cdd:cd18564 57 AAALVGIALLRGLasyaGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQD---LLVSGVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 523 QNVILVFFCVGMIAGVFpWF-----LVAVGPL-VILFSVLHIVSRvlIRELKRldniTQSPFLSHITS----SIQGLATI 592
Cdd:cd18564 134 PLLTNLLTLVGMLGVMF-WLdwqlaLIALAVApLLLLAARRFSRR--IKEASR----EQRRREGALASvaqeSLSAIRVV 206
|
170
....*....|....*
gi 1622900610 593 HAYNKGQEFLHRYQE 607
Cdd:cd18564 207 QAFGREEHEERRFAR 221
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
737-961 |
1.35e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 45.07 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADlrSKLSIIPQEPVLFSG-TVRSN 815
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 816 LD-----------PFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEA 884
Cdd:PRK10851 95 IAfgltvlprrerPNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 885 TAAMDTETDLLIQETIREAFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAENKV 961
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNRL 243
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
747-939 |
1.89e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.75 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 747 PKEKIGIVGRTGSGKSSLGMALFR-LVELSGGCIKIDGVRISDIGLADLRSKLsiipqepvlfsgtvrsnldpfnqyted 825
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 826 qiwdalerthmkeciaqlplkleseVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIR---- 901
Cdd:smart00382 54 -------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622900610 902 ---EAFADCTMLTIAHRLHTVLgsDRIMVLAQGQVVEFDTP 939
Cdd:smart00382 109 lllKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLLI 147
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
738-937 |
1.93e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 44.69 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrlvelsggcIKIdgvrISDIgladlrsklsIIPQepvlfSGTVRSN-L 816
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTT--------------IKM----LTGI----------LVPT-----SGEVRVLgY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 817 DPFNQYTE--DQI-----------WD--ALERTHMKECIAQLP-------LKLESEVMENGD-------NFSVGERQLLC 867
Cdd:COG4586 85 VPFKRRKEfaRRIgvvfgqrsqlwWDlpAIDSFRLLKAIYRIPdaeykkrLDELVELLDLGElldtpvrQLSLGQRMRCE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 868 IARALLRHCKILILDEATAAMdtetDLLIQETIREAFAD------CTMLTIAHRLHTV--LgSDRIMVLAQGQVVeFD 937
Cdd:COG4586 165 LAAALLHRPKILFLDEPTIGL----DVVSKEAIREFLKEynrergTTILLTSHDMDDIeaL-CDRVIVIDHGRII-YD 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
109-297 |
2.40e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 109 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVA------------------QQAWILNATLRDN 170
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRsprdairagimlcpedrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 171 ILFGKeydeeRYNSVLNSCCLRP------------DLAILPSSDLTEIGergaNLSGGQRQRISLARALYSDRSIYILDD 238
Cdd:PRK11288 352 INISA-----RRHHLRAGCLINNrweaenadrfirSLNIKTPSREQLIM----NLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900610 239 PLSALDahVG------NHIFNSAIRKhlksKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEE 297
Cdd:PRK11288 423 PTRGID--VGakheiyNVIYELAAQG----VAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
738-934 |
2.61e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 43.32 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 738 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD---LRSKLSIIPQEP-VLFSGTVR 813
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 814 SNLD-PF---NQYTED---QIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATA 886
Cdd:PRK10908 98 DNVAiPLiiaGASGDDirrRVSAALDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622900610 887 AMDTEtdllIQETIREAFAD-----CTMLTIAHRLHTVLGSD-RIMVLAQGQVV 934
Cdd:PRK10908 167 NLDDA----LSEGILRLFEEfnrvgVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
119-298 |
2.65e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 44.02 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 119 VGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQA--WILNATLRDNILFG-------KE 176
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkenirevrkFVGLVFQNPddQIFSPTVEQDIAFGpinlgldEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 177 YDEERYNSVLNSCCLRPDLAILPSsdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIF---N 253
Cdd:PRK13652 113 TVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIdflN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622900610 254 SAIRKHlkSKTVLFVTHQLQYLVDCDEVIF-MKEGCITERGTHEEL 298
Cdd:PRK13652 182 DLPETY--GMTVIFSTHQLDLVPEMADYIYvMDKGRIVAYGTVEEI 225
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
447-614 |
2.69e-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: 44.02 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 447 ALSMAVMLILKAIRGVVFVKGTLRASSR-LHD---ELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVrlpfqaemFI 522
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERlLYDlrlRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSE--------LL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 523 QN-----VILVFFCVGMIAGVF----PWFLVAVGPLVILFsvlhIVSRVLIRELKRL-----DNITQSpfLSHITSSIQG 588
Cdd:cd18546 114 QTglvqlVVSLLTLVGIAVVLLvldpRLALVALAALPPLA----LATRWFRRRSSRAyrrarERIAAV--NADLQETLAG 187
|
170 180
....*....|....*....|....*.
