|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
41-1211 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 851.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 41 IYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRLSRTSLGGTTTGQVVNLLSNDLNRFDRCLIHFHFL 120
Cdd:PLN03130 342 IYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 121 WLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKLRLQTALRTDQRVRMMNEIISGIQVIKMYTWERPF 200
Cdd:PLN03130 422 WSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSF 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 201 GKLIGQMRRSEMSSIRQMNLLrGILLSFeiTLGRIAIFVSLLGF---VLGGGELTAERAFCVTAFYNILRRTVSkFFPSG 277
Cdd:PLN03130 502 QSKVQTVRDDELSWFRKAQLL-SAFNSF--ILNSIPVLVTVVSFgvfTLLGGDLTPARAFTSLSLFAVLRFPLF-MLPNL 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 278 MSQFAELLVSMRRITNFMMreeanvidmserrdekAEEEQHLLKEVEKRSYPVgigkepdtlVEIKALRARWGQEQHDLV 357
Cdd:PLN03130 578 ITQAVNANVSLKRLEELLL----------------AEERVLLPNPPLEPGLPA---------ISIKNGYFSWDSKAERPT 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPES-GSVQVSGKYSYASQEPWLFNASVRDNILFGLPMDKQRYRT 436
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYER 712
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 437 VLKRCALERDLELLHG-DGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQL 515
Cdd:PLN03130 713 AIDVTALQHDLDLLPGgDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKT 792
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 516 VILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQLLvestQNSGGGDEIITSP---NLSRQSSALSTKSSN 592
Cdd:PLN03130 793 RVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLM----ENAGKMEEYVEENgeeEDDQTSSKPVANGNA 868
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 593 GSSSSLESMVEKEKPKPSAVSSQESRSGGQIGLSMYKKYFGAGCGVLVFVVLIMLCIGTQILASGGDYFLSYWVKNTASS 672
Cdd:PLN03130 869 NNLKKDSSSKKKSKEGKSVLIKQEERETGVVSWKVLERYKNALGGAWVVMILFLCYVLTEVFRVSSSTWLSEWTDQGTPK 948
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 673 STLDIYY---FTAINVGLVICALLRTLLFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDE-VM 748
Cdd:PLN03130 949 THGPLFYnliYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRnVA 1028
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 749 PAVMLDCIQIFLTLTGIICVLCVTNpwylINTFAMM---LAFYYWRDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPT 825
Cdd:PLN03130 1029 VFVNMFLGQIFQLLSTFVLIGIVST----ISLWAIMpllVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLST 1104
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 826 IRAMGAqqtligqYD-----NYQDLHSSGYYTFV--STSRAFGYYLD-----LFCVAYVISVILHNFFNPPLHNAGQIGL 893
Cdd:PLN03130 1105 IRAYKA-------YDrmaeiNGRSMDNNIRFTLVnmSSNRWLAIRLEtlgglMIWLTASFAVMQNGRAENQAAFASTMGL 1177
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 894 AITQALGMTGMVQWGMRQSAELENAMTSVERVLEYKDLDPEgdfnSPAE---KQPPKSWPKEGKLVTKDLSLRYEPDTns 970
Cdd:PLN03130 1178 LLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSE----APLVienNRPPPGWPSSGSIKFEDVVLRYRPEL-- 1251
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 971 PCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRY 1049
Cdd:PLN03130 1252 PPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIvELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRF 1331
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1050 NLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDA 1129
Cdd:PLN03130 1332 NLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDA 1411
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1130 LIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLTaSKAKVFHGMVMQTGKASFDHLLKVAENTK 1209
Cdd:PLN03130 1412 LIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS-NEGSAFSKMVQSTGAANAQYLRSLVFGGD 1490
|
..
gi 665408680 1210 QN 1211
Cdd:PLN03130 1491 ED 1492
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-1194 |
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: 828.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 18 PLLLAGLIsEFSEHGNGHSYNAQIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRLSRTSLGGTTTG 97
Cdd:TIGR00957 337 PQILSLLI-RFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 98 QVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKLRLQTALRTDQR 177
Cdd:TIGR00957 416 EIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNR 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 178 VRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRG------ILLSFEITLGRIAIFVsllgFVLGGGEL 251
Cdd:TIGR00957 496 IKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAvgtftwVCTPFLVALITFAVYV----TVDENNIL 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 252 TAERAFCVTAFYNILRRTVSkFFPSGMSQFAELLVSMRRITNFMMREEANVidmserrdekaeeeqhllKEVEKRSYPVG 331
Cdd:TIGR00957 572 DAEKAFVSLALFNILRFPLN-ILPMVISSIVQASVSLKRLRIFLSHEELEP------------------DSIERRTIKPG 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 332 IGKEpdtlVEIKALRARWGQEQHDlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQE 411
Cdd:TIGR00957 633 EGNS----ITVHNATFTWARDLPP-TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQ 707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 412 PWLFNASVRDNILFGLPMDKQRYRTVLKRCALERDLELL-HGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDP 490
Cdd:TIGR00957 708 AWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILpSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 491 LSAVDTHVGRHLFDECM--RGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQLLVE------ 562
Cdd:TIGR00957 788 LSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTyapdeq 867
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 563 --------STQNSGGGDEIITSPN-----------LSRQSSALSTK---SSNGSSSSLESMVEKEKPKPSAVSSQESRSG 620
Cdd:TIGR00957 868 qghledswTALVSGEGKEAKLIENgmlvtdvvgkqLQRQLSASSSDsgdQSRHHGSSAELQKAEAKEETWKLMEADKAQT 947
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 621 GQIGLSMYKKYFGAgCGVLVFVVLIMLCIGTQILASGGDYFLSYWVKNTASSST-------LDIYYFTAINVGLVIcaLL 693
Cdd:TIGR00957 948 GQVELSVYWDYMKA-IGLFITFLSIFLFVCNHVSALASNYWLSLWTDDPMVNGTqnntslrLSVYGALGILQGFAV--FG 1024
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 694 RTLLFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTN 773
Cdd:TIGR00957 1025 YSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLAT 1104
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 774 PWYLINTFAMMLAFYYWRDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTF 853
Cdd:TIGR00957 1105 PIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPS 1184
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 854 VSTSRAFGYYLDlfCVAYVISVILHNFFNPPLH--NAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEYKDL 931
Cdd:TIGR00957 1185 IVANRWLAVRLE--CVGNCIVLFAALFAVISRHslSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSET 1262
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 932 DPEGDFNSpAEKQPPKSWPKEGKLVTKDLSLRYEPDTNspCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYN- 1010
Cdd:TIGR00957 1263 EKEAPWQI-QETAPPSGWPPRGRVEFRNYCLRYREDLD--LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESa 1339
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1011 DGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGG 1090
Cdd:TIGR00957 1340 EGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGG 1419
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1091 TNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVE 1170
Cdd:TIGR00957 1420 ENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAE 1499
|
1210 1220
....*....|....*....|....
gi 665408680 1171 FGSPYELLTASkaKVFHGMVMQTG 1194
Cdd:TIGR00957 1500 FGAPSNLLQQR--GIFYSMAKDAG 1521
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
41-1211 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 787.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 41 IYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRLSRTSLGGTTTGQVVNLLSNDLNRFDRCLIHFHFL 120
Cdd:PLN03232 342 VYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 121 WLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKLRLQTALRTDQRVRMMNEIISGIQVIKMYTWERPF 200
Cdd:PLN03232 422 WSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSF 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 201 GKLIGQMRRSEMSSIRQMNLLRGiLLSFeiTLGRIAIFVSLLGF---VLGGGELTAERAFCVTAFYNILRRTVSkFFPSG 277
Cdd:PLN03232 502 ESRIQGIRNEELSWFRKAQLLSA-FNSF--ILNSIPVVVTLVSFgvfVLLGGDLTPARAFTSLSLFAVLRSPLN-MLPNL 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 278 MSQFAELLVSMRRITNFMMREEanvidmserrdekaeeeqhllkEVEKRSYPVgigkEPDT-LVEIKALRARWGQEQHDL 356
Cdd:PLN03232 578 LSQVVNANVSLQRIEELLLSEE----------------------RILAQNPPL----QPGApAISIKNGYFSWDSKTSKP 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPP-ESGSVQVSGKYSYASQEPWLFNASVRDNILFGLPMDKQRYR 435
Cdd:PLN03232 632 TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYW 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 436 TVLKRCALERDLELLHG-DGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQ 514
Cdd:PLN03232 712 RAIDVTALQHDLDLLPGrDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGK 791
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 515 LVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQLLvestQNSGGGDEIITSPNLSRQSSALSTKSSNGS 594
Cdd:PLN03232 792 TRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM----ENAGKMDATQEVNTNDENILKLGPTVTIDV 867
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 595 SSSLESMVEKEKPKPSAVSSQESRSGGQIGLSMYKKYFGAGCGVLVFVVLIMLCIGTQILASGGDYFLSYWVKNTASSST 674
Cdd:PLN03232 868 SERNLGSTKQGKRGRSVLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQSTPKSY 947
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 675 LDIYY---FTAINVGLVICALLRTLLFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAV 751
Cdd:PLN03232 948 SPGFYivvYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANL 1027
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 752 MldciQIFLTLTgiicvlcvtnpWYLINTFAM---------------MLAFYYWRDFYLKTSRDVKRLEAVARSPMYSHF 816
Cdd:PLN03232 1028 M----NMFMNQL-----------WQLLSTFALigtvstislwaimplLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQF 1092
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 817 SATLVGLPTIRAMGAqqtligqYD-----NYQDLHSSGYYTFVSTSRAFGYYLDLFCVAYVI-------SVILHNFFNPP 884
Cdd:PLN03232 1093 GEALNGLSSIRAYKA-------YDrmakiNGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMiwltatfAVLRNGNAENQ 1165
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 885 LHNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEYKDLDPEgdfnSPA---EKQPPKSWPKEGKLVTKDLS 961
Cdd:PLN03232 1166 AGFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSE----ATAiieNNRPVSGWPSRGSIKFEDVH 1241
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 962 LRYEPDTnsPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRSKISIIPQEP 1040
Cdd:PLN03232 1242 LRYRPGL--PPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIvELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSP 1319
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1041 VLFSGTMRYNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEAT 1120
Cdd:PLN03232 1320 VLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1121 ANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLTaSKAKVFHGMVMQTGKASFDH 1200
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS-RDTSAFFRMVHSTGPANAQY 1478
|
1210
....*....|.
gi 665408680 1201 LLKVAENTKQN 1211
Cdd:PLN03232 1479 LSNLVFERREN 1489
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-1179 |
0e+00 |
|
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: 637.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 13 TRATVPLLLAGLISEFSEHgngHSYNAQI-YAVLLIACIL--ASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRLSRT 89
Cdd:TIGR01271 95 TKAVQPLLLGRIIASYDPF---NAPEREIaYYLALGLCLLfiVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 90 SLGGTTTGQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKLRLQ 169
Cdd:TIGR01271 172 VLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDK 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 170 TALRTDQRVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGRIAIFVSLLGFVLGGG 249
Cdd:TIGR01271 252 RAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVFLSVVPYALIKG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 250 eLTAERAFCVTAFYNILRRTVSKFFPSGMSQFAELLVSMRRITNFMMREEANVIdmserrdekaeEEQHLLKEVE----K 325
Cdd:TIGR01271 332 -IILRRIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTL-----------EYNLTTTEVEmvnvT 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 326 RSYPVGIGkepDTLVEIKALRARWGQEQHDL-------------VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGEL 392
Cdd:TIGR01271 400 ASWDEGIG---ELFEKIKQNNKARKQPNGDDglffsnfslyvtpVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGEL 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 393 PPESGSVQVSGKYSYASQEPWLFNASVRDNILFGLPMDKQRYRTVLKRCALERDLELL-HGDGTIVGERGASLSGGQRAR 471
Cdd:TIGR01271 477 EPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFpEKDKTVLGEGGITLSGGQRAR 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 472 ICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLK 551
Cdd:TIGR01271 557 ISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQA 636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 552 SGQDFAQLL--------------------------VESTQNSGGGDE--------------------IITSP-NLSRQSS 584
Cdd:TIGR01271 637 KRPDFSSLLlgleafdnfsaerrnsiltetlrrvsIDGDSTVFSGPEtikqsfkqpppefaekrkqsIILNPiASARKFS 716
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 585 ALSTKSSNGSSSSLES-----------------MVEKEKPKPSAVSS-----------------QESRSGGQI------- 623
Cdd:TIGR01271 717 FVQMGPQKAQATTIEDavrepserkfslvpedeQGEESLPRGNQYHHglqhqaqrrqsvlqlmtHSNRGENRReqlqtsf 796
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 624 --------------GLSMYKKYFGAGCGV----------------------------------------LVFV-VLIMLC 648
Cdd:TIGR01271 797 rkkssitqqnelasELDIYSRRLSKDSVYeiseeineedlkecfaderenvfetttwntylryittnrnLVFVlIFCLVI 876
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 649 IGTQILASGGDYFL--------SYWVKNTASSSTLDI-----------YYFTAINVG----LVICALLRTLLFFNITMHS 705
Cdd:TIGR01271 877 FLAEVAASLLGLWLitdnpsapNYVDQQHANASSPDVqkpviitptsaYYIFYIYVGtadsVLALGFFRGLPLVHTLLTV 956
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 706 STELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMML 785
Cdd:TIGR01271 957 SKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAV 1036
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 786 AFYYWRDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVSTSRAFGYYLD 865
Cdd:TIGR01271 1037 IFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRID 1116
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 866 LFCVAYVISVIlhnFFNPPLHN--AGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEYKDLDPE-------GD 936
Cdd:TIGR01271 1117 IIFVFFFIAVT---FIAIGTNQdgEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEeprpsggGG 1193
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 937 FNSPAE------KQPPKSWPKEGKLVTKDLSLRYEPDTNSpcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYN 1010
Cdd:TIGR01271 1194 KYQLSTvlvienPHAQKCWPSGGQMDVQGLTAKYTEAGRA--VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST 1271
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1011 DGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGG 1090
Cdd:TIGR01271 1272 EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGG 1351
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1091 TNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVE 1170
Cdd:TIGR01271 1352 YVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
....*....
gi 665408680 1171 FGSPYELLT 1179
Cdd:TIGR01271 1432 YDSIQKLLN 1440
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-1206 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 636.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 16 TVPLLLAGLISEFSEHGNGHSYNAQIYAVLLIACILASVLLTHPYMMGMmHLAMKMRVAVSSAIYRKALRLSRTSLG--G 93
Cdd:PTZ00243 262 TLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISI-RCGLQYRSALNALIFEKCFTISSKSLAqpD 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 94 TTTGQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKLRLQTALR 173
Cdd:PTZ00243 341 MNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKA 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 174 TDQRVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGRIAIFVSLLGFVLGGGELTA 253
Cdd:PTZ00243 421 ADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATSFVNNATPTLMIAVVFTVYYLLGHELTP 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 254 ERAFCVTAFYNILRRTvskFF--PSGMSQFAELLVSMRRITNFMMREEA---NVIDMSERRDEKAE-----EEQHLLKEV 323
Cdd:PTZ00243 501 EVVFPTIALLGVLRMP---FFmiPWVFTTVLQFLVSIKRISTFLECDNAtcsTVQDMEEYWREQREhstacQLAAVLENV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 324 EKRSY-PVGIGKEPDTLVEI--KALR-----------------------------------------------------A 347
Cdd:PTZ00243 578 DVTAFvPVKLPRAPKVKTSLlsRALRmlcceqcrptkrhpspsvvvedtdygspssasrhiveggtgggheatptsersA 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 348 RWGQEQHD--------LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLFNASV 419
Cdd:PTZ00243 658 KTPKMKTDdffelepkVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATV 737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 420 RDNILFGLPMDKQRYRTVLKRCALERDLELLHGD-GTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHV 498
Cdd:PTZ00243 738 RGNILFFDEEDAARLADAVRVSQLEADLAQLGGGlETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 499 GRHLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEemlksgqDFAQLLVESTQNSGGGDeiitSPN 578
Cdd:PTZ00243 818 GERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSA-------DFMRTSLYATLAAELKE----NKD 886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 579 LsRQSSALSTKSSNGSSSSLESMVEKEKPKPSAVSS----------------QESRSGGQIGLSMYKKYFGAGCGVLVFV 642
Cdd:PTZ00243 887 S-KEGDADAEVAEVDAAPGGAVDHEPPVAKQEGNAEggdgaaldaaagrlmtREEKASGSVPWSTYVAYLRFCGGLHAAG 965
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 643 VLIMLCIGTQILASGGDYFLSYWVKNTAS-SSTLDIYYFTAINVGLVICALLRTLLFFNITMHSSTELHNTMFQGLSRTA 721
Cdd:PTZ00243 966 FVLATFAVTELVTVSSGVWLSMWSTRSFKlSAATYLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGT 1045
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 722 LYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMMLAFYYWRDFYLKTSRDV 801
Cdd:PTZ00243 1046 MSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREI 1125
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 802 KRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDL-HSSGYYTFVsTSRAFGYYLDLFCVAYVISVILHNF 880
Cdd:PTZ00243 1126 RRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVvYSCSYLENV-ANRWLGVRVEFLSNIVVTVIALIGV 1204
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 881 FNPPL----HNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEYKD---------LDPEGD-----FNSPAE 942
Cdd:PTZ00243 1205 IGTMLratsQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDevphedmpeLDEEVDalerrTGMAAD 1284
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 943 K---------QPPKSWP---KEGKLVTKDLSLRYEPDTnsPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SY 1009
Cdd:PTZ00243 1285 VtgtvviepaSPTSAAPhpvQAGSLVFEGVQMRYREGL--PLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMvEV 1362
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1010 NDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEG 1089
Cdd:PTZ00243 1363 CGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEG 1442
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1090 GTNFSVGQRQLVCLARAIL-RENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHV 1168
Cdd:PTZ00243 1443 GSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAV 1522
|
1290 1300 1310
....*....|....*....|....*....|....*...
gi 665408680 1169 VEFGSPYELLTaSKAKVFHGMVMQTGKASFDHLLKVAE 1206
Cdd:PTZ00243 1523 AEMGSPRELVM-NRQSIFHSMVEALGRSEAKRFLQLVG 1559
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
953-1174 |
3.93e-130 |
|
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: 396.86 E-value: 3.93e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 953 GKLVTKDLSLRYEPdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYN-DGAILIDSLDTNDIGLHDLRS 1031
Cdd:cd03244 1 GDIEFKNVSLRYRP--NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELsSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1032 KISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILREN 1111
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665408680 1112 RILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSP 1174
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
641-1181 |
3.16e-109 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 354.86 E-value: 3.16e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 641 FVVLIMLCIGTQILASGGDYFLSYWVKNTASSSTLD-IYYFTAINVGLV----ICALLRTLLFFNITMHSSTELHNTMFQ 715
Cdd:COG1132 23 LILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSaLLLLLLLLLGLAllraLLSYLQRYLLARLAQRVVADLRRDLFE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 716 GLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMMLAFYYWRDFYL 795
Cdd:COG1132 103 HLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 796 KTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVSTSRAFGYYLDLF---CVAYV 872
Cdd:COG1132 183 RRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLgnlGLALV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 873 ISVILHNFFNPPLhNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEYKDLDPEGDfnSPAEKQPPKswPKE 952
Cdd:COG1132 263 LLVGGLLVLSGSL-TVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP--DPPGAVPLP--PVR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 953 GKLVTKDLSLRYEPDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsY--NDGAILIDSLDTNDIGLHDLR 1030
Cdd:COG1132 338 GEIEFENVSFSYPGDRP---VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF-YdpTSGRILIDGVDIRDLTLESLR 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1031 SKISIIPQEPVLFSGTMRYNL---DPfeQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAI 1107
Cdd:COG1132 414 RQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARAL 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665408680 1108 LRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLTAS 1181
Cdd:COG1132 492 LKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARG 565
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
340-538 |
1.52e-106 |
|
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: 333.28 E-value: 1.52e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQHD--LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLFNA 417
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 418 SVRDNILFGLPMDKQRYRTVLKRCALERDLELL-HGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDT 496
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILpDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 665408680 497 HVGRHLFDECMRGFLGKQ-LVILVTHQLQFLEDADLIVIMDKG 538
Cdd:cd03250 161 HVGRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
637-928 |
1.87e-103 |
|
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: 329.67 E-value: 1.87e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 637 GVLVFVVLIMLCIGTQILASGGDYFLSYWV---------------KNTASSSTLD------IYYFTAINVGLVICALLRT 695
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWAnleeklndttdrvqgENSTNVDIEDldrdfnLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 696 LLFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPW 775
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 776 YLINTFAMMLAFYYWRDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVS 855
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665408680 856 TSRAFGYYLDLFCVAYVISVILHNFFNPPLHNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEY 928
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
18-291 |
1.72e-102 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350037 [Multi-domain] Cd Length: 291 Bit Score: 326.10 E-value: 1.72e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 18 PLLLAGLISEFSEHGNGHSYN-AQIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRLSRTSLGGTTT 96
Cdd:cd18593 17 PIFLGKLIRYFEGNGSSISLTeAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKALRLSQAALGKTTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 97 GQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKLRLQTALRTDQ 176
Cdd:cd18593 97 GQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 177 RVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGRIAIFVSLLGFVLGGGELTAERA 256
Cdd:cd18593 177 RIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLGNILTAERV 256
|
250 260 270
....*....|....*....|....*....|....*
gi 665408680 257 FCVTAFYNILRRTVSKFFPSGMSQFAELLVSMRRI 291
Cdd:cd18593 257 FVTMALYNAVRLTMTLFFPFAIQFGSELSVSIRRI 291
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
3-291 |
1.19e-100 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 320.97 E-value: 1.19e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 3 GITIAALELGTRATVPLLLAGLISEFSEHGNGHSYNAQIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRK 82
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 83 ALRLSRTSLGGTTTGQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRV 162
Cdd:cd18579 82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 163 TSKLRLQTALRTDQRVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGRIAIFVSLL 242
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 665408680 243 GFVLGGGELTAERAFCVTAFYNILRRTVSkFFPSGMSQFAELLVSMRRI 291
Cdd:cd18579 242 TYVLLGNPLTAAKVFTALSLFNLLRFPLL-MLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
641-928 |
3.89e-98 |
|
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: 314.44 E-value: 3.89e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 641 FVVLIMLCIGTQILASGGDYFLSYWVKNTASSSTLD-----IYYFTAINVGLVICALLRTLLFFNITMHSSTELHNTMFQ 715
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSsgyylGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 716 GLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMMLAFYYWRDFYL 795
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 796 KTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVSTSRAFGYYLDLFCVAYVISV 875
Cdd:cd18580 161 RTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 665408680 876 ILHNFFNPPLHNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEY 928
Cdd:cd18580 241 ALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
949-1174 |
2.47e-97 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 308.57 E-value: 2.47e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 949 WPKEGKLVTKDLSLRYEPDtnSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLS-YNDGAILIDSLDTNDIGLH 1027
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPD--LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGKIEIDGIDISTIPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1028 DLRSKISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALEdvhlkeeiselpsglqsiISEGGTNFSVGQRQLVCLARAI 1107
Cdd:cd03369 79 DLRSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 1108 LRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSP 1174
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
9-291 |
5.73e-93 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 300.32 E-value: 5.73e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 9 LELGTRATVPLLLAGLISEFSEHGNGHSYNAQIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRLSR 88
Cdd:cd18594 8 LEESLKIVQPLLLGRLVAYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 89 TSLGGTTTGQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKLRL 168
Cdd:cd18594 88 SALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 169 QTALRTDQRVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGRIAIFVSLLGFVLGG 248
Cdd:cd18594 168 KTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 665408680 249 GELTAERAFCVTAFYNILRRTVSKFFPSGMSQFAELLVSMRRI 291
Cdd:cd18594 248 NTLTARKVFTVISLLNALRMTITRFFPESIQTLSESRVSLKRI 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
606-1178 |
1.04e-84 |
|
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: 291.35 E-value: 1.04e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 606 KPKPSAVSSQESRSGGQ--IGLSM-YKKYFGAGCGVLVFVVLIMLC--IGTQILAsggDYFLSywvknTASSSTLdiyYF 680
Cdd:COG2274 129 EPTPEFDKRGEKPFGLRwfLRLLRrYRRLLLQVLLASLLINLLALAtpLFTQVVI---DRVLP-----NQDLSTL---WV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 681 TAINVGLVICA-----LLRTLLFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFaNDLGQVDEVMP----AV 751
Cdd:COG2274 198 LAIGLLLALLFegllrLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTgsllTA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 752 MLDCIQIFLTLTgiicVLCVTNPWYLINTFAMMLAFYYWRDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGA 831
Cdd:COG2274 277 LLDLLFVLIFLI----VLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 832 QQTLIGQYDNYQDLH----------SSGYYTFVSTSRAFGYYLDLFCVAYviSVILHNFfnpplhNAGQ-------IGLA 894
Cdd:COG2274 353 ESRFRRRWENLLAKYlnarfklrrlSNLLSTLSGLLQQLATVALLWLGAY--LVIDGQL------TLGQliafnilSGRF 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 895 ITQALGMTGMVQwgmrqsaELENAMTSVERVLEYKDLDPEGDFNSPAEKQPPKswpkEGKLVTKDLSLRYEPDtnSPCVL 974
Cdd:COG2274 425 LAPVAQLIGLLQ-------RFQDAKIALERLDDILDLPPEREEGRSKLSLPRL----KGDIELENVSFRYPGD--SPPVL 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 975 KGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsY--NDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNL- 1051
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL-YepTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENIt 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1052 --DPfeQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDA 1129
Cdd:COG2274 571 lgDP--DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEA 648
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 665408680 1130 LIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELL 1178
Cdd:COG2274 649 IILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
953-1191 |
1.51e-74 |
|
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: 247.90 E-value: 1.51e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 953 GKLVTKDLSLRYepDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRS 1031
Cdd:cd03288 18 GEIKIHDLCVRY--ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMvDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1032 KISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILREN 1111
Cdd:cd03288 96 RLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1112 RILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLtASKAKVFHGMVM 1191
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL-AQEDGVFASLVR 254
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
953-1178 |
4.24e-73 |
|
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: 242.52 E-value: 4.24e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 953 GKLVTKDLSLRYEPDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsYN--DGAILIDSLDTNDIGLHDLR 1030
Cdd:cd03254 1 GEIEFENVNFSYDEKKP---VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRF-YDpqKGQILIDGIDIRDISRKSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1031 SKISIIPQEPVLFSGTMRYNLDPFEQYPDDKLW-KALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILR 1109
Cdd:cd03254 77 SMIGVVLQDTFLFSGTIMENIRLGRPNATDEEViEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 1110 ENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELL 1178
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
917-1178 |
1.00e-70 |
|
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: 247.75 E-value: 1.00e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 917 NAMTSVERVLEYKDLDPEgdfnSPAEKQPPKSWPKEGKLVTKDLSLRYEPDTNspcVLKGLSFTIQPMEKVGIVGRTGAG 996
Cdd:COG4988 303 NGIAAAEKIFALLDAPEP----AAPAGTAPLPAAGPPSIELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAG 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 997 KSSLINALFRLSYND-GAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNL---DPfeQYPDDKLWKALEDVHLK 1072
Cdd:COG4988 376 KSTLLNLLLGFLPPYsGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRP--DASDEELEAALEAAGLD 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1073 EEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLN 1152
Cdd:COG4988 454 EFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLA 533
|
250 260
....*....|....*....|....*.
gi 665408680 1153 TIMDSDKVLVMDAGHVVEFGSPYELL 1178
Cdd:COG4988 534 LLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
18-291 |
3.28e-67 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350039 [Multi-domain] Cd Length: 290 Bit Score: 228.51 E-value: 3.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 18 PLLLAGLISeFSEHGNGHSYNAQIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRLSRTSLGGTTTG 97
Cdd:cd18595 17 PQLLKLLIN-FVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKALRLSNSARKKSTVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 98 QVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKLRLQTALRTDQR 177
Cdd:cd18595 96 EIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDER 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 178 VRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGRIAIFVSLLGFVLGGGE--LTAER 255
Cdd:cd18595 176 IKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATYVLSDPDnvLDAEK 255
|
250 260 270
....*....|....*....|....*....|....*.
gi 665408680 256 AFCVTAFYNILRRTVSkFFPSGMSQFAELLVSMRRI 291
Cdd:cd18595 256 AFVSLSLFNILRFPLS-MLPMVISNLVQASVSLKRL 290
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-559 |
1.13e-66 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 236.21 E-value: 1.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 3 GITIAALELGTRATVPLLLAGLISEFSEHGNGHSYNAqiYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRK 82
Cdd:COG1132 26 ALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLL--LLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 83 ALRLSRTSLGGTTTGQVVNLLSNDLNRFDRCLIH-FHFLWLGPLELLIASYFL-YEQIGMAsFYGISILVLYLPLQTYLS 160
Cdd:COG1132 104 LLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHgLPQLVRSVVTLIGALVVLfVIDWRLA-LIVLLVLPLLLLVLRLFG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 161 RVTSKLRLQTALRTDQRVRMMNEIISGIQVIKMYTWE----RPFGKLIGQMRRSEMSSIRQMNLLRGILLSFeITLGRIA 236
Cdd:COG1132 183 RRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREerelERFREANEELRRANLRAARLSALFFPLMELL-GNLGLAL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 237 IFVSLLGFVLGGgELTAERafcVTAFYNILRRTVSKFFPSGM--SQFAELLVSMRRITNFMMREEanviDMSERRDEKAe 314
Cdd:COG1132 262 VLLVGGLLVLSG-SLTVGD---LVAFILYLLRLFGPLRQLANvlNQLQRALASAERIFELLDEPP----EIPDPPGAVP- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 315 eeqhlLKEVEKRsypvgigkepdtlVEIKALRARWGQEQHdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPP 394
Cdd:COG1132 333 -----LPPVRGE-------------IEFENVSFSYPGDRP--VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 395 ESGSVQVSG-------------KYSYASQEPWLFNASVRDNILFGLP-MDKQRYRTVLKRCALERDLELL-HGDGTIVGE 459
Cdd:COG1132 393 TSGRILIDGvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGRPdATDEEVEEAAKAAQAHEFIEALpDGYDTVVGE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 460 RGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDEcMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGH 539
Cdd:COG1132 473 RGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA-LERLMKGRTTIVIAHRLSTIRNADRILVLDDGR 551
|
570 580
....*....|....*....|
gi 665408680 540 VSACGTYEEMLKSGQDFAQL 559
Cdd:COG1132 552 IVEQGTHEELLARGGLYARL 571
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
641-928 |
7.10e-65 |
|
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: 221.97 E-value: 7.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 641 FVVLIMLCIGTQILASGGDYFLSYW----VKNTASSSTLDIYY---FTAINVGLVICALLRTLLFFNITMHSSTELHNTM 713
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWsddpALNGTQDTEQRDYRlgvYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 714 FQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMMLAFYYWRDF 793
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 794 YLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVSTSRAFGYYLDL------F 867
Cdd:cd18603 161 YVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFlgnlivL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665408680 868 CVAyVISVILHNFFNPplhnaGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEY 928
Cdd:cd18603 241 FAA-LFAVLSRDSLSP-----GLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEY 295
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
641-928 |
8.45e-65 |
|
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: 221.57 E-value: 8.45e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 641 FVVLIMLCIGTQILASGGDYFLSYWVKNTASSSTLD------IYY---FTAINVGLVICALLRTLLFFNITMHSSTELHN 711
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPpsevsvLYYlgiYALISLLSVLLGTLRYLLFFFGSLRASRKLHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 712 TMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMMLAFYYWR 791
Cdd:cd18604 81 RLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 792 DFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVSTSRAFGYYLDL----- 866
Cdd:cd18604 161 RLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLlgalf 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665408680 867 --FCVAYVISVilhnffnpPLHNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEY 928
Cdd:cd18604 241 sfATAALLVYG--------PGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEY 296
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
641-928 |
1.66e-63 |
|
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: 217.73 E-value: 1.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 641 FVVLIMLCIGTQILASGGDYFLSYWVKNTASSST---LDIYyfTAINVGLVICALLRTLLFFNITMHSSTELHNTMFQGL 717
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTEDFFGLSQgfyIGIY--AGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 718 SRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMMLAFYYWRDFYLKT 797
Cdd:cd18606 79 LRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 798 SRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVSTSRAFGYYLD-----------L 866
Cdd:cd18606 159 SRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDllgsllvlivaL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408680 867 FCVAYVISVilhnffnpplhNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEY 928
Cdd:cd18606 239 LCVTRRFSI-----------SPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
14-291 |
1.92e-63 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 217.71 E-value: 1.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 14 RATVPLLLAGLIS-------EFSEHGNGHSYnaqIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRL 86
Cdd:cd18597 13 QVLSPLLLKYLINfvedaylGGPPPSIGYGI---GYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAIYRKSLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 87 SRTSLGGTTTGQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKL 166
Cdd:cd18597 90 SGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFLMKKLFKL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 167 RLQTALRTDQRVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLgriAIFVSLLGFV- 245
Cdd:cd18597 170 RKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSL---PVLASMLSFIt 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 665408680 246 --LGGGELTAERAFCVTAFYNILRRTVSkFFPSGMSQFAELLVSMRRI 291
Cdd:cd18597 247 yyATGHTLDPANIFSSLALFNVLRMPLM-FLPLALSSLADALVALKRI 293
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
955-1167 |
4.55e-61 |
|
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: 206.08 E-value: 4.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYePDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRSKI 1033
Cdd:cd03228 1 IEFKNVSFSY-PGRPKP-VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLyDPTSGEILIDGVDLRDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1034 SIIPQEPVLFSGTMRYNLdpfeqypddklwkaledvhlkeeiselpsglqsiiseggtnFSVGQRQLVCLARAILRENRI 1113
Cdd:cd03228 79 AYVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 665408680 1114 LVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGH 1167
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
958-1189 |
5.77e-60 |
|
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: 205.54 E-value: 5.77e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPdtNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsY--NDGAILIDSLDTNDIGLHDLRSKISI 1035
Cdd:cd03253 4 ENVTFAYDP--GRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRF-YdvSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1036 IPQEPVLFSGTMRYNLdpfeQY-----PDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRE 1110
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 1111 NRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLtaSKAKVFHGM 1189
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL--AKGGLYAEM 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
958-1178 |
8.07e-59 |
|
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: 202.08 E-value: 8.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPDTNSpcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRSKISII 1036
Cdd:cd03251 4 KNVTFRYPGDGPP--VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFyDVDSGRILIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1037 PQEPVLFSGTMRYNL---DPFEqyPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRI 1113
Cdd:cd03251 82 SQDVFLFNDTVAENIaygRPGA--TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 1114 LVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELL 1178
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
953-1179 |
9.64e-59 |
|
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: 203.55 E-value: 9.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 953 GKLVTKDLSLRYEPDTNSpcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAILIDSLDTNDIGLHDLRSK 1032
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA--VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1033 ISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENR 1112
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 1113 ILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLT 1179
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
43-559 |
2.49e-58 |
|
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: 215.08 E-value: 2.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 43 AVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRLSRTSLGGTTTGQVVNLLsNDLNRFDRclihfhFLWL 122
Cdd:COG2274 199 AIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIRE------FLTG 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 123 GPLELLIASYF--LYeqIGMASFYGIS---ILVLYLPLQTYLSRVTSKLRLQTALRT----DQRVRMMNEIISGIQVIKM 193
Cdd:COG2274 272 SLLTALLDLLFvlIF--LIVLFFYSPPlalVVLLLIPLYVLLGLLFQPRLRRLSREEseasAKRQSLLVETLRGIETIKA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 194 Y--------TWERPFGKLIGQMRRSEMSSIRQMNLLRGIllsfeITLGRIAIFVslLG--FVLGG----GELTAerafcv 259
Cdd:COG2274 350 LgaesrfrrRWENLLAKYLNARFKLRRLSNLLSTLSGLL-----QQLATVALLW--LGayLVIDGqltlGQLIA------ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 260 taFYNILRRTVSKF--FPSGMSQFAELLVSMRRITNFMmreeanvidmsERRDEKAEEEQHLLKEVEKRSypvgigkepd 337
Cdd:COG2274 417 --FNILSGRFLAPVaqLIGLLQRFQDAKIALERLDDIL-----------DLPPEREEGRSKLSLPRLKGD---------- 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 338 tlVEIKALRARWGqEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY------------ 405
Cdd:COG2274 474 --IELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDlrqidpaslrrq 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 406 -SYASQEPWLFNASVRDNILFGLP-MDKQRYRTVLKRCALERDLELL-HGDGTIVGERGASLSGGQRARICLARAVYRRA 482
Cdd:COG2274 551 iGVVLQDVFLFSGTIRENITLGDPdATDEEIIEAARLAGLHDFIEALpMGYDTVVGEGGSNLSGGQRQRLAIARALLRNP 630
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 483 DVYLLDDPLSAVDTHVGRHlFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 559
Cdd:COG2274 631 RILILDEATSALDAETEAI-ILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
358-538 |
1.33e-57 |
|
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: 198.32 E-value: 1.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY-----------------SYASQEPWLFNASVR 420
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNesepsfeatrsrnrysvAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 421 DNILFGLPMDKQRYRTVLKRCALERDLELL-HGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVG 499
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTDACSLQPDIDLLpFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 665408680 500 RHLFDECMRGFL--GKQLVILVTHQLQFLEDADLIVIMDKG 538
Cdd:cd03290 177 DHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
637-928 |
2.75e-57 |
|
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: 200.87 E-value: 2.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 637 GVLVFVVLIMLCIGTQILASGGDYFLSYWVK----NTASSSTLDIYYFTAIN----------------VGLVICALLRTL 696
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKqgsgNTTNNVDNSTVDSGNISdnpdlnfyqlvyggsiLVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 697 LFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWY 776
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 777 LINTFAMMLAFYYWRDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVST 856
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408680 857 SRAFGYYLDLFCVAYVISVILHNFFNPPLHNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEY 928
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEY 312
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
958-1192 |
4.24e-57 |
|
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: 197.38 E-value: 4.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRY--EPDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsY--NDGAILIDSLDTNDIGLHDLRSKI 1033
Cdd:cd03249 4 KNVSFRYpsRPDVP---ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERF-YdpTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1034 SIIPQEPVLFSGTMRYNL---DPFEQYPDDKlwKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRE 1110
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygKPDATDEEVE--EAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1111 NRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLtaSKAKVFHGMV 1190
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELM--AQKGVYAKLV 235
|
..
gi 665408680 1191 MQ 1192
Cdd:cd03249 236 KA 237
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
895-1178 |
7.48e-57 |
|
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: 208.14 E-value: 7.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 895 ITQALGMTGMVQWGMRQsaelenAMTSVERVLEYKDLDPEgdfnsPAEK-QPPKSWPKEGKLVTKDLSLRYEPDtnSPcV 973
Cdd:COG5265 308 LYIPLNFLGFVYREIRQ------ALADMERMFDLLDQPPE-----VADApDAPPLVVGGGEVRFENVSFGYDPE--RP-I 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 974 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsY--NDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNL 1051
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF-YdvTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1052 dpfeQY-----PDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQ 1126
Cdd:COG5265 453 ----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSR 528
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 665408680 1127 TDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELL 1178
Cdd:COG5265 529 TERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELL 580
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
640-928 |
2.94e-56 |
|
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: 197.83 E-value: 2.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 640 VFVVLImLCIGTQILASGGDYFLSYW----------VKNTASSSTLD---IYY---FTAINVGLVICALLRTLLFFNITM 703
Cdd:cd18602 1 VALVLA-LALLKQGLRVATDFWLADWteanhdvasvVFNITSSSLEDdevSYYisvYAGLSLGAVILSLVTNLAGELAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 704 HSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAvMLDCI--QIFLTLTGIICVLCVTnPWYLINTF 781
Cdd:cd18602 80 RAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPT-TLERLlrFLLLCLSAIIVNAIVT-PYFLIALI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 782 AMMLAFYYWRDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVSTSRAFG 861
Cdd:cd18602 158 PIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLG 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665408680 862 YYLD------LFCVAYV-ISVILHNFFNPplhnaGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEY 928
Cdd:cd18602 238 IRLDylgaviVFLAALSsLTAALAGYISP-----SLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
19-553 |
8.44e-56 |
|
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: 204.22 E-value: 8.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 19 LLLAGLISEFSeHGNGHSYNAQIYAVLLIACILASVLLThpYMMGMM--HLAMKMRVAVSSAIYRKALRLSRTSLGGTTT 96
Cdd:COG4988 38 WLLASLLAGLI-IGGAPLSALLPLLGLLLAVLLLRALLA--WLRERAafRAAARVKRRLRRRLLEKLLALGPAWLRGKST 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 97 GQVVNLLSNDLNRFDRCLIHFH---FLW-LGPLELLIASYFLYEQIGMasfygisILVLYLPLqTYLSRVTSKLRLQTAL 172
Cdd:COG4988 115 GELATLLTEGVEALDGYFARYLpqlFLAaLVPLLILVAVFPLDWLSGL-------ILLVTAPL-IPLFMILVGKGAAKAS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 173 RtDQRVRMMN------EIISGIQVIKMYTWERPFGKLIGQM----RRSEMSSIRqMNLLRGILLSFEITLGrIAIFVSLL 242
Cdd:COG4988 187 R-RQWRALARlsghflDRLRGLTTLKLFGRAKAEAERIAEAsedfRKRTMKVLR-VAFLSSAVLEFFASLS-IALVAVYI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 243 GFVLGGGELTAERAFCV----TAFYNILRrTVSKFFPSGMsqfaELLVSMRRItnfmmreeANVIDMSERRDEKAEEEQH 318
Cdd:COG4988 264 GFRLLGGSLTLFAALFVlllaPEFFLPLR-DLGSFYHARA----NGIAAAEKI--------FALLDAPEPAAPAGTAPLP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 319 LLKEVEkrsypvgigkepdtlVEIKALRARWGQEQHdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGS 398
Cdd:COG4988 331 AAGPPS---------------IELEDVSFSYPGGRP--ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 399 VQVSG-------------KYSYASQEPWLFNASVRDNILFGLP-MDKQRYRTVLKRCALERDLELL-HGDGTIVGERGAS 463
Cdd:COG4988 394 ILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRPdASDEELEAALEAAGLDEFVAALpDGLDTPLGEGGRG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 464 LSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDEcMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSAC 543
Cdd:COG4988 474 LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQ 552
|
570
....*....|
gi 665408680 544 GTYEEMLKSG 553
Cdd:COG4988 553 GTHEELLAKN 562
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
686-1180 |
1.60e-55 |
|
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: 203.41 E-value: 1.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 686 GLVICALLRTLLFFNITMH----SSTELHN---TMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQI 758
Cdd:TIGR02203 59 VVIGLAVLRGICSFVSTYLlswvSNKVVRDirvRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 759 FLTLTGIICVLCVTNpWYLINTFAMML-----AFYYWRDFYLKTSRDVKRLEAVArspMYShFSATLVGLPTIRAMGAQQ 833
Cdd:TIGR02203 139 TLTVIGLFIVLLYYS-WQLTLIVVVMLpvlsiLMRRVSKRLRRISKEIQNSMGQV---TTV-AEETLQGYRVVKLFGGQA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 834 TLIGQYDNYQDlHSSGYYTFVSTSRAFGYYLDLFCVAYVISVILHNFFNPPLHNAGQIGlaiTQALGMTGMVQW--GMRQ 911
Cdd:TIGR02203 214 YETRRFDAVSN-RNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAG---DFTAFITAMIALirPLKS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 912 SAELENAM----TSVERVLEYKDLDPEGDfnsPAEKQPPKSwpkEGKLVTKDLSLRYePDTNSPcVLKGLSFTIQPMEKV 987
Cdd:TIGR02203 290 LTNVNAPMqrglAAAESLFTLLDSPPEKD---TGTRAIERA---RGDVEFRNVTFRY-PGRDRP-ALDSISLVIEPGETV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 988 GIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNL---DPfEQYPDDKLW 1063
Cdd:TIGR02203 362 ALVGRSGSGKSTLVNLIPRFYEPDsGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQADRAEIE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1064 KALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCT 1143
Cdd:TIGR02203 441 RALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRT 520
|
490 500 510
....*....|....*....|....*....|....*..
gi 665408680 1144 VLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLTA 1180
Cdd:TIGR02203 521 TLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
357-561 |
3.64e-55 |
|
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: 193.53 E-value: 3.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLFNASVRDNILFGLPMDKQRYRT 436
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 437 VLKRCALERDL-ELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQL 515
Cdd:cd03291 132 VVKACQLEEDItKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKT 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 665408680 516 VILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQLLV 561
Cdd:cd03291 212 RILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLM 257
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
70-560 |
3.86e-52 |
|
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: 193.44 E-value: 3.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 70 KMRVAVssaiYRKALRLSRTSLGGTTTGQVVNLLSNDLNRFD----RCLIHFHFLWLGPLELLIASYFLYEQIG--MASF 143
Cdd:COG4987 89 DLRVRL----YRRLEPLAPAGLARLRSGDLLNRLVADVDALDnlylRVLLPLLVALLVILAAVAFLAFFSPALAlvLALG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 144 YGISILVLYLpLQTYLSRVTSklRLQTALRTDQRVRMMnEIISGIQVIKMY----TWERPFGKLIGQMRRSEmssiRQMN 219
Cdd:COG4987 165 LLLAGLLLPL-LAARLGRRAG--RRLAAARAALRARLT-DLLQGAAELAAYgaldRALARLDAAEARLAAAQ----RRLA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 220 LLRGI---LLSFEITLGRIAIFVSLLGFVLGG---GELTAERAFCVTAFYNILRRtvskfFPSGMSQFAELLVSMRRItn 293
Cdd:COG4987 237 RLSALaqaLLQLAAGLAVVAVLWLAAPLVAAGalsGPLLALLVLAALALFEALAP-----LPAAAQHLGRVRAAARRL-- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 294 fmmreeANVIDMSERRDEKAEEEQHllkevekrsypvgigkEPDTLVEIKALRARWGQEQHDlVLNNVNMSLRRGQLVAV 373
Cdd:COG4987 310 ------NELLDAPPAVTEPAEPAPA----------------PGGPSLELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 374 IGPVGSGKSSLIQAILGELPPESGSVQVSGK-------------YSYASQEPWLFNASVRDNILFGLPM-DKQRYRTVLK 439
Cdd:COG4987 367 VGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrdldeddlrrrIAVVPQRPHLFDTTLRENLRLARPDaTDEELWAALE 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 440 RCALERDLE-LLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDEcMRGFLGKQLVIL 518
Cdd:COG4987 447 RVGLGDWLAaLPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAGRTVLL 525
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 665408680 519 VTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQLL 560
Cdd:COG4987 526 ITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLY 567
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
41-291 |
1.12e-51 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350036 [Multi-domain] Cd Length: 287 Bit Score: 183.92 E-value: 1.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 41 IYAVLLIAC-ILASVLLTHPYMMGMmHLAMKMRVAVSSAIYRKALRLSrtSLGGTTTGQVVNLLSNDLNR-FDRCLIhFH 118
Cdd:cd18592 40 LLVLGLFLTeLLRSLFFSLTWAISY-RTGIRLRGAVLGLLYKKILRLR--SLGDKSVGELINIFSNDGQRlFDAAVF-GP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 119 FLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKLRLQTALRTDQRVRMMNEIISGIQVIKMYTWER 198
Cdd:cd18592 116 LVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 199 PFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGRIAIFVSLLGFVLGGGELTAERAFCVTAFYNILRRTVSkFFPSGM 278
Cdd:cd18592 196 PFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLAHVALGNDLTAAQAFTVIAVFNSMRFSLR-MLPYAV 274
|
250
....*....|...
gi 665408680 279 SQFAELLVSMRRI 291
Cdd:cd18592 275 KALAEAKVALQRI 287
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
638-928 |
1.27e-51 |
|
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: 183.89 E-value: 1.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 638 VLVFVVLIMLCIGTQILasgGDYFLSYWVKNTASSSTLDI-----YY---FTAINVGLVICALLRTLLFFNITMHSSTEL 709
Cdd:cd18605 1 LILILLSLILMQASRNL---IDFWLSYWVSHSNNSFFNFIndsfnFFltvYGFLAGLNSLFTLLRAFLFAYGGLRAARRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 710 HNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMMLAFYY 789
Cdd:cd18605 78 HNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 790 WRDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQY----DNYQDlhssgyyTFVSTSRA---FGY 862
Cdd:cd18605 158 IQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYleklENNQR-------AQLASQAAsqwLSI 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408680 863 YLDL------FCVAyVISVILHnFFNPPLhNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEY 928
Cdd:cd18605 231 RLQLlgvlivTFVA-LTAVVQH-FFGLSI-DAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
18-291 |
5.46e-49 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 176.92 E-value: 5.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 18 PLLLAGLISEFSEHGNGHSYNAQIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRL----------- 86
Cdd:cd18596 17 PFFLNRLLRYLEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKALRRrdksgssksse 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 87 --------SRTSLGGTTTGQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTY 158
Cdd:cd18596 97 skkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLLLPLNGY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 159 LSRVTSKLRLQTALRTDQRVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLrGILLSFeITLGrIAIF 238
Cdd:cd18596 177 LAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLL-DLLLSL-LWFL-IPIL 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 239 VSLLGF----VLGGGELTAERAF-CVTAFyNILRRTVSkFFPSGMSQFAELLVSMRRI 291
Cdd:cd18596 254 VTVVTFatytLVMGQELTASVAFtSLALF-NMLRGPLN-VLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
18-291 |
5.94e-49 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350042 [Multi-domain] Cd Length: 288 Bit Score: 175.82 E-value: 5.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 18 PLLLAGLIsEFSEHGNGHSYNAQIYAVLLIA-CILASVLLTHpYMMGMMHLAMKMRVAVSSAIYRKALRLSRTSLGGTTT 96
Cdd:cd18598 17 PLLLNKLV-EFLEDSSEPLSDGYLYALGLVLsSLLGALLSSH-YNFQMNKVSLKVRAALVTAVYRKALRVRSSSLSKFST 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 97 GQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLS----RVTSKLRLQtal 172
Cdd:cd18598 95 GEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAkrigALSEKMMKH--- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 173 rTDQRVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGriaIFVSLLGF---VLGGG 249
Cdd:cd18598 172 -KDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTP---VLISILTFatyVLMGN 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 665408680 250 ELTAERAFCVTAFYNILrrtvskFFPsgMSQFA-------ELLVSMRRI 291
Cdd:cd18598 248 TLTAAKVFTSLALFNML------IGP--LNAFPwvlnglvEAWVSLKRL 288
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
699-1179 |
2.55e-47 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 181.84 E-value: 2.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 699 FNITM-HSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPavmlDCIQIFL-TLTGIICVLC--VTNP 774
Cdd:TIGR00958 225 FNYTMaRINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLS----LNVNVLLrNLVMLLGLLGfmLWLS 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 775 WYL-----INTFAMMLAFYYWRDFYLKTSRDVKrlEAVARSPMYSHfsATLVGLPTIRAMGAQQTligqydnyqdlHSSG 849
Cdd:TIGR00958 301 PRLtmvtlINLPLVFLAEKVFGKRYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFAAEEG-----------EASR 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 850 YYTFVSTSRAFGYYLDLFCVAYV-ISVILHNF-FNPPLHNAGQigLAITQALGMTGMVQWGMRQS-------------AE 914
Cdd:TIGR00958 366 FKEALEETLQLNKRKALAYAGYLwTTSVLGMLiQVLVLYYGGQ--LVLTGKVSSGNLVSFLLYQEqlgeavrvlsyvySG 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 915 LENAMTSVERVLEYKDLDPEgdFNSPAEKQPPkswPKEGKLVTKDLSLRYEPDTNSPcVLKGLSFTIQPMEKVGIVGRTG 994
Cdd:TIGR00958 444 MMQAVGASEKVFEYLDRKPN--IPLTGTLAPL---NLEGLIEFQDVSFSYPNRPDVP-VLKGLTFTLHPGEVVALVGPSG 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 995 AGKSSLINALFRLsY--NDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNLD-PFEQYPDDKLWKALEDVHL 1071
Cdd:TIGR00958 518 SGKSTVAALLQNL-YqpTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAAAKAANA 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1072 KEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATirNKFKDCTVLTIAHRL 1151
Cdd:TIGR00958 597 HDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRL 674
|
490 500
....*....|....*....|....*...
gi 665408680 1152 NTIMDSDKVLVMDAGHVVEFGSPYELLT 1179
Cdd:TIGR00958 675 STVERADQILVLKKGSVVEMGTHKQLME 702
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
914-1179 |
7.61e-47 |
|
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: 180.52 E-value: 7.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 914 ELENAMTSVERVLEYKdLDPEGDFNSPAEKQPPKSWPKEGKLVTKDLSLRYEPdTNSPcVLKGLSFTIQPMEKVGIVGRT 993
Cdd:TIGR03796 438 ELEGDLNRLDDVLRNP-VDPLLEEPEGSAATSEPPRRLSGYVELRNITFGYSP-LEPP-LIENFSLTLQPGQRVALVGGS 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 994 GAGKSS---LINALFRLSynDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNL---DPfeQYPDDKLWKALE 1067
Cdd:TIGR03796 515 GSGKSTiakLVAGLYQPW--SGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLtlwDP--TIPDADLVRACK 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1068 DVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNkfKDCTVLTI 1147
Cdd:TIGR03796 591 DAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIV 668
|
250 260 270
....*....|....*....|....*....|..
gi 665408680 1148 AHRLNTIMDSDKVLVMDAGHVVEFGSPYELLT 1179
Cdd:TIGR03796 669 AHRLSTIRDCDEIIVLERGKVVQRGTHEELWA 700
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
960-1180 |
2.05e-46 |
|
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: 166.89 E-value: 2.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 960 LSLRYEPDtnSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSY-NDGAILIDSLDTNDIGLHDLRSKISIIPQ 1038
Cdd:cd03252 6 VRFRYKPD--GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVpENGRVLVDGHDLALADPAWLRRQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1039 EPVLFSGTMRYNLDPFEQYPD-DKLWKA--LEDVHlkEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILV 1115
Cdd:cd03252 84 ENVLFNRSIRDNIALADPGMSmERVIEAakLAGAH--DFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 1116 MDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLTA 1180
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
953-1169 |
1.66e-44 |
|
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: 160.45 E-value: 1.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 953 GKLVTKDLSLRYEPDTNSpcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsY--NDGAILIDSLDTNDIGLHDLR 1030
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIP--ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL-YkpTSGSVLLDGTDIRQLDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1031 SKISIIPQEPVLFSGTMRYNLDPFEQYPDD-KLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILR 1109
Cdd:cd03245 78 RNIGYVPQDVTLFYGTLRDNITLGAPLADDeRILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1110 ENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVV 1169
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
340-539 |
2.10e-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: 158.32 E-value: 2.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQHdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------KYS 406
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 407 YASQEPWLFNASVRDNIlfglpmdkqryrtvlkrcalerdlellhgdgtivgergasLSGGQRARICLARAVYRRADVYL 486
Cdd:cd03228 80 YVPQDPFLFSGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 665408680 487 LDDPLSAVDTHvGRHLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGH 539
Cdd:cd03228 120 LDEATSALDPE-TEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
911-1180 |
1.13e-43 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 168.74 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 911 QSAELENAMTSVERVLEYKDlDPEGDFNSpaEKQPPKSwpkeGKLVTKDLSLRYEPDTNspcVLKGLSFTIQPMEKVGIV 990
Cdd:PRK10790 304 QQSMLQQAVVAGERVFELMD-GPRQQYGN--DDRPLQS----GRIDIDNVSFAYRDDNL---VLQNINLSVPSRGFVALV 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 991 GRTGAGKSSLINALfrLSY---NDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALE 1067
Cdd:PRK10790 374 GHTGSGKSTLASLL--MGYyplTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1068 DVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTI 1147
Cdd:PRK10790 452 TVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVI 531
|
250 260 270
....*....|....*....|....*....|...
gi 665408680 1148 AHRLNTIMDSDKVLVMDAGHVVEFGSPYELLTA 1180
Cdd:PRK10790 532 AHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
912-1163 |
1.82e-43 |
|
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: 166.69 E-value: 1.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 912 SAELENAMTSVERVLEYKDLdpegdfnsPAEKQPPKSWPKEGKLVTKDLSLRYEpdtNSPCVLKGLSFTIQPMEKVGIVG 991
Cdd:TIGR02857 287 RADGVAAAEALFAVLDAAPR--------PLAGKAPVTAAPASSLEFSGVSVAYP---GRRPALRPVSFTVPPGERVALVG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 992 RTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNLDPFEQY-PDDKLWKALEDV 1069
Cdd:TIGR02857 356 PSGAGKSTLLNLLLGFvDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDaSDAEIREALERA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1070 HLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAH 1149
Cdd:TIGR02857 436 GLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH 515
|
250
....*....|....
gi 665408680 1150 RLNTIMDSDKVLVM 1163
Cdd:TIGR02857 516 RLALAALADRIVVL 529
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
912-1178 |
8.06e-43 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 165.96 E-value: 8.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 912 SAELENAMTSVERVLEYKDLDPEGDfNSPAEKQPPKswpkeGKLVTKDLSLRYePDTNSPcVLKGLSFTIQPMEKVGIVG 991
Cdd:PRK11176 305 NAQFQRGMAACQTLFAILDLEQEKD-EGKRVIERAK-----GDIEFRNVTFTY-PGKEVP-ALRNINFKIPAGKTVALVG 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 992 RTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNLD--PFEQYPDDKLWKALED 1068
Cdd:PRK11176 377 RSGSGKSTIANLLTRFyDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARM 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1069 VHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIA 1148
Cdd:PRK11176 457 AYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA 536
|
250 260 270
....*....|....*....|....*....|
gi 665408680 1149 HRLNTIMDSDKVLVMDAGHVVEFGSPYELL 1178
Cdd:PRK11176 537 HRLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
953-1190 |
1.22e-42 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 167.06 E-value: 1.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 953 GKLVTKDLSLRYEPDtnSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLinalFRL-----SYNDGAILIDSLDTNDIGLH 1027
Cdd:TIGR03797 450 GAIEVDRVTFRYRPD--GPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRLllgfeTPESGSVFYDGQDLAGLDVQ 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1028 DLRSKISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAI 1107
Cdd:TIGR03797 524 AVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARAL 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1108 LRENRILVMDEATANVDPQTDALIQATIrNKFKdCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELltASKAKVFH 1187
Cdd:TIGR03797 604 VRKPRILLFDEATSALDNRTQAIVSESL-ERLK-VTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDEL--MAREGLFA 679
|
...
gi 665408680 1188 GMV 1190
Cdd:TIGR03797 680 QLA 682
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
661-1151 |
3.13e-42 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 163.30 E-value: 3.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 661 FLSYWVKNTASSSTLDIYYFTAInVGLVICALLRTLLFF-------NITMHSSTELHNTMFQGLSRTALYFFHTNPSGRI 733
Cdd:TIGR02868 34 GVSAWLISRAAEMPPVLYLSVAA-VAVRAFGIGRAVFRYlerlvghDAALRSLGALRVRVYERLARQALAGRRRLRRGDL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 734 LNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMML-AFYYWRDFYLKTSRDVKRLEAVARSPM 812
Cdd:TIGR02868 113 LGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLlAGFVAPLVSLRAARAAEQALARLRGEL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 813 YSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDlhssgYYTFVSTSRAFGYYLD-----LFCVAYVISVILhnfFNPPLHN 887
Cdd:TIGR02868 193 AAQLTDALDGAAELVASGALPAALAQVEEADR-----ELTRAERRAAAATALGaaltlLAAGLAVLGALW---AGGPAVA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 888 AGQIG-----------LAITQALG-MTGMVQwgmrqsaELENAMTSVERVLEYkdLDPEGDFNSPAEKQPPKSWPKEGKL 955
Cdd:TIGR02868 265 DGRLApvtlavlvllpLAAFEAFAaLPAAAQ-------QLTRVRAAAERIVEV--LDAAGPVAEGSAPAAGAVGLGKPTL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 956 VTKDLSLRYEPDtnsPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFR-LSYNDGAILIDSLDTNDIGLHDLRSKIS 1034
Cdd:TIGR02868 336 ELRDLSAGYPGA---PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGlLDPLQGEVTLDGVPVSSLDQDEVRRRVS 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1035 IIPQEPVLFSGTMRYNLD-PFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRI 1113
Cdd:TIGR02868 413 VCAQDAHLFDTTVRENLRlARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPI 492
|
490 500 510
....*....|....*....|....*....|....*...
gi 665408680 1114 LVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRL 1151
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
977-1180 |
5.90e-42 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 163.48 E-value: 5.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 977 LSFTIQPMEKVGIVGRTGAGKSSLINAL--FrLSYNdGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNL--- 1051
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALlgF-LPYQ-GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllg 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1052 DPfeQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALI 1131
Cdd:PRK11174 447 NP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 665408680 1132 QATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLTA 1180
Cdd:PRK11174 525 MQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQA 573
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
952-1168 |
1.48e-41 |
|
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: 152.24 E-value: 1.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 952 EGKLVTKDLSLRY--EPDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHD 1028
Cdd:cd03248 9 KGIVKFQNVTFAYptRPDTL---VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFyQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1029 LRSKISIIPQEPVLFSGTMRYNLD-PFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAI 1107
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665408680 1108 LRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHV 1168
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
356-559 |
4.57e-41 |
|
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: 151.48 E-value: 4.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 356 LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------KYSYASQEPWLFNASVRDN 422
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 423 ILFGLP-MDKQRYRTVLKRC-ALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHvGR 500
Cdd:cd03252 96 IALADPgMSMERVIEAAKLAgAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE-SE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 501 HLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 559
Cdd:cd03252 175 HAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
952-1178 |
8.52e-40 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 157.04 E-value: 8.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 952 EGKLVTKDLSLRYEpdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLR 1030
Cdd:PRK13657 332 KGAVEFDDVSFSYD---NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVfDPQSGRILIDGTDIRTVTRASLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1031 SKISIIPQEPVLFSGTMRYNLD-PFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILR 1109
Cdd:PRK13657 409 RNIAVVFQDAGLFNRSIEDNIRvGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 1110 ENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELL 1178
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELV 557
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
350-544 |
1.01e-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: 146.97 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 350 GQEQHdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------KYSYASQEPWLFN 416
Cdd:cd03245 14 NQEIP--ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 417 ASVRDNILFGLPM-DKQRYRTVLKRCALErDLELLHGDG--TIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSA 493
Cdd:cd03245 92 GTLRDNITLGAPLaDDERILRAAELAGVT-DFVNKHPNGldLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 665408680 494 VDTHVGRHLFDEcMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACG 544
Cdd:cd03245 171 MDMNSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
628-928 |
5.28e-39 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350044 [Multi-domain] Cd Length: 324 Bit Score: 148.41 E-value: 5.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 628 YKKYFGAGCGVLVFVVLIMLCIGTQILASGGDYFL---SYWVKNTASS-----------STLDIYYFTAINVG----LVI 689
Cdd:cd18600 6 YLRYITSHKSLIFVLILCLVIFAIEVAASLVGLWLlrsQADRVNTTRPesssntyavivTFTSSYYVFYIYVGvadsLLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 690 CALLRTLLFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVL 769
Cdd:cd18600 86 MGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 770 CVTNPWYLINTFAMMLAFYYWRDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSG 849
Cdd:cd18600 166 SILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTAN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 850 YYTFVSTSRAFGYYLDLFCVAYVISV----ILHNFFNPplhnaGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERV 925
Cdd:cd18600 246 WFLYLSTLRWFQMRIEMIFVIFFTAVtfisIGTTGDGE-----GRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
...
gi 665408680 926 LEY 928
Cdd:cd18600 321 FKF 323
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-535 |
2.62e-38 |
|
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: 151.29 E-value: 2.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 20 LLAGLISEFSEHGNG-HSYNAQIYAVLLIACILASVLLTHPYMMgmMHLAMKMRVAVSSAIYRKALRLSRTSLGGTTTGQ 98
Cdd:TIGR02857 25 LLARVVDGLISAGEPlAELLPALGALALVLLLRALLGWLQERAA--ARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 99 VVNLLSNDL----NRFDRCLIHFHFLWLGPLELLIAsyflyeqIGMASFYGISILVLYLPLQTYLSRVTSKlrlQTALRT 174
Cdd:TIGR02857 103 LATLALEGVealdGYFARYLPQLVLAVIVPLAILAA-------VFPQDWISGLILLLTAPLIPIFMILIGW---AAQAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 175 DQRVRMMN-------EIISGIQVIKMY---TWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGrIAIFVSLLGF 244
Cdd:TIGR02857 173 RKQWAALSrlsghflDRLRGLPTLKLFgraKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLS-VALVAVYIGF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 245 VLGGGELTAERAFCV----TAFYNILRRTVSKFFPS--GMSQFAELlvsmrritnfmmreeANVIDMSERrdEKAEEEqh 318
Cdd:TIGR02857 252 RLLAGDLDLATGLFVlllaPEFYLPLRQLGAQYHARadGVAAAEAL---------------FAVLDAAPR--PLAGKA-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 319 llkevekrsyPVGIGkePDTLVEIKALRARwgQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGS 398
Cdd:TIGR02857 313 ----------PVTAA--PASSLEFSGVSVA--YPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 399 VQVSG-------------KYSYASQEPWLFNASVRDNILFGLP-MDKQRYRTVLKRCALERDL-ELLHGDGTIVGERGAS 463
Cdd:TIGR02857 379 IAVNGvpladadadswrdQIAWVPQHPFLFAGTIAENIRLARPdASDAEIREALERAGLDEFVaALPQGLDTPIGEGGAG 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408680 464 LSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDEcMRGFLGKQLVILVTHQLQFLEDADLIVIM 535
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEA-LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
919-1179 |
2.72e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 152.29 E-value: 2.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 919 MTSVERVLEYKDLDPEGDFNSPAEKQPpkswpKEGKLVTKDLSLRYePDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKS 998
Cdd:PRK11160 308 IASARRINEITEQKPEVTFPTTSTAAA-----DQVSLTLNNVSFTY-PDQPQP-VLKGLSLQIKAGEKVALLGRTGCGKS 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 999 SLINALFR-LSYNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNL---DPfeQYPDDKLWKALEDVHLkEE 1074
Cdd:PRK11160 381 TLLQLLTRaWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGL-EK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1075 ISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTI 1154
Cdd:PRK11160 458 LLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGL 537
|
250 260
....*....|....*....|....*
gi 665408680 1155 MDSDKVLVMDAGHVVEFGSPYELLT 1179
Cdd:PRK11160 538 EQFDRICVMDNGQIIEQGTHQELLA 562
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
953-1178 |
3.08e-38 |
|
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: 153.74 E-value: 3.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 953 GKLVTKDLSLRYEPDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRS 1031
Cdd:TIGR01193 472 GDIVINDVSYSYGYGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFfQARSGEILLNGFSLKDIDRHTLRQ 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1032 KISIIPQEPVLFSGTMRYNL--DPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILR 1109
Cdd:TIGR01193 549 FINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLT 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 1110 ENRILVMDEATANVDPQTDALIQATIRNkFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELL 1178
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL 696
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
340-559 |
3.20e-38 |
|
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: 143.14 E-value: 3.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----KYSYAS------ 409
Cdd:cd03251 1 VEFKNVTFRYPGDG-PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrDYTLASlrrqig 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 410 ---QEPWLFNASVRDNILFGLP-MDKQRYRTVLKR-CALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADV 484
Cdd:cd03251 80 lvsQDVFLFNDTVAENIAYGRPgATREEVEEAARAaNAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 485 YLLDDPLSAVDThVGRHLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 559
Cdd:cd03251 160 LILDEATSALDT-ESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
335-565 |
3.29e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 152.31 E-value: 3.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 335 EPDTLVEIKAlrarwgqeqHDLV---------LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPEsGSVQVSG-- 403
Cdd:PRK11174 343 ASNDPVTIEA---------EDLEilspdgktlAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGie 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 404 -----------KYSYASQEPWLFNASVRDNILFGLP-MDKQRYRTVLKRC-ALERDLELLHGDGTIVGERGASLSGGQRA 470
Cdd:PRK11174 413 lreldpeswrkHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAwVSEFLPLLPQGLDTPIGDQAAGLSVGQAQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 471 RICLARAVYRRADVYLLDDPLSAVDTHVGRHLFD---ECMRGflgkQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYE 547
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDAHSEQLVMQalnAASRR----QTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYA 568
|
250
....*....|....*...
gi 665408680 548 EMLKSGQDFAQLLVESTQ 565
Cdd:PRK11174 569 ELSQAGGLFATLLAHRQE 586
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
44-291 |
5.01e-37 |
|
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350035 [Multi-domain] Cd Length: 309 Bit Score: 141.99 E-value: 5.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 44 VLLIACILASVLLTHPYMMGMMHlAMKMRVAVSSAIYRKALRLSRTSLGG--TTTGQVVNLLSNDLNRFDRCLIHFHFLW 121
Cdd:cd18591 61 ILFLALLLQATFSQASYHIVIRE-GIRLKTALQAMIYEKALRLSSWNLSSgsMTIGQITNHMSEDANNIMFFFWLIHYLW 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 122 LGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKLRLQTALRTDQRVRMMNEIISGIQVIKMYTWERPFG 201
Cdd:cd18591 140 AIPLKIIVGLILLYLKLGVSALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 202 KLIGQMRRSEMSSIRQMNLLRgILLSFeITLGrIAIFVSLLGFVL----GGGELTAERAFCVTAFYNILrrTVSKF-FPS 276
Cdd:cd18591 220 DKIQEARRKELKLLLKDAVYW-SLMTF-LTQA-SPILVTLVTFGLypylEGEPLTAAKAFSSLALFNQL--TVPLFiFPV 294
|
250
....*....|....*
gi 665408680 277 GMSQFAELLVSMRRI 291
Cdd:cd18591 295 VIPILINAVVSTRRL 309
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
348-559 |
7.79e-37 |
|
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: 139.29 E-value: 7.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 348 RWGQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----KYSYAS---------QEPWL 414
Cdd:cd03253 7 TFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirEVTLDSlrraigvvpQDTVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 415 FNASVRDNILFGLP--MDKQRYRTVLKRCALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLS 492
Cdd:cd03253 87 FNDTIGYNIRYGRPdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 493 AVDTHVGRHLFdECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 559
Cdd:cd03253 167 ALDTHTEREIQ-AALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
357-553 |
8.67e-37 |
|
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: 138.90 E-value: 8.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------KYSYASQEPWLFNASVRDNI 423
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDTFLFSGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 424 LFGLPMDKQryrTVLKRCALE-------RDLEllHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDT 496
Cdd:cd03254 98 RLGRPNATD---EEVIEAAKEagahdfiMKLP--NGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 497 HVgRHLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSG 553
Cdd:cd03254 173 ET-EKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
938-1178 |
1.80e-36 |
|
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: 146.43 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 938 NSPAEKQPPkSWPK-EGKLVTKDLSLRYePDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL----------FR 1006
Cdd:COG4618 314 AVPAEPERM-PLPRpKGRLSVENLTVVP-PGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvgvwpptagsVR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1007 LsynDGAIlIDSLDTNDIGLHdlrskISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKA--LEDVHlkEEISELPSGLQS 1084
Cdd:COG4618 391 L---DGAD-LSQWDREELGRH-----IGYLPQDVELFDGTIAENIARFGDADPEKVVAAakLAGVH--EMILRLPDGYDT 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1085 IISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMDSDKVLVM 1163
Cdd:COG4618 460 RIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAlKARGATVVVITHRPSLLAAVDKLLVL 539
|
250
....*....|....*
gi 665408680 1164 DAGHVVEFGSPYELL 1178
Cdd:COG4618 540 RDGRVQAFGPRDEVL 554
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
357-559 |
1.84e-36 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 138.06 E-value: 1.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY-------------SYASQEPWLFNASVRDNI 423
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDirdlnlrwlrsqiGLVSQEPVLFDGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 424 LFGLP--MDKQRYRTVLKRCALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRH 501
Cdd:cd03249 98 RYGKPdaTDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665408680 502 L---FDECMRGFlgkqLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 559
Cdd:cd03249 178 VqeaLDRAMKGR----TTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
955-1179 |
3.57e-36 |
|
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: 137.08 E-value: 3.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSynDGAILIDSLDTNDIGLHDLRS 1031
Cdd:COG1122 1 IELENLSFSYPGGTP---ALDDVSLSIEKGEFVAIIGPNGSGKSTLlrlLNGLLKPT--SGEVLVDGKDITKKNLRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1032 KISIIPQEPV--LFSGT---------MRYNLDPFEQypDDKLWKALEDVHLKE----EISELpSGlqsiiseggtnfsvG 1096
Cdd:COG1122 76 KVGLVFQNPDdqLFAPTveedvafgpENLGLPREEI--RERVEEALELVGLEHladrPPHEL-SG--------------G 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1097 QRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSP 1174
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTP 218
|
....*
gi 665408680 1175 YELLT 1179
Cdd:COG1122 219 REVFS 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
955-1168 |
1.55e-35 |
|
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: 133.11 E-value: 1.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYePDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSY-NDGAILIDSLDTNDIGLHDLRSKI 1033
Cdd:cd03246 1 LEVENVSFRY-PGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRpTSGRVRLDGADISQWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1034 SIIPQEPVLFSGTMRYNLdpfeqypddklwkaledvhlkeeiselpsglqsiiseggtnFSVGQRQLVCLARAILRENRI 1113
Cdd:cd03246 79 GYLPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 1114 LVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMDSDKVLVMDAGHV 1168
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
354-540 |
4.10e-35 |
|
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: 133.75 E-value: 4.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 354 HDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-------------YSYASQEPWLFNASVR 420
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVGQEPVLFARSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 421 DNILFGLPMDKQRYRTVLKRCALERDL--ELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHv 498
Cdd:cd03248 106 DNIAYGLQSCSFECVKEAAQKAHAHSFisELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE- 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 665408680 499 GRHLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHV 540
Cdd:cd03248 185 SEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
336-552 |
2.14e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.52 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 336 PDTLVEIKALRARWGQEqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY--------SY 407
Cdd:COG1121 3 MMPAIELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPprrarrriGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 408 ASQE---PWLFNASVRDNILFGL--------PMDKQRYRTVLKrcALERdLELLHGDGTIVGErgasLSGGQRARICLAR 476
Cdd:COG1121 80 VPQRaevDWDFPITVRDVVLMGRygrrglfrRPSRADREAVDE--ALER-VGLEDLADRPIGE----LSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 477 AVYRRADVYLLDDPLSAVDtHVGRHLFDECMRGF--LGKqLVILVTHQLQFLED-ADLIVIMDKGHVsACGTYEEMLKS 552
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVD-AATEEALYELLRELrrEGK-TILVVTHDLGAVREyFDRVLLLNRGLV-AHGPPEEVLTP 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
955-1166 |
3.81e-34 |
|
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: 130.28 E-value: 3.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPD-TNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIdsldtndiglhdlRSK 1032
Cdd:cd03250 1 ISVEDASFTWDSGeQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLgELEKLSGSVSV-------------PGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1033 ISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENR 1112
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 1113 ILVMDEATANVDPQT-DALIQATIRNKFKDC-TVLTIAHRLNTIMDSDKVLVMDAG 1166
Cdd:cd03250 148 IYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
15-291 |
4.38e-34 |
|
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: 133.11 E-value: 4.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 15 ATVPLLLAGLISeFSEHGNGHSYNAQIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRLSRTSLGGT 94
Cdd:cd18559 14 FSGPSNLWLLLW-FDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 95 TTGQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKLRLQTALRT 174
Cdd:cd18559 93 PSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 175 DQRVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGRIAIFVSLLGFVLGG--GELT 252
Cdd:cd18559 173 DPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHslAGLV 252
|
250 260 270
....*....|....*....|....*....|....*....
gi 665408680 253 AERAFCVTAFYNILRRTVsKFFPSGMSQFAELLVSMRRI 291
Cdd:cd18559 253 ALKVFYSLALTTYLNWPL-NMSPEVITNIVAAEVSLERS 290
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
358-492 |
5.30e-34 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 127.76 E-value: 5.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY-------------SYASQEPWLFNA-SVRDNI 423
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltdderkslrkeiGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665408680 424 LFGLPMDKQRYRTVLKRC--ALERdLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLS 492
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAeeALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
318-523 |
9.95e-34 |
|
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: 137.49 E-value: 9.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 318 HLLKEVEKRSYPVGIGKEP--------DTLVEIKALRARWGQEQhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAIL 389
Cdd:TIGR02868 305 ERIVEVLDAAGPVAEGSAPaagavglgKPTLELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLA 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 390 GELPPESGSVQVSG-------------KYSYASQEPWLFNASVRDNILFGLP-MDKQRYRTVLKRCALERDLE-LLHGDG 454
Cdd:TIGR02868 383 GLLDPLQGEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRaLPDGLD 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 455 TIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKqLVILVTHQL 523
Cdd:TIGR02868 463 TVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR-TVVLITHHL 530
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
340-545 |
2.61e-33 |
|
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: 128.38 E-value: 2.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------KYS 406
Cdd:cd03244 3 IEFKNVSLRYRPNL-PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 407 YASQEPWLFNASVRDNI-LFGLPMDKQRYRtVLKRCAL-ERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADV 484
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLdPFGEYSDEELWQ-ALERVGLkEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 485 YLLDDPLSAVDTH-------VGRHLFDECMrgflgkqlVILVTHQLQFLEDADLIVIMDKGHVSACGT 545
Cdd:cd03244 161 LVLDEATASVDPEtdaliqkTIREAFKDCT--------VLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
357-535 |
4.46e-33 |
|
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: 127.59 E-value: 4.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY--------SYASQE----PWLfnaSVRDNIL 424
Cdd:cd03293 19 ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPvtgpgpdrGYVFQQdallPWL---TVLDNVA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 425 FGLpmdkqRYRTVLKRCALERDLELLHgdgtIVGERGAS------LSGGQRARICLARAVYRRADVYLLDDPLSAVDTHV 498
Cdd:cd03293 96 LGL-----ELQGVPKAEARERAEELLE----LVGLSGFEnayphqLSGGMRQRVALARALAVDPDVLLLDEPFSALDALT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 665408680 499 GRHLFDECMRGFLGKQL-VILVTHQLQ---FLedADLIVIM 535
Cdd:cd03293 167 REQLQEELLDIWRETGKtVLLVTHDIDeavFL--ADRVVVL 205
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
340-552 |
6.46e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 127.87 E-value: 6.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG------------KYSY 407
Cdd:COG1131 1 IEVRGLTKRYGDKT---ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 408 ASQEPWLF-NASVRDNI-----LFGLPMD--KQRYRTVLKRCALERDLellhgdgtivGERGASLSGGQRARICLARAVY 479
Cdd:COG1131 78 VPQEPALYpDLTVRENLrffarLYGLPRKeaRERIDELLELFGLTDAA----------DRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 480 RRADVYLLDDPLSAVDThVGRHLFDECMRGFLGKQL-VILVTHQLQFLED-ADLIVIMDKGHVSACGTYEEMLKS 552
Cdd:COG1131 148 HDPELLILDEPTSGLDP-EARRELWELLRELAAEGKtVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
955-1172 |
8.50e-33 |
|
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: 125.50 E-value: 8.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFR-LSYNDGAILIDSLDTNDIGlHDLRSKI 1033
Cdd:cd03247 1 LSINNVSFSYPE--QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEITLDGVPVSDLE-KALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1034 SIIPQEPVLFSGTMRYNLdpfeqypddklwkaledvhlkeeiselpsglqsiisegGTNFSVGQRQLVCLARAILRENRI 1113
Cdd:cd03247 78 SVLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 1114 LVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFG 1172
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
312-1180 |
9.13e-33 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 138.62 E-value: 9.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 312 KAEEEQHLLKEVEKRSYPVGIGKEPDTL-----VEIKALRARWGQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQ 386
Cdd:PTZ00265 350 KSLEATNSLYEIINRKPLVENNDDGKKLkdikkIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILK 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 387 AILGELPPESGSVQVS--------------GKYSYASQEPWLFNASVRDNILFGL--------------------PMDKQ 432
Cdd:PTZ00265 430 LIERLYDPTEGDIIINdshnlkdinlkwwrSKIGVVSQDPLLFSNSIKNNIKYSLyslkdlealsnyynedgndsQENKN 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 433 RYRTVLKRCALERDL--------ELLHGDG-------------------------------TIVGERGASLSGGQRARIC 473
Cdd:PTZ00265 510 KRNSCRAKCAGDLNDmsnttdsnELIEMRKnyqtikdsevvdvskkvlihdfvsalpdkyeTLVGSNASKLSGGQKQRIS 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 474 LARAVYRRADVYLLDDPLSAVDTHvGRHLFDECMRGFLGKQ--LVILVTHQLQFLEDADLIVIM---DKGHVSAC----- 543
Cdd:PTZ00265 590 IARAIIRNPKILILDEATSSLDNK-SEYLVQKTINNLKGNEnrITIIIAHRLSTIRYANTIFVLsnrERGSTVDVdiige 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 544 ---------------------------------------GTYEEMLKSGQDFAQLLVE----STQNSGGGDEIITSPNls 580
Cdd:PTZ00265 669 dptkdnkennnknnkddnnnnnnnnnnkinnagsyiieqGTHDALMKNKNGIYYTMINnqkvSSKKSSNNDNDKDSDM-- 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 581 rQSSALSTK--------SSNGSSSSLESMVEKEKPKPSAVSSQESRSGGQIGL--SMYKKYFGAGCGVLVFVVLI----- 645
Cdd:PTZ00265 747 -KSSAYKDSergydpdeMNGNSKHENESASNKKSCKMSDENASENNAGGKLPFlrNLFKRKPKAPNNLRIVYREIfsykk 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 646 -MLCIGTQILASGGDY--FLSYWVK---------NTASSSTLDIYYFTAINVGLVICALLRTllFFNITMHSSTE--LHN 711
Cdd:PTZ00265 826 dVTIIALSILVAGGLYpvFALLYAKyvstlfdfaNLEANSNKYSLYILVIAIAMFISETLKN--YYNNVIGEKVEktMKR 903
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 712 TMFQGLSRTALYFFH--TNPSGRILNRFANDLgqvdEVMPAVMLDCIQIFLTLTGIICVLCVTNpWYLINTFAMMLAFYY 789
Cdd:PTZ00265 904 RLFENILYQEISFFDqdKHAPGLLSAHINRDV----HLLKTGLVNNIVIFTHFIVLFLVSMVMS-FYFCPIVAAVLTGTY 978
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 790 W---RDFYLKT----SRDVKRLEAVARSPMYSHFS-------------ATLVGLPTIRAMGAQQ---TLIGQYDNYQD-- 844
Cdd:PTZ00265 979 FifmRVFAIRArltaNKDVEKKEINQPGTVFAYNSddeifkdpsfliqEAFYNMNTVIIYGLEDyfcNLIEKAIDYSNkg 1058
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 845 -----LHSSGYYTFVSTSR----AFGYYLDLFCVAYviSVILHNFFNPPLHNAGQIGLAITQALGMTGmvqwgmrqsaEL 915
Cdd:PTZ00265 1059 qkrktLVNSMLWGFSQSAQlfinSFAYWFGSFLIRR--GTILVDDFMKSLFTFLFTGSYAGKLMSLKG----------DS 1126
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 916 ENAMTSVERVLEYKDLDPEGDFNSPAEKQPPKSWPKEGKLVTKDLSLRYEPDTNSPcVLKGLSFTIQPMEKVGIVGRTGA 995
Cdd:PTZ00265 1127 ENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNKNDIKGKIEIMDVNFRYISRPNVP-IYKDLTFSCDSKKTTAIVGETGS 1205
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 996 GKSSLINALFR-------------------------------------------------------LSYNDGAILIDSLD 1020
Cdd:PTZ00265 1206 GKSTVMSLLMRfydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVD 1285
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1021 TNDIGLHDLRSKISIIPQEPVLFsgtmryNLDPFEQYPDDKLWKALEDVH-------LKEEISELPSGLQSIISEGGTNF 1093
Cdd:PTZ00265 1286 ICDYNLKDLRNLFSIVSQEPMLF------NMSIYENIKFGKEDATREDVKrackfaaIDEFIESLPNKYDTNVGPYGKSL 1359
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1094 SVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQAT---IRNKfKDCTVLTIAHRLNTIMDSDKVLVMD----AG 1166
Cdd:PTZ00265 1360 SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTivdIKDK-ADKTIITIAHRIASIKRSDKIVVFNnpdrTG 1438
|
1130
....*....|....*
gi 665408680 1167 HVVEF-GSPYELLTA 1180
Cdd:PTZ00265 1439 SFVQAhGTHEELLSV 1453
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
352-559 |
2.43e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 134.18 E-value: 2.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 352 EQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK----YSYA---------SQEPWLFNAS 418
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadYSEAalrqaisvvSQRVHLFSAT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 419 VRDNILFGLP-MDKQRYRTVLKRCALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTH 497
Cdd:PRK11160 430 LRDNLLLAAPnASDEALIEVLQQVGLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAE 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408680 498 VGRHLFDECMRGFLGKQLvILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 559
Cdd:PRK11160 510 TERQILELLAEHAQNKTV-LMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
340-544 |
2.85e-32 |
|
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: 125.32 E-value: 2.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-----------YSYA 408
Cdd:cd03259 1 LELKGLSKTYGSVR---ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 409 SQEPWLF-NASVRDNILFGLPMDKQRYRTVLKRCALErdLELLHGDGTIvGERGASLSGGQRARICLARAVYRRADVYLL 487
Cdd:cd03259 78 FQDYALFpHLTVAENIAFGLKLRGVPKAEIRARVREL--LELVGLEGLL-NRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 488 DDPLSAVDTHVGRHLFDEcMRGFLGKQ--LVILVTH-QLQFLEDADLIVIMDKGHVSACG 544
Cdd:cd03259 155 DEPLSALDAKLREELREE-LKELQRELgiTTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
336-538 |
3.75e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 126.36 E-value: 3.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 336 PDTLVEIKALRARWGQEQHDL-VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--------YS 406
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGVtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgpdRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 407 YASQE----PWLfnaSVRDNILFGLPMdkqryRTVLKRCALERDLELLHgdgtIVGERGAS------LSGGQRARICLAR 476
Cdd:COG1116 84 VVFQEpallPWL---TVLDNVALGLEL-----RGVPKAERRERARELLE----LVGLAGFEdayphqLSGGMRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 477 AVYRRADVYLLDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTHQLQ---FLedADLIVIMDKG 538
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLR--LWQETgktVLFVTHDVDeavFL--ADRVVVLSAR 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
958-1172 |
4.63e-32 |
|
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: 124.93 E-value: 4.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDL---RSKI 1033
Cdd:cd03257 5 KNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLlKPTSGSIIFDGKDLLKLSRRLRkirRKEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1034 SIIPQEPvlFSgtmryNLDP------------FEQYPDDKLWKALEDVHLKEEISELPSG-LQSIISEggtnFSVGQRQL 1100
Cdd:cd03257 85 QMVFQDP--MS-----SLNPrmtigeqiaeplRIHGKLSKKEARKEAVLLLLVGVGLPEEvLNRYPHE----LSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 1101 VCLARAILRENRILVMDEATANVDPQTDALIQATIRN--KFKDCTVLTIAHRLNTI-MDSDKVLVMDAGHVVEFG 1172
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqEELGLTLLFITHDLGVVaKIADRVAVMYAGKIVEEG 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
340-548 |
2.42e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 126.41 E-value: 2.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--YSYAS-------- 409
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlFTNLPprerrvgf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 410 --QEPWLF-NASVRDNILFGLPMDKQRYRTVLKRCalERDLELLHGDGtiVGERGAS-LSGGQRARICLARAVYRRADVY 485
Cdd:COG1118 80 vfQHYALFpHMTVAENIAFGLRVRPPSKAEIRARV--EELLELVQLEG--LADRYPSqLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665408680 486 LLDDPLSAVDTHVG-------RHLFDECmrgflgKQLVILVTH-QLQFLEDADLIVIMDKGHVSACGTYEE 548
Cdd:COG1118 156 LLDEPFGALDAKVRkelrrwlRRLHDEL------GGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDE 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
357-552 |
4.09e-31 |
|
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: 130.25 E-value: 4.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSV------------QVSGKY-SYASQEPWLFNASVRDNI 423
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdrEELGRHiGYLPQDVELFDGTIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 424 -LFGLPmDKQRyrtVLKRCAL----ERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDThV 498
Cdd:COG4618 427 aRFGDA-DPEK---VVAAAKLagvhEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD-E 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 499 GRHLFDECMRGFlgKQ---LVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKS 552
Cdd:COG4618 502 GEAALAAAIRAL--KArgaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
974-1121 |
6.11e-31 |
|
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: 119.29 E-value: 6.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 974 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSG-TMRYNL 1051
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTeGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 1052 -------DPFEQYPDDKLWKALEDVHLKEEISElpsglqsIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATA 1121
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGLGDLADR-------PVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
340-552 |
1.58e-30 |
|
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: 121.07 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGqEQHdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG---------------- 403
Cdd:cd03261 1 IELRGLTKSFG-GRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrlrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 404 KYSYASQEPWLFNA-SVRDNILFGLPMDKQRYRTVLKRCALERdLELlhgdgtiVGERG------ASLSGGQRARICLAR 476
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLREHTRLSEEEIREIVLEK-LEA-------VGLRGaedlypAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 477 AVYRRADVYLLDDPLSAVDThVGRHLFDECMRGfLGKQL---VILVTHQLQF-LEDADLIVIMDKGHVSACGTYEEMLKS 552
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDP-IASGVIDDLIRS-LKKELgltSIMVTHDLDTaFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
956-1167 |
3.58e-30 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 119.11 E-value: 3.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 956 VTKDLSLRYePDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL-FRLSYNDGAILIDSLDTNDIGLHDLRSKIS 1034
Cdd:cd03225 1 ELKNLSFSY-PDGARP-ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLnGLLGPTSGEVLVDGKDLTKLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1035 IIPQEP------------VLFsGTMRYNLDPFEQypDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVC 1102
Cdd:cd03225 79 LVFQNPddqffgptveeeVAF-GLENLGLPEEEI--EERVEEALELVGLEGLRDRSPFTL-----------SGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 1103 LARAILRENRILVMDEATANVDPQTDALIQATIRnKFKDC--TVLTIAHRLNTIMD-SDKVLVMDAGH 1167
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLK-KLKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
955-1187 |
4.65e-30 |
|
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: 120.15 E-value: 4.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFR-LSYNDGAILIDSLDTNDIGLHDLRSKI 1033
Cdd:COG1120 2 LEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGlLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1034 SIIPQEPVL-FSGT------M-RYN-LDPFEQYPDD---KLWKALEDV---HLKE-EISELpSGlqsiiseggtnfsvGQ 1097
Cdd:COG1120 78 AYVPQEPPApFGLTvrelvaLgRYPhLGLFGRPSAEdreAVEEALERTgleHLADrPVDEL-SG--------------GE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1098 RQLVCLARAILRENRILVMDEATANVDP--QTDALiqATIR--NKFKDCTVLTIAHRLN-TIMDSDKVLVMDAGHVVEFG 1172
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLahQLEVL--ELLRrlARERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQG 220
|
250
....*....|....*.