gi 1622900610 589 LATIHAYNKGQEFLHRYQELLDDNQA 614
Cdd:cd18546 188 IRVVQAFRRERRNAERFAELSDDYRD 213
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
470-510 |
2.87e-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: 2.87e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1622900610 470 RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEV 510
Cdd:cd18574 72 RVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEF 112
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
737-936 |
3.49e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.49 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 737 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG--GCIKIDGVRISDiglaDLRSKLSIIPQEPVLFSG-TVR 813
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK----QILKRTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 814 SNLDPFNQYTEDQIWDALERTHMKE-CIAQLPL-KLESEVMENG--DNFSVGERQLLCIARALLRHCKILILDEATAAMD 889
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAEsVISELGLtKCENTIIGNSfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 890 TETDL-LIQetireafadcTMLTIAHRLHTVLGS------------DRIMVLAQGQVVEF 936
Cdd:PLN03211 239 ATAAYrLVL----------TLGSLAQKGKTIVTSmhqpssrvyqmfDSVLVLSEGRCLFF 288
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
475-673 |
3.90e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 43.68 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 475 LHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNViLVFFCVGMIAGVFPWFLVAVG----PLV 550
Cdd:cd18778 75 LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNV-LTLVGVAIILFSINPKLALLTlipiPFL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 551 ILFSVLH-IVSRVLIRELKRldnitqspFLSHITS----SIQGLATIHAYNKGQEFLHRYQELLDDnqapffLFTCAMRw 625
Cdd:cd18778 154 ALGAWLYsKKVRPRYRKVRE--------ALGELNAllqdNLSGIREIQAFGREEEEAKRFEALSRR------YRKAQLR- 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622900610 626 lAVRLDLI---SIALITTTGLMIVLMHGqippayAGLAISYAVQLTGLFQF 673
Cdd:cd18778 219 -AMKLWAIfhpLMEFLTSLGTVLVLGFG------GRLVLAGELTIGDLVAF 262
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
730-946 |
3.91e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.54 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 730 YRENLPLVLK---KVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCI--------------KIDGVRISDI--- 789
Cdd:PRK13651 12 FNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkEKEKVLEKLViqk 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 790 -------GLADLRSKLSIIPQ--EPVLFSGTVRSNL--DPFNQYTEDQiwDALERThmKECIAQLPLKlESEVMENGDNF 858
Cdd:PRK13651 92 trfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIifGPVSMGVSKE--EAKKRA--AKYIELVGLD-ESYLQRSPFEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 859 SVGERQLLCIARALLRHCKILILDEATAAMD---TETDLLIQETIREAFAdcTMLTIAHRLHTVLG-SDRIMVLAQGQVV 934
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGK--TIILVTHDLDNVLEwTKRTIFFKDGKII 244
|
250
....*....|...
gi 1622900610 935 -EFDTPSVLLSND 946
Cdd:PRK13651 245 kDGDTYDILSDNK 257
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
721-889 |
4.19e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 43.19 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 721 VTFENAEMRYRENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIS------DIgl 791
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 792 ADLRSKLSIIPQ--EPVLFSGTVRSNL----DPFNQYTEDQIWDALERTHM----KECIAQLPLKLesevmengdnfSVG 861
Cdd:PRK13649 81 KQIRKKVGLVFQfpESQLFEETVLKDVafgpQNFGVSQEEAEALAREKLALvgisESLFEKNPFEL-----------SGG 149
|
170 180
....*....|....*....|....*...
gi 1622900610 862 ERQLLCIARALLRHCKILILDEATAAMD 889
Cdd:PRK13649 150 QMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
114-277 |
4.53e-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: 44.00 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 114 QEGKLVGICGSVGSGKTSLISAILGQMT------------------------------LLEGSIAISGTFAYVAQQAWIL 163
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKpnlgdydeepswdevlkrfrgtelqdyfkkLANGEIKVAHKPQYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 164 NATLRDnILfgKEYDEErynSVLNSccLRPDLAILPSSDlTEIGErganLSGGQRQRISLARALYSDRSIYILDDPLSAL 243
Cdd:COG1245 177 KGTVRE-LL--EKVDER---GKLDE--LAEKLGLENILD-RDISE----LSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622900610 244 DahVGNHIfNSA--IRKHLKS-KTVLFVTHQ---LQYLVD 277
Cdd:COG1245 244 D--IYQRL-NVArlIRELAEEgKYVLVVEHDlaiLDYLAD 280
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
208-305 |
4.53e-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: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 208 ERGAN-LSGGQRQRISLARALYSDRS--IYILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFM 284
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDI 562
|
90 100 110
....*....|....*....|....*....|.