gi 665408680 1173 SPYELLTASK-AKVFH 1187
Cdd:COG1120 221 PPEEVLTPELlEEVYG 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
955-1183 |
4.93e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 126.17 E-value: 4.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTNSpcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND----GAILIDSLDTNDIGLHDLR 1030
Cdd:COG1123 5 LEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgrisGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1031 SKISIIPQEPvlfsgtmRYNLDP---FEQYPDDKLWKALEDVHLKEEISELPS--GLQSIISEGGTNFSVGQRQLVCLAR 1105
Cdd:COG1123 83 RRIGMVFQDP-------MTQLNPvtvGDQIAEALENLGLSRAEARARVLELLEavGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1106 AILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASK 1182
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
.
gi 665408680 1183 A 1183
Cdd:COG1123 236 A 236
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
340-551 |
5.93e-30 |
|
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: 118.97 E-value: 5.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQHdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKySYASQEPW------ 413
Cdd:COG1122 1 IELENLSFSYPGGTP--ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGK-DITKKNLRelrrkv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 414 ----------LFNASVRDNILFG-----LPMD--KQRYRTVLKRCALErdlELLHgdgtivgERGASLSGGQRARICLAR 476
Cdd:COG1122 78 glvfqnpddqLFAPTVEEDVAFGpenlgLPREeiRERVEEALELVGLE---HLAD-------RPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 477 AVYRRADVYLLDDPLSAVDtHVGRHLFDECMRGFLGKQL-VILVTHQLQFLED-ADLIVIMDKGHVSACGTYEEMLK 551
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLD-PRGRRELLELLKRLNKEGKtVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
340-548 |
9.67e-30 |
|
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: 118.98 E-value: 9.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-----------YSYA 408
Cdd:cd03296 3 IEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqernVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 409 SQEPWLF-NASVRDNILFGLPMDKQRYRT--VLKRCALERDLELLHGDGtiVGER-GASLSGGQRARICLARAVYRRADV 484
Cdd:cd03296 80 FQHYALFrHMTVFDNVAFGLRVKPRSERPpeAEIRAKVHELLKLVQLDW--LADRyPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408680 485 YLLDDPLSAVDTHVGRHLfdecmRGFLgKQL-------VILVTH-QLQFLEDADLIVIMDKGHVSACGTYEE 548
Cdd:cd03296 158 LLLDEPFGALDAKVRKEL-----RRWL-RRLhdelhvtTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
341-540 |
2.93e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 116.45 E-value: 2.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 341 EIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK---------Y----SY 407
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppeWrrqvAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 408 ASQEPWLFNASVRDNILFGLPMDKQRYrtvlKRCALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLL 487
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFQLRERKF----DRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 488 DDPLSAVDTHvGRHLFDECMRGFLGKQ--LVILVTHQLQFLED-ADLIVIMDKGHV 540
Cdd:COG4619 155 DEPTSALDPE-NTRRVEELLREYLAEEgrAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
966-1181 |
3.74e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 124.05 E-value: 3.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 966 PDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFR-LSYNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFS 1044
Cdd:PRK10789 324 PQTDHP-ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRhFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1045 GTMRYNL---DPFEQYPDDKLWKALEDVHlkEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATA 1121
Cdd:PRK10789 403 DTVANNIalgRPDATQQEIEHVARLASVH--DDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1122 NVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLTAS 1181
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
958-1167 |
3.80e-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: 114.26 E-value: 3.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRSKISII 1036
Cdd:cd00267 3 ENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLlKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1037 PQepvlfsgtmrynldpfeqypddklwkaledvhlkeeiselpsglqsiiseggtnFSVGQRQLVCLARAILRENRILVM 1116
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 665408680 1117 DEATANVDPQTDALIQATIRNKFKD-CTVLTIAHRLNTIMD-SDKVLVMDAGH 1167
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
357-560 |
4.10e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 125.22 E-value: 4.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------KYSYASQEPWLFNASVRDNI 423
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQEPVLFSGSVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 424 LFGL---PMDKQRYRTVlKRCALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVgR 500
Cdd:TIGR00958 576 AYGLtdtPDEEIMAAAK-AANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC-E 653
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 501 HLFDECMRgfLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQLL 560
Cdd:TIGR00958 654 QLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
336-548 |
4.43e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 120.20 E-value: 4.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 336 PDTLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY---------- 405
Cdd:COG3842 2 AMPALELENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvtglppekrn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 406 ------SYAsqepwLF-NASVRDNILFGLPMDKQRYRTVLKRcaLERDLELLHGDGtiVGERGAS-LSGGQRARICLARA 477
Cdd:COG3842 79 vgmvfqDYA-----LFpHLTVAENVAFGLRMRGVPKAEIRAR--VAELLELVGLEG--LADRYPHqLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 478 VYRRADVYLLDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTHQlqfLEDA----DLIVIMDKGHVSACGTYEE 548
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRR--LQRELgitFIYVTHD---QEEAlalaDRIAVMNDGRIEQVGTPEE 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
336-552 |
7.74e-29 |
|
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: 116.23 E-value: 7.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 336 PDTLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-YSYAS----- 409
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQdITGLSekely 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 410 ----------QEPWLFNA-SVRDNILFGLpmdkqRYRTVLKRcALERDL--ELLHgdgtIVGERGA------SLSGGQRA 470
Cdd:COG1127 79 elrrrigmlfQGGALFDSlTVFENVAFPL-----REHTDLSE-AEIRELvlEKLE----LVGLPGAadkmpsELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 471 RICLARAVYRRADVYLLDDPLSAVDThVGRHLFDECMRGfLGKQL---VILVTHQLQFLED-ADLIVIMDKGHVSACGTY 546
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDP-ITSAVIDELIRE-LRDELgltSVVVTHDLDSAFAiADRVAVLADGKIIAEGTP 226
|
....*.
gi 665408680 547 EEMLKS 552
Cdd:COG1127 227 EELLAS 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
341-539 |
1.87e-28 |
|
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: 114.10 E-value: 1.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 341 EIKALRARWGQEQHdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYAS----------- 409
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLslkelrrkvgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 410 --QEP--WLFNASVRDNILFGL-------PMDKQRYRTVLKRCALErdlELLHgdgtivgERGASLSGGQRARICLARAV 478
Cdd:cd03225 80 vfQNPddQFFGPTVEEEVAFGLenlglpeEEIEERVEEALELVGLE---GLRD-------RSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 479 YRRADVYLLDDPLSAVDTHVGRHLFDecmrgFLgKQL------VILVTHQLQFLED-ADLIVIMDKGH 539
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLE-----LL-KKLkaegktIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
358-560 |
2.02e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 121.99 E-value: 2.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----KYSYAS---------QEPWLFNASVRDNIL 424
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirTVTRASlrrniavvfQDAGLFNRSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 425 FGLP--MDKQRYRTVLKRCALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHL 502
Cdd:PRK13657 431 VGRPdaTDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665408680 503 ---FDECMRGflgkQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQLL 560
Cdd:PRK13657 511 kaaLDELMKG----RTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALL 567
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
339-550 |
2.37e-28 |
|
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: 115.14 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 339 LVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK----YS-------- 406
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlasLSrrelarri 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 407 -YASQEPWL-FNASVRDNILFGL--------PMDKQRYRTVLKrcALERdLELLHGDGTIVGErgasLSGGQRARICLAR 476
Cdd:COG1120 78 aYVPQEPPApFGLTVRELVALGRyphlglfgRPSAEDREAVEE--ALER-TGLEHLADRPVDE----LSGGERQRVLIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 477 AVYRRADVYLLDDPLSAVDTHvgrHLFD--ECMRGFLGKQ--LVILVTHQL----QFledADLIVIMDKGHVSACGTYEE 548
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLA---HQLEvlELLRRLARERgrTVVMVLHDLnlaaRY---ADRLVLLKDGRIVAQGPPEE 224
|
..
gi 665408680 549 ML 550
Cdd:COG1120 225 VL 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
955-1178 |
2.96e-28 |
|
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: 114.57 E-value: 2.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHdLRSKI 1033
Cdd:COG4555 2 IEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDsGSILIDGEDVRKEPRE-ARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1034 SIIPQEPVLFSG-TMRYNLDPF-EQYPDDKlwkalEDVHLK-EEISELpSGLQSIISEGGTNFSVGQRQLVCLARAILRE 1110
Cdd:COG4555 77 GVLPDERGLYDRlTVRENIRYFaELYGLFD-----EELKKRiEELIEL-LGLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665408680 1111 NRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHrlntIMD-----SDKVLVMDAGHVVEFGSPYELL 1178
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSH----IMQevealCDRVVILHKGKVVAQGSLDELR 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
357-548 |
3.62e-28 |
|
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: 114.18 E-value: 3.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYS------------YASQEPWLF-NASVRDNI 423
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVrkeprearrqigVLPDERGLYdRLTVRENI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 424 -----LFGLPMDKQRYRT--VLKRCALERDLEllhgdgtivgERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDT 496
Cdd:COG4555 96 ryfaeLYGLFDEELKKRIeeLIELLGLEEFLD----------RRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 497 HVGRhlfdeCMRGFLgKQL------VILVTHQLQFLED-ADLIVIMDKGHVSACGTYEE 548
Cdd:COG4555 166 MARR-----LLREIL-RALkkegktVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDE 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
341-544 |
4.69e-28 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 113.01 E-value: 4.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 341 EIKALRARWGQEqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY--------SYASQE- 411
Cdd:cd03235 1 EVEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPlekerkriGYVPQRr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 412 --PWLFNASVRDNILFGL--------PMDKQRYRTVLKrcALERdLELLH-GDGTIvgergASLSGGQRARICLARAVYR 480
Cdd:cd03235 78 siDRDFPISVRDVVLMGLyghkglfrRLSKADKAKVDE--ALER-VGLSElADRQI-----GELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 481 RADVYLLDDPLSAVDTHVGRHLFDecmrgfLGKQL------VILVTHQLQFLEDADLIVIMDKGHVSACG 544
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYE------LLRELrregmtILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
958-1182 |
5.14e-28 |
|
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: 113.44 E-value: 5.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRlsYNDGAILIDSLD---TNDIGLHDLRS 1031
Cdd:cd03258 5 KNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLircINGLER--PTSGSVLVDGTDltlLSGKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1032 KISIIPQEPVLFSG-TMRYNLdpfeQYPdDKLWKaLEDVHLKEEISELPS--GLQSIISEGGTNFSVGQRQLVCLARAIL 1108
Cdd:cd03258 83 RIGMIFQHFNLLSSrTVFENV----ALP-LEIAG-VPKAEIEERVLELLElvGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 1109 RENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASK 1182
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRdiNRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
955-1183 |
5.57e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 114.13 E-value: 5.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHDLRSKI 1033
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWsGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1034 SIIPQEPvlfsgtmRYNLDPF---------------EQYPDDKLWKALEDVHLKEEI-----SELpSGlqsiiseggtnf 1093
Cdd:COG1124 82 QMVFQDP-------YASLHPRhtvdrilaeplrihgLPDREERIAELLEQVGLPPSFldrypHQL-SG------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1094 svGQRQLVCLARAILRENRILVMDEATANVdpqtDALIQATIRNKFKD------CTVLTIAHRLNTI--MdSDKVLVMDA 1165
Cdd:COG1124 142 --GQRQRVAIARALILEPELLLLDEPTSAL----DVSVQAEILNLLKDlreergLTYLFVSHDLAVVahL-CDRVAVMQN 214
|
250 260 270
....*....|....*....|....*....|
gi 665408680 1166 GHVVEFG----------SPY--ELLTASKA 1183
Cdd:COG1124 215 GRIVEELtvadllagpkHPYtrELLAASLA 244
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
340-540 |
7.64e-28 |
|
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: 110.95 E-value: 7.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKysyasqEPWLFNASV 419
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK------DIKKEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 420 RDNILFgLPMDKQRYR--TVLkrcalerdlELLHgdgtivgergasLSGGQRARICLARAVYRRADVYLLDDPLSAVDTh 497
Cdd:cd03230 72 KRRIGY-LPEEPSLYEnlTVR---------ENLK------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDP- 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 665408680 498 VGRHLFDECMRGFLGKQ-LVILVTHQLQFLED-ADLIVIMDKGHV 540
Cdd:cd03230 129 ESRREFWELLRELKKEGkTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
335-550 |
7.93e-28 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 120.20 E-value: 7.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 335 EPDTL-VEIKALRarWGQEQHDlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVS----------- 402
Cdd:PRK10789 310 GRGELdVNIRQFT--YPQTDHP-ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHdipltklqlds 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 403 --GKYSYASQEPWLFNASVRDNILFGLPMDKQRYRTVLKRCALERD--LELLHGDGTIVGERGASLSGGQRARICLARAV 478
Cdd:PRK10789 387 wrSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDdiLRLPQGYDTEVGERGVMLSGGQKQRISIARAL 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408680 479 YRRADVYLLDDPLSAVDTHVGRHLFDEcMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEML 550
Cdd:PRK10789 467 LLNAEILILDDALSAVDGRTEHQILHN-LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLA 537
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
341-539 |
8.57e-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: 110.41 E-value: 8.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 341 EIKALRARWGqeqHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKysyasqepwlfnasvr 420
Cdd:cd00267 1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 421 dnilfglPMDKQRYRTVLKRCALErdlellhgdgtivgergASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHvGR 500
Cdd:cd00267 62 -------DIAKLPLEELRRRIGYV-----------------PQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-SR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 665408680 501 HLFDECMRGFLGKQL-VILVTHQLQFLEDA-DLIVIMDKGH 539
Cdd:cd00267 117 ERLLELLRELAEEGRtVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
341-540 |
1.10e-27 |
|
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: 110.77 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 341 EIKALRARWGQEQHdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGkysyASQEPWLFNAsVR 420
Cdd:cd03246 2 EVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG----ADISQWDPNE-LG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 421 DNIlfGlpmdkqryrtvlkrcALERDLELLhgDGTIvgeRGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGR 500
Cdd:cd03246 76 DHV--G---------------YLPQDDELF--SGSI---AENILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 665408680 501 HLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHV 540
Cdd:cd03246 134 ALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
339-536 |
1.61e-27 |
|
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: 111.42 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 339 LVEIKALRARWGQEqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY------------S 406
Cdd:COG4133 2 MLEAENLSCRRGER---LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPirdaredyrrrlA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 407 YASQEPWLFNA-SVRDNILF-----GLPMDKQRYRTVLKRCALERdlellHGDgtivgERGASLSGGQRARICLARAVYR 480
Cdd:COG4133 79 YLGHADGLKPElTVRENLRFwaalyGLRADREAIDEALEAVGLAG-----LAD-----LPVRQLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 481 RADVYLLDDPLSAVDTHvGRHLFDECMRGFLGKQ-LVILVTHQLQFLEDADLIVIMD 536
Cdd:COG4133 149 PAPLWLLDEPFTALDAA-GVALLAELIAAHLARGgAVLLTTHQPLELAAARVLDLGD 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
958-1172 |
1.80e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 110.22 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRSKISII 1036
Cdd:cd03214 3 ENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLlKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1037 PQepvlfsgtmrynldpfeqypddklwkALEDV---HLKE-EISELpSGlqsiiseggtnfsvGQRQLVCLARAILRENR 1112
Cdd:cd03214 79 PQ--------------------------ALELLglaHLADrPFNEL-SG--------------GERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665408680 1113 ILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLN-TIMDSDKVLVMDAGHVVEFG 1172
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRrlARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
957-1177 |
4.50e-27 |
|
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: 110.73 E-value: 4.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 957 TKDLSLRYEPDtnspCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYN------DGAILIDSLDTNDIGLHD-- 1028
Cdd:cd03260 3 LRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapdEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1029 LRSKISIIPQEPVLFSGTMRYNLDpfeqYP------------DDKLWKALEDVHLKEEISELPSGLQsiiseggtnFSVG 1096
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVA----YGlrlhgiklkeelDERVEEALRKAALWDEVKDRLHALG---------LSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1097 QRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAH------RLntimdSDKVLVMDAGHVVE 1170
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVE 220
|
....*..
gi 665408680 1171 FGSPYEL 1177
Cdd:cd03260 221 FGPTEQI 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
340-549 |
5.32e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 114.01 E-value: 5.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY-------------- 405
Cdd:COG3839 4 LELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdlppkdrniamv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 406 --SYAsqepwLF-NASVRDNILFGLPMDK-------QRYRTVLKRCALErdlELLHgdgtivgERGASLSGGQRARICLA 475
Cdd:COG3839 81 fqSYA-----LYpHMTVYENIAFPLKLRKvpkaeidRRVREAAELLGLE---DLLD-------RKPKQLSGGQRQRVALG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 476 RAVYRRADVYLLDDPLSAVDthvgRHLFDEcMRGFLgKQL-------VILVTH-QLQFLEDADLIVIMDKGHVSACGTYE 547
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLD----AKLRVE-MRAEI-KRLhrrlgttTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPE 219
|
..
gi 665408680 548 EM 549
Cdd:COG3839 220 EL 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
340-552 |
2.00e-26 |
|
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: 108.96 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGqeqhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-----------YSYA 408
Cdd:cd03299 1 LKVENLSKDWK----EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 409 SQEPWLF-NASVRDNILFGLPMdKQRYRTVLKRCALE--RDLELLHgdgtIVGERGASLSGGQRARICLARAVYRRADVY 485
Cdd:cd03299 77 PQNYALFpHMTVYKNIAYGLKK-RKVDKKEIERKVLEiaEMLGIDH----LLNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665408680 486 LLDDPLSAVDTHVGRHLFDEcMRgFLGKQL---VILVTHQlqfLEDA----DLIVIMDKGHVSACGTYEEMLKS 552
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREE-LK-KIRKEFgvtVLHVTHD---FEEAwalaDKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
18-270 |
2.58e-26 |
|
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: 110.04 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 18 PLLLAGLISEFSEHGNGHSYNAQIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRLSRTSLGGTTTG 97
Cdd:pfam00664 19 PLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 98 QVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIG-MASFYGISILVLYLPLQTYLSRVTSKLRLQTALRTDQ 176
Cdd:pfam00664 99 ELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGwKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 177 RVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFeitLGRIAIFVSLLGFVLGG-----GEL 251
Cdd:pfam00664 179 ASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGI---TQFIGYLSYALALWFGAylvisGEL 255
|
250
....*....|....*....
gi 665408680 252 TAERAFCVTAFYNILRRTV 270
Cdd:pfam00664 256 SVGDLVAFLSLFAQLFGPL 274
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
337-557 |
3.38e-26 |
|
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: 114.23 E-value: 3.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 337 DTLVEIKALRARWGQEQHDlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPE---SGSVQVSGKY-------- 405
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVP-AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDllelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 406 -----SYASQEPW--LFNASVRDNILFGLpmdkqRYRTVLKRCALERDLELLH--GDGTIVGERGASLSGGQRARICLAR 476
Cdd:COG1123 81 rgrriGMVFQDPMtqLNPVTVGDQIAEAL-----ENLGLSRAEARARVLELLEavGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 477 AVYRRADVYLLDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEMLKS 552
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRE--LQRERgttVLLITHDLgVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
....*
gi 665408680 553 GQDFA 557
Cdd:COG1123 234 PQALA 238
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
357-535 |
6.33e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 106.16 E-value: 6.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYA-----SQEPWLFNASVRDNILFGL--PM 429
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAyvpqrSEVPDSLPLTVRDLVAMGRwaRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 430 DKQRYRTVLKRCALERDLELLHGDGtIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFD----E 505
Cdd:NF040873 87 GLWRRLTRDDRAAVDDALERVGLAD-LAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIAllaeE 165
|
170 180 190
....*....|....*....|....*....|
gi 665408680 506 CMRGflgkQLVILVTHQLQFLEDADLIVIM 535
Cdd:NF040873 166 HARG----ATVVVVTHDLELVRRADPCVLL 191
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
955-1180 |
6.41e-26 |
|
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: 113.46 E-value: 6.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRY-EPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIG---LHDL 1029
Cdd:COG1123 261 LEVRNLSKRYpVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLlRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1030 RSKISIIPQEPV--LF-----SGTMRYNLDPFEQYPDDKLWK----ALEDVHLKEE-ISELPSGlqsiiseggtnFSVGQ 1097
Cdd:COG1123 341 RRRVQMVFQDPYssLNprmtvGDIIAEPLRLHGLLSRAERRErvaeLLERVGLPPDlADRYPHE-----------LSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1098 RQLVCLARAILRENRILVMDEATANVDPqtdaLIQATIRNKFKD------CTVLTIAHRLNTIMD-SDKVLVMDAGHVVE 1170
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDV----SVQAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDGRIVE 485
|
250
....*....|
gi 665408680 1171 FGSPYELLTA 1180
Cdd:COG1123 486 DGPTEEVFAN 495
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
340-538 |
1.12e-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: 106.50 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI--LGELPPE---SGSVQVSGKYSYAS----- 409
Cdd:cd03260 1 IELRDLNVYYGDKH---ALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrLNDLIPGapdEGEVLLDGKDIYDLdvdvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 410 ----------QEPWLFNASVRDNILFGLpmdkqRYRTVLKRCAL-ERDLELLHGDG--TIVGER--GASLSGGQRARICL 474
Cdd:cd03260 78 elrrrvgmvfQKPNPFPGSIYDNVAYGL-----RLHGIKLKEELdERVEEALRKAAlwDEVKDRlhALGLSGGQQQRLCL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 475 ARAVYRRADVYLLDDPLSAVDThVGRHLFDECMRGFLGKQLVILVTHQL-QFLEDADLIVIMDKG 538
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMqQAARVADRTAFLLNG 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
352-544 |
1.34e-25 |
|
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: 104.70 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 352 EQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK------------YSYASQEPWLFNASV 419
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVLNQRPYLFDTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 420 RDNIlfglpmdkqryrtvlkrcalerdlellhgdgtivgerGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVG 499
Cdd:cd03247 92 RNNL-------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 665408680 500 RHLFdECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACG 544
Cdd:cd03247 135 RQLL-SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
337-542 |
1.78e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 105.90 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 337 DTLVEIKALRARWGQEQHDL-VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--YSYASQE-- 411
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdiSSLSEREla 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 412 -----------------PWLfnaSVRDNILfgLPMdkqRYRTVLKRCALERDLELLH--GDGTIVGERGASLSGGQRARI 472
Cdd:COG1136 82 rlrrrhigfvfqffnllPEL---TALENVA--LPL---LLAGVSRKERRERARELLErvGLGDRLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665408680 473 CLARAVYRRADVYLLDDPLSAVDTHVGRH---LFDECMRGFlgKQLVILVTHQLQFLEDADLIVIMDKGHVSA 542
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEvleLLRELNREL--GTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
955-1190 |
1.79e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 106.71 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINA---LFRLSynDGAILIDSLDtndigLHDLRS 1031
Cdd:COG1121 7 IELENLTVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAilgLLPPT--SGTVRLFGKP-----PRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1032 KISIIPQEP------------VLFSGtmRYNLDPFEQYPD----DKLWKALEDVHLKE----EISELpSGlqsiiseggt 1091
Cdd:COG1121 76 RIGYVPQRAevdwdfpitvrdVVLMG--RYGRRGLFRRPSradrEAVDEALERVGLEDladrPIGEL-SG---------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1092 nfsvGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIR--NKfKDCTVLTIAHRLNTIMD-SDKVLVMDaGHV 1168
Cdd:COG1121 143 ----GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRelRR-EGKTILVVTHDLGAVREyFDRVLLLN-RGL 216
|
250 260
....*....|....*....|...
gi 665408680 1169 VEFGSPYELLTASK-AKVFHGMV 1190
Cdd:COG1121 217 VAHGPPEEVLTPENlSRAYGGPV 239
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
340-540 |
1.83e-25 |
|
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: 105.57 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQHDlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------KYS 406
Cdd:cd03369 7 IEVENLSVRYAPDLPP-VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 407 YASQEPWLFNASVRDNI-LFGLPMDKQRYrTVLKrcalerdlellhgdgtiVGERGASLSGGQRARICLARAVYRRADVY 485
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLdPFDEYSDEEIY-GALR-----------------VSEGGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 486 LLDDPLSAVDTHVGrHLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHV 540
Cdd:cd03369 148 VLDEATASIDYATD-ALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
340-548 |
2.16e-25 |
|
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: 106.17 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQeqhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--------------- 404
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlpphkrpvntv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 405 -YSYAsqepwLF-NASVRDNILFGLPMdKQRYRTVLKRcALERDLELLHGDGtIVGERGASLSGGQRARICLARAVYRRA 482
Cdd:cd03300 78 fQNYA-----LFpHLTVFENIAFGLRL-KKLPKAEIKE-RVAEALDLVQLEG-YANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665408680 483 DVYLLDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTH-QLQFLEDADLIVIMDKGHVSACGT----YEE 548
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKR--LQKELgitFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTpeeiYEE 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
341-544 |
2.85e-25 |
|
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: 104.05 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 341 EIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKysyasqepwlfnasvr 420
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGK---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 421 dnilfglPMDKQRYRTVLKRCA-----LERdLELLHgdgtiVGERG-ASLSGGQRARICLARAVYRRADVYLLDDPLSAV 494
Cdd:cd03214 62 -------DLASLSPKELARKIAyvpqaLEL-LGLAH-----LADRPfNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 495 DTHVGRHLFDECMRgfLGKQL---VILVTHQL----QFledADLIVIMDKGHVSACG 544
Cdd:cd03214 129 DIAHQIELLELLRR--LARERgktVVMVLHDLnlaaRY---ADRVILLKDGRIVAQG 180
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
955-1178 |
3.46e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 105.53 E-value: 3.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDiGLHDLRSKI 1033
Cdd:COG1131 1 IEVRGLTKRYGDKT----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTsGEVRVLGEDVAR-DPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1034 SIIPQEPVLFSG-TMRYNLDPF-------EQYPDDKLWKALEDVHLKEEISELPSglqsiiseggtNFSVGQRQLVCLAR 1105
Cdd:COG1131 76 GYVPQEPALYPDlTVRENLRFFarlyglpRKEARERIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1106 AILRENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLtiahrLNT-IMD-----SDKVLVMDAGHVVEFGSPYELL 1178
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRElAAEGKTVL-----LSThYLEeaerlCDRVAIIDKGRIVADGTPDELK 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
340-539 |
4.83e-25 |
|
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: 103.04 E-value: 4.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--------------- 404
Cdd:cd03229 1 LELKNVSKRYGQKT---VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdltdledelpplrrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 405 YSYASQEPWLF-NASVRDNILFGlpmdkqryrtvlkrcalerdlellhgdgtivgergasLSGGQRARICLARAVYRRAD 483
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG-------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 484 VYLLDDPLSAVDTHVGRHLFDEC--MRGFLGKQlVILVTHQLQFLED-ADLIVIMDKGH 539
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLksLQAQLGIT-VVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
340-540 |
5.33e-25 |
|
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: 104.26 E-value: 5.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQeqhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--------------- 404
Cdd:cd03301 1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkdrdiamv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 405 -YSYAsqepwLF-NASVRDNILFGLPMDKQRYRTVLKRcaLERDLELLHGDgTIVGERGASLSGGQRARICLARAVYRRA 482
Cdd:cd03301 78 fQNYA-----LYpHMTVYDNIAFGLKLRKVPKDEIDER--VREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408680 483 DVYLLDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTH-QLQFLEDADLIVIMDKGHV 540
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKR--LQQRLgttTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
955-1168 |
2.27e-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: 100.94 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGlHDLRSKI 1033
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDsGEIKVLGKDIKKEP-EEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1034 SIIPQEPVLFSgtmryNLDPFEqypddklwkaledvHLKeeiselpsglqsiiseggtnFSVGQRQLVCLARAILRENRI 1113
Cdd:cd03230 76 GYLPEEPSLYE-----NLTVRE--------------NLK--------------------LSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 1114 LVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHV 1168
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
340-540 |
3.00e-24 |
|
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: 102.18 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWG-QEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--YSYASQEPWLF- 415
Cdd:cd03255 1 IELKNLSKTYGgGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdiSKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 416 ---------------NASVRDNILfgLPMdkqRYRTVLKRCALERDLELLH--GDGTIVGERGASLSGGQRARICLARAV 478
Cdd:cd03255 81 rrhigfvfqsfnllpDLTALENVE--LPL---LLAGVPKKERRERAEELLErvGLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665408680 479 YRRADVYLLDDPLSAVDTHVGRHLFDEcMRGFLGKQ--LVILVTHQLQFLEDADLIVIMDKGHV 540
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMEL-LRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
339-563 |
3.23e-24 |
|
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: 102.96 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 339 LVEIKALRARWGQEQHDL-VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK------------- 404
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 405 ------YSYASQEPWLfnaSVRDNI-----LFGLPMDKQRYRTVLKRCALERDLellhgdgtiVGERGASLSGGQRARIC 473
Cdd:COG1124 81 vqmvfqDPYASLHPRH---TVDRILaeplrIHGLPDREERIAELLEQVGLPPSF---------LDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 474 LARAVYRRADVYLLDDPLSAVDTHVGRHLFDecmrgfLGKQL-------VILVTHQLQFLED-ADLIVIMDKGHVSACGT 545
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILN------LLKDLreergltYLFVSHDLAVVAHlCDRVAVMQNGRIVEELT 222
|
250
....*....|....*....
gi 665408680 546 YEEMLKSGQ-DFAQLLVES 563
Cdd:COG1124 223 VADLLAGPKhPYTRELLAA 241
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
951-1183 |
8.68e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 102.79 E-value: 8.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 951 KEGKLVTKDLSLRYePDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSynDGAILIDSLDTNDIGLH 1027
Cdd:PRK13635 2 KEEIIRVEHISFRY-PDAATY-ALKDVSFSVYEGEWVAIVGHNGSGKSTLaklLNGLLLPE--AGTITVGGMVLSEETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1028 DLRSKISIIPQEP-VLFSGTMRYNLDPF----EQYPDDKLWK----ALEDVHLKEEISELPSGLqsiiseggtnfSVGQR 1098
Cdd:PRK13635 78 DVRRQVGMVFQNPdNQFVGATVQDDVAFglenIGVPREEMVErvdqALRQVGMEDFLNREPHRL-----------SGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1099 QLVCLARAILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYE 1176
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEE 226
|
....*..
gi 665408680 1177 LLTASKA 1183
Cdd:PRK13635 227 IFKSGHM 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
325-563 |
1.03e-23 |
|
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: 106.53 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 325 KRSYPVGIGKEPDTLVEIKALRARWGQEQHDLV--LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVS 402
Cdd:COG1123 246 ARGRAAPAAAAAEPLLEVRNLSKRYPVRGKGGVraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 403 GK----YSYAS------------QEPWL-FNA--SVRDNILFGL----PMDK----QRYRTVLKRCALERDLEllhgdgt 455
Cdd:COG1123 326 GKdltkLSRRSlrelrrrvqmvfQDPYSsLNPrmTVGDIIAEPLrlhgLLSRaerrERVAELLERVGLPPDLA------- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 456 ivGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTHQLQFLED-ADL 531
Cdd:COG1123 399 --DRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRD--LQRELgltYLFISHDLAVVRYiADR 474
|
250 260 270
....*....|....*....|....*....|...
gi 665408680 532 IVIMDKGHVSACGTYEEMLKSGQ-DFAQLLVES 563
Cdd:COG1123 475 VAVMYDGRIVEDGPTEEVFANPQhPYTRALLAA 507
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
340-540 |
1.07e-23 |
|
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: 100.30 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPW------ 413
Cdd:cd03262 1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNInelrqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 414 ---------LF-NASVRDNILFGLpmdkqryRTVLKRC---ALERDLELLhgdgTIVG------ERGASLSGGQRARICL 474
Cdd:cd03262 78 vgmvfqqfnLFpHLTVLENITLAP-------IKVKGMSkaeAEERALELL----EKVGladkadAYPAQLSGGQQQRVAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665408680 475 ARAVYRRADVYLLDDPLSAVDTH-VGRHLfdECMrgflgKQL------VILVTHQLQFLED-ADLIVIMDKGHV 540
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPElVGEVL--DVM-----KDLaeegmtMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
358-559 |
2.01e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 106.26 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----KYSYA---------SQEPWLFNASVRDNIL 424
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrDYTLAslrnqvalvSQNVHLFNDTIANNIA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 425 FGlpmDKQRY-RTVLKR-----CALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHV 498
Cdd:PRK11176 439 YA---RTEQYsREQIEEaarmaYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 499 GRHL---FDEcmrgfLGKQLVILV-THQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 559
Cdd:PRK11176 516 ERAIqaaLDE-----LQKNRTSLViAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
820-1163 |
3.54e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 107.42 E-value: 3.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 820 LVGLPTIRAMGAQQTLIGQ-------YDNY-------QDLHSSGYYTFVSTSRAFGYYldlFCVAYVISVILHNFFNPPL 885
Cdd:PTZ00265 243 LVGIRTVVSYCGEKTILKKfnlseklYSKYilkanfmESLHIGMINGFILASYAFGFW---YGTRIIISDLSNQQPNNDF 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 886 HNAGQIGLAITQALGMTgMVQWGMRQSAELENAMTSVERVLEYKDLDPEGDFNSPAEKQPPKSwpkegKLVTKDLSLRYe 965
Cdd:PTZ00265 320 HGGSVISILLGVLISMF-MLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIK-----KIQFKNVRFHY- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 966 pDTNSPC-VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsYN--DGAILI-DSLDTNDIGLHDLRSKISIIPQEPV 1041
Cdd:PTZ00265 393 -DTRKDVeIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERL-YDptEGDIIInDSHNLKDINLKWWRSKIGVVSQDPL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1042 LFSGTMR-------------------YNLDPFEQYPDD------------------------------KLWKALED---- 1068
Cdd:PTZ00265 471 LFSNSIKnnikyslyslkdlealsnyYNEDGNDSQENKnkrnscrakcagdlndmsnttdsneliemrKNYQTIKDsevv 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1069 -----VHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCT 1143
Cdd:PTZ00265 551 dvskkVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEN 630
|
410 420
....*....|....*....|..
gi 665408680 1144 VLT--IAHRLNTIMDSDKVLVM 1163
Cdd:PTZ00265 631 RITiiIAHRLSTIRYANTIFVL 652
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
339-540 |
5.06e-23 |
|
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: 99.12 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 339 LVEIKALRARWGQEQHDL-VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK------------- 404
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 405 ---------YSYASQEPWLfnaSVRDNILFGLPMDKQRYRTVLKRCALERDLELLHGDGTIVGERGASLSGGQRARICLA 475
Cdd:cd03257 81 rkeiqmvfqDPMSSLNPRM---TIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408680 476 RAVYRRADVYLLDDPLSAVDTHVGR---HLFDEcmrgfLGKQL---VILVTHQLQFLED-ADLIVIMDKGHV 540
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAqilDLLKK-----LQEELgltLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
368-540 |
7.36e-23 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 98.14 E-value: 7.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 368 GQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-----------------KYSYASQEPWLF-NASVRDNILFGLPM 429
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkinlppqqrKIGLVFQQYALFpHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 430 DKQRYRTVLkrcaLERDLELLHGDGtIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLfdecmRG 509
Cdd:cd03297 103 KRNREDRIS----VDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL-----LP 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 665408680 510 FLGKQL------VILVTHQLQFLED-ADLIVIMDKGHV 540
Cdd:cd03297 173 ELKQIKknlnipVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
638-861 |
8.11e-23 |
|
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: 99.64 E-value: 8.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 638 VLVFVVLIMLCIGTQILASggdYFLSYW-----VKNTASSSTLDIY--YFTAINVGLVICALLRTLLFFNITMHSSTELH 710
Cdd:pfam00664 1 LILAILLAILSGAISPAFP---LVLGRIldvllPDGDPETQALNVYslALLLLGLAQFILSFLQSYLLNHTGERLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 711 NTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMMLAFYYW 790
Cdd:pfam00664 78 RKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665408680 791 RDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVSTSRAFG 861
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSF 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
338-559 |
1.28e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 99.32 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 338 TLVEIKALRARWgQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------K 404
Cdd:PRK13635 4 EIIRVEHISFRY-PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwdvrrQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 405 YSYASQEP--WLFNASVRDNILFGL-----PMDK--QRYRTVLKRCALErdlELLHgdgtivgERGASLSGGQRARICLA 475
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGLenigvPREEmvERVDQALRQVGME---DFLN-------REPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 476 RAVYRRADVYLLDDPLSAVDThVGRHLFDECMRGfLGKQL---VILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKS 552
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDP-RGRREVLETVRQ-LKEQKgitVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
....*..
gi 665408680 553 GQDFAQL 559
Cdd:PRK13635 231 GHMLQEI 237
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
339-555 |
1.30e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 98.14 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 339 LVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPW----- 413
Cdd:COG1126 1 MIEIENLHKSFGDLE---VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDInklrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 414 ----------LF-NASVRDNILFGLpmdkqryRTVLKRC---ALERDLELLhgdgTIVG--ERG----ASLSGGQRARIC 473
Cdd:COG1126 78 kvgmvfqqfnLFpHLTVLENVTLAP-------IKVKKMSkaeAEERAMELL----ERVGlaDKAdaypAQLSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 474 LARAVYRRADVYLLDDPLSAVDTH-VG------RHLFDECMRgflgkqlVILVTHQLQFLED-ADLIVIMDKGHVSACGT 545
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPElVGevldvmRDLAKEGMT-------MVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
250
....*....|
gi 665408680 546 YEEMLKSGQD 555
Cdd:COG1126 220 PEEFFENPQH 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
958-1172 |
1.50e-22 |
|
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: 97.22 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDtndigLHDLRSKISII 1036
Cdd:cd03235 3 EDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTsGSIRVFGKP-----LEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1037 PQE-------PVL---FSGTMRYNLDPFEQYPDDKLWK----ALEDVHLKE----EISELpSGlqsiiseggtnfsvGQR 1098
Cdd:cd03235 74 PQRrsidrdfPISvrdVVLMGLYGHKGLFRRLSKADKAkvdeALERVGLSEladrQIGEL-SG--------------GQQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 1099 QLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMDS-DKVLVMDaGHVVEFG 1172
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLLN-RTVVASG 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
356-550 |
1.72e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 97.52 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 356 LVLNNV-----------NMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKySYASQEPW----------- 413
Cdd:COG3840 2 LRLDDLtyrygdfplrfDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ-DLTALPPAerpvsmlfqen 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 414 -LFNA-SVRDNILFGL-------PMDKQRYRTVLKRCALErDLEllhgdgtivGERGASLSGGQRARICLARAVYRRADV 484
Cdd:COG3840 81 nLFPHlTVAQNIGLGLrpglkltAEQRAQVEQALERVGLA-GLL---------DRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 485 YLLDDPLSAVD---THVGRHLFDEcmrgfLGKQL---VILVTHQlqfLEDA----DLIVIMDKGHVSACGTYEEML 550
Cdd:COG3840 151 LLLDEPFSALDpalRQEMLDLVDE-----LCRERgltVLMVTHD---PEDAariaDRVLLVADGRIAADGPTAALL 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
958-1179 |
2.12e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 98.52 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPDTNSpcVLKGLSFTIQPMEKVGIVGRTGAGKSS---LINALFRLsyNDGAILIDSLDTNDIGLHDLRSKIS 1034
Cdd:PRK13632 11 ENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLKP--QSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1035 IIPQEP------------VLFsGTMRYNLDPfeqypdDKLWKALEDVHLKeeiselpSGLQSIISEGGTNFSVGQRQLVC 1102
Cdd:PRK13632 87 IIFQNPdnqfigatveddIAF-GLENKKVPP------KKMKDIIDDLAKK-------VGMEDYLDKEPQNLSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 1103 LARAILRENRILVMDEATANVDPQTDALIQATIRN--KFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLT 1179
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
888-1150 |
2.59e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.96 E-value: 2.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 888 AGQIGL-AITQALGMTGMVQ----WGMRQSAELENAMTSVERVLEYKDLDPEGDfnSPAEKQPPKSWPKEGKLVTKDLSL 962
Cdd:COG4178 293 AGEITLgGLMQAASAFGQVQgalsWFVDNYQSLAEWRATVDRLAGFEEALEAAD--ALPEAASRIETSEDGALALEDLTL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 963 R---YEPdtnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDtndiglhdlrsKISIIPQ 1038
Cdd:COG4178 371 RtpdGRP------LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwPYGSGRIARPAGA-----------RVLFLPQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1039 EPVLFSGTMR----YNLDPfEQYPDDKLWKALEDVHLkeeiselpSGLQSIISEG---GTNFSVGQRQLVCLARAILREN 1111
Cdd:COG4178 434 RPYLPLGTLReallYPATA-EAFSDAELREALEAVGL--------GHLAERLDEEadwDQVLSLGEQQRLAFARLLLHKP 504
|
250 260 270
....*....|....*....|....*....|....*....
gi 665408680 1112 RILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHR 1150
Cdd:COG4178 505 DWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
357-552 |
3.72e-22 |
|
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: 96.99 E-value: 3.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------KYSYASQEPWLF-NASVRDN 422
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFpHMTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 423 I-----LFGLPmdKQRYRtvlkrcalERDLELLH----GDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSA 493
Cdd:cd03295 96 IalvpkLLKWP--KEKIR--------ERADELLAlvglDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665408680 494 VDTHVGRHLFDECMRgfLGKQL---VILVTHQLQ-FLEDADLIVIMDKGHVSACGTYEEMLKS 552
Cdd:cd03295 166 LDPITRDQLQEEFKR--LQQELgktIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
341-521 |
4.60e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 97.24 E-value: 4.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 341 EIKALRARW-GQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYAS--------QE 411
Cdd:COG4525 5 TVRHVSVRYpGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPgadrgvvfQK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 412 ----PWLfnaSVRDNILFGLpmdkqRYRTVLKRCALERDLELLHgdgtIVGERGA------SLSGGQRARICLARAVYRR 481
Cdd:COG4525 85 dallPWL---NVLDNVAFGL-----RLRGVPKAERRARAEELLA----LVGLADFarrriwQLSGGMRQRVGIARALAAD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 665408680 482 ADVYLLDDPLSAVDThvgrhLFDECMRGFL-------GKQlVILVTH 521
Cdd:COG4525 153 PRFLLMDEPFGALDA-----LTREQMQELLldvwqrtGKG-VFLITH 193
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
955-1168 |
5.50e-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: 95.63 E-value: 5.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDL---- 1029
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1030 RSKISIIPQEpvlfsgtmrYNLDPF---------------EQYPDDKLW--KALEDVHLKEEISELPSGLqsiiseggtn 1092
Cdd:cd03255 81 RRHIGFVFQS---------FNLLPDltalenvelplllagVPKKERRERaeELLERVGLGDRLNHYPSEL---------- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 1093 fSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHV 1168
Cdd:cd03255 142 -SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
335-548 |
6.08e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 99.25 E-value: 6.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 335 EPDTLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK---------- 404
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvpaenr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 405 ------YSYAsqepwLF-NASVRDNILFGLPMDKQRYRTVLKRcaLERDLELLHGDGTIvGERGASLSGGQRARICLARA 477
Cdd:PRK09452 87 hvntvfQSYA-----LFpHMTVFENVAFGLRMQKTPAAEITPR--VMEALRMVQLEEFA-QRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 478 VYRRADVYLLDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTH-QLQFLEDADLIVIMDKGHVSACGT----YEE 548
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKA--LQRKLgitFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTpreiYEE 235
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
958-1179 |
6.57e-22 |
|
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: 96.03 E-value: 6.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDT---NDIGLHDLRSKI 1033
Cdd:cd03261 4 RGLTKSFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEVLIDGEDIsglSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1034 SIIPQEPVLFSGT---------MRYNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLA 1104
Cdd:cd03261 80 GMLFQSGALFDSLtvfenvafpLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAEL-----------SGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 1105 RAILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLT 1179
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRslKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
955-1172 |
9.07e-22 |
|
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: 94.89 E-value: 9.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSynDGAILIDSLDTNDIGLHdlRS 1031
Cdd:cd03259 1 LELKGLSKTYGSVR----ALDDLSLTVEPGEFLALLGPSGCGKTTLlrlIAGLERPD--SGEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1032 KISIIPQEPVLFSgtmryNLDPFE--QYP-----------DDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQR 1098
Cdd:cd03259 73 NIGMVFQDYALFP-----HLTVAEniAFGlklrgvpkaeiRARVRELLELVGLEGLLNRYPHEL-----------SGGQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 1099 QLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFK--DCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1172
Cdd:cd03259 137 QRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
360-536 |
9.31e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.86 E-value: 9.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 360 NVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPE---SGSVQVSGKYSYAS-----------QEPWLF-NASVRDNIL 424
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALpaeqrrigilfQDDLLFpHLSVGENLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 425 FGLPMD---KQRYRTVLKrcALErDLELLHgdgtiVGERG-ASLSGGQRARICLARAVYRRADVYLLDDPLSAVDThvgr 500
Cdd:COG4136 99 FALPPTigrAQRRARVEQ--ALE-EAGLAG-----FADRDpATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA---- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 665408680 501 HLFDEcMRGFLGKQL------VILVTHQLQFLEDADLIVIMD 536
Cdd:COG4136 167 ALRAQ-FREFVFEQIrqrgipALLVTHDEEDAPAAGRVLDLG 207
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
340-548 |
1.06e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 98.23 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-----------YSYA 408
Cdd:PRK10851 3 IEIANIKKSFGRTQ---VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 409 SQEPWLF-NASVRDNILFGLPMDKQRYR---TVLKR---CALERdLELLHgdgtiVGER-GASLSGGQRARICLARAVYR 480
Cdd:PRK10851 80 FQHYALFrHMTVFDNIAFGLTVLPRRERpnaAAIKAkvtQLLEM-VQLAH-----LADRyPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 481 RADVYLLDDPLSAVDTHVGRHLfdecmRGFLgKQL-------VILVTH-QLQFLEDADLIVIMDKGHVSACGTYEE 548
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKEL-----RRWL-RQLheelkftSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQ 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
336-551 |
1.27e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.14 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 336 PDTLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG--KYSYASQEPW 413
Cdd:COG0488 312 GKKVLELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGEtvKIGYFDQHQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 414 LF--NASVRDNILFGLPMDKQRY-RTVLKRCalerdleLLHGD--GTIVGergaSLSGGQRARICLARAVYRRADVYLLD 488
Cdd:COG0488 389 ELdpDKTVLDELRDGAPGGTEQEvRGYLGRF-------LFSGDdaFKPVG----VLSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 489 DP---LSaVDThvgRHLFDECMRGFLGKqlVILVTHQLQFLED-ADLIVIMDKGHVSAC-GTYEEMLK 551
Cdd:COG0488 458 EPtnhLD-IET---LEALEEALDDFPGT--VLLVSHDRYFLDRvATRILEFEDGGVREYpGGYDDYLE 519
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
339-558 |
1.60e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 95.16 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 339 LVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYAS--------- 409
Cdd:PRK09493 1 MIEFKNVSKHFGPTQ---VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPkvderlirq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 410 ------QEPWLF-NASVRDNILFGlPMdkqRYRTVLKRCALERDLELLHGDGtiVGERG----ASLSGGQRARICLARAV 478
Cdd:PRK09493 78 eagmvfQQFYLFpHLTALENVMFG-PL---RVRGASKEEAEKQARELLAKVG--LAERAhhypSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 479 YRRADVYLLDDPLSAVDTHVgRHLFDECMRGFL--GKQLVIlVTHQLQFLED-ADLIVIMDKGHVSACGTYEEMLKSG-- 553
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPEL-RHEVLKVMQDLAeeGMTMVI-VTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKNPps 229
|
....*...
gi 665408680 554 ---QDFAQ 558
Cdd:PRK09493 230 qrlQEFLQ 237
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
335-524 |
1.66e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 95.49 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 335 EPDTLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI--LGELPPE---SGSVQVSGKYSYAS 409
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPGarvEGEILLDGEDIYDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 410 ---------------QEPWLFNASVRDNILFGLPM----DK----QRYRTVLKRCAL-----ERdlelLHgdgtivgERG 461
Cdd:COG1117 84 dvdvvelrrrvgmvfQKPNPFPKSIYDNVAYGLRLhgikSKseldEIVEESLRKAALwdevkDR----LK-------KSA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 462 ASLSGGQRARICLARAVYRRADVYLLDDPLSAVD---THVGRHLFDEcmrgfLGKQL-VILVTHQLQ 524
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpisTAKIEELILE-----LKKDYtIVIVTHNMQ 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
341-540 |
2.03e-21 |
|
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: 94.56 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 341 EIKALRARWGQEQHdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----------------K 404
Cdd:cd03256 2 EVENLSKTYPNGKK--ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkalrqlrrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 405 YSYASQEPWLFN-ASVRDNILFGL---------------PMDKQRYRTVLKRCALerdLELLHgdgtivgERGASLSGGQ 468
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGRlgrrstwrslfglfpKEEKQRALAALERVGL---LDKAY-------QRADQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 469 RARICLARAVYRRADVYLLDDPLSAVD----THVGRHLFDECMRgflgKQL-VILVTHQLQF-LEDADLIVIMDKGHV 540
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDpassRQVMDLLKRINRE----EGItVIVSLHQVDLaREYADRIVGLKDGRI 223
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
357-550 |
2.44e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 94.80 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKySYASQEPWL---------------FNASVRD 421
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR-PLAAWSPWElarrravlpqhsslaFPFTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 422 NILFGL---PMDKQRYRTVLKRcALER-DLELLhgdgtivGERG-ASLSGGQRARICLARA-------VYRRADVYLLDD 489
Cdd:COG4559 95 VVALGRaphGSSAAQDRQIVRE-ALALvGLAHL-------AGRSyQTLSGGEQQRVQLARVlaqlwepVDGGPRWLFLDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 490 PLSAVDTHVGRHLFdECMRGFLGKQL-VILVTHQL----QFledADLIVIMDKGHVSACGTYEEML 550
Cdd:COG4559 167 PTSALDLAHQHAVL-RLARQLARRGGgVVAVLHDLnlaaQY---ADRILLLHQGRLVAQGTPEEVL 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
344-550 |
2.70e-21 |
|
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: 97.09 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 344 ALRARWGQEQHDLVLNnVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY-----------------S 406
Cdd:COG4148 2 MLEVDFRLRRGGFTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrriG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 407 YASQEPWLF-NASVRDNILFGLPMDKQRYRTVlkrcALERDLELLhGDGTIVGERGASLSGGQRARICLARAVYRRADVY 485
Cdd:COG4148 81 YVFQEARLFpHLSVRGNLLYGRKRAPRAERRI----SFDEVVELL-GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 486 LLDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTHQLQ-FLEDADLIVIMDKGHVSACGTYEEML 550
Cdd:COG4148 156 LMDEPLAALDLARKAEILPYLER--LRDELdipILYVSHSLDeVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
973-1167 |
4.29e-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: 91.86 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSYndGAILID--SLDTNDIGLHDLRSKISIIPQEPVLFSgtm 1047
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLlrcIAGLEEPDS--GSILIDgeDLTDLEDELPPLRRRIGMVFQDFALFP--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1048 rynldpfeqypddklwkaledvHL--KEEISELPSGlqsiiseggtnfsvGQRQLVCLARAILRENRILVMDEATANVDP 1125
Cdd:cd03229 90 ----------------------HLtvLENIALGLSG--------------GQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 665408680 1126 QTDALIQATIRNKFKD--CTVLTIAHRLNTIMD-SDKVLVMDAGH 1167
Cdd:cd03229 134 ITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
356-559 |
4.33e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.09 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 356 LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQ-------------------EPWLFN 416
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKknkklkplrkkvgivfqfpEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 417 ASVRDNILFGlPMD--------KQRYRTVLKRCALERDLEllhgdgtivgERGA-SLSGGQRARICLARAVYRRADVYLL 487
Cdd:PRK13634 101 ETVEKDICFG-PMNfgvseedaKQKAREMIELVGLPEELL----------ARSPfELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 488 DDPLSAVDTHvGRHlfdECMRGF--LGKQ---LVILVTHQlqfLED----ADLIVIMDKGHVSACGTYEEMLKSGQDFAQ 558
Cdd:PRK13634 170 DEPTAGLDPK-GRK---EMMEMFykLHKEkglTTVLVTHS---MEDaaryADQIVVMHKGTVFLQGTPREIFADPDELEA 242
|
.
gi 665408680 559 L 559
Cdd:PRK13634 243 I 243
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
357-559 |
4.90e-21 |
|
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: 99.12 E-value: 4.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----KYSYAS---------QEPWLFNASVRDNI 423
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirDVTQASlraaigivpQDTVLFNDTIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 424 LFGLP-MDKQRYRTVLKRCALERDLELL-HGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRH 501
Cdd:COG5265 453 AYGRPdASEEEVEAAARAAQIHDFIESLpDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERA 532
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665408680 502 LFDECMRgfLGKQ---LVIlvTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 559
Cdd:COG5265 533 IQAALRE--VARGrttLVI--AHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
341-550 |
7.48e-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: 92.50 E-value: 7.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 341 EIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--------------YS 406
Cdd:cd03224 2 EVENLNAGYGKSQ---ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 407 YASQEPWLF-NASVRDNILFGLpmdKQRYRTVLKRcALERDLELLhgdgTIVGER----GASLSGGQRARICLARAVYRR 481
Cdd:cd03224 79 YVPEGRRIFpELTVEENLLLGA---YARRRAKRKA-RLERVYELF----PRLKERrkqlAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665408680 482 ADVYLLDDP---LS-AVDTHVGRHLFDECMRGflgkQLVILVTHQLQF-LEDADLIVIMDKGHVSACGTYEEML 550
Cdd:cd03224 151 PKLLLLDEPsegLApKIVEEIFEAIRELRDEG----VTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELL 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
337-532 |
8.97e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.30 E-value: 8.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 337 DTLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI--LGELPPE---SGSVQVSGKYSYAS-- 409
Cdd:PRK14239 3 EPILQVSDLSVYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPrt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 410 -------------QEPWLFNASVRDNILFGLPMDKQRYRTVLKRcALERDL----------ELLHgdgtivgERGASLSG 466
Cdd:PRK14239 80 dtvdlrkeigmvfQQPNPFPMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLkgasiwdevkDRLH-------DSALGLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 467 GQRARICLARAVYRRADVYLLDDPLSAVDThVGRHLFDECMRGFLGKQLVILVTHQLQ----------FLEDADLI 532
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDP-ISAGKIEETLLGLKDDYTMLLVTRSMQqasrisdrtgFFLDGDLI 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
357-552 |
1.15e-20 |
|
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: 92.50 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQ-----VSGKYSYAS---------QEPWLF-NASVRD 421
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgedITGLPPHEIarlgigrtfQIPRLFpELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 422 NILFGLPMDKQRYRTVLKRCALERDL-----ELLHgdgtIVG------ERGASLSGGQRARICLARAVYRRADVYLLDDP 490
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREEREAreraeELLE----RVGladladRPAGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 491 ---LSAVDTHVGRHLFDEcMRGFlgKQLVILVTHQLQFLED-ADLIVIMDKGHVSACGTYEEMLKS 552
Cdd:cd03219 171 aagLNPEETEELAELIRE-LRER--GITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
340-551 |
2.06e-20 |
|
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: 91.03 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQHdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY------------SY 407
Cdd:cd03263 1 LQIRNLTKTYKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSirtdrkaarqslGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 408 ASQEPWLFNA-SVRDNILF-----GLPmDKQRYRTVLKrcaLERDLELLHgdgtiVGERGAS-LSGGQRARICLARAVYR 480
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyarlkGLP-KSEIKEEVEL---LLRVLGLTD-----KANKRARtLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 481 RADVYLLDDPLSAVDtHVGRHLFDECMRGFLGKQLVILVTHqlqFLEDADL----IVIMDKGHVSACGTYEEmLK 551
Cdd:cd03263 151 GPSVLLLDEPTSGLD-PASRRAIWDLILEVRKGRSIILTTH---SMDEAEAlcdrIAIMSDGKLRCIGSPQE-LK 220
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
955-1170 |
2.33e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 91.26 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDT---NDIGLHDLR 1030
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVLIDGQDIsslSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1031 -SKISIIPQepvlfsgtmRYNLDPF-----------------EQYPDDKLWKALEDVHLKEEISELPSGLqsiiseggtn 1092
Cdd:COG1136 85 rRHIGFVFQ---------FFNLLPEltalenvalplllagvsRKERRERARELLERVGLGDRLDHRPSQL---------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1093 fSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVE 1170
Cdd:COG1136 146 -SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRelNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
958-1180 |
4.38e-20 |
|
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: 92.81 E-value: 4.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL----SYNDGAILIDSLDTNDIGLHDLRS-- 1031
Cdd:COG0444 5 RNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlpppGITSGEILFDGEDLLKLSEKELRKir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1032 --KISIIPQEPvlfsgtmrYN-LDP--------------FEQYPDDKLWK----ALEDVHL---KEEISELPSglqsiis 1087
Cdd:COG0444 85 grEIQMIFQDP--------MTsLNPvmtvgdqiaeplriHGGLSKAEAREraieLLERVGLpdpERRLDRYPH------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1088 eggtNFSVGQRQLVCLARAILRENRILVMDEATANVdpqtDALIQATIRNKFKD------CTVLTIAHRLNTI--MdSDK 1159
Cdd:COG0444 150 ----ELSGGMRQRVMIARALALEPKLLIADEPTTAL----DVTIQAQILNLLKDlqrelgLAILFITHDLGVVaeI-ADR 220
|
250 260
....*....|....*....|.
gi 665408680 1160 VLVMDAGHVVEFGSPYELLTA 1180
Cdd:COG0444 221 VAVMYAGRIVEEGPVEELFEN 241
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
336-548 |
6.27e-20 |
|
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: 90.87 E-value: 6.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 336 PDTLVEIKALRARWGqeqhDLV-LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKySYASQEPW- 413
Cdd:COG0411 1 SDPLLEVRGLTKRFG----GLVaVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGR-DITGLPPHr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 414 --------------LF-NASVRDNI---------------LFGLPMDKQRYRTVLKRC--ALERdLELLHgdgtIVGERG 461
Cdd:COG0411 76 iarlgiartfqnprLFpELTVLENVlvaaharlgrgllaaLLRLPRARREEREARERAeeLLER-VGLAD----RADEPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 462 ASLSGGQRARICLARAVYRRADVYLLDDP---LSAVDTH-VGRHLFDecMRGFLGKqLVILVTHQLQFLED-ADLIVIMD 536
Cdd:COG0411 151 GNLSYGQQRRLEIARALATEPKLLLLDEPaagLNPEETEeLAELIRR--LRDERGI-TILLIEHDMDLVMGlADRIVVLD 227
|
250
....*....|..
gi 665408680 537 KGHVSACGTYEE 548
Cdd:COG0411 228 FGRVIAEGTPAE 239
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
958-1185 |
6.34e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 92.45 E-value: 6.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRlsYNDGAILIDSLDTNDI---GLHDLRS 1031
Cdd:COG1135 5 ENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLircINLLER--PTSGSVLVDGVDLTALserELRAARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1032 KISIIPQEPVLFSG-TMRYNLD-PFEQypdDKLWKA---------LEDVHLKEEISELPSGLqsiiseggtnfSVGQRQL 1100
Cdd:COG1135 83 KIGMIFQHFNLLSSrTVAENVAlPLEI---AGVPKAeirkrvaelLELVGLSDKADAYPSQL-----------SGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1101 VCLARAILRENRILVMDEATANVDPQTD----ALIQaTIRNKFKdCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPY 1175
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTrsilDLLK-DINRELG-LTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVL 226
|
250
....*....|
gi 665408680 1176 ELLTASKAKV 1185
Cdd:COG1135 227 DVFANPQSEL 236
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
357-533 |
8.39e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.77 E-value: 8.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-------------YSYASQEPWLFNASVRDNI 423
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 424 LFGLPMDKQRyrtvLKRCALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLF 503
Cdd:PRK10247 102 IFPWQIRNQQ----PDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVN 177
|
170 180 190
....*....|....*....|....*....|.
gi 665408680 504 DECMRGFLGKQLVIL-VTHQLQFLEDADLIV 533
Cdd:PRK10247 178 EIIHRYVREQNIAVLwVTHDKDEINHADKVI 208
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
954-1179 |
1.59e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 89.71 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 954 KLVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsyND--------GAILIDSLDTND-- 1023
Cdd:COG1117 11 KIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRM--NDlipgarveGEILLDGEDIYDpd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1024 IGLHDLRSKISIIPQEPVLFSGT--------MRYNLDPFEQYPDDKLWKALEDVHLKEEISElpsglqsIISEGGTNFSV 1095
Cdd:COG1117 85 VDVVELRRRVGMVFQKPNPFPKSiydnvaygLRLHGIKSKSELDEIVEESLRKAALWDEVKD-------RLKKSALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1096 GQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRlntiMD-----SDKVLVMDAGHVVE 1170
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHN----MQqaarvSDYTAFFYLGELVE 233
|
....*....
gi 665408680 1171 FGSPYELLT 1179
Cdd:COG1117 234 FGPTEQIFT 242
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
338-550 |
1.61e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.45 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 338 TLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKySYASQEPWL--- 414
Cdd:PRK13548 1 AMLEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR-PLADWSPAElar 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 415 ------------FNASVRDNILFGL---PMDKQRYRTVLKRcALERdLELLHgdgtIVGERGASLSGGQRARICLARA-- 477
Cdd:PRK13548 77 rravlpqhsslsFPFTVEEVVAMGRaphGLSRAEDDALVAA-ALAQ-VDLAH----LAGRDYPQLSGGEQQRVQLARVla 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 478 -VYRRAD---VYLLDDPLSAVDT----HVGRHLFDECMRGFLGkqlVILVTHQL----QFledADLIVIMDKGHVSACGT 545
Cdd:PRK13548 151 qLWEPDGpprWLLLDEPTSALDLahqhHVLRLARQLAHERGLA---VIVVLHDLnlaaRY---ADRIVLLHQGRLVADGT 224
|
....*
gi 665408680 546 YEEML 550
Cdd:PRK13548 225 PAEVL 229
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
649-928 |
1.69e-19 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 90.35 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 649 IGTQILASG-GDYFLSYWVKNTASSSTLDIYYFTAinvGLVICALLRTLLFFN-------ITMHSSTELHNTMFQGLSRT 720
Cdd:cd18559 8 VLCNHVFSGpSNLWLLLWFDDPVNGPQEHGQVYLS---VLGALAILQGITVFQysmavsiGGIFASRAVHLDLYHKALRS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 721 ALYFFHTNPSGRILNRFANDLGQVDEVMPAV-MLDCIQIFLTLTGIICVLCVTnPWYLINTFAMMLAFYYWRdFYLKTSR 799
Cdd:cd18559 85 PISFFERTPSGELVNLFSKDLDRVDSMAPQViKMWMGPLQNVIGLYLLILLAG-PMAAVGIPLGLLYVPVNR-VYAASSR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 800 DVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDlHSSGYYTFVSTSRAFGYYldLFCVAYVIsVILHN 879
Cdd:cd18559 163 QLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVR--LWCVGPCI-VLFAS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 665408680 880 FFNPPL--HNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEY 928
Cdd:cd18559 239 FFAYVSrhSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
320-551 |
2.29e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.99 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 320 LKEVEKRsYPVGiGKEPDTLVEIKALRARWGQEQHdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSV 399
Cdd:COG1134 7 VENVSKS-YRLY-HEPSRSLKELLLRRRRTRREEF-WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 400 QVSGKYSyasqepWL------FN--ASVRDNILFG---LPMDKQRYRTVLKRCA----LER--DLELlhgdgtivgergA 462
Cdd:COG1134 84 EVNGRVS------ALlelgagFHpeLTGRENIYLNgrlLGLSRKEIDEKFDEIVefaeLGDfiDQPV------------K 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 463 SLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDEcMRGFLGK-QLVILVTHQLQFLED-ADLIVIMDKGHV 540
Cdd:COG1134 146 TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLAR-IRELRESgRTVIFVSHSMGAVRRlCDRAIWLEKGRL 224
|
250
....*....|.
gi 665408680 541 SACGTYEEMLK 551
Cdd:COG1134 225 VMDGDPEEVIA 235
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
973-1169 |
2.40e-19 |
|
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: 86.33 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDSLDTNDIGLHD-LRSKISIIPQepvlfsgtmryn 1050
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSgLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1051 ldpfeqypddklwkaledvhlkeeiselpsglqsiiseggtnFSVGQRQLVCLARAILRENRILVMDEATANVDPQ-TDA 1129
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAeVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 665408680 1130 LIqATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVV 1169
Cdd:cd03216 121 LF-KVIRRlRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
362-560 |
2.55e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.49 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 362 NMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYAS-----------QEPWLFN-ASVRDNILFGL-- 427
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTppsrrpvsmlfQENNLFShLTVAQNIGLGLnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 428 -----PMDKQRYRTVLKRCALERDLELLHGDgtivgergasLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVgRH- 501
Cdd:PRK10771 99 glklnAAQREKLHAIARQMGIEDLLARLPGQ----------LSGGQRQRVALARCLVREQPILLLDEPFSALDPAL-RQe 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 502 ---LFDE-CMRgflgKQLVIL-VTHQlqfLEDADLI----VIMDKGHVSACGTYEEMLKSGQDFAQLL 560
Cdd:PRK10771 168 mltLVSQvCQE----RQLTLLmVSHS---LEDAARIaprsLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
958-1177 |
2.73e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.43 E-value: 2.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPDTnsPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLS-YNDGAILIDSLDTNDIGLHDLRSKISII 1036
Cdd:PRK13648 11 KNVSFQYQSDA--SFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEkVKSGEIFYNNQAITDDNFEKLRKHIGIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1037 PQEPV-LFSG-TMRY--------NLDPFEQYpDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARA 1106
Cdd:PRK13648 89 FQNPDnQFVGsIVKYdvafglenHAVPYDEM-HRRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665408680 1107 ILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYEL 1177
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
358-555 |
3.31e-19 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 88.85 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-----------------KYSYASQEPWLF-NASV 419
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 420 RDNILFGLPMdkqryRTVLKRCALERDLELLHgdgtIVGERGAS------LSGGQRARICLARAVYRRADVYLLDDPLSA 493
Cdd:cd03294 120 LENVAFGLEV-----QGVPRAEREERAAEALE----LVGLEGWEhkypdeLSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 494 VDTHVGRHLFDECMRgfLGKQL---VILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEMLKSGQD 555
Cdd:cd03294 191 LDPLIRREMQDELLR--LQAELqktIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTNPAN 254
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
337-552 |
3.50e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 88.22 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 337 DTLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESG-SVQVSGK----------- 404
Cdd:COG1119 1 DPLLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGErrggedvwelr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 405 -----YSYASQEPWLFNASVRDNILFGL-----------PMDKQRYRTVLKRcalerdLELLHgdgtIVGERGASLSGGQ 468
Cdd:COG1119 78 kriglVSPALQLRFPRDETVLDVVLSGFfdsiglyreptDEQRERARELLEL------LGLAH----LADRPFGTLSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 469 RARICLARAVYRRADVYLLDDPLSAVDTHvGRHLFDECMRGFLGKQL--VILVTHQlqfLEDA----DLIVIMDKGHVSA 542
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLG-ARELLLALLDKLAAEGAptLVLVTHH---VEEIppgiTHVLLLKDGRVVA 223
|
250
....*....|
gi 665408680 543 CGTYEEMLKS 552
Cdd:COG1119 224 AGPKEEVLTS 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
357-540 |
3.57e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.80 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGkYSYASQEPW------------------LFNAS 418
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNG-QDLSRLKRReipylrrrigvvfqdfrlLPDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 419 VRDNILF-----GLPMDKQRYRTvlkRCALERdLELLHGDGTIVGErgasLSGGQRARICLARAVYRRADVYLLDDPLSA 493
Cdd:COG2884 96 VYENVALplrvtGKSRKEIRRRV---REVLDL-VGLSDKAKALPHE----LSGGEQQRVAIARALVNRPELLLADEPTGN 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 665408680 494 VDTHVGR---HLFDECMRgfLGKQlVILVTHQLQFLEDADLIVI-MDKGHV 540
Cdd:COG2884 168 LDPETSWeimELLEEINR--RGTT-VLIATHDLELVDRMPKRVLeLEDGRL 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
339-524 |
3.62e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.60 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 339 LVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK------------YS 406
Cdd:PRK11248 1 MLQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpvegpgaergvvFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 407 YASQEPWLfnaSVRDNILFGLpmdkqRYRTVLKRCALERDLELLhgdgTIVGERGA------SLSGGQRARICLARAVYR 480
Cdd:PRK11248 78 NEGLLPWR---NVQDNVAFGL-----QLAGVEKMQRLEIAHQML----KKVGLEGAekryiwQLSGGQRQRVGIARALAA 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 665408680 481 RADVYLLDDPLSAVDTHVgrhlfDECMRGFL-------GKQlVILVTHQLQ 524
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFT-----REQMQTLLlklwqetGKQ-VLLITHDIE 190
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
337-559 |
5.13e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 88.64 E-value: 5.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 337 DTLVEIKALRARWGQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG------------- 403
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteenvwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 404 KYSYASQEP--WLFNASVRDNILFGLPMDKQRYRTVLKRcaLERDLELLhGDGTIVGERGASLSGGQRARICLARAVYRR 481
Cdd:PRK13650 82 KIGMVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKER--VNEALELV-GMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 482 ADVYLLDDPLSAVDTHvGRHLFDECMRGFLGK-QL-VILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 559
Cdd:PRK13650 159 PKIIILDEATSMLDPE-GRLELIKTIKGIRDDyQMtVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDLLQL 237
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
367-544 |
8.11e-19 |
|
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: 86.39 E-value: 8.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 367 RGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-----------KYSYASQEPWLF-NASVRDNILFGL------- 427
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaappadrPVSMLFQENNLFaHLTVEQNVGLGLspglklt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 428 PMDKQRYRTVLKRCALERDLELLHGdgtivgergaSLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECM 507
Cdd:cd03298 103 AEDRQAIEVALARVGLAGLEKRLPG----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 665408680 508 RGFLGKQL-VILVTHQLQFLED-ADLIVIMDKGHVSACG 544
Cdd:cd03298 173 DLHAETKMtVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
973-1178 |
9.37e-19 |
|
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: 86.33 E-value: 9.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLS-YNDGAILIDSLDTNDIGLHD-LRSKISIIPQEPVLFSG-TMRY 1049
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLpPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1050 NLD-PFEQYPDDKLWKALEDVH-----LKEEISELpsglqsiiseGGTnFSVGQRQLVCLARAILRENRILVMDEATANV 1123
Cdd:cd03224 95 NLLlGAYARRRAKRKARLERVYelfprLKERRKQL----------AGT-LSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 1124 DPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELL 1178
Cdd:cd03224 164 APKIVEEIFEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
957-1177 |
1.07e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 87.84 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 957 TKDLSLRYEPD--TNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSynDGAILIDSLDTNDIG-LHDLR 1030
Cdd:PRK13633 7 CKNVSYKYESNeeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIPS--EGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1031 SKISIIPQEP------------VLFsGTMRYNLDPFE--QYPDDklwkALEDVHLKEEISELPSGLqsiiseggtnfSVG 1096
Cdd:PRK13633 85 NKAGMVFQNPdnqivativeedVAF-GPENLGIPPEEirERVDE----SLKKVGMYEYRRHAPHLL-----------SGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1097 QRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSP 1174
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTP 228
|
...
gi 665408680 1175 YEL 1177
Cdd:PRK13633 229 KEI 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
357-553 |
1.17e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.90 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYAS-------------QEPWL-FNASVRDN 422
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALsaraasrrvasvpQDTSLsFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 423 ILFGLPMDKQRY--RTVLKRCALERDLEllHGDGTIVGERG-ASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTH-- 497
Cdd:PRK09536 98 VEMGRTPHRSRFdtWTETDRAAVERAME--RTGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINhq 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408680 498 -----VGRHLFDEcmrgflGKQlVILVTHQLQFLED-ADLIVIMDKGHVSACGTYEEMLKSG 553
Cdd:PRK09536 176 vrtleLVRRLVDD------GKT-AVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
340-542 |
1.35e-18 |
|
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: 84.02 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-YSYASqepwlfnas 418
Cdd:cd03216 1 LELRGITKRFGGVK---ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKeVSFAS--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 419 vrdnilfglPMDKQRyrtvlkrcalerdlellHGDGTIvgergASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHV 498
Cdd:cd03216 69 ---------PRDARR-----------------AGIAMV-----YQLSVGERQMVEIARALARNARLLILDEPTAALTPAE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 665408680 499 GRHLFdECMRGFLGKQL-VILVTHQLQ-FLEDADLIVIMDKGHVSA 542
Cdd:cd03216 118 VERLF-KVIRRLRAQGVaVIFISHRLDeVFEIADRVTVLRDGRVVG 162
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
958-1170 |
1.80e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 85.49 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEpdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFR-LSYNDGAILIDSLDTNDI---GLHDLRSKI 1033
Cdd:COG2884 5 ENVSKRYP---GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeERPTSGQVLVNGQDLSRLkrrEIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1034 SIIPQ-----------EPVLFSgtMRYnldpfeQYPDDKLWK-----ALEDVHLKEEISELPSGLqsiiseggtnfSVGQ 1097
Cdd:COG2884 82 GVVFQdfrllpdrtvyENVALP--LRV------TGKSRKEIRrrvreVLDLVGLSDKAKALPHEL-----------SGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1098 RQLVCLARAILRENRILVMDEATANVDPQT-----DALIQAtirNKfKDCTVLtIA-HRLNtIMDS--DKVLVMDAGHVV 1169
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETsweimELLEEI---NR-RGTTVL-IAtHDLE-LVDRmpKRVLELEDGRLV 216
|
.
gi 665408680 1170 E 1170
Cdd:COG2884 217 R 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
974-1176 |
2.10e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 87.03 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 974 LKGLSFTIQPMEKVGIVGRTGAGKSSLI---NALfrLSYNDGAILIDSLDTND--IGLHDLRSKISIIPQEP--VLFSGT 1046
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIqhlNGL--LKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQYPeyQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1047 MR-------YNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQsiiseggtnFSVGQRQLVCLARAILRENRILVMDEA 1119
Cdd:PRK13637 101 IEkdiafgpINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFE---------LSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1120 TANVDPQTDALIQATIRN--KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYE 1176
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
326-544 |
2.16e-18 |
|
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: 85.28 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 326 RSYPvgIGKEPDTLVEIKALRARWGQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY 405
Cdd:cd03220 8 KSYP--TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 406 SyasqepWLF--------NASVRDNILFG---LPMDKQRYRTVLKRCA----LERDLELlhgdgtivgeRGASLSGGQRA 470
Cdd:cd03220 86 S------SLLglgggfnpELTGRENIYLNgrlLGLSRKEIDEKIDEIIefseLGDFIDL----------PVKTYSSGMKA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 471 RICLARAVYRRADVYLLDDPLSAVDTHvgrhlFDE-CMRGFLGKQL----VILVTHQLQFLED-ADLIVIMDKGHVSACG 544
Cdd:cd03220 150 RLAFAIATALEPDILLIDEVLAVGDAA-----FQEkCQRRLRELLKqgktVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
958-1177 |
2.27e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 86.71 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSS---LINALfrLSYNDGAILIDSLDTNDIGLHDLRSKIS 1034
Cdd:PRK13650 8 KNLTFKYKEDQEKY-TLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGL--LEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1035 IIPQEP-VLFSGTMrynldpfeqYPDDKLW----KALEDVHLKEEISELPS--GLQSIISEGGTNFSVGQRQLVCLARAI 1107
Cdd:PRK13650 85 MVFQNPdNQFVGAT---------VEDDVAFglenKGIPHEEMKERVNEALElvGMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665408680 1108 LRENRILVMDEATANVDPQTD-ALIQA--TIRNKFkDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYEL 1177
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRlELIKTikGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
958-1149 |
3.38e-18 |
|
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: 84.77 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPDTNSpcvLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSY-NDGAILIDSLDTNDigLHD-----LRS 1031
Cdd:cd03292 4 INVTKTYPNGTAA---LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELpTSGTIRVNGQDVSD--LRGraipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1032 KISIIPQEPVLFsgtmrYNLDPFEQ--------YPDDKLWK-----ALEDVHLKEEISELPSGLqsiiseggtnfSVGQR 1098
Cdd:cd03292 79 KIGVVFQDFRLL-----PDRNVYENvafalevtGVPPREIRkrvpaALELVGLSHKHRALPAEL-----------SGGEQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 665408680 1099 QLVCLARAILRENRILVMDEATANVDPQTDALIqATIRNKFKD--CTVLTIAH 1149
Cdd:cd03292 143 QRVAIARAIVNSPTILIADEPTGNLDPDTTWEI-MNLLKKINKagTTVVVATH 194
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
958-1177 |
4.75e-18 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 84.93 E-value: 4.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIG---LHDLRSKI 1033
Cdd:cd03256 4 ENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTsGSVLIDGTDINKLKgkaLRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1034 SIIPQEP-----------VLFS-----GTMRYNLDPFeqYPDDKL--WKALEDVHLKEEISELPSGLqsiiseggtnfSV 1095
Cdd:cd03256 81 GMIFQQFnlierlsvlenVLSGrlgrrSTWRSLFGLF--PKEEKQraLAALERVGLLDKAYQRADQL-----------SG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1096 GQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1172
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDG 227
|
....*
gi 665408680 1173 SPYEL 1177
Cdd:cd03256 228 PPAEL 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
974-1180 |
6.62e-18 |
|
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: 88.59 E-value: 6.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 974 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAIL-----IDSLDTNDigLHDLRSKISIIPQEP-------- 1040
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRfdgqdLDGLSRRA--LRPLRRRMQVVFQDPfgslsprm 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1041 -----------VLFSGtmrynLDPFEQypDDKLWKALEDVHLKEEIselpsgLQSIISEggtnFSVGQRQLVCLARAILR 1109
Cdd:COG4172 380 tvgqiiaeglrVHGPG-----LSAAER--RARVAEALEEVGLDPAA------RHRYPHE----FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1110 ENRILVMDEATAnvdpqtdAL---IQATIRNKFKDC------TVLTIAHRLNTI--MdSDKVLVMDAGHVVEFGSPYELL 1178
Cdd:COG4172 443 EPKLLVLDEPTS-------ALdvsVQAQILDLLRDLqrehglAYLFISHDLAVVraL-AHRVMVMKDGKVVEQGPTEQVF 514
|
..
gi 665408680 1179 TA 1180
Cdd:COG4172 515 DA 516
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
950-1170 |
7.05e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 84.76 E-value: 7.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 950 PKEGKLVTKDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINA---LFRLSynDGAILIDsldtnDIGL 1026
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLiagLEKPT--SGEVLVD-----GKPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1027 HDLRSKISIIPQEPVLFsgtmrynldpfeqyPddklWK--------------------------ALEDVHLKEEISELPS 1080
Cdd:COG1116 76 TGPGPDRGVVFQEPALL--------------P----WLtvldnvalglelrgvpkaerrerareLLELVGLAGFEDAYPH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1081 GLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQ---ATIRNKFKdCTVLTIAH------RL 1151
Cdd:COG1116 138 QL-----------SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQdelLRLWQETG-KTVLFVTHdvdeavFL 205
|
250 260
....*....|....*....|.
gi 665408680 1152 ntimdSDKVLVMDA--GHVVE 1170
Cdd:COG1116 206 -----ADRVVVLSArpGRIVE 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
357-550 |
7.61e-18 |
|
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: 84.17 E-value: 7.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----------------KYSYASQEPWLFNA-SV 419
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllsgkelrkarrRIGMIFQHFNLLSSrTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 420 RDNILFGLPMDKQRyrtvlKRCALERDLELLHgdgtIVG--ERG----ASLSGGQRARICLARAVYRRADVYLLDDPLSA 493
Cdd:cd03258 100 FENVALPLEIAGVP-----KAEIEERVLELLE----LVGleDKAdaypAQLSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 494 VD---TH-VGRHLFDecmrgfLGKQL---VILVTHQLQFLED-ADLIVIMDKGHVSACGTYEEML 550
Cdd:cd03258 171 LDpetTQsILALLRD------INRELgltIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
354-490 |
9.46e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.20 E-value: 9.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 354 HDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY--SYASQEPWLF-NASVRDNILFGlpmD 430
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLriGYLPQEPPLDdDLTVLDTVLDG---D 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 431 KQRYRTVLKRCALERDLELLHGDGTIVGE-------RGA--------------------------SLSGGQRARICLARA 477
Cdd:COG0488 87 AELRALEAELEELEAKLAEPDEDLERLAElqeefeaLGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARA 166
|
170
....*....|...
gi 665408680 478 VYRRADVYLLDDP 490
Cdd:COG0488 167 LLSEPDLLLLDEP 179
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
337-551 |
1.10e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 86.31 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 337 DTLVEIKALRARWGQeqhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK------------ 404
Cdd:PRK11432 4 KNFVVLKNITKRFGS---NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 405 ----YSYAsqepwLF-NASVRDNILFGLPMDKQRYRTVLKRcaLERDLELLHGDGtiVGERGA-SLSGGQRARICLARAV 478
Cdd:PRK11432 81 cmvfQSYA-----LFpHMSLGENVGYGLKMLGVPKEERKQR--VKEALELVDLAG--FEDRYVdQISGGQQQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 479 YRRADVYLLDDPLSAVDTHVGRHLFDECMRgfLGKQLVI---LVTH-QLQFLEDADLIVIMDKGHVSACGTYEEMLK 551
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRE--LQQQFNItslYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
338-554 |
1.18e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.03 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 338 TLVEIKALRARW-GQEqhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVsGKYSYASQEPW--- 413
Cdd:PRK11264 2 SAIEVKNLVKKFhGQT----VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIDTARSLsqq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 414 -------------------LF-NASVRDNILFGLPMDKQRYRTVlkrcALERDLELLHGDGtIVGERGA---SLSGGQRA 470
Cdd:PRK11264 77 kglirqlrqhvgfvfqnfnLFpHRTVLENIIEGPVIVKGEPKEE----ATARARELLAKVG-LAGKETSyprRLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 471 RICLARAVYRRADVYLLDDPLSAVDTH-VG------RHLFDEcmrgflgKQLVILVTHQLQFLED-ADLIVIMDKGHVSA 542
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDPElVGevlntiRQLAQE-------KRTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
250
....*....|..