gi 1622900610 285 KE------GCITERGTHEELMN----LNGDY 305
Cdd:TIGR00630 563 GPgagehgGEVVASGTPEEILAnpdsLTGQY 593
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
214-253 |
5.97e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.69 E-value: 5.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1622900610 214 SGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN 253
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIIN 504
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
95-241 |
6.20e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 95 IHLGHLRL----QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAIL-------GQMTLLEGSIAISGTFAYVAQQ-AWI 162
Cdd:NF033858 2 ARLEGVSHrygkTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgarkiqqGRVEVLGGDMADARHRRAVCPRiAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 163 -------LNATL--RDNI-----LFGKEYDEERYnsvlnscclRPDlAILPSSDLTEIGERGA-NLSGGQRQRISLARAL 227
Cdd:NF033858 82 pqglgknLYPTLsvFENLdffgrLFGQDAAERRR---------RID-ELLRATGLAPFADRPAgKLSGGMKQKLGLCCAL 151
|
170 180
....*....|....*....|
gi 1622900610 228 YSDRSIYILD------DPLS 241
Cdd:NF033858 152 IHDPDLLILDepttgvDPLS 171
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
458-506 |
7.72e-04 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 42.62 E-value: 7.72e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622900610 458 AIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKD 506
Cdd:cd18780 60 FLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSD 108
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
206-298 |
9.99e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.08 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 206 IGERGANLSGGQRQRISLARALY---SDRSIYILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVI 282
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYII 902
|
90 100
....*....|....*....|..
gi 1622900610 283 FM------KEGCITERGTHEEL 298
Cdd:TIGR00630 903 DLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
211-277 |
1.20e-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: 1.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 211 ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAH-VgnhifnSAIRKHLK--SKTVLFVTHQlQYLVD 277
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) ... |
202-277 |
1.41e-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: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 202 DLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDahVGNHIfNSA--IRKHLK-SKTVLFVTHQ---LQY 274
Cdd:cd03236 128 ELRHVLDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD--IKQRL-NAArlIRELAEdDNYVLVVEHDlavLDY 204
|
...
gi 1622900610 275 LVD 277
Cdd:cd03236 205 LSD 207
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
96-298 |
1.62e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.03 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 96 HLGHLRlqrTLHSIDLEIQEGKLVGICGSVGSG--KTSLISAILGQ---------MTLLEGSIAISGTFAY--VAQQAWI 162
Cdd:NF000106 22 HFGEVK---AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPdagrrpwrf*TWCANRRALRRTIG*hrPVR*GRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 163 LNATLRDNI-LFGKEYDEERYNSVLnscclRPDlAILPSSDLTEI-GERGANLSGGQRQRISLARALYSDRSIYILDDPL 240
Cdd:NF000106 99 ESFSGRENLyMIGR*LDLSRKDARA-----RAD-ELLERFSLTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900610 241 SALDAHVGNHIFNSAIRKHLKSKTVLFVThqlQYLVDCD----EVIFMKEGCITERGTHEEL 298
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMVRDGATVLLTT---QYMEEAEqlahELTVIDRGRVIADGKVDEL 231
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
446-600 |
1.75e-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: 41.63 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 446 YALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD---VR-LP-- 515
Cdd:cd18584 39 LLLLLLAALLLRALlawaQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTEGVDALDgyfARyLPql 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 516 FQAeMFIQNVILVF-FCVGMIAGVfpwFLVAVGPLVILFSVL-----HIVSRVLIRELKRLDNitqspflsHITSSIQGL 589
Cdd:cd18584 119 VLA-AIVPLLILVAvFPLDWVSAL---ILLVTAPLIPLFMILigkaaQAASRRQWAALSRLSG--------HFLDRLRGL 186
|
170
....*....|.