gi 665408680 543 CGTYEEMLKSGQ 554
Cdd:PRK11264 225 QGPAKALFADPQ 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
357-552 |
1.30e-17 |
|
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: 83.36 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----KY----------SYASQEPWLF-NASVRD 421
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditKLpmhkrarlgiGYLPQEASIFrKLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 422 NILFGLPMDKQRYRTVLKRcaLERDLELLHGDgTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVD------ 495
Cdd:cd03218 95 NILAVLEIRGLSKKEREEK--LEELLEEFHIT-HLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpiavqd 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 496 -THVGRHLFDecmrgflgKQLVILVT-HQL-QFLEDADLIVIMDKGHVSACGTYEEMLKS 552
Cdd:cd03218 172 iQKIIKILKD--------RGIGVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
950-1177 |
1.73e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 84.08 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 950 PKEGKLVTKDLSLRYePDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSS---LINALFRLSYNDGA-ILIDSLDTNDIG 1025
Cdd:PRK13640 1 MKDNIVEFKHVSFTY-PDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSkITVDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1026 LHDLRSKISIIPQEP------------VLFSGTMRynldpfeQYPDDKLWK----ALEDVHLKEEISELPSglqsiiseg 1089
Cdd:PRK13640 79 VWDIREKVGIVFQNPdnqfvgatvgddVAFGLENR-------AVPRPEMIKivrdVLADVGMLDYIDSEPA--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1090 gtNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN--KFKDCTVLTIAHRLNTIMDSDKVLVMDAGH 1167
Cdd:PRK13640 143 --NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQVLVLDDGK 220
|
250
....*....|
gi 665408680 1168 VVEFGSPYEL 1177
Cdd:PRK13640 221 LLAQGSPVEI 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
340-549 |
1.89e-17 |
|
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: 82.42 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQeqhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG------------KYSY 407
Cdd:cd03265 1 IEVENLVKKYGD---FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 408 ASQEPWLFNA-SVRDNI-----LFGLPMDKQRyrtvlkrcalERDLELLH--GDGTIVGERGASLSGGQRARICLARAVY 479
Cdd:cd03265 78 VFQDLSVDDElTGWENLyiharLYGVPGAERR----------ERIDELLDfvGLLEAADRLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 480 RRADVYLLDDPLSAVDTHVGRHLFD--ECMRGFLGKQlVILVTHqlqFLEDADL----IVIMDKGHVSACGTYEEM 549
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEyiEKLKEEFGMT-ILLTTH---YMEEAEQlcdrVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
955-1170 |
2.26e-17 |
|
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: 82.52 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDtndigLHDLRSKI 1033
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLeRPTSGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1034 SIIPQEPVLFS-GTMRYN--LDPFEQYPDDKLWKA-----LEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLAR 1105
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvaLGLELQGVPKAEAREraeelLELVGLSGFENAYPHQL-----------SGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665408680 1106 AILRENRILVMDEATANVDPQTDALIQATI-----RNKFkdcTVLTIAHRLN-TIMDSDKVLVMDA--GHVVE 1170
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELldiwrETGK---TVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
340-538 |
2.41e-17 |
|
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: 81.88 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQE-------- 411
Cdd:cd03268 1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEalrrigal 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 412 ---PWLF-NASVRDNILFglpmdKQRYRTVLKRcALERDLELLhGDGTIVGERGASLSGGQRARICLARAVYRRADVYLL 487
Cdd:cd03268 78 ieaPGFYpNLTARENLRL-----LARLLGIRKK-RIDEVLDVV-GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 488 DDPLSAVDThVGRHLfdecMRGFL------GKQlVILVTHQLQFLED-ADLIVIMDKG 538
Cdd:cd03268 151 DEPTNGLDP-DGIKE----LRELIlslrdqGIT-VLISSHLLSEIQKvADRIGIINKG 202
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
340-539 |
2.45e-17 |
|
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: 79.80 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQeqhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG--KYSYASQepwlfna 417
Cdd:cd03221 1 IELENLSKTYGG---KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGStvKIGYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 418 svrdnilfglpmdkqryrtvlkrcalerdlellhgdgtivgergasLSGGQRARICLARAVYRRADVYLLDDPLSAVDTH 497
Cdd:cd03221 71 ----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 665408680 498 vGRHLFDECMRGFlgKQLVILVTHQLQFLED-ADLIVIMDKGH 539
Cdd:cd03221 105 -SIEALEEALKEY--PGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
955-1177 |
2.74e-17 |
|
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: 82.17 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTNSpcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDSLDTNDiGLHDLRSKI 1033
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTgELRPTSGTAYINGYSIRT-DRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1034 SIIPQEPVLFSG-TMRYNLdpfeqypddKLW---KALEDVHLKEEISELPS--GLQSIISEGGTNFSVGQRQLVCLARAI 1107
Cdd:cd03263 78 GYCPQFDALFDElTVREHL---------RFYarlKGLPKSEIKEEVELLLRvlGLTDKANKRARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 1108 LRENRILVMDEATANVDPQTD----ALIQATIRNKfkdCTVLTIAHrlntiMD-----SDKVLVMDAGHVVEFGSPYEL 1177
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRraiwDLILEVRKGR---SIILTTHS-----MDeaealCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
340-544 |
2.84e-17 |
|
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: 81.94 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK---------YSYASQ 410
Cdd:cd03269 1 LEVENVTKRFGRVT---ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 411 EPWLF-NASVRDNILF-----GLPMD--KQRYRTVLKRCALERDLEllhgdgtivgERGASLSGGQRARICLARAVYRRA 482
Cdd:cd03269 78 ERGLYpKMKVIDQLVYlaqlkGLKKEeaRRRIDEWLERLELSEYAN----------KRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665408680 483 DVYLLDDPLSAVDThVGRHLFDECMRGFLGK-QLVILVTHQLQFLED-ADLIVIMDKGHVSACG 544
Cdd:cd03269 148 ELLILDEPFSGLDP-VNVELLKDVIRELARAgKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
355-522 |
3.19e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 355 DLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKysyASQEPWLF---------NA-----SVR 420
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG---DIDDPDVAeachylghrNAmkpalTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 421 DNILFglpmdkqrYRTVL--KRCALERDLELLhGDGTIVGERGASLSGGQRARICLAR--AVYRRadVYLLDDPLSAVDT 496
Cdd:PRK13539 92 ENLEF--------WAAFLggEELDIAAALEAV-GLAPLAHLPFGYLSAGQKRRVALARllVSNRP--IWILDEPTAALDA 160
|
170 180
....*....|....*....|....*..
gi 665408680 497 HvGRHLFDECMRGFLGKQ-LVILVTHQ 522
Cdd:PRK13539 161 A-AVALFAELIRAHLAQGgIVIAATHI 186
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
955-1189 |
4.63e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.83 E-value: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSS---LINALFRlsYNDGAILIDSLDTNDIGLHDLRS 1031
Cdd:PRK13642 5 LEVENLVFKYEKESDVN-QLNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLFE--EFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1032 KISIIPQEP-VLFSGTMRYNLDPF----EQYPDDKLWKALEDVHLKEEISELPsglqsiiSEGGTNFSVGQRQLVCLARA 1106
Cdd:PRK13642 82 KIGMVFQNPdNQFVGATVEDDVAFgmenQGIPREEMIKRVDEALLAVNMLDFK-------TREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1107 ILRENRILVMDEATANVDPQTDALIQATIrNKFKD---CTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLTASKA 1183
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVI-HEIKEkyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSED 233
|
....*.
gi 665408680 1184 KVFHGM 1189
Cdd:PRK13642 234 MVEIGL 239
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
336-568 |
4.93e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 83.32 E-value: 4.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 336 PDTLVEIKALRARWGQEqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQ-----VSGKYSYASQ 410
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepVPSRARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 411 E----PWLFNA----SVRDNIL-----FGLPMDKQRYR--TVLKRCALERDLEllhgdgTIVGErgasLSGGQRARICLA 475
Cdd:PRK13537 81 RvgvvPQFDNLdpdfTVRENLLvfgryFGLSAAAARALvpPLLEFAKLENKAD------AKVGE----LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 476 RAVYRRADVYLLDDPLSAVDTHvGRHLFDECMRGFLGKQLVILVThqLQFLEDA----DLIVIMDKGHVSACGTYEEMLK 551
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQ-ARHLMWERLRSLLARGKTILLT--THFMEEAerlcDRLCVIEEGRKIAEGAPHALIE 227
|
250 260 270
....*....|....*....|....*....|...
gi 665408680 552 S----------GQDFAQL------LVESTQNSG 568
Cdd:PRK13537 228 SeigcdvieiyGPDPVALrdelapLAERTEISG 260
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
989-1166 |
5.25e-17 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 81.22 E-value: 5.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 989 IVGRTGAGKSSLINALF-RLSYNDGAILIDSLDTNDIGLHDLRSK----ISIIPQEPVLFSGTMRYNLdPFEQYPDDKLW 1063
Cdd:cd03290 32 IVGQVGCGKSSLLLAILgEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVEENI-TFGSPFNKQRY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1064 KALEDV-HLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQ-TDALIQATIRNKFKD 1141
Cdd:cd03290 111 KAVTDAcSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQD 190
|
170 180
....*....|....*....|....*..
gi 665408680 1142 --CTVLTIAHRLNTIMDSDKVLVMDAG 1166
Cdd:cd03290 191 dkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
353-540 |
5.70e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.37 E-value: 5.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 353 QHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQ----AILGELPPES------GSVQVSGKYS-----------YASQE 411
Cdd:PRK09984 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGShiellgRTVQREGRLArdirksrantgYIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 412 PWLFNA-SVRDNILFGLPMDKQRYRTVLK---RCALERDLELLH--GDGTIVGERGASLSGGQRARICLARAVYRRADVY 485
Cdd:PRK09984 95 FNLVNRlSVLENVLIGALGSTPFWRTCFSwftREQKQRALQALTrvGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 486 LLDDPLSAVDTHVGRHLFDECMRGFLGKQLVILVT-HQLQF-LEDADLIVIMDKGHV 540
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYaLRYCERIVALRQGHV 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
954-1195 |
6.69e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 81.88 E-value: 6.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 954 KLVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL------SYNDGAILIDSLDTNDIGLH 1027
Cdd:PRK14247 3 KIEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypeARVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1028 DLRSKISIIPQEPVLFSgtmryNLDPFEQYP---------------DDKLWKALEDVHLKEEISE---LPSGlqsiiseg 1089
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIP-----NLSIFENVAlglklnrlvkskkelQERVRWALEKAQLWDEVKDrldAPAG-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1090 gtNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAH------RLntimdSDKVLVM 1163
Cdd:PRK14247 146 --KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFL 218
|
250 260 270
....*....|....*....|....*....|..
gi 665408680 1164 DAGHVVEFGSPYELLTASKAKVFHGMVmqTGK 1195
Cdd:PRK14247 219 YKGQIVEWGPTREVFTNPRHELTEKYV--TGR 248
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
955-1136 |
7.54e-17 |
|
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: 80.60 E-value: 7.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDSLDTNDIGlHDLRSKI 1033
Cdd:COG4133 3 LEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAgLLPPSAGEVLWNGEPIRDAR-EDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1034 SIIPQEPVLFSG-TMRYNLDpF------EQYPDDKLWKALEDVHLkEEISELPSGlqsiiseggtNFSVGQRQLVCLARA 1106
Cdd:COG4133 78 AYLGHADGLKPElTVRENLR-FwaalygLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARL 145
|
170 180 190
....*....|....*....|....*....|
gi 665408680 1107 ILRENRILVMDEATANVDPQTDALIQATIR 1136
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
955-1184 |
7.92e-17 |
|
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: 81.05 E-value: 7.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDlRSKI 1033
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLvKPDSGKILLDGQDITKLPMHK-RARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1034 SII--PQEPVLFSG-TMRYNLDPF--EQYPDDKLWKALedvhLKEEISELpsGLQSIISEGGTNFSVGQRQLVCLARAIL 1108
Cdd:cd03218 76 GIGylPQEASIFRKlTVEENILAVleIRGLSKKEREEK----LEELLEEF--HITHLRKSKASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 1109 RENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASKAK 1184
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKIlKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
337-524 |
9.29e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 81.75 E-value: 9.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 337 DTLVEIKALRARWGQEqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI--LGELPPE---SGSVQVSGKYSYAS-- 409
Cdd:PRK14243 8 ETVLRTENLNVYYGSF---LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGKNLYAPdv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 410 -------------QEPWLFNASVRDNILFGL-------PMDKQRYRTvLKRCALERDLEllhgdgTIVGERGASLSGGQR 469
Cdd:PRK14243 85 dpvevrrrigmvfQKPNPFPKSIYDNIAYGAringykgDMDELVERS-LRQAALWDEVK------DKLKQSGLSLSGGQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 470 ARICLARAVYRRADVYLLDDPLSAVDThVGRHLFDECMRGFLGKQLVILVTHQLQ 524
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDP-ISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
974-1213 |
1.00e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.96 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 974 LKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLsyNDGAILIDSLDTNDIG-LHDLRSKISIIPQEPV-------- 1041
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLRP--QKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPEtqfvgrtv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1042 ---LFSGTMRYNLDPFEqypddklWKALEDVHLKEeiselpSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDE 1118
Cdd:PRK13644 96 eedLAFGPENLCLPPIE-------IRKRVDRALAE------IGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1119 ATANVDPQT-DALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPyelltaskAKVFHGMVMQTGKAS 1197
Cdd:PRK13644 163 VTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEP--------ENVLSDVSLQTLGLT 234
|
250
....*....|....*.
gi 665408680 1198 FDHLLKVAENTKQNHI 1213
Cdd:PRK13644 235 PPSLIELAENLKMHGV 250
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
973-1178 |
1.65e-16 |
|
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: 80.07 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLIN--ALFrLSYNDGAILIDSLD-TNdigLHDLRSKISIIPQEPVLFSgtmry 1049
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLEtiAGF-IKPDSGKILLNGKDiTN---LPPEKRDISYVPQNYALFP----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1050 NLDPFE--QYPDDKLWKALEDVHLK-EEISELpSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQ 1126
Cdd:cd03299 85 HMTVYKniAYGLKKRKVDKKEIERKvLEIAEM-LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 1127 T-DALIQ--ATIRNKFkDCTVLTIAHRLNTI-MDSDKVLVMDAGHVVEFGSPYELL 1178
Cdd:cd03299 164 TkEKLREelKKIRKEF-GVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
358-551 |
2.12e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 81.25 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG---------------KYSYASQEP--WLFNASVR 420
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 421 DNILFGlPMD--------KQRYRTVLKRCALERDlellhgdgTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLS 492
Cdd:PRK13637 103 KDIAFG-PINlglseeeiENRVKRAMNIVGLDYE--------DYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 493 AVDTHvGRhlfDECMrgFLGKQL-------VILVTHQlqfLED----ADLIVIMDKGHVSACGTYEEMLK 551
Cdd:PRK13637 174 GLDPK-GR---DEIL--NKIKELhkeynmtIILVSHS---MEDvaklADRIIVMNKGKCELQGTPREVFK 234
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
339-549 |
2.44e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 82.58 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 339 LVEIKALRARWgQEQHdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-------------- 404
Cdd:PRK11607 19 LLEIRNLTKSF-DGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlshvppyqrpinm 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 405 --YSYAsqepwLF-NASVRDNILFGLPMDKQRYRTVLKRcaLERDLELLHGDgTIVGERGASLSGGQRARICLARAVYRR 481
Cdd:PRK11607 96 mfQSYA-----LFpHMTVEQNIAFGLKQDKLPKAEIASR--VNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665408680 482 ADVYLLDDPLSAVDTHVGRHLFDECMrGFLGKQLV--ILVTH-QLQFLEDADLIVIMDKGHVSACGTYEEM 549
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMQLEVV-DILERVGVtcVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
355-522 |
2.93e-16 |
|
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: 78.55 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 355 DLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYS------------YASQEPWLFNA-SVRD 421
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqrdephenilYLGHLPGLKPElSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 422 NILFGLPMDKQRYRTVLKrcALERdLELLHGDGTIVgergASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHvGRH 501
Cdd:TIGR01189 93 NLHFWAAIHGGAQRTIED--ALAA-VGLTGFEDLPA----AQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVA 164
|
170 180
....*....|....*....|..
gi 665408680 502 LFDECMRGFLGKQ-LVILVTHQ 522
Cdd:TIGR01189 165 LLAGLLRAHLARGgIVLLTTHQ 186
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
359-544 |
3.67e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 81.61 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 359 NNVNMSLRRGQLVAVIGPVGSGKSSLIQAILG-----------------ELPPESGSVQVSGKySYASQePWLfnaSVRD 421
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGleditsgdlfigekrmnDVPPAERGVGMVFQ-SYALY-PHL---SVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 422 NILFGLPMDKQRYRTVLKRC-ALERDLELLHgdgtIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGR 500
Cdd:PRK11000 95 NMSFGLKLAGAKKEEINQRVnQVAEVLQLAH----LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 665408680 501 HLFDECMRgfLGKQL---VILVTH-QLQFLEDADLIVIMDKGHVSACG 544
Cdd:PRK11000 171 QMRIEISR--LHKRLgrtMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
958-1182 |
3.72e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.26 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPDTnsPCVLKGL---SFTIQPMEKVGIVGRTGAGKSSLI---NALFRLSynDGAILID----SLDTNDIGLH 1027
Cdd:PRK13641 6 ENVDYIYSPGT--PMEKKGLdniSFELEEGSFVALVGHTGSGKSTLMqhfNALLKPS--SGTITIAgyhiTPETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1028 DLRSKISIIPQ--EPVLFSGTM-------RYNLDPFEQYPDDKLWKALEDVHLKEEiselpsglqsIISEGGTNFSVGQR 1098
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVlkdvefgPKNFGFSEDEAKEKALKWLKKVGLSED----------LISKSPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1099 QLVCLARAILRENRILVMDEATANVDPQTdaliQATIRNKFKDC-----TVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1172
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFKDYqkaghTVILVTHNMDDVAEyADDVLVLEHGKLIKHA 227
|
250
....*....|
gi 665408680 1173 SPYELLTASK 1182
Cdd:PRK13641 228 SPKEIFSDKE 237
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
340-544 |
4.49e-16 |
|
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: 78.39 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGqeqHDLVLNNVNMSLRRGqLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG------------KYSY 407
Cdd:cd03264 1 LQLENLTKRYG---KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 408 ASQEPWLF-NASVRDNIlfglpmdkqRYRTVLKRC-------ALERDLELLHgDGTIVGERGASLSGGQRARICLARAVY 479
Cdd:cd03264 77 LPQEFGVYpNFTVREFL---------DYIAWLKGIpskevkaRVDEVLELVN-LGDRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 480 RRADVYLLDDPLSAVDT---HVGRHLFDEcmrgfLGK-QLVILVTHQLQFLED-ADLIVIMDKGHVSACG 544
Cdd:cd03264 147 GDPSILIVDEPTAGLDPeerIRFRNLLSE-----LGEdRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
958-1193 |
4.97e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.00 E-value: 4.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLI---NALFRLSynDGAILIDSLDT---NDIGLHDLRS 1031
Cdd:PRK11153 5 KNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIrciNLLERPT--SGRVLVDGQDLtalSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1032 KISIIPQEPVLFSG-TMRYNLD-PFE--QYPDDKLWKA----LEDVHLKEEISELPSglqsiiseggtNFSVGQRQLVCL 1103
Cdd:PRK11153 83 QIGMIFQHFNLLSSrTVFDNVAlPLElaGTPKAEIKARvtelLELVGLSDKADRYPA-----------QLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1104 ARAILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRlntiMD-----SDKVLVMDAGHVVEFGSPYE 1176
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPATTRSILELLKdiNRELGLTIVLITHE----MDvvkriCDRVAVIDAGRLVEQGTVSE 227
|
250
....*....|....*..
gi 665408680 1177 LLTASKAKVFHGMVMQT 1193
Cdd:PRK11153 228 VFSHPKHPLTREFIQST 244
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
973-1170 |
5.04e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.37 E-value: 5.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDSLDTNDIGLHD-LRSKISIIPQEPVLF------- 1043
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSgVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVpnlsvae 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1044 ----------SGTMRynldpfeqypddklWKALE------------DVHLKEEISELpsglqsiiseggtnfSVGQRQLV 1101
Cdd:COG1129 99 niflgreprrGGLID--------------WRAMRrrarellarlglDIDPDTPVGDL---------------SVAQQQLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665408680 1102 CLARAILRENRILVMDEATANVDPQ-TDALIqATIRnKFKD--CTVLTIAHRLNTIMD-SDKVLVMDAGHVVE 1170
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLTEReVERLF-RIIR-RLKAqgVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
955-1184 |
5.64e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 79.05 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-------------SYNDGAILIDSLDT 1021
Cdd:PRK14239 6 LQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpevtitgsiVYNGHNIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1022 NDiglhdLRSKISIIPQEPVLFSGT--------MRYNLDPFEQYPDDKLWKALEDVHLKEEISElpsglqsIISEGGTNF 1093
Cdd:PRK14239 82 VD-----LRKEIGMVFQQPNPFPMSiyenvvygLRLKGIKDKQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1094 SVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1172
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYN 229
|
250
....*....|..
gi 665408680 1173 SPYELLTASKAK 1184
Cdd:PRK14239 230 DTKQMFMNPKHK 241
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
356-544 |
6.21e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 78.47 E-value: 6.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 356 LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPE---SGSVQVSGK----------YSYASQ-EPWLFNASVRD 421
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQprkpdqfqkcVAYVRQdDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 422 NILFGLPMDKQRYRTVLKRCALERDLELLH-GDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTH--- 497
Cdd:cd03234 101 TLTYTAILRLPRKSSDAIRKKRVEDVLLRDlALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFtal 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 665408680 498 -VGRHLFDECMRGflgkQLVILVTHQ-----LQFLedaDLIVIMDKGHVSACG 544
Cdd:cd03234 181 nLVSTLSQLARRN----RIVILTIHQprsdlFRLF---DRILLLSSGEIVYSG 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
972-1150 |
6.46e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 76.42 E-value: 6.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 972 CVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGailidsldtnDIGLHDlRSKISIIPQEPVLFSGTMRyn 1050
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwPWGSG----------RIGMPE-GEDLLFLPQRPYLPLGTLR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1051 ldpfEQ--YPddklWkaledvhlkeeiselpsglqsiisegGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTD 1128
Cdd:cd03223 82 ----EQliYP----W--------------------------DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180
....*....|....*....|..
gi 665408680 1129 ALIQATIRNKFkdCTVLTIAHR 1150
Cdd:cd03223 128 DRLYQLLKELG--ITVISVGHR 147
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
973-1168 |
8.35e-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: 77.57 E-value: 8.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILID--SLDTNDIGLHDLRSKISIIPQepvlfsgtmRY 1049
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLeEPDSGTIIIDglKLTDDKKNINELRQKVGMVFQ---------QF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1050 NLDPF------------------EQYPDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILREN 1111
Cdd:cd03262 86 NLFPHltvlenitlapikvkgmsKAEAEERALELLEKVGLADKADAYPAQL-----------SGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 1112 RILVMDEATANVDPQTDALIQATIRNKFKD-CTVLTIAHRLNTIMD-SDKVLVMDAGHV 1168
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
182-550 |
1.03e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 82.07 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 182 NEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGRIAIFVSLL---GF----VLGGGELTAe 254
Cdd:PRK10790 208 NEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSALILCGLLmlfGFsasgTIEVGVLYA- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 255 rafcvtaFYNILRRTVSKF--FPSGMSQFAELLVSMRRITNFMMREeanvidmserRDEKAEEEQhllkevekrsyPVGI 332
Cdd:PRK10790 287 -------FISYLGRLNEPLieLTTQQSMLQQAVVAGERVFELMDGP----------RQQYGNDDR-----------PLQS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 333 GKepdtlVEIKALRARWGQEQhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK----YSYA 408
Cdd:PRK10790 339 GR-----IDIDNVSFAYRDDN--LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplssLSHS 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 409 S---------QEPWLFNASVRDNILFGLPMDKQRYRTVLKRCALErdlELLHG--DG--TIVGERGASLSGGQRARICLA 475
Cdd:PRK10790 412 VlrqgvamvqQDPVVLADTFLANVTLGRDISEEQVWQALETVQLA---ELARSlpDGlyTPLGEQGNNLSVGQKQLLALA 488
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 476 RAVYRRADVYLLDDPLSAVDTHVGRHLfDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEML 550
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAI-QQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
955-1177 |
1.17e-15 |
|
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: 77.41 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLD-TNDIGlhDLRSK 1032
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTsGRATVAGHDvVREPR--EVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1033 ISIIPQEPVLFSG-TMRYNLDPFEQ---YPDDKLwkaledvhlKEEISELPS--GLQSIISEGGTNFSVGQRQLVCLARA 1106
Cdd:cd03265 75 IGIVFQDLSVDDElTGWENLYIHARlygVPGAER---------RERIDELLDfvGLLEAADRLVKTYSGGMRRRLEIARS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 1107 ILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHrlntIMD-----SDKVLVMDAGHVVEFGSPYEL 1177
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYIEklKEEFGMTILLTTH----YMEeaeqlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
357-549 |
1.60e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 78.31 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK---------------YSYASQEPWLFNASVRD 421
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfvgLVFQNPDDQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 422 NILFG---LPMD----KQRYRTVLKRCALE--RDLELLHgdgtivgergasLSGGQRARICLARAVYRRADVYLLDDPLS 492
Cdd:PRK13652 99 DIAFGpinLGLDeetvAHRVSSALHMLGLEelRDRVPHH------------LSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 493 AVDTHVGRHLFDeCMRGFLGK--QLVILVTHQLQFL-EDADLIVIMDKGHVSACGTYEEM 549
Cdd:PRK13652 167 GLDPQGVKELID-FLNDLPETygMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
358-540 |
1.68e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 78.33 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-----------------KYSYASQ--EPWLFNAS 418
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 419 VRDNILFGlPM------DKQRYRTV--LKRCALERDLellhgdgtiVGERGASLSGGQRARICLARAVYRRADVYLLDDP 490
Cdd:PRK13641 103 VLKDVEFG-PKnfgfseDEAKEKALkwLKKVGLSEDL---------ISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 491 LSAVDTHvGRHlfdECMRGFLGKQ----LVILVTHQLQFLED-ADLIVIMDKGHV 540
Cdd:PRK13641 173 AAGLDPE-GRK---EMMQLFKDYQkaghTVILVTHNMDDVAEyADDVLVLEHGKL 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
357-550 |
1.85e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.75 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--YSYASQE--------PWLFNA----SVRDN 422
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpiSMLSSRQlarrlallPQHHLTpegiTVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 423 ILFG----LPM-------DKQRyrtvlkrcaLERDLELLHGDgTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPL 491
Cdd:PRK11231 97 VAYGrspwLSLwgrlsaeDNAR---------VNQAMEQTRIN-HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 492 SAVDTHvgrHLFdECMRgfLGKQL------VILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEML 550
Cdd:PRK11231 167 TYLDIN---HQV-ELMR--LMRELntqgktVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
340-552 |
1.92e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.43 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--YSYAS-------- 409
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvATTPSrelakrla 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 410 ---QEPwLFNA--SVRDNILFG---------LPMDKQRYRTVLKRCALErDLELLHGDgtivgergaSLSGGQRARICLA 475
Cdd:COG4604 79 ilrQEN-HINSrlTVRELVAFGrfpyskgrlTAEDREIIDEAIAYLDLE-DLADRYLD---------ELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 476 RAVYRRADVYLLDDPLSAVDTH-------VGRHLFDEcmrgfLGKQlVILVTHQLQFLED-ADLIVIMDKGHVSACGTYE 547
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKhsvqmmkLLRRLADE-----LGKT-VVIVLHDINFASCyADHIVAMKDGRVVAQGTPE 221
|
....*
gi 665408680 548 EMLKS 552
Cdd:COG4604 222 EIITP 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
357-548 |
2.34e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-YSYAS-------------QEPWLF-NASVRD 421
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpCARLTpakahqlgiylvpQEPLLFpNLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 422 NILFGLP---MDKQRYRTVLKRCALERDLELLHGdgtivgergaSLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHV 498
Cdd:PRK15439 106 NILFGLPkrqASMQKMKQLLAALGCQLDLDSSAG----------SLEVADRQIVEILRGLMRDSRILILDEPTASLTPAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 665408680 499 GRHLFDEcMRGFLGKQL-VILVTHQL-QFLEDADLIVIMDKGHVSACGTYEE 548
Cdd:PRK15439 176 TERLFSR-IRELLAQGVgIVFISHKLpEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
958-1179 |
2.36e-15 |
|
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: 76.96 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEpdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHDLRSKISII 1036
Cdd:cd03295 4 ENVTKRYG---GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTsGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1037 PQEPVLFSG-TMRYN--LDP-FEQYP----DDKLWKALEDVHLKEE--ISELPSGLqsiiseggtnfSVGQRQLVCLARA 1106
Cdd:cd03295 81 IQQIGLFPHmTVEENiaLVPkLLKWPkekiRERADELLALVGLDPAefADRYPHEL-----------SGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 1107 ILRENRILVMDEATANVDPQTDALIQATIRNKFKDC--TVLTIAHRLN-TIMDSDKVLVMDAGHVVEFGSPYELLT 1179
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
357-556 |
3.04e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 76.61 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-------Y-------SYASQEPWLF-NASVRD 421
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmHkrarlgiGYLPQEASIFrKLTVED 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 422 NIL-----FGLPMDKQRYRTVlkrcALERDLELLHgdgtIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVD- 495
Cdd:COG1137 98 NILavlelRKLSKKEREERLE----ELLEEFGITH----LRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDp 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 496 ------THVGRHLFDecmRGfLGkqlvILVT-HQ----LQfledadlIV----IMDKGHVSACGTYEEMLKS-------- 552
Cdd:COG1137 170 iavadiQKIIRHLKE---RG-IG----VLITdHNvretLG-------ICdrayIISEGKVLAEGTPEEILNNplvrkvyl 234
|
....
gi 665408680 553 GQDF 556
Cdd:COG1137 235 GEDF 238
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
330-550 |
3.35e-15 |
|
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: 76.87 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 330 VGIGKEpdtlVEIKALRARWgQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG------ 403
Cdd:cd03288 14 VGLGGE----IKIHDLCVRY-ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidiskl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 404 -------KYSYASQEPWLFNASVRDNILFGLPMDKQRYRTVLKRCALERDLELLHGD-GTIVGERGASLSGGQRARICLA 475
Cdd:cd03288 89 plhtlrsRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGlDAVVTEGGENFSVGQRQLFCLA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 476 RAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFlGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEML 550
Cdd:cd03288 169 RAFVRKSSILIMDEATASIDMATENILQKVVMTAF-ADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
357-522 |
3.80e-15 |
|
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: 75.22 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG------KYSYASQEPWLFNA-------SVRDNI 423
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpldfqRDSIARGLLYLGHApgikttlSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 424 LFGLPmdkqryrtvlkrcalerdlelLHGDGTI------VGERG------ASLSGGQRARICLARAVYRRADVYLLDDPL 491
Cdd:cd03231 95 RFWHA---------------------DHSDEQVeealarVGLNGfedrpvAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|..
gi 665408680 492 SAVDTHvGRHLFDECMRGFLGK-QLVILVTHQ 522
Cdd:cd03231 154 TALDKA-GVARFAEAMAGHCARgGMVVLTTHQ 184
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
339-540 |
4.72e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.15 E-value: 4.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 339 LVEIKALRARW--GQEQHDlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQaILGEL-PPESGSVQVSGKySYASQEPWLF 415
Cdd:PRK10535 4 LLELKDIRRSYpsGEEQVE-VLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLdKPTSGTYRVAGQ-DVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 416 NASVRDNilFGLPMdkQRYRT------------------VLKRCALERDLELLH--GDGTIVGERGASLSGGQRARICLA 475
Cdd:PRK10535 81 AQLRREH--FGFIF--QRYHLlshltaaqnvevpavyagLERKQRLLRAQELLQrlGLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665408680 476 RAVYRRADVYLLDDPLSAVDTHVGrhlfDECMRgfLGKQL------VILVTHQLQFLEDADLIVIMDKGHV 540
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSG----EEVMA--ILHQLrdrghtVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
976-1177 |
5.16e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 77.85 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 976 GLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIG---LHDLRSKISIIPQEPvlFSgtmryNL 1051
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLeEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP--YA-----SL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1052 DP--------------FEQYP----DDKLWKALEDVHLKEE-ISELPSglqsiisEggtnFSVGQRQLVCLARAILRENR 1112
Cdd:COG4608 109 NPrmtvgdiiaeplriHGLASkaerRERVAELLELVGLRPEhADRYPH-------E----FSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 1113 ILVMDEATAnvdpqtdAL---IQATIRNKFKD------CTVLTIAHRLNT---ImdSDKVLVMDAGHVVEFGSPYEL 1177
Cdd:COG4608 178 LIVCDEPVS-------ALdvsIQAQVLNLLEDlqdelgLTYLFISHDLSVvrhI--SDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
358-496 |
5.19e-15 |
|
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: 75.52 E-value: 5.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----------------KYSYASQE-PWLFNASVR 420
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraipylrrKIGVVFQDfRLLPDRNVY 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 421 DNILFGLPMDKQRYRTVLKRC--ALERdLELLHGDGTIVGErgasLSGGQRARICLARAVYRRADVYLLDDPLSAVDT 496
Cdd:cd03292 97 ENVAFALEVTGVPPREIRKRVpaALEL-VGLSHKHRALPAE----LSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
342-540 |
5.37e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 76.25 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 342 IKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVqVSGKYSYAS---------QE- 411
Cdd:PRK11247 15 LNAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEaredtrlmfQDa 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 412 ---PWlfnASVRDNILFGLPMD-KQRYRTVLKRCAL-ERdlellhgdgtiVGERGASLSGGQRARICLARAVYRRADVYL 486
Cdd:PRK11247 91 rllPW---KKVIDNVGLGLKGQwRDAALQALAAVGLaDR-----------ANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 487 LDDPLSAVD--THVG-RHLFDECMR--GFlgkqLVILVTHQL-QFLEDADLIVIMDKGHV 540
Cdd:PRK11247 157 LDEPLGALDalTRIEmQDLIESLWQqhGF----TVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
959-1172 |
6.12e-15 |
|
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: 75.10 E-value: 6.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 959 DLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLhDLRSKISIIP 1037
Cdd:cd03266 6 ALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLlEPDAGFATVDGFDVVKEPA-EARRRLGFVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1038 QEPVLFSG-TMRYNLDPFEQY---PDDKLWKALEDVHLKEEISELpsglqsiISEGGTNFSVGQRQLVCLARAILRENRI 1113
Cdd:cd03266 85 DSTGLYDRlTARENLEYFAGLyglKGDELTARLEELADRLGMEEL-------LDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665408680 1114 LVMDEATANVD-PQTDALIQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1172
Cdd:cd03266 158 LLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
358-551 |
6.67e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.70 E-value: 6.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQ-------------------EPWLFNAS 418
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeikpvrkkvgvvfqfpESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 419 VRDNILFGlPMDKQRYRTVLKRCALERdLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHV 498
Cdd:PRK13643 102 VLKDVAFG-PQNFGIPKEKAEKIAAEK-LEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 665408680 499 GRHLFDECMRGFLGKQLVILVTHQLQFLED-ADLIVIMDKGHVSACGTYEEMLK 551
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
357-544 |
6.99e-15 |
|
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: 74.51 E-value: 6.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPE--SGSVQVSGKysyaSQEPWLFNASV----RDNILFGlpmd 430
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGR----PLDKRSFRKIIgyvpQDDILHP---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 431 kqrYRTVlkRCALERDLELlhgdgtivgeRGasLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFdECMRGf 510
Cdd:cd03213 96 ---TLTV--RETLMFAAKL----------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM-SLLRR- 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 665408680 511 LGKQ--LVILVTHQL--QFLEDADLIVIMDKGHVSACG 544
Cdd:cd03213 157 LADTgrTIICSIHQPssEIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
336-550 |
7.83e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 76.43 E-value: 7.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 336 PDTLVEIKALRARWGQEQHdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK---YS------ 406
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidYSrkglmk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 407 --------YASQEPWLFNASVRDNILFG-----LPMD--KQRYRTVLKRCALERdlelLHGDGTivgergASLSGGQRAR 471
Cdd:PRK13636 80 lresvgmvFQDPDNQLFSASVYQDVSFGavnlkLPEDevRKRVDNALKRTGIEH----LKDKPT------HCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 472 ICLARAVYRRADVYLLDDPLSAVD---THVGRHLFDECMRGfLGKQLVIlVTHQLQFLE-DADLIVIMDKGHVSACGTYE 547
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDpmgVSEIMKLLVEMQKE-LGLTIII-ATHDIDIVPlYCDNVFVMKEGRVILQGNPK 227
|
...
gi 665408680 548 EML 550
Cdd:PRK13636 228 EVF 230
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
30-564 |
7.98e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 80.17 E-value: 7.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 30 EHGNGHsYNaQIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRLSRTSlggtTTGQVVNLLSNDLNR 109
Cdd:PLN03130 949 THGPLF-YN-LIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTN----PLGRIINRFAKDLGD 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 110 FDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVL-----YLPLQTYLSRVTsklRLQTALRTDQRVRMmNEI 184
Cdd:PLN03130 1023 IDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVlfygaYLYYQSTAREVK---RLDSITRSPVYAQF-GEA 1098
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 185 ISGIQVIKMYtweRPFGKLIGQMRRSEMSSIR----QMNLLRGILLSFEiTLGRIAIFVSLLGFVLGGGELTAERAFCvt 260
Cdd:PLN03130 1099 LNGLSTIRAY---KAYDRMAEINGRSMDNNIRftlvNMSSNRWLAIRLE-TLGGLMIWLTASFAVMQNGRAENQAAFA-- 1172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 261 afynilrrtvskffpsgmSQFAELLVSMRRITNFM---MREEA---NVIDMSERRDEKAEEEQHLLKEVEKRSYPVGIGK 334
Cdd:PLN03130 1173 ------------------STMGLLLSYALNITSLLtavLRLASlaeNSLNAVERVGTYIDLPSEAPLVIENNRPPPGWPS 1234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 335 EPDTLVEIKALRARwgqeqHDL--VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----KYSYA 408
Cdd:PLN03130 1235 SGSIKFEDVVLRYR-----PELppVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdisKFGLM 1309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 409 S---------QEPWLFNASVRDNI-LFGLPMD--------KQRYRTVLKRCALERDLEllhgdgtiVGERGASLSGGQRA 470
Cdd:PLN03130 1310 DlrkvlgiipQAPVLFSGTVRFNLdPFNEHNDadlwesleRAHLKDVIRRNSLGLDAE--------VSEAGENFSVGQRQ 1381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 471 RICLARAVYRRADVYLLDDPLSAVDthVG---------RHLFDECmrgflgKQLVIlvTHQLQFLEDADLIVIMDKGHVS 541
Cdd:PLN03130 1382 LLSLARALLRRSKILVLDEATAAVD--VRtdaliqktiREEFKSC------TMLII--AHRLNTIIDCDRILVLDAGRVV 1451
|
570 580
....*....|....*....|....
gi 665408680 542 ACGTYEEML-KSGQDFAQlLVEST 564
Cdd:PLN03130 1452 EFDTPENLLsNEGSAFSK-MVQST 1474
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
342-540 |
8.37e-15 |
|
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: 75.45 E-value: 8.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 342 IKALRARWGQEQHDLV-LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLFNASV- 419
Cdd:cd03267 20 IGSLKSLFKRKYREVEaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 420 ---RDNILFGLP-------------MDKQRYRTVLKRCALERDLE-LLHgdgTIVgergASLSGGQRARICLARAVYRRA 482
Cdd:cd03267 100 fgqKTQLWWDLPvidsfyllaaiydLPPARFKKRLDELSELLDLEeLLD---TPV----RQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 483 DVYLLDDPLSAVDTHVGRHLfdecmRGFLgKQL-------VILVTHQLQFLED-ADLIVIMDKGHV 540
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENI-----RNFL-KEYnrergttVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
405-555 |
8.45e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.07 E-value: 8.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 405 YSYASQEPWLFNASVRDNILFGLP-MDKQRYRTVLKRCALERDLELLHGD-GTIVGERGASLSGGQRARICLARAVYRRA 482
Cdd:PTZ00265 1298 FSIVSQEPMLFNMSIYENIKFGKEdATREDVKRACKFAAIDEFIESLPNKyDTNVGPYGKSLSGGQKQRIAIARALLREP 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 483 DVYLLDDPLSAVDTHvGRHLFDECMRGFLGK--QLVILVTHQLQFLEDADLIVIMDK-----GHVSACGTYEEMLkSGQD 555
Cdd:PTZ00265 1378 KILLLDEATSSLDSN-SEKLIEKTIVDIKDKadKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELL-SVQD 1455
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
953-1177 |
8.92e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 77.42 E-value: 8.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 953 GKLVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINA---LFRLSynDGAILIDSLDTNDIGLHDl 1029
Cdd:COG3839 2 ASLELENVSKSYGGVE----ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMiagLEDPT--SGEILIGGRDVTDLPPKD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1030 RsKISIIPQEPVLF-SGTMRYNLdpfeQYP-----------DDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQ 1097
Cdd:COG3839 75 R-NIAMVFQSYALYpHMTVYENI----AFPlklrkvpkaeiDRRVREAAELLGLEDLLDRKPKQL-----------SGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1098 RQLVCLARAILRENRILVMDEATANVDPQtdalIQATIRNKFKDctvltIAHRLNTIM-----D-------SDKVLVMDA 1165
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDAK----LRVEMRAEIKR-----LHRRLGTTTiyvthDqveamtlADRIAVMND 209
|
250
....*....|..
gi 665408680 1166 GHVVEFGSPYEL 1177
Cdd:COG3839 210 GRIQQVGTPEEL 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
958-1179 |
9.73e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.84 E-value: 9.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYepDTNSpcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAILID--------SLDTNDIGLHDL 1029
Cdd:PRK14258 11 NNLSFYY--DTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEgrveffnqNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1030 RSKISIIPQEPVLFSGTM----RYNLDPFEQYP----DDKLWKALEDVHLKEEIselpsglQSIISEGGTNFSVGQRQLV 1101
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVydnvAYGVKIVGWRPkleiDDIVESALKDADLWDEI-------KHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1102 CLARAILRENRILVMDEATANVDPQTDALIQATIRNKF--KDCTVLTIAHRLNTIMD-SDKVLVMDA-----GHVVEFGS 1173
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFGL 239
|
....*.
gi 665408680 1174 PYELLT 1179
Cdd:PRK14258 240 TKKIFN 245
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
972-1172 |
9.95e-15 |
|
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: 74.12 E-value: 9.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 972 CVLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL--FRLSYND-GAILIDSLdtnDIGLHDLRSKISIIPQEPVLFSgtmr 1048
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVsGEVLINGR---PLDKRSFRKIIGYVPQDDILHP---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1049 yNLDPFEQypddkLWKALEdvhlkeeiselpsgLQSIiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVDPQTD 1128
Cdd:cd03213 96 -TLTVRET-----LMFAAK--------------LRGL--------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 665408680 1129 ALIQATIRNKFKD-CTVLTIAHRLNTIMDS--DKVLVMDAGHVVEFG 1172
Cdd:cd03213 148 LQVMSLLRRLADTgRTIICSIHQPSSEIFElfDKLLLLSQGRVIYFG 194
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
350-540 |
1.00e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 75.61 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 350 GQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSV--------QVSGKYSYASQE---------P 412
Cdd:TIGR02769 19 GAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVsfrgqdlyQLDRKQRRAFRRdvqlvfqdsP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 413 WLFNA--SVRDNIlfGLPMdkqRYRTVLKRCA-LERDLELLHG---DGTIVGERGASLSGGQRARICLARAVYRRADVYL 486
Cdd:TIGR02769 99 SAVNPrmTVRQII--GEPL---RHLTSLDESEqKARIAELLDMvglRSEDADKLPRQLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 487 LDDPLSAVDTHVGRHLFD--ECMRGFLGKQLViLVTHQLQFLED-ADLIVIMDKGHV 540
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILEllRKLQQAFGTAYL-FITHDLRLVQSfCQRVAVMDKGQI 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
973-1174 |
1.15e-14 |
|
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: 74.78 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL---FRLSYndGAILIDSLDTNDIGLHDlRSKISIIP--QEPVLFSG-T 1046
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsgfLRPTS--GSVLFDGEDITGLPPHE-IARLGIGRtfQIPRLFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1047 MRYNLD---------------PFEQYPD--DKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILR 1109
Cdd:cd03219 92 VLENVMvaaqartgsglllarARREEREarERAEELLERVGLADLADRPAGEL-----------SYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 1110 ENRILVMDEATANVDPQ-TDALIQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSP 1174
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTP 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
955-1178 |
1.17e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.79 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTnspcvlKGLSFTIQPMEKVGIVGRTGAGKSSLINAL--FrLSYNDGAILIDSLDTNDIGLHDlRsK 1032
Cdd:COG3840 2 LRLDDLTYRYGDFP------LRFDLTIAAGERVAILGPSGAGKSTLLNLIagF-LPPDSGRILWNGQDLTALPPAE-R-P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1033 ISIIPQEPVLFSG-TMRYN----------LDPFEQypdDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLV 1101
Cdd:COG3840 73 VSMLFQENNLFPHlTVAQNiglglrpglkLTAEQR---AQVEQALERVGLAGLLDRLPGQL-----------SGGQRQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1102 CLARAILRENRILVMDEATANVDP----QTDALIQATIRNkfKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYE 1176
Cdd:COG3840 139 ALARCLVRKRPILLLDEPFSALDPalrqEMLDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAA 216
|
..
gi 665408680 1177 LL 1178
Cdd:COG3840 217 LL 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
259-495 |
1.27e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.31 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 259 VTAFyNILRRTVSkFFPSGMSQFAELLVSMRRITNFMmreeaNVIDMSERRDEKAEeeqhllkevekrsypvGIGKEPDT 338
Cdd:COG4178 305 ASAF-GQVQGALS-WFVDNYQSLAEWRATVDRLAGFE-----EALEAADALPEAAS----------------RIETSEDG 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 339 LVEIKALRARWGQEQhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQV--SGKYSYASQEPWLFN 416
Cdd:COG4178 362 ALALEDLTLRTPDGR--PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPL 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 417 ASVRDNILFGLP---MDKQRYRTVLKRCALERDLELLHgdgtIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSA 493
Cdd:COG4178 440 GTLREALLYPATaeaFSDAELREALEAVGLGHLAERLD----EEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
..
gi 665408680 494 VD 495
Cdd:COG4178 516 LD 517
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
333-555 |
1.32e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.57 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 333 GKEPDTLVEIKALRARWGQEqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG--------- 403
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNR---CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenipamsrs 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 404 -------KYSYASQEPWLF-NASVRDNILFGLPMDKQRYRTVLKRCALERdLEllhgdgtIVGERGAS------LSGGQR 469
Cdd:PRK11831 78 rlytvrkRMSMLFQSGALFtDMNVFDNVAYPLREHTQLPAPLLHSTVMMK-LE-------AVGLRGAAklmpseLSGGMA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 470 ARICLARAVYRRADVYLLDDPLSAVD---THVGRHLFDEcMRGFLGKQLVIlVTHQL-QFLEDADLIVIMDKGHVSACGT 545
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDpitMGVLVKLISE-LNSALGVTCVV-VSHDVpEVLSIADHAYIVADKKIVAHGS 227
|
250
....*....|
gi 665408680 546 YEEmLKSGQD 555
Cdd:PRK11831 228 AQA-LQANPD 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
298-544 |
1.63e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.41 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 298 EEANVIDMSERRDEKAEEEQHLLKEVEKRSYPvgiGKEPDTLVEIKALRARWGQEqhdLVLNNVNMSLRRGQLVAVIGPV 377
Cdd:PRK13536 3 TRAVAEEAPRRLELSPIERKHQGISEAKASIP---GSMSTVAIDLAGVSKSYGDK---AVVNGLSFTVASGECFGLLGPN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 378 GSGKSSLIQAILGELPPESGSVQVSG------------KYSYASQEPWL-FNASVRDNIL-FG--LPMDKQRYRTV---- 437
Cdd:PRK13536 77 GAGKSTIARMILGMTSPDAGKITVLGvpvpararlaraRIGVVPQFDNLdLEFTVRENLLvFGryFGMSTREIEAVipsl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 438 LKRCALERDLELlhgdgtivgeRGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHvGRHLFDECMRGFLGK-QLV 516
Cdd:PRK13536 157 LEFARLESKADA----------RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLARgKTI 225
|
250 260 270
....*....|....*....|....*....|..
gi 665408680 517 ILVTHqlqFLEDA----DLIVIMDKGHVSACG 544
Cdd:PRK13536 226 LLTTH---FMEEAerlcDRLCVLEAGRKIAEG 254
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
358-550 |
1.67e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.41 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYS----------------YASQEPWLFNASVRD 421
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfsklqgirklvgivFQNPETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 422 NILFG---LPMDKQRYRTVLKRCALERDLELLHGDGTivgergASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHV 498
Cdd:PRK13644 98 DLAFGpenLCLPPIEIRKRVDRALAEIGLEKYRHRSP------KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 665408680 499 GRHLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEML 550
Cdd:PRK13644 172 GIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
955-1178 |
1.76e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.27 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTNSpcvLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSynDGAILIDS--LDTNDIGLHDL 1029
Cdd:PRK13636 6 LKVEELNYNYSDGTHA---LKGININIKKGEVTAILGGNGAGKSTLfqnLNGILKPS--SGRILFDGkpIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1030 RSKISIIPQEP--VLFSGTMRYNLD--PFE-QYPDDKLWKALEDVHLKEEISELPSGLQSIISeggtnfsVGQRQLVCLA 1104
Cdd:PRK13636 81 RESVGMVFQDPdnQLFSASVYQDVSfgAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLS-------FGQKKRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 1105 RAILRENRILVMDEATANVDPQTDALIQATIRNKFK--DCTVLTIAHRLNTI-MDSDKVLVMDAGHVVEFGSPYELL 1178
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
954-1186 |
1.89e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.67 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 954 KLVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFR-LSYNDGAILIDSLDTNDIGLHDLRSK 1032
Cdd:PRK11231 2 TLRTENLTVGYGTKR----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARlLTPQSGTVFLGDKPISMLSSRQLARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1033 ISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKAL--EDVHL------KEEISELPSGLQsiiseggTNFSVGQRQLVCLA 1104
Cdd:PRK11231 78 LALLPQHHLTPEGITVRELVAYGRSPWLSLWGRLsaEDNARvnqameQTRINHLADRRL-------TDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1105 RAILRENRILVMDEATANVDPQTDALIQATIR---NKFKdcTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTA 1180
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRelnTQGK--TVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTP 228
|
....*..
gi 665408680 1181 SKAK-VF 1186
Cdd:PRK11231 229 GLLRtVF 235
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
942-1179 |
2.88e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 75.27 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 942 EKQPPKSWPKEGKLVTKDLSLRYEPDTNSPC-VLKGLSFTIQPMEKVGIVGRTGAGKSSLI---NALFRLSYND------ 1011
Cdd:PRK13631 9 KLKVPNPLSDDIILRVKNLYCVFDEKQENELvALNNISYTFEKNKIYFIIGNSGSGKSTLVthfNGLIKSKYGTiqvgdi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1012 --GAILIDSLDTNDIG------LHDLRSKISIIPQEP--VLFSGTMR-------YNLDPFEQYPDDKLWKALEDVHLKEE 1074
Cdd:PRK13631 89 yiGDKKNNHELITNPYskkiknFKELRRRVSMVFQFPeyQLFKDTIEkdimfgpVALGVKKSEAKKLAKFYLNKMGLDDS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1075 ISEL-PSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVDPQTDA-LIQATIRNKFKDCTVLTIAHRLN 1152
Cdd:PRK13631 169 YLERsPFGL-----------SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTME 237
|
250 260
....*....|....*....|....*...
gi 665408680 1153 TIMD-SDKVLVMDAGHVVEFGSPYELLT 1179
Cdd:PRK13631 238 HVLEvADEVIVMDKGKILKTGTPYEIFT 265
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
336-542 |
4.13e-14 |
|
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: 73.24 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 336 PDTLVEIKALRARWGQEQHDL-VLNNVNMSLRRGQLVAVIGPVGSGKSSLIqAILGEL-PPESGSVQVSGkysyasQEpw 413
Cdd:COG4181 5 SAPIIELRGLTKTVGTGAGELtILKGISLEVEAGESVAIVGASGSGKSTLL-GLLAGLdRPTSGTVRLAG------QD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 414 LFN------ASVR--------------------DNI-----LFGLPMDKQRYRTVLKRCALErdlELLHgdgtivgERGA 462
Cdd:COG4181 76 LFAldedarARLRarhvgfvfqsfqllptltalENVmlpleLAGRRDARARARALLERVGLG---HRLD-------HYPA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 463 SLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRH----LFDecMRGFLGKQLViLVTHQLQFLEDADLIVIMDKG 538
Cdd:COG4181 146 QLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQiidlLFE--LNRERGTTLV-LVTHDPALAARCDRVLRLRAG 222
|
....
gi 665408680 539 HVSA 542
Cdd:COG4181 223 RLVE 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
973-1176 |
5.30e-14 |
|
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: 73.15 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL---FRLSynDGAILIDSLDTNDIGLHDL-RSKISIIPQEPVLFSG--- 1045
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLItgfYRPT--SGRILFDGRDITGLPPHRIaRLGIARTFQNPRLFPEltv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1046 ----------TMRYNLDPFEQYPD----------DKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLAR 1105
Cdd:COG0411 97 lenvlvaahaRLGRGLLAALLRLPrarreerearERAEELLERVGLADRADEPAGNL-----------SYGQQRRLEIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 1106 AILRENRILVMDEATANVDPQ-TDALIQaTIR--NKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYE 1176
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEeTEELAE-LIRrlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
955-1183 |
6.13e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.50 E-value: 6.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSL-INALFRLSYNDGAILI--DSLDTNDIGLHDLRS 1031
Cdd:PRK13638 2 LATSDLWFRYQDEP----VLKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLLRPQKGAVLWqgKPLDYSKRGLLALRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1032 KISIIPQEPvlfsgtmryNLDPFEQYPDDKLWKALEDVHLKE-EISELPSGLQSIISEGGTN------FSVGQRQLVCLA 1104
Cdd:PRK13638 78 QVATVFQDP---------EQQIFYTDIDSDIAFSLRNLGVPEaEITRRVDEALTLVDAQHFRhqpiqcLSHGQKKRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1105 RAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTI-AHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASK 1182
Cdd:PRK13638 149 GALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACTE 228
|
.
gi 665408680 1183 A 1183
Cdd:PRK13638 229 A 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
973-1177 |
6.76e-14 |
|
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: 75.99 E-value: 6.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL--------------FRLSY-----------NDG-----------AILI 1016
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptsgriiYHVALcekcgyverpsKVGepcpvcggtlePEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1017 DSLDTNDIGLHDLRSKISIIPQEPVLFSG--TMRYN-LDPFEQ--YP-DDKLWKA---LEDVHLKEEISELPSGLqsiis 1087
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNvLEALEEigYEgKEAVGRAvdlIEMVQLSHRITHIARDL----- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1088 eggtnfSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN--KFKDCTVLTIAHRLNTIMD-SDKVLVMD 1164
Cdd:TIGR03269 170 ------SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDlSDKAIWLE 243
|
250
....*....|...
gi 665408680 1165 AGHVVEFGSPYEL 1177
Cdd:TIGR03269 244 NGEIKEEGTPDEV 256
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
337-540 |
8.32e-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: 70.92 E-value: 8.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 337 DTLVEIKALRARwgqeqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASqepwlfn 416
Cdd:cd03215 2 EPVLEVRGLSVK-------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRR------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 417 aSVRDNILFGL---PMDKQRYRTVLKRcALERDLELlhgdgtivgerGASLSGGQRARICLARAVYRRADVYLLDDPLSA 493
Cdd:cd03215 68 -SPRDAIRAGIayvPEDRKREGLVLDL-SVAENIAL-----------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 665408680 494 VDthVG-----RHLFDECMRGFLGkqlVILVTHQLQ-FLEDADLIVIMDKGHV 540
Cdd:cd03215 135 VD--VGakaeiYRLIRELADAGKA---VLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
958-1180 |
8.73e-14 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 72.42 E-value: 8.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEpDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL---SYNDGAILIDsldtNDIG---LHDLRS 1031
Cdd:COG1119 7 RNVTVRRG-GKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlppTYGNDVRLFG----ERRGgedVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1032 KISII---------PQEPVL------FSGTmrynLDPFEQYPD---DKLWKALEDVHLKEEISELPSGLqsiiseggtnf 1093
Cdd:COG1119 79 RIGLVspalqlrfpRDETVLdvvlsgFFDS----IGLYREPTDeqrERARELLELLGLAHLADRPFGTL----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1094 SVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN--KFKDCTVLTIAHRLNTIMDS-DKVLVMDAGHVVE 1170
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVA 223
|
250
....*....|
gi 665408680 1171 FGSPYELLTA 1180
Cdd:COG1119 224 AGPKEEVLTS 233
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
975-1177 |
9.13e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.97 E-value: 9.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 975 KGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILI---DSLDTNDIGLHDLRSKISIIPQEPvLFSGTMRYN 1050
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLvKATDGEVAWlgkDLLGMKDDEWRAVRSDIQMIFQDP-LASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1051 L-----DPFEQY-PDdklwkaLEDVHLKEEISE--LPSGL-QSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATA 1121
Cdd:PRK15079 117 IgeiiaEPLRTYhPK------LSRQEVKDRVKAmmLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665408680 1122 NVDPQtdalIQATIRNKFKDC------TVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYEL 1177
Cdd:PRK15079 191 ALDVS----IQAQVVNLLQQLqremglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
358-585 |
9.30e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 9.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK------------YSYASQE-PWLFNASVRDNIL 424
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlvaYVPQSEEvDWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 425 FGL-----------PMDKQRYRTVLKRCALerdLELLHGDgtiVGErgasLSGGQRARICLARAVYRRADVYLLDDPLSA 493
Cdd:PRK15056 103 MGRyghmgwlrrakKRDRQIVTAALARVDM---VEFRHRQ---IGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 494 VDTHVG-------RHLFDEcmrgflGKQLVIlVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSG---QDFAQLLVES 563
Cdd:PRK15056 173 VDVKTEariisllRELRDE------GKTMLV-STHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAEnleLAFSGVLRHV 245
|
250 260
....*....|....*....|....*
gi 665408680 564 TQnSGGGDEIITS---PNLSRQSSA 585
Cdd:PRK15056 246 AL-NGSEESIITDderPFISHRPAA 269
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-550 |
9.75e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 72.64 E-value: 9.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI--LGELPPE---SGSVQVSGKYSYAS----- 409
Cdd:PRK14247 4 IEIRDLKVSFGQVE---VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPEarvSGEVYLDGQDIFKMdviel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 410 --------QEP-WLFNASVRDNILFGLPMDK---------QRYRTVLKRCALERDLEllhgdgTIVGERGASLSGGQRAR 471
Cdd:PRK14247 81 rrrvqmvfQIPnPIPNLSIFENVALGLKLNRlvkskkelqERVRWALEKAQLWDEVK------DRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 472 ICLARAVYRRADVYLLDDP---LSAVDTHVGRHLFDEcmrgfLGKQL-VILVTH-QLQFLEDADLIVIMDKGHVSACGTY 546
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPtanLDPENTAKIESLFLE-----LKKDMtIVLVTHfPQQAARISDYVAFLYKGQIVEWGPT 229
|
....
gi 665408680 547 EEML 550
Cdd:PRK14247 230 REVF 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
357-581 |
1.17e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.38 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAiLGELPPESGSVQVSGKYSYASQ---------------------EPWLF 415
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQniyerrvnlnrlrrqvsmvhpKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 416 NASVRDNILFGLPMDKQRYRTVLK---RCALeRDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLS 492
Cdd:PRK14258 101 PMSVYDNVAYGVKIVGWRPKLEIDdivESAL-KDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 493 AVDTHVGRHLFDECMRGFLGKQL-VILVTHQLQfledadlivimdkgHVSACGTYEEMLKSGQDFAQLLVEstqnSGGGD 571
Cdd:PRK14258 180 GLDPIASMKVESLIQSLRLRSELtMVIVSHNLH--------------QVSRLSDFTAFFKGNENRIGQLVE----FGLTK 241
|
250
....*....|
gi 665408680 572 EIITSPNLSR 581
Cdd:PRK14258 242 KIFNSPHDSR 251
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
357-549 |
1.22e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 72.80 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG---KYSYAS------------QEP--WLFNASV 419
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepiKYDKKSllevrktvgivfQNPddQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 420 RDNILFG-----LPMD--KQRYRTVLKRCALErdlellhgdgtivG-ERGAS--LSGGQRARICLARAVYRRADVYLLDD 489
Cdd:PRK13639 97 EEDVAFGplnlgLSKEevEKRVKEALKAVGME-------------GfENKPPhhLSGGQKKRVAIAGILAMKPEIIVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 490 PLSAVD----THVGRHLFDECMRGFlgkqLVILVTHQLQFLED-ADLIVIMDKGHVSACGTYEEM 549
Cdd:PRK13639 164 PTSGLDpmgaSQIMKLLYDLNKEGI----TIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
352-552 |
1.23e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 72.72 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 352 EQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-YSYAS------------QEP--WLFN 416
Cdd:PRK13632 19 NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGItISKENlkeirkkigiifQNPdnQFIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 417 ASVRDNILFGLP---MDKQRYRTVLKRCALERDLEllhgdgTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSA 493
Cdd:PRK13632 99 ATVEDDIAFGLEnkkVPPKKMKDIIDDLAKKVGME------DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665408680 494 VDTHvGRHLFDECMRGF--LGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKS 552
Cdd:PRK13632 173 LDPK-GKREIKKIMVDLrkTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
978-1185 |
1.26e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.54 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 978 SFTIQPMEKVGIVGRTGAGKSSLIN--ALFrLSYNDGAILIDSLDTNDIGlhDLRSKISIIPQEPVLFSG-TMRYN---- 1050
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNliAGF-LTPASGSLTLNGQDHTTTP--PSRRPVSMLFQENNLFSHlTVAQNiglg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1051 LDP---FEQYPDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVDP-- 1125
Cdd:PRK10771 96 LNPglkLNAAQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDEPFSALDPal 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 1126 --QTDALIQATIRNkfKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLT--ASKAKV 1185
Cdd:PRK10771 165 rqEMLTLVSQVCQE--RQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLSgkASASAL 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
350-540 |
1.33e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.41 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 350 GQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----KYSYASQE-------------P 412
Cdd:PRK10419 20 GKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplaKLNRAQRKafrrdiqmvfqdsI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 413 WLFNA--SVRDNIlfGLPMdkqRYRTVLKRCA-LERDLELLHG---DGTIVGERGASLSGGQRARICLARAVYRRADVYL 486
Cdd:PRK10419 100 SAVNPrkTVREII--REPL---RHLLSLDKAErLARASEMLRAvdlDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 487 LDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTHQLQFLED-ADLIVIMDKGHV 540
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKK--LQQQFgtaCLFITHDLRLVERfCQRVMVMDNGQI 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
974-1169 |
1.70e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 74.68 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 974 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILID--------SLDTNDIGlhdlrskISIIPQEPVLF- 1043
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDsGEILIDgkpvrirsPRDAIALG-------IGMVHQHFMLVp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1044 ------------SGTMRYNLDPfeqypdDKLWKALE--------DVHLKEEISELpsglqsiiseggtnfSVGQRQLVCL 1103
Cdd:COG3845 94 nltvaenivlglEPTKGGRLDR------KAARARIRelseryglDVDPDAKVEDL---------------SVGEQQRVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1104 ARAILRENRILVMDEATANVDPQ-TDALIqATIRnKFKD--CTVLTIAHRLNTIMD-SDKVLVMDAGHVV 1169
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPQeADELF-EILR-RLAAegKSIIFITHKLREVMAiADRVTVLRRGKVV 220
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
357-538 |
1.96e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.76 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELP--PESGSVQVsgkysyaSQEPWLFNASVRDNILFGLPMDKQRY 434
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV-------PDNQFGREASLIDAIGRKGDFKDAVE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 435 rtVLKRCALerdlellhGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTH----VGRHLFDECMRgf 510
Cdd:COG2401 118 --LLNAVGL--------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQtakrVARNLQKLARR-- 185
|
170 180 190
....*....|....*....|....*....|
gi 665408680 511 LGKQLVIlVTHQLQFLED--ADLIVIMDKG 538
Cdd:COG2401 186 AGITLVV-ATHHYDVIDDlqPDLLIFVGYG 214
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
358-559 |
2.53e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 71.73 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------KYSYASQ------------EPWLFNAS 418
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktKDKYIRPvrkrigmvfqfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 419 VRDNILFG-----LPMD--KQRYRTVLKRCALERDlellhgdgtIVGERGASLSGGQRARICLARAVYRRADVYLLDDPL 491
Cdd:PRK13646 103 VEREIIFGpknfkMNLDevKNYAHRLLMDLGFSRD---------VMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665408680 492 SAVDTHvGRHlfdECMRGFLGKQL-----VILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 559
Cdd:PRK13646 174 AGLDPQ-SKR---QVMRLLKSLQTdenktIILVSHDMnEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLADW 243
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
955-1183 |
2.61e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 71.65 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSynDGAILID--SLDTNDIGLHDL 1029
Cdd:PRK13639 2 LETRDLKYSYPDGTE---ALKGINFKAEKGEMVALLGPNGAGKSTLflhFNGILKPT--SGEVLIKgePIKYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1030 RSKISIIPQEpvlfsgtmrynldpfeqyPDDKLW--KALEDVHL--------KEEISE-LPSGLQSIISEGGTN-----F 1093
Cdd:PRK13639 77 RKTVGIVFQN------------------PDDQLFapTVEEDVAFgplnlglsKEEVEKrVKEALKAVGMEGFENkpphhL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1094 SVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIR--NKfKDCTVLTIAHRLNTI-MDSDKVLVMDAGHVVE 1170
Cdd:PRK13639 139 SGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYdlNK-EGITIIISTHDVDLVpVYADKVYVMSDGKIIK 217
|
250
....*....|...
gi 665408680 1171 FGSPYELLTASKA 1183
Cdd:PRK13639 218 EGTPKEVFSDIET 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
357-535 |
2.96e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.90 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-YSYAS-------------QEPWLF-NASVRD 421
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpVRFRSprdaqaagiaiihQELNLVpNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 422 NILFGLP------MDK----QRYRTVLKRCALERDLEllhgdgTIVGErgasLSGGQRARICLARAVYRRADVYLLDDP- 490
Cdd:COG1129 99 NIFLGREprrgglIDWramrRRARELLARLGLDIDPD------TPVGD----LSVAQQQLVEIARALSRDARVLILDEPt 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 665408680 491 --LSAVDThvgRHLFDeCMRgflgkQL------VILVTHQL-QFLEDADLIVIM 535
Cdd:COG1129 169 asLTEREV---ERLFR-IIR-----RLkaqgvaIIYISHRLdEVFEIADRVTVL 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
339-544 |
3.89e-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: 70.09 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 339 LVEIKALRARWGQEQ-HDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGkySYASQEP----- 412
Cdd:cd03266 1 MITADALTKRFRDVKkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPaearr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 413 ---WLFNA-------SVRDNI-----LFGLPMD--KQRYRTVLKRCALERDLEllhgdgtivgERGASLSGGQRARICLA 475
Cdd:cd03266 79 rlgFVSDStglydrlTARENLeyfagLYGLKGDelTARLEELADRLGMEELLD----------RRVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 476 RAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQLVILVTHQLQFLED-ADLIVIMDKGHVSACG 544
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
340-558 |
3.92e-13 |
|
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: 71.04 E-value: 3.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQHdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPEsGSVQVSG-------------KYS 406
Cdd:cd03289 3 MTVKDLTAKYTEGGN-AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGvswnsvplqkwrkAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 407 YASQEPWLFNASVRDNI-LFGLPMDKQRYR--------TVLKRCALERDLELLHGdgtivgerGASLSGGQRARICLARA 477
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLdPYGKWSDEEIWKvaeevglkSVIEQFPGQLDFVLVDG--------GCVLSHGHKQLMCLARS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 478 VYRRADVYLLDDPLSAVD-------THVGRHLFDECMrgflgkqlVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEML 550
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDpityqviRKTLKQAFADCT--------VILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL 224
|
....*...
gi 665408680 551 KSGQDFAQ 558
Cdd:cd03289 225 NEKSHFKQ 232
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
67-508 |
4.35e-13 |
|
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: 73.63 E-value: 4.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 67 LAMKMRVAVSSAIYRKalrlsrtSLGGTTTGQVVNL----------LSNDLNRFDRCLIHFHFLWLGP-LELLIASYFLY 135
Cdd:TIGR00954 162 LKLRFRVRLTRYLYSK-------YLSGFTFYKVSNLdsriqnpdqlLTQDVEKFCDSVVELYSNLTKPiLDVILYSFKLL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 136 EQIG------MASFYGISILVLylplqTYLSRVTSKLRLQTAlRTDQRVRMMN-EIISGIQVIKMY--------TWERPF 200
Cdd:TIGR00954 235 TALGsvgpagLFAYLFATGVVL-----TKLRPPIGKLTVEEQ-ALEGEYRYVHsRLIMNSEEIAFYqgnkvekeTVMSSF 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 201 GKLIGQMRRSEMSSIrQMNLLRGILLSFEIT-LGRIAIFVSLLgFVLGGGELTAERAFCVTAFYNILRRTVSkfFPSGMS 279
Cdd:TIGR00954 309 YRLVEHLNLIIKFRF-SYGFLDNIVAKYTWSaVGLVAVSIPIF-DKTHPAFLEMSEEELMQEFYNNGRLLLK--AADALG 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 280 QFAELLVSMRRITNFMMR--EEANVIDMSERRDEK--AEEEQHLLKEVEKRSYPV-GIGKEPDTLVEIKALRARWGQEQH 354
Cdd:TIGR00954 385 RLMLAGRDMTRLAGFTARvdTLLQVLDDVKSGNFKrpRVEEIESGREGGRNSNLVpGRGIVEYQDNGIKFENIPLVTPNG 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 355 DLVLNNVNMSLRRGQLVAVIGPVGSGKSSLiQAILGELPPESG---SVQVSGKYSYASQEPWLFNASVRDNILFglPMDK 431
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSL-FRILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIY--PDSS 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 432 -QRYRTVLKRCALERDLELLHGDGTIVGERGAS--------LSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHL 502
Cdd:TIGR00954 542 eDMKRRGLSDKDLEQILDNVQLTHILEREGGWSavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYM 621
|
....*.
gi 665408680 503 FDECMR 508
Cdd:TIGR00954 622 YRLCRE 627
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
958-1169 |
4.59e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.89 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPDT-NSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL---FRLSynDGAILIDSLDTNDIGLHDlRSK- 1032
Cdd:COG1101 5 KNLSKTFNPGTvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIagsLPPD--SGSILIDGKDVTKLPEYK-RAKy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1033 ISIIPQEPVLfsGT---M--------------RYNLDPfeqypddKLWKALEDvHLKEEISELPSGLQSIISEGGTNFSV 1095
Cdd:COG1101 82 IGRVFQDPMM--GTapsMtieenlalayrrgkRRGLRR-------GLTKKRRE-LFRELLATLGLGLENRLDTKVGLLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 1096 GQRQLVCLARAILRENRILVMDEATANVDPQTDALI-QATirNKF---KDCTVLTIAHRLNTIMD-SDKVLVMDAGHVV 1169
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVlELT--EKIveeNNLTTLMVTHNMEQALDyGNRLIMMHEGRII 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
357-540 |
6.73e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.11 E-value: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-------YSYAS------QEPWL---FNASVR 420
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtklpeYKRAKyigrvfQDPMMgtaPSMTIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 421 DNIL--------FGLPM-----DKQRYRTVLKRcaLERDLE--LlhgdGTIVGergaSLSGGQRARICLARAVYRRADVY 485
Cdd:COG1101 101 ENLAlayrrgkrRGLRRgltkkRRELFRELLAT--LGLGLEnrL----DTKVG----LLSGGQRQALSLLMATLTKPKLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665408680 486 LLDDPLSAVDTHVGRHLFDecmrgfLGKQLV-------ILVTHQLQF-LEDADLIVIMDKGHV 540
Cdd:COG1101 171 LLDEHTAALDPKTAALVLE------LTEKIVeennlttLMVTHNMEQaLDYGNRLIMMHEGRI 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-521 |
7.82e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 69.87 E-value: 7.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI--LGELPPES---GSVQVSGKYSYAS----- 409
Cdd:PRK14267 5 IETVNLRVYYGSNH---VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrLLELNEEArveGEVRLFGRNIYSPdvdpi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 410 ----------QEPWLF-NASVRDNILFGLPMDK---------QRYRTVLKRCALERDLEllhgdgTIVGERGASLSGGQR 469
Cdd:PRK14267 82 evrrevgmvfQYPNPFpHLTIYDNVAIGVKLNGlvkskkeldERVEWALKKAALWDEVK------DRLNDYPSNLSGGQR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 665408680 470 ARICLARAVYRRADVYLLDDPLSAVDThVGRHLFDECMRGFLGKQLVILVTH 521
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDP-VGTAKIEELLFELKKEYTIVLVTH 206
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
337-547 |
8.71e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.65 E-value: 8.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 337 DTLVEIKALRARWGQEQHD--LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY--------- 405
Cdd:PRK13631 19 DIILRVKNLYCVFDEKQENelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYigdkknnhe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 406 --------------------SYASQEP--WLFNASVRDNILFG---LPMDKQRYRTVLKRCalerdLELLHGDGTIVGER 460
Cdd:PRK13631 99 litnpyskkiknfkelrrrvSMVFQFPeyQLFKDTIEKDIMFGpvaLGVKKSEAKKLAKFY-----LNKMGLDDSYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 461 GASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQLVILVTHQL-QFLEDADLIVIMDKGH 539
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMeHVLEVADEVIVMDKGK 253
|
....*....
gi 665408680 540 VSACGT-YE 547
Cdd:PRK13631 254 ILKTGTpYE 262
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
309-576 |
1.18e-12 |
|
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: 73.12 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 309 RDEKA-EEEQHLLKEVEKRSYPVGIGkepDTLVEIKALRARWGQEQHDLV----------LNNVNMSLRRGQLVAVIGPV 377
Cdd:TIGR01257 889 REERAlEKTEPLTEEMEDPEHPEGIN---DSFFERELPGLVPGVCVKNLVkifepsgrpaVDRLNITFYENQITAFLGHN 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 378 GSGKSSLIQAILGELPPESGSVQVSGK------------YSYASQEPWLF-NASVRDNILFGLPMDKQRYRTV-LKRCAL 443
Cdd:TIGR01257 966 GAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrqsLGMCPQHNILFhHLTVAEHILFYAQLKGRSWEEAqLEMEAM 1045
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 444 ERDLELLHGDgtivGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQlVILVTHQl 523
Cdd:TIGR01257 1046 LEDTGLHHKR----NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRT-IIMSTHH- 1119
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408680 524 qfLEDADL----IVIMDKGHVSACGTyEEMLKS--GQDFAQLLV---ESTQNSGGGDEIITS 576
Cdd:TIGR01257 1120 --MDEADLlgdrIAIISQGRLYCSGT-PLFLKNcfGTGFYLTLVrkmKNIQSQRGGCEGTCS 1178
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
360-534 |
1.35e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.91 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 360 NVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK------YSYASQEPWLFNA-------SVRDNILFG 426
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpirrqrDEYHQDLLYLGHQpgiktelTALENLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 427 LPMdKQRYRTVLKRCALERdlellhgdgtiVGERG------ASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTH--- 497
Cdd:PRK13538 99 QRL-HGPGDDEALWEALAQ-----------VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQgva 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 665408680 498 -VGRHLFDECMRGflGkqLVILVTHQLQFLEDADLIVI 534
Cdd:PRK13538 167 rLEALLAQHAEQG--G--MVILTTHQDLPVASDKVRKL 200
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
358-562 |
1.36e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 69.65 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVsGKYS---------------------YASQEPWLFN 416
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GDYAipanlkkikevkrlrkeiglvFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 417 ASVRDNILFG---LPMDKQR-YRTV---LKRCALERDLellhgdgtiVGERGASLSGGQRARICLARAVYRRADVYLLDD 489
Cdd:PRK13645 106 ETIEKDIAFGpvnLGENKQEaYKKVpelLKLVQLPEDY---------VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 490 PLSAVDTHVGR---HLFDECMRGFlgKQLVILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQLLVE 562
Cdd:PRK13645 177 PTGGLDPKGEEdfiNLFERLNKEY--KKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKIEID 251
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
958-1180 |
1.42e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 71.64 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-----SYNDGAILIDSLDTNDIGLHDLR-- 1030
Cdd:COG4172 10 EDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpaAHPSGSILFDGQDLLGLSERELRri 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1031 --SKISIIPQEPvlfsgtMRyNLDPF----EQ----------YPDDKLWK----ALEDVHLKEE---ISELP---SGlqs 1084
Cdd:COG4172 90 rgNRIAMIFQEP------MT-SLNPLhtigKQiaevlrlhrgLSGAAARAraleLLERVGIPDPerrLDAYPhqlSG--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1085 iiseggtnfsvGQRQLVCLARAILRENRILVMDEatanvdPQT--DALIQATIRNKFKDCT------VLTIAHRLNTIMD 1156
Cdd:COG4172 160 -----------GQRQRVMIAMALANEPDLLIADE------PTTalDVTVQAQILDLLKDLQrelgmaLLLITHDLGVVRR 222
|
250 260
....*....|....*....|....*
gi 665408680 1157 -SDKVLVMDAGHVVEFGSPYELLTA 1180
Cdd:COG4172 223 fADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
955-1172 |
1.62e-12 |
|
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: 68.05 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSynDGAILIDSLDTNDIGLHDlrS 1031
Cdd:cd03301 1 VELENVTKRFGNVT----ALDDLNLDIADGEFVVLLGPSGCGKTTTlrmIAGLEEPT--SGRIYIGGRDVTDLPPKD--R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1032 KISIIPQEPVLFS-----GTMRYNLDpFEQYPDDKLWKALEDV----HLKEEISELPSGLqsiiseggtnfSVGQRQLVC 1102
Cdd:cd03301 73 DIAMVFQNYALYPhmtvyDNIAFGLK-LRKVPKDEIDERVREVaellQIEHLLDRKPKQL-----------SGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 1103 LARAILRENRILVMDEATANVdpqtDALIQATIRNKFK------DCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1172
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNL----DAKLRVQMRAELKrlqqrlGTTTIYVTHDQVEAMTmADRIAVMNDGQIQQIG 213
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
973-1177 |
1.74e-12 |
|
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: 69.50 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILidsldtndiglHDLRskISIIPQEPVLFSGTMRYNL 1051
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKIK-----------HSGR--ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1052 DPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALI 1131
Cdd:cd03291 119 IFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 665408680 1132 qatirnkFKDC--------TVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYEL 1177
Cdd:cd03291 199 -------FESCvcklmankTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
353-548 |
1.94e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 70.29 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 353 QHDLvlnNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-----------------KYSYASQEPWLF 415
Cdd:PRK11144 12 DLCL---TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaekgiclppekrRIGYVFQDARLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 416 -NASVRDNILFGL-PMDKQRYRTVLKRCALERDLELLHgdgtivgergASLSGGQRARICLARAVYRRADVYLLDDPLSA 493
Cdd:PRK11144 89 pHYKVRGNLRYGMaKSMVAQFDKIVALLGIEPLLDRYP----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 494 VDTHVGRHLFDECMRgfLGKQL---VILVTHQLQ-FLEDADLIVIMDKGHVSACGTYEE 548
Cdd:PRK11144 159 LDLPRKRELLPYLER--LAREInipILYVSHSLDeILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
350-559 |
2.63e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 68.58 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 350 GQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPW---------------- 413
Cdd:PRK13633 18 EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdirnkagmvfqnpdnq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 414 LFNASVRDNILFG---LPMDKQRYRTVLKRCaLERdlellhgdgtiVG----ERGAS--LSGGQRARICLARAVYRRADV 484
Cdd:PRK13633 98 IVATIVEEDVAFGpenLGIPPEEIRERVDES-LKK-----------VGmyeyRRHAPhlLSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 485 YLLDDPLSAVDTHVGRHLFDECMRgfLGKQ---LVILVTHQLQFLEDADLIVIMDKGHVSACGT-------YEEMLKSGQ 554
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKE--LNKKygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTpkeifkeVEMMKKIGL 243
|
....*
gi 665408680 555 DFAQL 559
Cdd:PRK13633 244 DVPQV 248
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
973-1180 |
3.13e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.46 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDslDTNDIGL-----HDLrsKISIIPQEPVLFSG- 1045
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDsGTLEIG--GNPCARLtpakaHQL--GIYLVPQEPLLFPNl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1046 TMRYNLD---PFEQYPDDKLwkaledvhlKEEISELPSGLQSIISEGGTNfsVGQRQLVCLARAILRENRILVMDEATAN 1122
Cdd:PRK15439 102 SVKENILfglPKRQASMQKM---------KQLLAALGCQLDLDSSAGSLE--VADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1123 VDP-QTDALIQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTA 1180
Cdd:PRK15439 171 LTPaETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTD 230
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
955-1173 |
3.21e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 69.37 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYE-PDTNSPCVlKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAIL-------IDSLDTNDIGL 1026
Cdd:PRK09473 13 LDVKDLRVTFStPDGDVTAV-NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGgsatfngREILNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1027 HDLRS-KISIIPQEPVLfsgtmryNLDPFEQYPDdklwKALEDVHLKEEISELPSGLQSI-------ISEGGT------- 1091
Cdd:PRK09473 92 NKLRAeQISMIFQDPMT-------SLNPYMRVGE----QLMEVLMLHKGMSKAEAFEESVrmldavkMPEARKrmkmyph 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1092 NFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQaTIRNKFKD---CTVLTIAHRLNTIMDS-DKVLVMDAGH 1167
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIM-TLLNELKRefnTAIIMITHDLGVVAGIcDKVLVMYAGR 239
|
....*.
gi 665408680 1168 VVEFGS 1173
Cdd:PRK09473 240 TMEYGN 245
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
973-1184 |
3.31e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.61 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHD-LRSKISIIPQEPVLFSGTMRY- 1049
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDaGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRRLSVYd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1050 NLDPFEQYPDDKLWKALED--VHLKEE--ISELPSGLqsiisegGTNFSVGQRQLVCLARAILRENRILVMDEATANVDP 1125
Cdd:PRK10895 98 NLMAVLQIRDDLSAEQREDraNELMEEfhIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408680 1126 QTDALIQATIRNkFKD--CTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASKAK 1184
Cdd:PRK10895 171 ISVIDIKRIIEH-LRDsgLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDEHVK 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
337-544 |
4.07e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.22 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 337 DTLVEIKALRARWGQEQHdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPW--- 413
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTK--ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 414 ------------LFNASVRDNILFGlPMD--------KQRYRTVLKRCALE--RDLELLHgdgtivgergasLSGGQRAR 471
Cdd:PRK13647 80 kvglvfqdpddqVFSSTVWDDVAFG-PVNmgldkdevERRVEEALKAVRMWdfRDKPPYH------------LSYGQKKR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 472 ICLARAVYRRADVYLLDDPLSAVDTHVGRHLFdECMRGF--LGKQlVILVTHQLQF-LEDADLIVIMDKGHVSACG 544
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM-EILDRLhnQGKT-VIVATHDVDLaAEWADQVIVLKEGRVLAEG 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
357-574 |
4.14e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 68.95 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--YSYASQEpwL-------------FN----A 417
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdlTALSERE--LraarrkigmifqhFNllssR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 418 SVRDNILF-----GLPMDKQRyrtvlkrcalERDLELLHgdgtIVG--ERGAS----LSGGQRARICLARAVYRRADVYL 486
Cdd:COG1135 98 TVAENVALpleiaGVPKAEIR----------KRVAELLE----LVGlsDKADAypsqLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 487 LDDPLSAVDTHVGR---HLFDEcmrgfLGKQL---VILVTHQLQFLED-ADLIVIMDKGHVSACGTYEEM-LKSGQDFAQ 558
Cdd:COG1135 164 CDEATSALDPETTRsilDLLKD-----INRELgltIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLDVfANPQSELTR 238
|
250
....*....|....*.
gi 665408680 559 LLVESTQNSGGGDEII 574
Cdd:COG1135 239 RFLPTVLNDELPEELL 254
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
340-548 |
5.45e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 68.21 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKysyasqepwLFNASV 419
Cdd:COG4152 2 LELKGLTKRFGDKT---AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE---------PLDPED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 420 RDNIlfG-LP-----------------------MDKQRYRTVLKRcALERdLELlhgdgtivGERGA----SLSGGQRAR 471
Cdd:COG4152 70 RRRI--GyLPeerglypkmkvgeqlvylarlkgLSKAEAKRRADE-WLER-LGL--------GDRANkkveELSKGNQQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 472 ICLARAVYRRADVYLLDDPLSAVDThVGRHLFDECMRgflgkQL------VILVTHQLQFLED-ADLIVIMDKGHVSACG 544
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDP-VNVELLKDVIR-----ELaakgttVIFSSHQMELVEElCDRIVIINKGRKVLSG 211
|
....