gi 1622900610 590 ATIHAYNKGQE 600
Cdd:cd18584 187 PTLKLFGRARA 197
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
454-609 |
2.44e-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: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 454 LILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDmDEVDVRLPFQAEMFIQNVILVFFCVG 533
Cdd:cd18568 56 ILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQEN-QKIRRFLTRSALTTILDLLMVFIYLG 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 534 MIAgVFPWFL--VAVGpLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELL 609
Cdd:cd18568 135 LMF-YYNLQLtlIVLA-FIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKF 210
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
213-302 |
3.80e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 213 LSGGQRQRISLARALYS---DRSIYILDDPLSAL---DAHVGNHIFNSAIRkhlKSKTVLFVTHQLQYLVDCDEVIFM-- 284
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhthDIKALIYVLQSLTH---QGHTVVIIEHNMHVVKVADYVLELgp 886
|
90 100
....*....|....*....|..
gi 1622900610 285 ----KEGCITERGTHEELMNLN 302
Cdd:PRK00635 887 eggnLGGYLLASCSPEELIHLH 908
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
440-594 |
3.81e-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: 40.58 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 440 QYYASIYALSMAVML------ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRIlnrfSKDMDEVD-V 512
Cdd:cd18783 36 QSYSTLYVLTIGVVIallfegILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVL----TKHMQQIErI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 513 RlpfqaeMFI-QNVILVFFCVGMIAGVFP---WFLVAVGPLVILFSVL-----HIVSRVLIRELKRLDNITQSPfLSHIT 583
Cdd:cd18783 112 R------QFLtGQLFGTLLDATSLLVFLPvlfFYSPTLALVVLAFSALialiiLAFLPPFRRRLQALYRAEGER-QAFLV 184
|
170
....*....|.
gi 1622900610 584 SSIQGLATIHA 594
Cdd:cd18783 185 ETVHGIRTVKS 195
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
179-246 |
5.61e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 5.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900610 179 EERYNSVLNSCCLRPDLAIlpssdlteigERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAH 246
Cdd:PLN03073 321 EARAASILAGLSFTPEMQV----------KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLH 378
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
671-936 |
5.71e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 671 FQFTVRLASETEARFTSVERINHYIKTLSleaPARIKNKAPSP-DWPQEGEVTFENAEMRYRENlPLVLKKVSFTIKPKE 749
Cdd:PLN03073 461 FRYNAKRASLVQSRIKALDRLGHVDAVVN---DPDYKFEFPTPdDRPGPPIISFSDASFGYPGG-PLLFKNLNFGIDLDS 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 750 KIGIVGRTGSGKSSLgmalfrLVELSGgcikidgvrisdiglaDLrsklsiipqEPVlfSGTV-RS---NLDPFNQYTED 825
Cdd:PLN03073 537 RIAMVGPNGIGKSTI------LKLISG----------------EL---------QPS--SGTVfRSakvRMAVFSQHHVD 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 826 QIwdALERT---HMKECIAQLP-LKLESEVMENGDN----------FSVGERQLLCIARALLRHCKILILDEATAAMDTE 891
Cdd:PLN03073 584 GL--DLSSNpllYMMRCFPGVPeQKLRAHLGSFGVTgnlalqpmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD 661
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1622900610 892 -TDLLIQETireAFADCTMLTIAHRLHTVLGS-DRIMVLAQGQVVEF 936
Cdd:PLN03073 662 aVEALIQGL---VLFQGGVLMVSHDEHLISGSvDELWVVSEGKVTPF 705
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
474-596 |
6.73e-03 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 39.72 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 474 RLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAgVFPWFLVAVgpLVILF 553
Cdd:cd18551 70 DLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMF-LLDWVLTLV--TLAVV 146
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622900610 554 SVLHIVSRVLIRELKRLDNITQ---SPFLSHITSSIQGLATIHAYN 596
Cdd:cd18551 147 PLAFLIILPLGRRIRKASKRAQdalGELSAALERALSAIRTVKASN 192
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
751-770 |
8.36e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 39.36 E-value: 8.36e-03
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
107-227 |
8.71e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.79 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900610 107 HSIDLE-IQEGKLVGICGSVGSGKTSLISAI----LGQMTLLEGSIAISGTFAYVAQQAWI-LNATLRdnilfGKEYDEE 180
Cdd:cd03279 18 QVIDFTgLDNNGLFLICGPTGAGKSTILDAItyalYGKTPRYGRQENLRSVFAPGEDTAEVsFTFQLG-----GKKYRVE 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622900610 181 R-----YNSVLNScclrpdlAILPSSDLTEIGERGA-NLSGGQRQRISLARAL 227
Cdd:cd03279 93 RsrgldYDQFTRI-------VLLPQGEFDRFLARPVsTLSGGETFLASLSLAL 138
|
|
| |