gi 665408680 545 TYEE 548
Cdd:COG4152 212 SVDE 215
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
973-1170 |
5.89e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.40 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAIL------IDSLDTND---------------IGLHDLRS 1031
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgepLAKLNRAQrkafrrdiqmvfqdsISAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1032 KISIIPQEPvlfsgtMRY--NLDPFEQypDDKLWKALEDVHLKEEI-SELPSGLqsiiseggtnfSVGQRQLVCLARAIL 1108
Cdd:PRK10419 107 TVREIIREP------LRHllSLDKAER--LARASEMLRAVDLDDSVlDKRPPQL-----------SGGQLQRVCLARALA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 1109 RENRILVMDEATANVDP--QTDALIQ-ATIRNKFkDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVE 1170
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLvlQAGVIRLlKKLQQQF-GTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
958-1179 |
6.05e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.45 E-value: 6.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPDTNSpcvLKGLSFTIQPMEKVGIVGRTGAGKSSLI---NALFRLSynDGAILIDSLDTNDIGLHDLRSKIS 1034
Cdd:PRK13647 8 EDLHFRYKDGTKA---LKGLSLSIPEGSKTALLGPNGAGKSTLLlhlNGIYLPQ--RGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1035 IIPQEP--VLFSGT---------MRYNLDPFEQypDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCL 1103
Cdd:PRK13647 83 LVFQDPddQVFSSTvwddvafgpVNMGLDKDEV--ERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 1104 ARAILRENRILVMDEATANVDPQTDALIQaTIRNKF--KDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPyELLT 1179
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLM-EILDRLhnQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDK-SLLT 226
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
17-291 |
7.27e-12 |
|
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: 67.58 E-value: 7.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 17 VPLLLAGLISEFSEHGNGHSYNaqIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRLSRTSLGGTTT 96
Cdd:cd07346 18 LPLLTKLLIDDVIPAGDLSLLL--WIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 97 GQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLyeqigMAS------FYGISILVLYLPLQTYLSRVTSKLRLQT 170
Cdd:cd07346 96 GDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVI-----LFYlnwkltLVALLLLPLYVLILRYFRRRIRKASREV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 171 ALRTDQRVRMMNEIISGIQVIKMYTWERP----FGKLIGQMRRSEMSSIRQMNLLrGILLSFEITLGRIAIFVsLLGFVL 246
Cdd:cd07346 171 RESLAELSAFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLSALF-SPLIGLLTALGTALVLL-YGGYLV 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 665408680 247 GGGELTAERAFCVTAFYNILRRTVsKFFPSGMSQFAELLVSMRRI 291
Cdd:cd07346 249 LQGSLTIGELVAFLAYLGMLFGPI-QRLANLYNQLQQALASLERI 292
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
338-547 |
7.93e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.68 E-value: 7.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 338 TLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY--SYASQEPWLF 415
Cdd:PRK09544 3 SLVSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLriGYVPQKLYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 416 NAsvrdnilfgLPMDKQRY---RTVLKRCALERDLELLHGdGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLS 492
Cdd:PRK09544 80 TT---------LPLTVNRFlrlRPGTKKEDILPALKRVQA-GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 493 AVDTHVGRHLFD--ECMRGFLGKQlVILVTHQLQFLEDADLIVIMDKGHVSACGTYE 547
Cdd:PRK09544 150 GVDVNGQVALYDliDQLRRELDCA-VLMVSHDLHLVMAKTDEVLCLNHHICCSGTPE 205
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
340-545 |
8.96e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.95 E-value: 8.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQHdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--------------- 404
Cdd:PRK11650 4 LKLQAVRKSYDGKTQ--VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelepadrdiamv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 405 -YSYAsqepwLF-NASVRDNILFGLP---MDKQRYRTVLKRCAleRDLELlhgdGTIVGERGASLSGGQRARICLARAVY 479
Cdd:PRK11650 82 fQNYA-----LYpHMSVRENMAYGLKirgMPKAEIEERVAEAA--RILEL----EPLLDRKPRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 480 RRADVYLLDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTH-QLQFLEDADLIVIMDKGHVSACGT 545
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAKLRVQMRLEIQR--LHRRLkttSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
957-1179 |
9.44e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.14 E-value: 9.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 957 TKDLSLRYEPDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLinalFR-----LSYNDGAILIDSLDTNDIGLHDLRS 1031
Cdd:PRK13652 6 TRDLCYSYSGSKE---ALNNINFIAPRNSRIAVIGPNGAGKSTL----FRhfngiLKPTSGSVLIRGEPITKENIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1032 KISIIPQEP--VLFSGTMRY-------NLDPFEQYPDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVC 1102
Cdd:PRK13652 79 FVGLVFQNPddQIFSPTVEQdiafgpiNLGLDEETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1103 LARAILRENRILVMDEATANVDPQTDALIQATIRNKFKD--CTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLT 1179
Cdd:PRK13652 148 IAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFL 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
973-1180 |
9.55e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.52 E-value: 9.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAILIDSLDTNDIGLHDLRSKISIIPQ----EPVLfsgTMR 1048
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQfdnlDPDF---TVR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1049 YNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEggtnFSVGQRQLVCLARAILRENRILVMDEATANVDPQTD 1128
Cdd:PRK13537 99 ENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 1129 ALIQATIRNKF-KDCTVLTIAH------RLntimdSDKVLVMDAGHVVEFGSPYELLTA 1180
Cdd:PRK13537 175 HLMWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
958-1177 |
1.04e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 67.82 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL--FrLSYNDGAILIDSLDTNDIGLHDlRsKISI 1035
Cdd:COG3842 9 ENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagF-ETPDSGRILLDGRDVTGLPPEK-R-NVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1036 IPQEPVLFSgtmryNLDPFE--QYP-----------DDKLWKALEDVHLKE----EISELpSGlqsiiseggtnfsvGQR 1098
Cdd:COG3842 82 VFQDYALFP-----HLTVAEnvAFGlrmrgvpkaeiRARVAELLELVGLEGladrYPHQL-SG--------------GQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1099 QLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNkfkdctvltIAHRLN--TIM---D-------SDKVLVMDAG 1166
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRR---------LQRELGitFIYvthDqeealalADRIAVMNDG 212
|
250
....*....|.
gi 665408680 1167 HVVEFGSPYEL 1177
Cdd:COG3842 213 RIEQVGTPEEI 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
973-1177 |
1.09e-11 |
|
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: 66.11 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHdlRSKISIIPQEPVLFSgtmryNL 1051
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTsGEILLDGKDITNLPPH--KRPVNTVFQNYALFP-----HL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1052 DPFEQ--YP-----------DDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDE 1118
Cdd:cd03300 88 TVFENiaFGlrlkklpkaeiKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408680 1119 ATANVDPQTDALIQATIRNKFKDC--TVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYEL 1177
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEI 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
973-1180 |
1.19e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 66.33 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVL-FSGT---- 1046
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTveev 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1047 --M-RYNLDPFEQYPDDKLWKALEDV---HLKE-EISELpSGlqsiiseggtnfsvGQRQLVCLARAILR------ENRI 1113
Cdd:PRK13548 97 vaMgRAPHGLSRAEDDALVAAALAQVdlaHLAGrDYPQL-SG--------------GEQQRVQLARVLAQlwepdgPPRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1114 LVMDEATANVDPQTDALIQATIRNKFKD--CTVLTIAHRLN-TIMDSDKVLVMDAGHVVEFGSPYELLTA 1180
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHErgLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLTP 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
337-529 |
1.19e-11 |
|
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: 68.81 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 337 DTLVEIKALRARWGqeqHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQV--SGKYSYASQ---- 410
Cdd:TIGR03719 320 DKVIEAENLTKAFG---DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgeTVKLAYVDQsrda 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 411 -EPwlfNASVRDNILFGLPMDKQRYRTVLKRCALERdlelLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDD 489
Cdd:TIGR03719 397 lDP---NKTVWEEISGGLDIIKLGKREIPSRAYVGR----FNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDE 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 665408680 490 PLSAVDTHVGRHLfDECMRGFLGKQLVI---------LVTHQLQFLEDA 529
Cdd:TIGR03719 470 PTNDLDVETLRAL-EEALLNFAGCAVVIshdrwfldrIATHILAFEGDS 517
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
968-1163 |
1.26e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.51 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 968 TNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGT 1046
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLiSPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1047 MRYNLD-PFE---QYPD-DKLWKALEDVHLKEEIselpsgLQSIISEggtnFSVGQRQLVCLARAILRENRILVMDEATA 1121
Cdd:PRK10247 97 VYDNLIfPWQirnQQPDpAIFLDDLERFALPDTI------LTKNIAE----LSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 665408680 1122 NVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMDSDKVLVM 1163
Cdd:PRK10247 167 ALDESNKHNVNEIIHryVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
973-1183 |
1.33e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.58 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAILIDsldtnDIGLHDL--------RSKISIIPQEPvlfS 1044
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFD-----GQPLHNLnrrqllpvRHRIQVVFQDP---N 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1045 GTMRYNLDPFE--------QYP-------DDKLWKALEDVHLKeeiselPSGLQSIISEggtnFSVGQRQLVCLARAILR 1109
Cdd:PRK15134 373 SSLNPRLNVLQiieeglrvHQPtlsaaqrEQQVIAVMEEVGLD------PETRHRYPAE----FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1110 ENRILVMDEATANVDPQTDALIQATIRNkfkdctvLTIAHRLNTIMDS----------DKVLVMDAGHVVEFGSPYELLT 1179
Cdd:PRK15134 443 KPSLIILDEPTSSLDKTVQAQILALLKS-------LQQKHQLAYLFIShdlhvvralcHQVIVLRQGEVVEQGDCERVFA 515
|
....
gi 665408680 1180 ASKA 1183
Cdd:PRK15134 516 APQQ 519
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
973-1136 |
1.47e-11 |
|
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: 64.69 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNdiglhdlrsKISIIPQEPVLFSG------ 1045
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDsGEVRWNGTPLA---------EQRDEPHENILYLGhlpglk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1046 ---TMRYNLD---PFEQYPDDKLWKALEDVHLKEeISELPSGlqsiiseggtNFSVGQRQLVCLARAILRENRILVMDEA 1119
Cdd:TIGR01189 86 pelSALENLHfwaAIHGGAQRTIEDALAAVGLTG-FEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170
....*....|....*..
gi 665408680 1120 TANVDPQTDALIQATIR 1136
Cdd:TIGR01189 155 TTALDKAGVALLAGLLR 171
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
955-1170 |
1.55e-11 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 65.53 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLinalfrLSyndgaiLIDSLDTNDIG--------L 1026
Cdd:COG4181 9 IELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTL------LG------LLAGLDRPTSGtvrlagqdL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1027 HDL---------RSKISIIPQ-EPVLFSGTMRYNL----------DPFEQYPDdklwkALEDVHLKEEISELPSGLqsii 1086
Cdd:COG4181 77 FALdedararlrARHVGFVFQsFQLLPTLTALENVmlplelagrrDARARARA-----LLERVGLGHRLDHYPAQL---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1087 seggtnfSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMDSDKVLVMD 1164
Cdd:COG4181 148 -------SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFelNRERGTTLVLVTHDPALAARCDRVLRLR 220
|
....*.
gi 665408680 1165 AGHVVE 1170
Cdd:COG4181 221 AGRLVE 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
337-559 |
1.57e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 66.27 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 337 DTLVEIKALRARWGQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG------------- 403
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelltaenvwnlrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 404 KYSYASQEP--WLFNASVRDNILFGLPMDKQRYRTVLKRCalerDLELLHGDGTIVGERG-ASLSGGQRARICLARAVYR 480
Cdd:PRK13642 82 KIGMVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRV----DEALLAVNMLDFKTREpARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 481 RADVYLLDDPLSAVDThVGRHLFDECMRGFLGK-QLVIL-VTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQ 558
Cdd:PRK13642 158 RPEIIILDESTSMLDP-TGRQEIMRVIHEIKEKyQLTVLsITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVE 236
|
.
gi 665408680 559 L 559
Cdd:PRK13642 237 I 237
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
955-1172 |
1.71e-11 |
|
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: 64.99 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILID--SLDTNDiglhdlRS 1031
Cdd:cd03269 1 LEVENVTKRFGRVT----ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDsGEVLFDgkPLDIAA------RN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1032 KISIIPQEPVLFSGT-----MRY-----NLDPFEQYPDDKLWkaLEDVHL----KEEISELpsglqsiiseggtnfSVGQ 1097
Cdd:cd03269 71 RIGYLPEERGLYPKMkvidqLVYlaqlkGLKKEEARRRIDEW--LERLELseyaNKRVEEL---------------SKGN 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 1098 RQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1172
Cdd:cd03269 134 QQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
353-522 |
1.89e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 63.71 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 353 QHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQ--VSGKYSYASQEPWLFNASVRDNILFglPMD 430
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGmpEGEDLLFLPQRPYLPLGTLREQLIY--PWD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 431 KQryrtvlkrcalerdlellhgdgtivgergasLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECmrgf 510
Cdd:cd03223 90 DV-------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL---- 134
|
170
....*....|....*
gi 665408680 511 lgKQL---VILVTHQ 522
Cdd:cd03223 135 --KELgitVISVGHR 147
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
345-554 |
1.94e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.76 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 345 LRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEP------------ 412
Cdd:PRK10619 11 LHKRYGEHE---VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknql 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 413 ----------------WLFnASVRDNIL------FGLPMDKQRYRTVlkrcaleRDLELLHGDGTIVGERGASLSGGQRA 470
Cdd:PRK10619 88 rllrtrltmvfqhfnlWSH-MTVLENVMeapiqvLGLSKQEARERAV-------KYLAKVGIDERAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 471 RICLARAVYRRADVYLLDDPLSAVDThvgrHLFDECMRGFL-----GKQLVIlVTHQLQFLEDADLIVI-MDKGHVSACG 544
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRIMQqlaeeGKTMVV-VTHEMGFARHVSSHVIfLHQGKIEEEG 234
|
250
....*....|
gi 665408680 545 TYEEMLKSGQ 554
Cdd:PRK10619 235 APEQLFGNPQ 244
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
337-563 |
2.09e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.97 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 337 DTLVEIKAL------RARWGQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVS------GK 404
Cdd:PRK15112 2 ETLLEVRNLsktfryRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 405 YSYAS-------QEP-----------WLFNASVRDNILFGLPMDKQRYRTVLKRCALERDlellHgdgtiVGERGASLSG 466
Cdd:PRK15112 82 YSYRSqrirmifQDPstslnprqrisQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPD----H-----ASYYPHMLAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 467 GQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDeCMRGFLGKQLV--ILVTHQLQFLED-ADLIVIMDKGHVSAC 543
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLIN-LMLELQEKQGIsyIYVTQHLGMMKHiSDQVLVMHQGEVVER 231
|
250 260
....*....|....*....|.
gi 665408680 544 GTYEEMLKSGQ-DFAQLLVES 563
Cdd:PRK15112 232 GSTADVLASPLhELTKRLIAG 252
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
676-877 |
2.88e-11 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 65.65 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 676 DIYYFTAINVGLVICALLRTLLFFnITMHSSTELHNTMFQGLsRTALY---------FFHTNPSGRILNRFANDLGQVDE 746
Cdd:cd07346 34 DLSLLLWIALLLLLLALLRALLSY-LRRYLAARLGQRVVFDL-RRDLFrhlqrlslsFFDRNRTGDLMSRLTSDVDAVQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 747 VMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMM----LAFYYWRDFYLKTSRDVKrlEAVARspMYSHFSATLVG 822
Cdd:cd07346 112 LVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLplyvLILRYFRRRIRKASREVR--ESLAE--LSAFLQESLSG 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 823 LPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVSTSRAFGYYLDLFCVAYVISVIL 877
Cdd:cd07346 188 IRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLL 242
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
973-1166 |
3.39e-11 |
|
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: 64.38 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRlSY--NDGAILIDSLDT-------NDIGLHDLRSK--------ISI 1035
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG-NYlpDSGSILVRHDGGwvdlaqaSPREILALRRRtigyvsqfLRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1036 IPQ--------EPVLFSGTMRynldpfeqypDDKLWKA---LEDVHLKEEISELPSglqsiiseggTNFSVGQRQLVCLA 1104
Cdd:COG4778 105 IPRvsaldvvaEPLLERGVDR----------EEARARArelLARLNLPERLWDLPP----------ATFSGGEQQRVNIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 1105 RAILRENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTiMD--SDKVLVMDAG 1166
Cdd:COG4778 165 RGFIADPPLLLLDEPTASLDAANRAVVVELIEEaKARGTAIIGIFHDEEV-REavADRVVDVTPF 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
957-1178 |
4.74e-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: 66.75 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 957 TKDLSLRY-EPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSYNDGAILI--DSLDTNDIGLhDLR 1030
Cdd:TIGR03269 282 VRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLskiIAGVLEPTSGEVNVRVgdEWVDMTKPGP-DGR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1031 SK----ISIIPQEPVLFsgTMRYNLDPFE-----QYPDD----KLWKALEDVHLKEEISElpsglqSIISEGGTNFSVGQ 1097
Cdd:TIGR03269 361 GRakryIGILHQEYDLY--PHRTVLDNLTeaiglELPDElarmKAVITLKMVGFDEEKAE------EILDKYPDELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1098 RQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDC--TVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSP 1174
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDP 512
|
....
gi 665408680 1175 YELL 1178
Cdd:TIGR03269 513 EEIV 516
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
357-555 |
4.97e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 64.68 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLFNA------------------- 417
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiklrkevgmvfqqpnpfph 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 418 -SVRDNILFGLP----MDKQRYRTVLKRCAleRDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLS 492
Cdd:PRK14246 105 lSIYDNIAYPLKshgiKEKREIKKIVEECL--RKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665408680 493 AVDThVGRHLFDECMRGFLGKQLVILVTHQ-LQFLEDADLIVIMDKGHVSACGTYEEMLKSGQD 555
Cdd:PRK14246 183 MIDI-VNSQAIEKLITELKNEIAIVIVSHNpQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
357-552 |
5.13e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 64.73 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAiLGELPPE------SGSVQVSGK--YSYAS------------QEPWLFN 416
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRT-LNRMNDKvsgyrySGDVLLGGRsiFNYRDvlefrrrvgmlfQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 417 ASVRDNILFGLPMDKQRYRTVLKRCALERDLELLHGDGTI--VGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAV 494
Cdd:PRK14271 115 MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKdrLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 495 DTHVGRHLfDECMRGFLGKQLVILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEMLKS 552
Cdd:PRK14271 195 DPTTTEKI-EEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
367-537 |
5.61e-11 |
|
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: 62.01 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 367 RGQLVAVIGPVGSGKSSLIQAILGELPPESGSVqvsgkysyasqepwlfnasvrdnilfglpmdkqryrtVLKRCALERD 446
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-------------------------------------IYIDGEDILE 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 447 LELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQL------VILVT 520
Cdd:smart00382 44 EVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKseknltVILTT 123
|
170
....*....|....*..
gi 665408680 521 HQLQFLEDADLIVIMDK 537
Cdd:smart00382 124 NDEKDLGPALLRRRFDR 140
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
358-541 |
5.77e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.53 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-YSYASQEPW--LFNASVRDNILF-------GL 427
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpVTAEQPEDYrkLFSAVFTDFHLFdqllgpeGK 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 428 PMDKQRYRTVLKRCALERDLELlhGDGTIVGERgasLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDEC- 506
Cdd:PRK10522 419 PANPALVEKWLERLKMAHKLEL--EDGRISNLK---LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLl 493
|
170 180 190
....*....|....*....|....*....|....*..
gi 665408680 507 --MRGfLGKQlVILVTHQLQFLEDADLIVIMDKGHVS 541
Cdd:PRK10522 494 plLQE-MGKT-IFAISHDDHYFIHADRLLEMRNGQLS 528
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
957-1176 |
5.92e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.63 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 957 TKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDSldtndiglhDLRskISI 1035
Cdd:COG0488 1 LENLSKSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAgELEPDSGEVSIPK---------GLR--IGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1036 IPQEPVLFSGT---------------MRYNLDPFEQYPDDKLWKALEDVHLKEEISEL-----PSGLQSIISEGG----- 1090
Cdd:COG0488 66 LPQEPPLDDDLtvldtvldgdaelraLEAELEELEAKLAEPDEDLERLAELQEEFEALggweaEARAEEILSGLGfpeed 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1091 -----TNFSVGQRQLVCLARAILRENRILVMDEATANVDpqtdalIQATIR-----NKFKdCTVLTIAH-R--LNTImdS 1157
Cdd:COG0488 146 ldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD------LESIEWleeflKNYP-GTVLVVSHdRyfLDRV--A 216
|
250
....*....|....*....
gi 665408680 1158 DKVLVMDAGHVVEFGSPYE 1176
Cdd:COG0488 217 TRILELDRGKLTLYPGNYS 235
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
973-1180 |
6.20e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.02 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVL---FSGTM- 1047
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINgTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDVRQv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1048 --------RYNLDPFEQYPDDKLWKALEDVhlkeeiselpsGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEA 1119
Cdd:PRK09536 98 vemgrtphRSRFDTWTETDRAAVERAMERT-----------GVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 1120 TANVD----PQTDALIQATIRNkfkDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTA 1180
Cdd:PRK09536 167 TASLDinhqVRTLELVRRLVDD---GKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTA 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
977-1169 |
6.50e-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: 63.28 E-value: 6.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 977 LSFTIQPMEKVGIVGRTGAGKSSLIN--ALFRLSyNDGAILIDSLDTNdiGLHDLRSKISIIPQEPVLFSG-TMRYN--- 1050
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNliAGFETP-QSGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHlTVEQNvgl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1051 -------LDPFEQypdDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEATANV 1123
Cdd:cd03298 94 glspglkLTAEDR---QAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 665408680 1124 DPQTDALIQA---TIRNKFKDcTVLTIAHRLNTIMD-SDKVLVMDAGHVV 1169
Cdd:cd03298 160 DPALRAEMLDlvlDLHAETKM-TVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
973-1178 |
6.68e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 65.24 E-value: 6.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIdsLDTNDIGLHDL-RSKISIIPQEPVL-FSGTMRY 1049
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDaGKITV--LGVPVPARARLaRARIGVVPQFDNLdLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1050 NLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEggtnFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDA 1129
Cdd:PRK13536 134 NLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARH 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 1130 LIQATIRNKF-KDCTVLTIAHrlntIMDS-----DKVLVMDAGHVVEFGSPYELL 1178
Cdd:PRK13536 210 LIWERLRSLLaRGKTILLTTH----FMEEaerlcDRLCVLEAGRKIAEGRPHALI 260
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
358-562 |
6.86e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.38 E-value: 6.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQ-------------------EPWLFNAS 418
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdikqirkkvglvfqfpESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 419 VRDNILFGlPMDKQRYRTVLKRCALERdLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHv 498
Cdd:PRK13649 103 VLKDVAFG-PQNFGVSQEEAEALAREK-LALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 499 GRHlfdECMRGFlgKQL------VILVTHQLQFLED-ADLIVIMDKGHVSACGTYE------EMLKSGQ-------DFAQ 558
Cdd:PRK13649 180 GRK---ELMTLF--KKLhqsgmtIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKdifqdvDFLEEKQlgvpkitKFAQ 254
|
....
gi 665408680 559 LLVE 562
Cdd:PRK13649 255 RLAD 258
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
339-563 |
7.09e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.18 E-value: 7.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 339 LVEIKALRARWGQEQHdlvLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYS-----YASQEP- 412
Cdd:PRK11701 6 LLSVRGLTKLYGPRKG---CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGqlrdlYALSEAe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 413 --------WLFnasVRDNILFGLPMD--------------KQRYRTVLKRCALE--RDLELlhgDGTIVGERGASLSGGQ 468
Cdd:PRK11701 83 rrrllrteWGF---VHQHPRDGLRMQvsaggnigerlmavGARHYGDIRATAGDwlERVEI---DAARIDDLPTTFSGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 469 RARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDeCMRGfLGKQL---VILVTHQL---QFLedADLIVIMDKGHVSA 542
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLD-LLRG-LVRELglaVVIVTHDLavaRLL--AHRLLVMKQGRVVE 232
|
250 260
....*....|....*....|..
gi 665408680 543 CGTYEEMLKSGQD-FAQLLVES 563
Cdd:PRK11701 233 SGLTDQVLDDPQHpYTQLLVSS 254
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
357-554 |
7.30e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.76 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--------------YSYASQEPWLFNA-SVRD 421
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararrgIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 422 NILFGLPMDKQRYRTVLKRCALE--RDLELLHGDGTIvgerGASLSGGQRARICLARAVYRRADVYLLDDPLSAVD---- 495
Cdd:PRK10895 98 NLMAVLQIRDDLSAEQREDRANElmEEFHIEHLRDSM----GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDpisv 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665408680 496 ---THVGRHLFDECmrgfLGkqlVILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEMLKSGQ 554
Cdd:PRK10895 174 idiKRIIEHLRDSG----LG---VLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
969-1182 |
7.90e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.91 E-value: 7.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 969 NSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLS--YN-----DGAILIDSLDTNDIGLHDLRSKISIIPQEPV 1041
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiYDskikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1042 LFS-----GTMRYNLDPFEQYPDDKLWKALEDVHLKEEI-SELPSGLQSIISEggtnFSVGQRQLVCLARAILRENRILV 1115
Cdd:PRK14246 101 PFPhlsiyDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQ----LSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 1116 MDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASK 1182
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSPK 244
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
943-1176 |
8.15e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.86 E-value: 8.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 943 KQPPKSwpkeGKLV--TKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL-FRLSYNDGAIlidsl 1019
Cdd:COG0488 306 PPPERL----GKKVleLEGLSKSYGDKT----LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLaGELEPDSGTV----- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1020 dtnDIGlHDLrsKISIIPQEpvlfsgtmRYNLDpfeqyPDDKLWKALEDVHLKEEISEL----------PSGLQSIISeg 1089
Cdd:COG0488 373 ---KLG-ETV--KIGYFDQH--------QEELD-----PDKTVLDELRDGAPGGTEQEVrgylgrflfsGDDAFKPVG-- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1090 gtNFSVGQRQLVCLARAILRENRILVMDEATANVDPQT-DALIQATirNKFKDcTVLTIAH-R--LNTImdSDKVLVMDA 1165
Cdd:COG0488 432 --VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETlEALEEAL--DDFPG-TVLLVSHdRyfLDRV--ATRILEFED 504
|
250
....*....|.
gi 665408680 1166 GHVVEFGSPYE 1176
Cdd:COG0488 505 GGVREYPGGYD 515
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
973-1179 |
8.18e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 63.57 E-value: 8.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSynDGAILIDSLDTNDIglhdlRSKISIIPQEP-VLFSgtmR 1048
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLlrcINKLEEIT--SGDLIVDGLKVNDP-----KVDERLIRQEAgMVFQ---Q 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1049 YNLdpFEQYpddklwKALEDVHL---------KEEISELPS------GLQSIISEGGTNFSVGQRQLVCLARAILRENRI 1113
Cdd:PRK09493 86 FYL--FPHL------TALENVMFgplrvrgasKEEAEKQARellakvGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 1114 LVMDEATANVDPQTDALIQATIRNKFKD-CTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLT 1179
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
958-1177 |
8.51e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 64.27 E-value: 8.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPdtNSPC---VLKGLSFTIQPMEKVGIVGRTGAGKSSLI---NALfrLSYNDGAILIDSL----DTNDIGLH 1027
Cdd:PRK13634 6 QKVEHRYQY--KTPFerrALYDVNVSIPSGSYVAIIGHTGSGKSTLLqhlNGL--LQPTSGTVTIGERvitaGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1028 DLRSKISIIPQ--EPVLFSGTMR-------YNLDPFEQYPDDKLWKALEDVHLKEEISEL-PSGLqsiiseggtnfSVGQ 1097
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEkdicfgpMNFGVSEEDAKQKAREMIELVGLPEELLARsPFEL-----------SGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1098 RQLVCLARAILRENRILVMDEATANVDPQTdaliQATIRNKF------KDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVE 1170
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFyklhkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFL 226
|
....*..
gi 665408680 1171 FGSPYEL 1177
Cdd:PRK13634 227 QGTPREI 233
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
974-1177 |
8.73e-11 |
|
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: 63.51 E-value: 8.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 974 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHDlrSKISIIPQEPVLFSG-TMRYNL 1051
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDsGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHmTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1052 -----------DPFEQYPDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEAT 1120
Cdd:cd03296 96 afglrvkprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1121 ANVDPQTDALIQATIRNKFKDCTVLTI--AHRLNTIMD-SDKVLVMDAGHVVEFGSPYEL 1177
Cdd:cd03296 165 GALDAKVRKELRRWLRRLHDELHVTTVfvTHDQEEALEvADRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
974-1178 |
1.18e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.05 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 974 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDT---NDIGLHDLRSK--------ISIIPQEPV 1041
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLiEPTRGQVLIDGVDIakiSDAELREVRRKkiamvfqsFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1042 LFSGTMRYNLD--PFEQYPDDKLwKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEA 1119
Cdd:PRK10070 124 LDNTAFGMELAgiNAEERREKAL-DALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 1120 TANVDP-----QTDALIQATIRNKFkdcTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELL 1178
Cdd:PRK10070 192 FSALDPlirteMQDELVKLQAKHQR---TIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
309-493 |
1.18e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 309 RDEKAEEEQHLLKEVEKRsypvgigkepDTLVEIKALRARWGqeqhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI 388
Cdd:PRK13409 320 RPEPIEFEERPPRDESER----------ETLVEYPDLTKKLG----DFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 389 LGELPPESGSVQVSGKYSYASQ--EPwLFNASVRDNilfgLPMDKQRYRT------VLKRCALERDLELLHGDgtivger 460
Cdd:PRK13409 386 AGVLKPDEGEVDPELKISYKPQyiKP-DYDGTVEDL----LRSITDDLGSsyykseIIKPLQLERLLDKNVKD------- 453
|
170 180 190
....*....|....*....|....*....|...
gi 665408680 461 gasLSGGQRARICLARAVYRRADVYLLDDPlSA 493
Cdd:PRK13409 454 ---LSGGELQRVAIAACLSRDADLYLLDEP-SA 482
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
973-1169 |
1.24e-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: 63.12 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALfrlsynDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFS--GTMRYN 1050
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKIL------SGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGqkTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1051 LDPFEQYPDDKLWKALEDVHLKEEISELPSGLQ--SIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTD 1128
Cdd:cd03267 110 LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDleELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 665408680 1129 ALIQATIR--NKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVV 1169
Cdd:cd03267 190 ENIRNFLKeyNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
973-1182 |
1.25e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.23 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND------GAILID---SLDTNDIGLHDLRSKISIIPQEpvlf 1043
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEagtirvGDITIDtarSLSQQKGLIRQLRQHVGFVFQN---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1044 sgtmrYNLDPFEQypddklwkALEDV---------HLKEEISELPSGLQSIISEGGTN------FSVGQRQLVCLARAIL 1108
Cdd:PRK11264 94 -----FNLFPHRT--------VLENIiegpvivkgEPKEEATARARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 1109 RENRILVMDEATANVDPQTDALIQATIRNKFKDC-TVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASK 1182
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
317-495 |
1.72e-10 |
|
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: 65.09 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 317 QHLLkEVEKRSYPVGIGKEPDTLVEIKAL-------RARWGQEQHDLV-LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI 388
Cdd:COG4172 254 RKLL-AAEPRGDPRPVPPDAPPLLEARDLkvwfpikRGLFRRTVGHVKaVDGVSLTLRRGETLGLVGESGSGKSTLGLAL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 389 LGeLPPESGSVQVSGK----YS------------------YASQEPWLfnaSVRDNILFGL-----PMDK-QRYRTVLKr 440
Cdd:COG4172 333 LR-LIPSEGEIRFDGQdldgLSrralrplrrrmqvvfqdpFGSLSPRM---TVGQIIAEGLrvhgpGLSAaERRARVAE- 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408680 441 cALERdlellhgdgtiVGERGASL-------SGGQRARICLARAVYRRADVYLLDDPLSAVD 495
Cdd:COG4172 408 -ALEE-----------VGLDPAARhryphefSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
958-1167 |
1.74e-10 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 60.15 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDSldtndiglhdlRSKISII 1036
Cdd:cd03221 4 ENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAgELEPDEGIVTWGS-----------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1037 PQepvlFSGtmrynldpfeqypddklwkaledvhlkeeiselpsglqsiiseggtnfsvGQRQLVCLARAILRENRILVM 1116
Cdd:cd03221 69 EQ----LSG--------------------------------------------------GEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 1117 DEATANVDPQT-DALIQATirNKFKdCTVLTIAH-R--LNTImdSDKVLVMDAGH 1167
Cdd:cd03221 95 DEPTNHLDLESiEALEEAL--KEYP-GTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
978-1179 |
1.88e-10 |
|
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: 63.05 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 978 SFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIG---LHDLRSK-ISIIPQEPVLFSgtMRYNLD 1052
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLiEPTSGKVLIDGQDIAAMSrkeLRELRRKkISMVFQSFALLP--HRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1053 ----PFE------QYPDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEATAN 1122
Cdd:cd03294 122 nvafGLEvqgvprAEREERAAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 1123 VDP------QTDAL-IQATIRNkfkdcTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLT 1179
Cdd:cd03294 191 LDPlirremQDELLrLQAELQK-----TIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
953-1179 |
2.13e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 63.10 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 953 GKLVTKDLSLRYEPDTnsPCVLKGL---SFTIQPMEKVGIVGRTGAGKSSLI---NALFrLSYNDGAILIDSLDTNDIG- 1025
Cdd:PRK13645 5 KDIILDNVSYTYAKKT--PFEFKALnntSLTFKKNKVTCVIGTTGSGKSTMIqltNGLI-ISETGQTIVGDYAIPANLKk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1026 ---LHDLRSKISIIPQEP--VLFSGTMRYNLdpfeQYPDDKLWKALEDVHLK-EEISELPSGLQSIISEGGTNFSVGQRQ 1099
Cdd:PRK13645 82 ikeVKRLRKEIGLVFQFPeyQLFQETIEKDI----AFGPVNLGENKQEAYKKvPELLKLVQLPEDYVKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1100 LVCLARAILRENRILVMDEATANVDPQTDA-LIQATIR-NKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYE 1176
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEdFINLFERlNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFE 237
|
...
gi 665408680 1177 LLT 1179
Cdd:PRK13645 238 IFS 240
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
336-540 |
2.18e-10 |
|
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: 64.71 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 336 PDTLVEIKALRARWGQEQHD-LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPesGSVQVSGKYSYASQEpwL 414
Cdd:COG4172 3 SMPLLSVEDLSVAFGQGGGTvEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPD--PAAHPSGSILFDGQD--L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 415 FNAS------VRDN---ILFGLPM---------DKQ------RYRTVLKRCALERDLELLhgdgTIVG----ERGAS--- 463
Cdd:COG4172 79 LGLSerelrrIRGNriaMIFQEPMtslnplhtiGKQiaevlrLHRGLSGAAARARALELL----ERVGipdpERRLDayp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 464 --LSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDecmrgfLGKQL-------VILVTHQLQFLED-ADLIV 533
Cdd:COG4172 155 hqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILD------LLKDLqrelgmaLLLITHDLGVVRRfADRVA 228
|
....*..
gi 665408680 534 IMDKGHV 540
Cdd:COG4172 229 VMRQGEI 235
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
973-1172 |
3.34e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.17 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGA-------ILIDSLDTNDIGLHDLRSKISIIPQEPVLFS 1044
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlELNEEArvegevrLFGRNIYSPDVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1045 GTMRYN-----------LDPFEQYPDDKLWkALEDVHLKEEISELpsglqsiISEGGTNFSVGQRQLVCLARAILRENRI 1113
Cdd:PRK14267 99 HLTIYDnvaigvklnglVKSKKELDERVEW-ALKKAALWDEVKDR-------LNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1114 LVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHR-LNTIMDSDKVLVMDAGHVVEFG 1172
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
974-1173 |
3.41e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 63.06 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 974 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALF--------RLSYNDgailIDSLDTNDIGLHDLRSKISIIPQ------- 1038
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTmietptggELYYQG----QDLLKADPEAQKLLRQKIQIVFQnpygsln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1039 ----------EPVLfsgtMRYNLDPFEQypDDKLWKALEDVHLK-EEISELPSglqsiiseggtNFSVGQRQLVCLARAI 1107
Cdd:PRK11308 107 prkkvgqileEPLL----INTSLSAAER--REKALAMMAKVGLRpEHYDRYPH-----------MFSGGQRQRIAIARAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665408680 1108 LRENRILVMDEATANVDPQtdalIQATIRNKFKD------CTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGS 1173
Cdd:PRK11308 170 MLDPDVVVADEPVSALDVS----VQAQVLNLMMDlqqelgLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGT 238
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
955-1168 |
3.43e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.00 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDtndigLHDLRSKI 1033
Cdd:PRK11247 13 LLLNAVSKRYGERT----VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLeTPSAGELLAGTAP-----LAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1034 SIIPQEPVLFsgtmrynldPFEQYPD-----------DKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVC 1102
Cdd:PRK11247 84 RLMFQDARLL---------PWKKVIDnvglglkgqwrDAALQALAAVGLADRANEWPAAL-----------SGGQKQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 1103 LARAILRENRILVMDEATANVDPQTDALIQATIRNKFKD--CTVLTIAHRLN-TIMDSDKVLVMDAGHV 1168
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhgFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
309-493 |
3.52e-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: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 309 RDEKAEEEQHLLKEVEKRsypvgigkepDTLVEIKALRARWGqeqhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI 388
Cdd:COG1245 321 RDEPIEFEVHAPRREKEE----------ETLVEYPDLTKSYG----GFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKIL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 389 LGELPPESGSVQVSGKYSYASQ--EPwLFNASVRDNI--LFGLPMDKQRYRT-VLKRCALERDLEllhgdgtivgERGAS 463
Cdd:COG1245 387 AGVLKPDEGEVDEDLKISYKPQyiSP-DYDGTVEEFLrsANTDDFGSSYYKTeIIKPLGLEKLLD----------KNVKD 455
|
170 180 190
....*....|....*....|....*....|
gi 665408680 464 LSGGQRARICLARAVYRRADVYLLDDPlSA 493
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEP-SA 484
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
351-554 |
4.22e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.08 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 351 QEQHD--LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSV-------------QVSGKYSYASQEP--W 413
Cdd:PRK13648 16 QYQSDasFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeKLRKHIGIVFQNPdnQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 414 LFNASVRDNILFGL-----PMDKQrYRTVLKrcALErDLELL-HGDgtivgERGASLSGGQRARICLARAVYRRADVYLL 487
Cdd:PRK13648 96 FVGSIVKYDVAFGLenhavPYDEM-HRRVSE--ALK-QVDMLeRAD-----YEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 488 DDPLSAVDTHVGRHLFDECMRGFLGKQLVIL-VTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQ 554
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIIsITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
357-547 |
4.90e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 62.41 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSV------------------------------------- 399
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvleklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 400 ----QVSGKYSYAsqEPWLFNASVRDNILFG---LPMDKQRyrtvlkrcALERDLELLHgdgtIVG------ERGA-SLS 465
Cdd:PRK13651 102 eirrRVGVVFQFA--EYQLFEQTIEKDIIFGpvsMGVSKEE--------AKKRAAKYIE----LVGldesylQRSPfELS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 466 GGQRARICLARAVYRRADVYLLDDPLSAVDTH-------VGRHLFDEcmrgflGKQlVILVTHQL-QFLEDADLIVIMDK 537
Cdd:PRK13651 168 GGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgvkeileIFDNLNKQ------GKT-IILVTHDLdNVLEWTKRTIFFKD 240
|
250
....*....|.
gi 665408680 538 GHVSACG-TYE 547
Cdd:PRK13651 241 GKIIKDGdTYD 251
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
989-1173 |
6.71e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.20 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 989 IVGRTGAGKSSLINALFRLSYND-GAILIdsldtNDIGLHDLRSKISIIP---------QEPVLF-----SGTMRYNLDP 1053
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQkGRIVL-----NGRVLFDAEKGICLPPekrrigyvfQDARLFphykvRGNLRYGMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1054 FEQYPDDKLWKALEDVHLkeeISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVD-PQTDALIQ 1132
Cdd:PRK11144 104 SMVAQFDKIVALLGIEPL---LDRYPGSL-----------SGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELLP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 665408680 1133 --ATIRNKFKdCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGS 1173
Cdd:PRK11144 170 ylERLAREIN-IPILYVSHSLDEILRlADRVVVLEQGKVKAFGP 212
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
978-1179 |
8.05e-10 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 62.04 E-value: 8.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 978 SFTIQPMEKVGIVGRTGAGKSSLINAL----------FRLsynDGAILIDSldTNDIGL--HdlRSKISIIPQEPVLFSG 1045
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIaglerpdsgrIRL---GGEVLQDS--ARGIFLppH--RRRIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1046 -TMRYNLdpfeQYPDDKLWKALEDVHLkEEISEL----------PSGLqsiiseggtnfSVGQRQLVCLARAILRENRIL 1114
Cdd:COG4148 92 lSVRGNL----LYGRKRAPRAERRISF-DEVVELlgighlldrrPATL-----------SGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 1115 VMDEATANVDPQTDALIQ---ATIRNKFkDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLT 1179
Cdd:COG4148 156 LMDEPLAALDLARKAEILpylERLRDEL-DIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
364-495 |
8.65e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 60.50 E-value: 8.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 364 SLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-KYSYASQ--EPwLFNASVRDnILFGLPMDK---QRYRT- 436
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQyiKA-DYEGTVRD-LLSSITKDFythPYFKTe 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 437 VLKRCALERDLEllhgdgtivgERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVD 495
Cdd:cd03237 99 IAKPLQIEQILD----------REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
357-551 |
1.08e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.97 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGS---VQVSG-------------KYSYASQEP--WLFNAS 418
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGitltaktvwdireKVGIVFQNPdnQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 419 VRDNILFGLPmDKQRYRTVLKRcaLERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHv 498
Cdd:PRK13640 102 VGDDVAFGLE-NRAVPRPEMIK--IVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA- 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 499 GRHLFDECMRGFLGKQ--LVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLK 551
Cdd:PRK13640 178 GKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
974-1168 |
1.09e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 974 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL----SYnDGAILIDSLDTNDIGLHDL-RSKISIIPQEPVLF----- 1043
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgTY-EGEIIFEGEELQASNIRDTeRAGIAIIHQELALVkelsv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1044 ------------SGTMRYNldpfEQYPDDKLWkaLEDVHLkeEIS-ELPSGlqsiiseggtNFSVGQRQLVCLARAILRE 1110
Cdd:PRK13549 100 leniflgneitpGGIMDYD----AMYLRAQKL--LAQLKL--DINpATPVG----------NLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665408680 1111 NRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVM-DAGHV 1168
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDlKAHGIACIYISHKLNEVKAiSDTICVIrDGRHI 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
356-583 |
1.15e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.97 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 356 LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-----------------KYSYASQEPWLF-NA 417
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSFALMpHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 418 SVRDNILFGL-----PMDKQRYRTV--LKRCALErdlELLHGdgtivgeRGASLSGGQRARICLARAVYRRADVYLLDDP 490
Cdd:PRK10070 122 TVLDNTAFGMelagiNAEERREKALdaLRQVGLE---NYAHS-------YPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 491 LSAVDTHVGRHLFDECMRGFLGKQ-LVILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEMLKS-GQDFAQLLVESTQNS 567
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKHQrTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNpANDYVRTFFRGVDIS 271
|
250
....*....|....*.
gi 665408680 568 gggdEIITSPNLSRQS 583
Cdd:PRK10070 272 ----QVFSAKDIARRT 283
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
321-490 |
1.17e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 62.34 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 321 KEVEKRsYPVGIGKEPDTLVEIKALRARwgqeqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQ 400
Cdd:COG1129 239 RELEDL-FPKRAAAPGEVVLEVEGLSVG-------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 401 VSGK-YSYASqePW------------------LF-NASVRDNILFGLpMDKQRYRTVLKRcALERDL-----ELLH---- 451
Cdd:COG1129 311 LDGKpVRIRS--PRdairagiayvpedrkgegLVlDLSIRENITLAS-LDRLSRGGLLDR-RRERALaeeyiKRLRiktp 386
|
170 180 190
....*....|....*....|....*....|....*....
gi 665408680 452 GDGTIVGergaSLSGGQRARICLARAVYRRADVYLLDDP 490
Cdd:COG1129 387 SPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
357-539 |
1.20e-09 |
|
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: 62.26 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLI-------QAILGELPPESGSvqvsgKYSYASQEPWL-FNASVRDNILFGLP 428
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLrimagvdKDFNGEARPQPGI-----KVGYLPQEPQLdPTKTVRENVEEGVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 429 MDKQ---RYRTVLKRCA---------------------------LERDLE-------LLHGDGTIvgergASLSGGQRAR 471
Cdd:TIGR03719 95 EIKDaldRFNEISAKYAepdadfdklaaeqaelqeiidaadawdLDSQLEiamdalrCPPWDADV-----TKLSGGERRR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665408680 472 ICLARAVYRRADVYLLDDPLSAVDTH----VGRHLfdecmRGFLGKqlVILVTHQLQFLED-ADLIVIMDKGH 539
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLDAEsvawLERHL-----QEYPGT--VVAVTHDRYFLDNvAGWILELDRGR 235
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
973-1182 |
1.57e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.49 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLS-------YNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLF-- 1043
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgyrYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFpm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1044 -------SGTMRYNLDPFEQYpddklwKALEDVHLKEeiSELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVM 1116
Cdd:PRK14271 116 simdnvlAGVRAHKLVPRKEF------RGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 1117 DEATANVDPQTDALIQATIRNKFKDCTVLTIAHRL-NTIMDSDKVLVMDAGHVVEFGSPYELLTASK 1182
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSSPK 254
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
337-524 |
1.57e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.41 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 337 DTLVEIKALRARWGQEQHDL-VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWlf 415
Cdd:PRK10584 4 ENIVEVHHLKKSVGQGEHELsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEA-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 416 NASVR-DNILFGLpmdkQRYRTVLKRCALE------------------RDLELLHGDGtiVGER----GASLSGGQRARI 472
Cdd:PRK10584 82 RAKLRaKHVGFVF----QSFMLIPTLNALEnvelpallrgessrqsrnGAKALLEQLG--LGKRldhlPAQLSGGEQQRV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 473 CLARAVYRRADVYLLDDPLSAVDTHVGRHLFD---ECMRGFlgKQLVILVTHQLQ 524
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADllfSLNREH--GTTLILVTHDLQ 208
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
973-1172 |
1.74e-09 |
|
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: 59.47 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHdlrskISIIPQ----EPVLFSGTM 1047
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDsGTVTVRGRVSSLLGLG-----GGFNPEltgrENIYLNGRL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1048 rYNLDPfeQYPDDKLwkaledvhlkEEISELpSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQT 1127
Cdd:cd03220 112 -LGLSR--KEIDEKI----------DEIIEF-SELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 665408680 1128 DALIQATIRNKFKDC-TVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1172
Cdd:cd03220 178 QEKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
954-1182 |
1.94e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.49 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 954 KLVTKDLSLRYEPDTNSPC-VLKGLSFTIQPMEKVGIVGRTGAGKSSLI---NALfrLSYNDGAILI------------- 1016
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTELkALDNVSVEINQGEFIAIIGQTGSGKTTFIehlNAL--LLPDTGTIEWifkdeknkkktke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1017 --DSLDTNDIG---------LHDLRSKISIIPQ--EPVLFS---------GTMRYNLDPFEQYPDDKlwKALEDVHLKEE 1074
Cdd:PRK13651 80 keKVLEKLVIQktrfkkikkIKEIRRRVGVVFQfaEYQLFEqtiekdiifGPVSMGVSKEEAKKRAA--KYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1075 -ISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDC-TVLTIAHRLN 1152
Cdd:PRK13651 158 yLQRSPFEL-----------SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGkTIILVTHDLD 226
|
250 260 270
....*....|....*....|....*....|.
gi 665408680 1153 TIMD-SDKVLVMDAGHVVEFGSPYELLTASK 1182
Cdd:PRK13651 227 NVLEwTKRTIFFKDGKIIKDGDTYDILSDNK 257
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
974-1182 |
2.27e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.18 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 974 LKGLSFTIQPMEKVGIVGRTGAGKSSLI---NALFRLSYndGAILIDSLD----TNDIGLHDLRSKISIIPQEP------ 1040
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIqniNALLKPTT--GTVTVDDITithkTKDKYIRPVRKRIGMVFQFPesqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1041 ------VLFsGTMRYNLDpFEQYPDDKlWKALEDVHLKEEISELpSGLQsiiseggtnFSVGQRQLVCLARAILRENRIL 1114
Cdd:PRK13646 101 dtvereIIF-GPKNFKMN-LDEVKNYA-HRLLMDLGFSRDVMSQ-SPFQ---------MSGGQMRKIAIVSILAMNPDII 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 1115 VMDEATANVDPQTDALIQATIR------NKfkdcTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASK 1182
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMRLLKslqtdeNK----TIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
340-540 |
2.30e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 60.58 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQHDLV-LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWL---- 414
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 415 ---------FN--AS--VRDNILFGLPMDKQRYRTVLKRCAlerdlELLhgdgTIVG--ERG----ASLSGGQRARICLA 475
Cdd:PRK11153 82 rqigmifqhFNllSSrtVFDNVALPLELAGTPKAEIKARVT-----ELL----ELVGlsDKAdrypAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665408680 476 RAVYRRADVYLLDDPLSAVDTHVGRHLFDecmrgfLGKQL-------VILVTHQLQFL-EDADLIVIMDKGHV 540
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILE------LLKDInrelgltIVLITHEMDVVkRICDRVAVIDAGRL 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
955-1180 |
2.39e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.41 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAIL--------------IDSLD 1020
Cdd:PRK10261 13 LAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqvIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1021 TNDIGLHDLR-SKISIIPQEPVLfsgtmryNLDPF----EQYP-----------DDKLWKA---LEDVHLKEEiselpsg 1081
Cdd:PRK10261 93 QSAAQMRHVRgADMAMIFQEPMT-------SLNPVftvgEQIAesirlhqgasrEEAMVEAkrmLDQVRIPEA------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1082 lQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCT--VLTIAHRLNTIMD-SD 1158
Cdd:PRK10261 159 -QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiAD 237
|
250 260
....*....|....*....|..
gi 665408680 1159 KVLVMDAGHVVEFGSPYELLTA 1180
Cdd:PRK10261 238 RVLVMYQGEAVETGSVEQIFHA 259
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
340-545 |
2.46e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 59.26 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI-LGELPpESGSVQVSGKYSYASQEP------ 412
Cdd:PRK11124 3 IQLNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMP-RSGTLNIAGNHFDFSKTPsdkair 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 413 ---------------WLfNASVRDNiLFGLPMdkqRYRTVLKRCALERDLELLHgdgTIVGERGAS-----LSGGQRARI 472
Cdd:PRK11124 79 elrrnvgmvfqqynlWP-HLTVQQN-LIEAPC---RVLGLSKDQALARAEKLLE---RLRLKPYADrfplhLSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 473 CLARAVYRRADVYLLDDPLSAVDTHVGRHLFDecmrgfLGKQLV------ILVTHQLQFLED-ADLIVIMDKGHVSACGT 545
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITAQIVS------IIRELAetgitqVIVTHEVEVARKtASRVVYMENGHIVEQGD 224
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
353-495 |
2.51e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 353 QHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----KYSYASQEPWLF---------NASV 419
Cdd:PRK13540 12 HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikKDLCTYQKQLCFvghrsginpYLTL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 420 RDNILFglpmDKQRYRTVLKRCALERDLELLHgdgtIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVD 495
Cdd:PRK13540 92 RENCLY----DIHFSPGAVGITELCRLFSLEH----LIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
358-551 |
3.07e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.22 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPE---SGSVQVSGK----------YSYASQEPWLFNA-SVRDNI 423
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMpidakemraiSAYVQQDDLFIPTlTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 424 LFG--LPMDKQRYRTVlKRCALE---RDLELLHGDGTIVGERGA--SLSGGQRARICLARAVYRRADVYLLDDPLSAVDT 496
Cdd:TIGR00955 121 MFQahLRMPRRVTKKE-KRERVDevlQALGLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665408680 497 ----HVGRHLFDECMRGflgkQLVILVTHQ--LQFLEDADLIVIMDKGHVSACGTYEEMLK 551
Cdd:TIGR00955 200 fmaySVVQVLKGLAQKG----KTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
296-525 |
4.67e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 296 MREEanvidMSERRD---------EKAEEEQHLLKEVEKRSYPVGiGKepdTLVeikalrarwgqeqhdlvlNNVNMSLR 366
Cdd:PRK11147 291 LRRE-----RSERREvmgtakmqvEEASRSGKIVFEMENVNYQID-GK---QLV------------------KDFSAQVQ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 367 RGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY--SYASQ-----EPwlfNASVRDNILFGlpmdKQ------R 433
Cdd:PRK11147 344 RGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLevAYFDQhraelDP---EKTVMDNLAEG----KQevmvngR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 434 YRTVL----------KRCAlerdlellhgdgTIVgergASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVgRHLF 503
Cdd:PRK11147 417 PRHVLgylqdflfhpKRAM------------TPV----KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET-LELL 479
|
250 260
....*....|....*....|..
gi 665408680 504 DECMRGFLGKqlVILVTHQLQF 525
Cdd:PRK11147 480 EELLDSYQGT--VLLVSHDRQF 499
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
358-542 |
4.69e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.43 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-YSYAS-------------QEPWLFNA-SVRDN 422
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpVRIRSprdaialgigmvhQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 423 ILFGLP------MDKQRYRTVLKRCA----LERDLEllhgdgTIVGErgasLSGGQRARICLARAVYRRADVYLLDDPlS 492
Cdd:COG3845 101 IVLGLEptkggrLDRKAARARIRELSerygLDVDPD------AKVED----LSVGEQQRVEILKALYRGARILILDEP-T 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 665408680 493 AVDT--HVgRHLFDEcMRGFLGKQL-VILVTHQLQ-FLEDADLIVIMDKGHVSA 542
Cdd:COG3845 170 AVLTpqEA-DELFEI-LRRLAAEGKsIIFITHKLReVMAIADRVTVLRRGKVVG 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
350-542 |
5.43e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.90 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 350 GQEQHDlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----KYSYASQEP------------- 412
Cdd:PRK11629 18 GSVQTD-VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsKLSSAAKAElrnqklgfiyqfh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 413 -WLFNASVRDNILFGLPMDKQRyrtvlKRCALERDLELLHGDG--TIVGERGASLSGGQRARICLARAVYRRADVYLLDD 489
Cdd:PRK11629 97 hLLPDFTALENVAMPLLIGKKK-----PAEINSRALEMLAAVGleHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 490 PLSAVDTHVGRHLFDecMRGFLGKQ---LVILVTHQLQFLEDADLIVIMDKGHVSA 542
Cdd:PRK11629 172 PTGNLDARNADSIFQ--LLGELNRLqgtAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
955-1180 |
6.35e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.10 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL------SYNDGAILI---DSLDTNDIG 1025
Cdd:PRK15134 6 LAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppvVYPSGDIRFhgeSLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1026 LHDLR-SKISIIPQEPVLfsgtmryNLDPFEQypddkLWKALEDV---H--LKEEI--SELPSGLQSI--------ISEG 1089
Cdd:PRK15134 86 LRGVRgNKIAMIFQEPMV-------SLNPLHT-----LEKQLYEVlslHrgMRREAarGEILNCLDRVgirqaakrLTDY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1090 GTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN--KFKDCTVLTIAHRLNTIMD-SDKVLVMDAG 1166
Cdd:PRK15134 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRElqQELNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
250
....*....|....
gi 665408680 1167 HVVEFGSPYELLTA 1180
Cdd:PRK15134 234 RCVEQNRAATLFSA 247
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
364-539 |
8.56e-09 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 55.83 E-value: 8.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 364 SLRRGQLVAVIGPVGSGKSSLIQAILgelppesgsvqvsgkysyasqepwlfnasvrdnILFGLPMDKQRYRTVLKRCAL 443
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILDAIG---------------------------------LALGGAQSATRRRSGVKAGCI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 444 ERDLELlhgdgTIVGERGaSLSGGQRARICLARAV----YRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQLVILV 519
Cdd:cd03227 64 VAAVSA-----ELIFTRL-QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVI 137
|
170 180
....*....|....*....|
gi 665408680 520 THQLQFLEDADLIVIMDKGH 539
Cdd:cd03227 138 THLPELAELADKLIHIKKVI 157
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
973-1174 |
9.02e-09 |
|
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: 56.77 E-value: 9.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYN--DGAILIDSLDTNDIGLHDlRSK--ISIIPQEPVLFSGtm 1047
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMgHPKYEvtEGEILFKGEDITDLPPEE-RARlgIFLAFQYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1048 rynldpfeqypddklwkaledVHLKEEISELPSGlqsiiseggtnFSVGQRQLVCLARAILRENRILVMDEATANVDpqT 1127
Cdd:cd03217 92 ---------------------VKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD--I 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 665408680 1128 DAL--IQATIRN-KFKDCTVLTIAH--RLNTIMDSDKVLVMDAGHVVEFGSP 1174
Cdd:cd03217 138 DALrlVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDK 189
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
341-551 |
9.28e-09 |
|
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: 56.77 E-value: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 341 EIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPE--SGSVQVSGKYsyasqepwLFNAS 418
Cdd:cd03217 2 EIKDLHVSVGGKE---ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGED--------ITDLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 419 VRDNILFGLPMDKQRYRTV--LKRCALERDLellhgdgtivgerGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDT 496
Cdd:cd03217 71 PEERARLGIFLAFQYPPEIpgVKNADFLRYV-------------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 497 HVGRHLFDECMRGFLGKQLVILVTHQLQFLE--DADLIVIMDKGHVSACGTYEEMLK 551
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
977-1172 |
9.39e-09 |
|
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: 56.92 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 977 LSFTIqPMEKVGIVGRTGAGKSSLINALFRLS-------YNDGAILIDSldTNDIGLHDLRSKISIIPQEPVLFSG-TMR 1048
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEkpdggtiVLNGTVLFDS--RKKINLPPQQRKIGLVFQQYALFPHlNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1049 YNLDPFEQYPDDKlwkalEDVHLKEEISELpSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTD 1128
Cdd:cd03297 94 ENLAFGLKRKRNR-----EDRISVDELLDL-LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 665408680 1129 ALIQATIRNKFKD--CTVLTIAHRLNTI-MDSDKVLVMDAGHVVEFG 1172
Cdd:cd03297 168 LQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
336-572 |
1.00e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.41 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 336 PDTLVEIKALRARWGQEqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG--KYSYASQEPW 413
Cdd:PRK10636 309 PNPLLKMEKVSAGYGDR---IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgiKLGYFAQHQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 414 LFnasvrdnilfgLPMDKQ--RYRTVLKRCALERDL-ELLHG---DGTIVGERGASLSGGQRARICLARAVYRRADVYLL 487
Cdd:PRK10636 386 EF-----------LRADESplQHLARLAPQELEQKLrDYLGGfgfQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 488 DDPLSAVDTHVgRHLFDECMRGFLGKQLVilVTHQLQFLEDA--DLIVIMDkghvsacGTYEEMLKSGQDFAQLLVESTQ 565
Cdd:PRK10636 455 DEPTNHLDLDM-RQALTEALIDFEGALVV--VSHDRHLLRSTtdDLYLVHD-------GKVEPFDGDLEDYQQWLSDVQK 524
|
....*..
gi 665408680 566 NSGGGDE 572
Cdd:PRK10636 525 QENQTDE 531
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
954-1189 |
1.79e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.92 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 954 KLVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRSK 1032
Cdd:PRK10253 7 RLRGEQLTLGYGKYT----VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLmTPAHGHVWLDGEHIQHYASKEVARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1033 ISIIPQEPVLFSGTMRYNLDPFEQYPDDKL---WKALEDVHLKEEISelPSGLQSIISEGGTNFSVGQRQLVCLARAILR 1109
Cdd:PRK10253 83 IGLLAQNATTPGDITVQELVARGRYPHQPLftrWRKEDEEAVTKAMQ--ATGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1110 ENRILVMDEATA--NVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASKAKVF 1186
Cdd:PRK10253 161 ETAIMLLDEPTTwlDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVTAELIERI 240
|
...
gi 665408680 1187 HGM 1189
Cdd:PRK10253 241 YGL 243
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
964-1201 |
2.12e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.05 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 964 YEPdtNSPCVLKGL---SFTIQPMEKVGIVGRTGAGKSSLINALFRL------SYNDGAILIDSlDTNDIGLHDLRSKIS 1034
Cdd:PRK13643 11 YQP--NSPFASRALfdiDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlqptegKVTVGDIVVSS-TSKQKEIKPVRKKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1035 IIPQEP--VLFSGTM-------RYNLDPFEQYPDDKLWKALEDVHLKEEISElpsglqsiisEGGTNFSVGQRQLVCLAR 1105
Cdd:PRK13643 88 VVFQFPesQLFEETVlkdvafgPQNFGIPKEKAEKIAAEKLEMVGLADEFWE----------KSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1106 AILRENRILVMDEATANVDPQTDALIQATIRNKFKDC-TVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYEL------ 1177
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGqTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVfqevdf 237
|
250 260
....*....|....*....|....*....
gi 665408680 1178 -----LTASKAKVFHGMVMQTGKASFDHL 1201
Cdd:PRK13643 238 lkaheLGVPKATHFADQLQKTGAVTFEKL 266
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
358-495 |
2.46e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 57.05 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY----------------------SYASQEPWLf 415
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitglsgrelrplrrrmqmvfqdPYASLNPRM- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 416 naSVRDnILfGLPMDKQRYRTVLKRcaLERDLELLhgdgTIVGERGASL-------SGGQRARICLARAVYRRADVYLLD 488
Cdd:COG4608 113 --TVGD-II-AEPLRIHGLASKAER--RERVAELL----ELVGLRPEHAdryphefSGGQRQRIGIARALALNPKLIVCD 182
|
....*..
gi 665408680 489 DPLSAVD 495
Cdd:COG4608 183 EPVSALD 189
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
353-551 |
2.79e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.37 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 353 QHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELP--PESGSVQVSGKYSY----------------------A 408
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTggGAPRGARVTGDVTLngeplaaidaprlarlravlpqA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 409 SQEPWLFnaSVRDNILFGlpmdkqRYRTVLKRCALE-RDLEL------LHGDGTIVGERGASLSGGQRARICLARAV--- 478
Cdd:PRK13547 92 AQPAFAF--SAREIVLLG------RYPHARRAGALThRDGEIawqalaLAGATALVGRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 479 ------YRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQL-VILVTHQLQF-LEDADLIVIMDKGHVSACGTYEEML 550
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLaARHADRIAMLADGAIVAHGAPADVL 243
|
.
gi 665408680 551 K 551
Cdd:PRK13547 244 T 244
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
342-560 |
2.84e-08 |
|
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: 58.38 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 342 IKALRARWgQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPEsGSVQVSG-------------KYSYA 408
Cdd:TIGR01271 1220 VQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGvswnsvtlqtwrkAFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 409 SQEPWLFNASVRDNILFGLPMDKQRYRTVLKRCALERDLELLHGDGTIVGERGAS-LSGGQRARICLARAVYRRADVYLL 487
Cdd:TIGR01271 1298 PQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYvLSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 488 DDP---LSAVDTHVGR----HLFDECMrgflgkqlVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQLL 560
Cdd:TIGR01271 1378 DEPsahLDPVTLQIIRktlkQSFSNCT--------VILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAM 1449
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
357-581 |
3.03e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 57.89 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILG--ELPPESGSV-----------------------QVSGKySYASQE 411
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyverpskvgepcPVCGG-TLEPEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 412 P--WLFNASVRDNIL----------FGLPMDKQRYRTVLK---------RCALERDLELLhgDGTIVGER----GASLSG 466
Cdd:TIGR03269 94 VdfWNLSDKLRRRIRkriaimlqrtFALYGDDTVLDNVLEaleeigyegKEAVGRAVDLI--EMVQLSHRithiARDLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 467 GQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQLVILVT-HQLQFLED-ADLIVIMDKGHVSACG 544
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTsHWPEVIEDlSDKAIWLENGEIKEEG 251
|
250 260 270
....*....|....*....|....*....|....*....
gi 665408680 545 TYEEMLKSgqdFAQLL--VESTQNSGGGDEIITSPNLSR 581
Cdd:TIGR03269 252 TPDEVVAV---FMEGVseVEKECEVEVGEPIIKVRNVSK 287
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
977-1172 |
3.17e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 977 LSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDS--LDT-NDIGLHDLRSKISIIPQEPVLfsgtmryNLD 1052
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLvESQGGEIIFNGqrIDTlSPGKLQALRRDIQFIFQDPYA-------SLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1053 PfEQYPDDKLWKALEdVH--------------LKEEISELPSGLQSIISEggtnFSVGQRQLVCLARAILRENRILVMDE 1118
Cdd:PRK10261 416 P-RQTVGDSIMEPLR-VHgllpgkaaaarvawLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665408680 1119 ATANVDPQtdalIQATIRNKFKD------CTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1172
Cdd:PRK10261 490 AVSALDVS----IRGQIINLLLDlqrdfgIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
973-1180 |
3.70e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 55.86 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSY-NDGAILIDS-----LDTNdIGLH-DL--RskisiipqEPVLF 1043
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEpTSGRVEVNGrvsalLELG-AGFHpELtgR--------ENIYL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1044 SGTMrYNLDPFEqyPDDKlwkaLEDVhlkEEISEL------P-----SGLQSIISeggtnFSVgqrqlvclarAILRENR 1112
Cdd:COG1134 112 NGRL-LGLSRKE--IDEK----FDEI---VEFAELgdfidqPvktysSGMRARLA-----FAV----------ATAVDPD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665408680 1113 ILVMDEATAnVdpqTDALIQATIRNKFKD-----CTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTA 1180
Cdd:COG1134 167 ILLVDEVLA-V---GDAAFQKKCLARIRElresgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
338-548 |
3.70e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 55.77 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 338 TLVEIKALRARWGQEqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-------YSYAS- 409
Cdd:PRK11300 4 PLLSVSGLMMRFGGL---LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhieglpgHQIARm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 410 ------QEPWLFNA-------------SVRDNILFGLpMDKQRYRTVlKRCALERDLELLHGDG-TIVGERGA-SLSGGQ 468
Cdd:PRK11300 81 gvvrtfQHVRLFREmtvienllvaqhqQLKTGLFSGL-LKTPAFRRA-ESEALDRAATWLERVGlLEHANRQAgNLAYGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 469 RARICLARAVYRRADVYLLDDP---LSAVDTHVGRHLFDECMRGFlgKQLVILVTHQLQFLED-ADLIVIMDKGHVSACG 544
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPaagLNPKETKELDELIAELRNEH--NVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANG 236
|
....
gi 665408680 545 TYEE 548
Cdd:PRK11300 237 TPEE 240
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
340-552 |
5.37e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.82 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQvsgkysyasqepWLFNASV 419
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK------------WSENANI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 420 ------------RDNILFGLpM--------DKQRYRTVLKRcalerdleLLHGDGTIvGERGASLSGGQRARICLARAVY 479
Cdd:PRK15064 385 gyyaqdhaydfeNDLTLFDW-MsqwrqegdDEQAVRGTLGR--------LLFSQDDI-KKSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 480 RRADVYLLDDPLSAVDTHVGRHLFD--ECMRGFLgkqlvILVTHQLQFLED--ADLIVIMDKGHVSACGTYEEMLKS 552
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMESIESLNMalEKYEGTL-----IFVSHDREFVSSlaTRIIEITPDGVVDFSGTYEEYLRS 526
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
356-495 |
6.64e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.79 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 356 LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYA------------SQEPWLFNASVRDni 423
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAvfsqhhvdgldlSSNPLLYMMRCFP-- 600
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408680 424 lfGLPmdKQRYRTVLKRCALERDLELlhgdgtivgERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVD 495
Cdd:PLN03073 601 --GVP--EQKLRAHLGSFGVTGNLAL---------QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
974-1169 |
6.66e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.72 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 974 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSY-NDGAILIDSLDTNDIGlHDLRSK--ISIIPQE-PVLFSGTMRY 1049
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEpTKGTITINNINYNKLD-HKLAAQlgIGIIYQElSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1050 NLdPFEQYPDDKLWKA----LEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANV-D 1124
Cdd:PRK09700 100 NL-YIGRHLTKKVCGVniidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtN 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 665408680 1125 PQTDAL--IQATIRNKFKdcTVLTIAHRLNTIMD-SDKVLVMDAGHVV 1169
Cdd:PRK09700 179 KEVDYLflIMNQLRKEGT--AIVYISHKLAEIRRiCDRYTVMKDGSSV 224
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
932-1170 |
7.03e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.52 E-value: 7.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 932 DPEGDFNSPaekQPPKSWPKegkLVTKDLSLRYEPDTNSpcvLKGLSFTIQPMEKVGIVGRTGAGKSS---LINALFRLS 1008
Cdd:PRK10522 306 PYKAEFPRP---QAFPDWQT---LELRNVTFAYQDNGFS---VGPINLTIKRGELLFLIGGNGSGKSTlamLLTGLYQPQ 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1009 ynDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTmrynLDPFEQYPDDKL---WkaLEDVHLKEEISElpsglqsi 1085
Cdd:PRK10522 377 --SGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALvekW--LERLKMAHKLEL-------- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1086 isEGG----TNFSVGQRQLVCLARAILRENRILVMDEATANVDPQ------TDALIQATIRNKfkdcTVLTIAHRLNTIM 1155
Cdd:PRK10522 441 --EDGrisnLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfrrefyQVLLPLLQEMGK----TIFAISHDDHYFI 514
|
250
....*....|....*
gi 665408680 1156 DSDKVLVMDAGHVVE 1170
Cdd:PRK10522 515 HADRLLEMRNGQLSE 529
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
974-1168 |
7.90e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.37 E-value: 7.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 974 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL----SYnDGAILIDSLDTNDIGLHDLRSK-ISIIPQEPVLFsgtmr 1048
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgTW-DGEIYWSGSPLKASNIRDTERAgIVIIHQELTLV----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1049 ynldpfeqypddKLWKALEDVHLKEEISeLPSGLQ--------------------SIISEGGTNFSVGQRQLVCLARAIL 1108
Cdd:TIGR02633 91 ------------PELSVAENIFLGNEIT-LPGGRMaynamylraknllrelqldaDNVTRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665408680 1109 RENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVM-DAGHV 1168
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDlKAHGVACVYISHKLNEVKAvCDTICVIrDGQHV 220
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
340-549 |
8.09e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.90 E-value: 8.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSliqailGELPpesgsVQVSGkySYASQEPWLFNA-- 417
Cdd:NF000106 14 VEVRGLVKHFGEVK---AVDGVDLDVREGTVLGVLGP*GAA**R------GALP-----AHV*G--PDAGRRPWRF*Twc 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 418 ----SVRDNILFGLPMDKQRYRTVLKRCALE---RDLELLHGDG--------------TIVGERGASLSGGQRARICLAR 476
Cdd:NF000106 78 anrrALRRTIG*HRPVR*GRRESFSGRENLYmigR*LDLSRKDAraradellerfsltEAAGRAAAKYSGGMRRRLDLAA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 477 AVYRRADVYLLDDPLSAVDTHVGRHLFDEcMRGFLGKQLVILVThqLQFLEDADL----IVIMDKGHVSACGTYEEM 549
Cdd:NF000106 158 SMIGRPAVLYLDEPTTGLDPRTRNEVWDE-VRSMVRDGATVLLT--TQYMEEAEQlaheLTVIDRGRVIADGKVDEL 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
955-1172 |
1.31e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.16 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTNspcvLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDSLDTNDIGLHDLRSki 1033
Cdd:PRK11701 7 LSVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSaRLAPDAGEVHYRMRDGQLRDLYALSE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1034 siiPQEPVLfsgtMRYNLDPFEQYPDDKL-------------------------------WkaLEDVHLKEE-ISELPsg 1081
Cdd:PRK11701 81 ---AERRRL----LRTEWGFVHQHPRDGLrmqvsaggnigerlmavgarhygdiratagdW--LERVEIDAArIDDLP-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1082 lqsiiseggTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKD--CTVLTIAHRLNTI-MDSD 1158
Cdd:PRK11701 150 ---------TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElgLAVVIVTHDLAVArLLAH 220
|
250
....*....|....
gi 665408680 1159 KVLVMDAGHVVEFG 1172
Cdd:PRK11701 221 RLLVMKQGRVVESG 234
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
977-1180 |
1.42e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.81 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 977 LSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAILIDSLDTNDIGLHDL----RSK-----ISIIPQEPvlfsgtm 1047
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLspreRRKlvghnVSMIFQEP------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1048 RYNLDPFE--------------------QYPDDKLWKALEDVHlKEEISELPSGLQSIISEggtnFSVGQRQLVCLARAI 1107
Cdd:PRK15093 99 QSCLDPSErvgrqlmqnipgwtykgrwwQRFGWRKRRAIELLH-RVGIKDHKDAMRSFPYE----LTEGECQKVMIAIAL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 1108 LRENRILVMDEATANVDPQTDALI--QATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTA 1180
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIfrLLTRLNQNNNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVTT 249
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
973-1174 |
1.54e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.96 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAILIDSldtndiglHDLR-----SKISIIPQEPVLFSGTM 1047
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN--------GKLRigyvpQKLYLDTTLPLTVNRFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1048 RynLDPFEQYPDdkLWKALEDV---HLKEEISELPSGlqsiiseggtnfsvGQRQLVCLARAILRENRILVMDEATANVD 1124
Cdd:PRK09544 91 R--LRPGTKKED--ILPALKRVqagHLIDAPMQKLSG--------------GETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 1125 PQTDA----LIQaTIRNKFkDCTVLTIAHRLNTIM-DSDKVLVMDaGHVVEFGSP 1174
Cdd:PRK09544 153 VNGQValydLID-QLRREL-DCAVLMVSHDLHLVMaKTDEVLCLN-HHICCSGTP 204
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
358-561 |
1.54e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.56 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKySYAS---------------QEPWLFNA-SVRD 421
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI-NYNKldhklaaqlgigiiyQELSVIDElTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 422 NILFG-LPMDK-------------QRYRTVLKRCALERDLEllhgdgtivgERGASLSGGQRARICLARAVYRRADVYLL 487
Cdd:PRK09700 100 NLYIGrHLTKKvcgvniidwremrVRAAMMLLRVGLKVDLD----------EKVANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 488 DDPLSAVDTHVGRHLFdecmrgFLGKQL------VILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEMlkSGQDFAQLL 560
Cdd:PRK09700 170 DEPTSSLTNKEVDYLF------LIMNQLrkegtaIVYISHKLaEIRRICDRYTVMKDGSSVCSGMVSDV--SNDDIVRLM 241
|
.
gi 665408680 561 V 561
Cdd:PRK09700 242 V 242
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
954-1151 |
1.62e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.02 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 954 KLVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsyND--------GAILI--DSLDTND 1023
Cdd:PRK14243 10 VLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRL--NDlipgfrveGKVTFhgKNLYAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1024 IGLHDLRSKISIIPQEPVLFSGTMRYNL------DPFEQYPDDKLWKALEDVHLKEEISELpsglqsiISEGGTNFSVGQ 1097
Cdd:PRK14243 84 VDPVEVRRRIGMVFQKPNPFPKSIYDNIaygariNGYKGDMDELVERSLRQAALWDEVKDK-------LKQSGLSLSGGQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 665408680 1098 RQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRL 1151
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
322-404 |
1.86e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.03 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 322 EVEKRSYPVGigkepDTLVEIKALRARwgQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQV 401
Cdd:COG3845 245 RVEKAPAEPG-----EVVLEVENLSVR--DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRL 317
|
...
gi 665408680 402 SGK 404
Cdd:COG3845 318 DGE 320
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
308-550 |
2.12e-07 |
|
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: 55.19 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 308 RRDEKAEEEQHLLK--EVEKRSYPVGIGKepdtlveIKALrarwgqeqhdlvlNNVNMSLRRGQLVAVIGPVGSGKSSLI 385
Cdd:TIGR03269 268 EKECEVEVGEPIIKvrNVSKRYISVDRGV-------VKAV-------------DNVSLEVKEGEIFGIVGTSGAGKTTLS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 386 QAILGELPPESGSVQV-------------------SGKY-SYASQEPWLF-NASVRDN----ILFGLPMDKQRYRTV--L 438
Cdd:TIGR03269 328 KIIAGVLEPTSGEVNVrvgdewvdmtkpgpdgrgrAKRYiGILHQEYDLYpHRTVLDNlteaIGLELPDELARMKAVitL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 439 KRCALERDLELlhgdgTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECM--RGFLGKQLV 516
Cdd:TIGR03269 408 KMVGFDEEKAE-----EILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILkaREEMEQTFI 482
|
250 260 270
....*....|....*....|....*....|....*
gi 665408680 517 IlVTHQLQFLED-ADLIVIMDKGHVSACGTYEEML 550
Cdd:TIGR03269 483 I-VSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
351-496 |
2.24e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.27 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 351 QEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPES--GSV---------QVSGKYSYASQEPWLF-NAS 418
Cdd:PLN03211 77 QIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTIlannrkptkQILKRTGFVTQDDILYpHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 419 VRDNILF----GLPMDKQRYRTVLKRCALERDLELLHGDGTIVGE---RGasLSGGQRARICLARAVYRRADVYLLDDPL 491
Cdd:PLN03211 157 VRETLVFcsllRLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPT 234
|
....*
gi 665408680 492 SAVDT 496
Cdd:PLN03211 235 SGLDA 239
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
325-498 |
2.40e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.20 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 325 KRSYPV--GIGKEPDTLveiKALrarwgqeqhdlvlNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVS 402
Cdd:PRK11308 12 KKHYPVkrGLFKPERLV---KAL-------------DGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 403 G----KYS------------------YAS-----------QEPWLFNASvrdnilfglpMDKQRYRtvlkrcalERDLEL 449
Cdd:PRK11308 76 GqdllKADpeaqkllrqkiqivfqnpYGSlnprkkvgqilEEPLLINTS----------LSAAERR--------EKALAM 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 450 LhgdgTIVGERGAS-------LSGGQRARICLARAVYRRADVYLLDDPLSAVDTHV 498
Cdd:PRK11308 138 M----AKVGLRPEHydryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
973-1172 |
2.81e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 53.09 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSY-NDGAILID------SLDTNDIGLHDLRSKISIIPQEpvlfsg 1045
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMpRSGTLNIAgnhfdfSKTPSDKAIRELRRNVGMVFQQ------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1046 tmrYNLDPF------------------EQYPDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAI 1107
Cdd:PRK11124 91 ---YNLWPHltvqqnlieapcrvlglsKDQALARAEKLLERLRLKPYADRFPLHL-----------SGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 1108 LRENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1172
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRElAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQG 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
973-1177 |
3.44e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 53.93 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNdiGLHDLRSKISIIPQEPVLFSG-TMRYN 1050
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLeHQTSGHIRFHGTDVS--RLHARDRKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1051 LD------PFEQYP-----DDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEA 1119
Cdd:PRK10851 95 IAfgltvlPRRERPnaaaiKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665408680 1120 TANVDPQTDALIQATIRN-----KFkdcTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYEL 1177
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQlheelKF---TSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQV 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
339-540 |
3.85e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.57 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 339 LVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLFNA- 417
Cdd:PRK11614 5 MLSFDKVSAHYGKIQ---ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 418 --------------SVRDNI-LFGLPMDKQRYRTVLKRC--ALERDLELLHgdgtivgERGASLSGGQRARICLARAVYR 480
Cdd:PRK11614 82 vaivpegrrvfsrmTVEENLaMGGFFAERDQFQERIKWVyeLFPRLHERRI-------QRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 481 RADVYLLDDPLSAVDTHVGRHLFD-------ECMRGFLGKQlvilvtHQLQFLEDADLIVIMDKGHV 540
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDtieqlreQGMTIFLVEQ------NANQALKLADRGYVLENGHV 215
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
357-495 |
4.08e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.07 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY--SYASQEP------WLFNASVRDNILFGLP 428
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiqHYASKEVarriglLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 429 MDKQRY--RTVLKRCALErDLELLH------GDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVD 495
Cdd:PRK10253 102 VARGRYphQPLFTRWRKE-DEEAVTkamqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
356-527 |
4.13e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 356 LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYA--SQEPWLFNASVRDNILFGlpmDKQr 433
Cdd:PRK10636 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAwvNQETPALPQPALEYVIDG---DRE- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 434 YRtvlkrcALERDLE------------LLHG-----DGTIVGERGASL------------------SGGQRARICLARAV 478
Cdd:PRK10636 91 YR------QLEAQLHdanerndghaiaTIHGkldaiDAWTIRSRAASLlhglgfsneqlerpvsdfSGGWRMRLNLAQAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 665408680 479 YRRADVYLLDDPLSAVDTHVGRHLfDECMRGFLGKqlVILVTHQLQFLE 527
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLDLDAVIWL-EKWLKSYQGT--LILISHDRDFLD 210
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
358-523 |
4.39e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-YSYAS-------------QE----PWLfnaSV 419
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQeMRFASttaalaagvaiiyQElhlvPEM---TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 420 RDNILFG-LPmdkQRYRTVLKRCALERDLELLHGDGTIV--GERGASLSGGQRARICLARAVYRRADVYLLDDP---LSA 493
Cdd:PRK11288 97 AENLYLGqLP---HKGGIVNRRLLNYEAREQLEHLGVDIdpDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPtssLSA 173
|
170 180 190
....*....|....*....|....*....|....
gi 665408680 494 VDTH----VGRHLFDEcmrgflGKqLVILVTHQL 523
Cdd:PRK11288 174 REIEqlfrVIRELRAE------GR-VILYVSHRM 200
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
642-841 |
5.70e-07 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 52.81 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 642 VVLIMLCIgtqILASGGDYFLSYWVKNT--ASSSTLDIYYFTAINVGLVICALLRTLLFF--NITMHS-----STELHNT 712
Cdd:cd18552 1 LALAILGM---ILVAATTAALAWLLKPLldDIFVEKDLEALLLVPLAIIGLFLLRGLASYlqTYLMAYvgqrvVRDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 713 MFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMM-LAFYYWR 791
Cdd:cd18552 78 LFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLpLAALPIR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 792 dfylKTSRDVKRL-----EAVARspMYSHFSATLVGLPTIRAMGAQQTLIGQYDN 841
Cdd:cd18552 158 ----RIGKRLRKIsrrsqESMGD--LTSVLQETLSGIRVVKAFGAEDYEIKRFRK 206
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
972-1136 |
6.06e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 51.41 E-value: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 972 CVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSynDGAIlidSLDTNDIGLHDLRSKISII----PQEPVLfs 1044
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLlrlIAGLLPPA--AGTI---KLDGGDIDDPDVAEACHYLghrnAMKPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1045 gTMRYNLDpfeqypddkLWKAL---EDVHLKEEISELpsGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATA 1121
Cdd:PRK13539 89 -TVAENLE---------FWAAFlggEELDIAAALEAV--GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170
....*....|....*
gi 665408680 1122 NVDPQTDALIQATIR 1136
Cdd:PRK13539 157 ALDAAAVALFAELIR 171
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
318-548 |
6.76e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.98 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 318 HLLKEVEKRSY-PVGI-----GKEPDTLVEIKALRARWGqeqhDLV-LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILG 390
Cdd:NF033858 239 ALLPEEKRRGHqPVVIpprpaDDDDEPAIEARGLTMRFG----DFTaVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTG 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 391 ELPPESGSVQVSGK------------YSYASQEPWLFNA-SVRDNI-----LFGLPMDK--QRYRTVLKRCALERDLEll 450
Cdd:NF033858 315 LLPASEGEAWLFGQpvdagdiatrrrVGYMSQAFSLYGElTVRQNLelharLFHLPAAEiaARVAEMLERFDLADVAD-- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 451 hgdgtivgERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDThVGRHLFDECMRGFLGKQLV-ILV-THqlqFLED 528
Cdd:NF033858 393 --------ALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP-VARDMFWRLLIELSREDGVtIFIsTH---FMNE 460
|
250 260
....*....|....*....|...
gi 665408680 529 A---DLIVIMDKGHVSACGTYEE 548
Cdd:NF033858 461 AercDRISLMHAGRVLASDTPAA 483
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
337-525 |
7.66e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.20 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 337 DTLVEIKALRARWGqeqhDLVL-NNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQV--SGKYSYASQ--- 410
Cdd:PRK11819 322 DKVIEAENLSKSFG----DRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgeTVKLAYVDQsrd 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 411 --EPwlfNASVRDNILFGLPMDKQRYRTVLKRCALER------DLEllhgdgTIVGErgasLSGGQRARICLARAVYRRA 482
Cdd:PRK11819 398 alDP---NKTVWEEISGGLDIIKVGNREIPSRAYVGRfnfkggDQQ------KKVGV----LSGGERNRLHLAKTLKQGG 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 665408680 483 DVYLLDDPLSAVDTHVGRHLfDECMRGFLGKQLVI---------LVTHQLQF 525
Cdd:PRK11819 465 NVLLLDEPTNDLDVETLRAL-EEALLEFPGCAVVIshdrwfldrIATHILAF 515
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
955-1181 |
7.87e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.19 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEpdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF---RLSYNDGAILidSLDTNDIGLHDLrs 1031
Cdd:PRK15056 7 IVVNDVTVTWR---NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMgfvRLASGKISIL--GQPTRQALQKNL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1032 kISIIPQE-------PVLFSGTM---RYNLDPFEQYPDDK----LWKALEDVHLKE----EISELpsglqsiiseggtnf 1093
Cdd:PRK15056 80 -VAYVPQSeevdwsfPVLVEDVVmmgRYGHMGWLRRAKKRdrqiVTAALARVDMVEfrhrQIGEL--------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1094 SVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFG 1172
Cdd:PRK15056 144 SGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
....*....
gi 665408680 1173 SPYELLTAS 1181
Cdd:PRK15056 224 PTETTFTAE 232
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
933-1170 |
8.69e-07 |
|
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: 53.26 E-value: 8.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 933 PEGDFNSPAEKQPPKSWpkeGKLVTKDLSLRYEPDTNSPC-VLKGLSFTIQPMEKVGIVGRTGAGKSSLIN---ALFRLS 1008
Cdd:COG4615 309 AEPAAADAAAPPAPADF---QTLELRGVTYRYPGEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKlltGLYRPE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1009 ynDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSgtmryNLDPFEQYPDDKLWKA-LEDVHLKEEISelpsglqsiIS 1087
Cdd:COG4615 386 --SGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD-----RLLGLDGEADPARARElLERLELDHKVS---------VE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1088 EGG---TNFSVGQRQLVCLARAILrENR-ILVMDEATANVDPQ------TDALIQATIRNKfkdcTVLTIAHrlntimD- 1156
Cdd:COG4615 450 DGRfstTDLSQGQRKRLALLVALL-EDRpILVFDEWAADQDPEfrrvfyTELLPELKARGK----TVIAISH------Dd 518
|
250
....*....|....*....
gi 665408680 1157 -----SDKVLVMDAGHVVE 1170
Cdd:COG4615 519 ryfdlADRVLKMDYGKLVE 537
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
357-539 |
1.25e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 357 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYS--YASQEPWL-FNASVRDNI---------- 423
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKvgYLPQEPQLdPEKTVRENVeegvaevkaa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 424 ---------LFGLPMDKqrYRTVLKRCA-------------LERDLE-------LLHGDGTIvgergASLSGGQRARICL 474
Cdd:PRK11819 102 ldrfneiyaAYAEPDAD--FDALAAEQGelqeiidaadawdLDSQLEiamdalrCPPWDAKV-----TKLSGGERRRVAL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 475 ARAVYRRADVYLLDDPLSAVDTH----VGRHLfdecmRGFLGKqlVILVTHQLQFLED-ADLIVIMDKGH 539
Cdd:PRK11819 175 CRLLLEKPDMLLLDEPTNHLDAEsvawLEQFL-----HDYPGT--VVAVTHDRYFLDNvAGWILELDRGR 237
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
958-1172 |
1.25e-06 |
|
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: 50.34 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALfrlsyndgailidsldTNDIGlhdlrSKISIip 1037
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAL----------------ANRTE-----GNVSV-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1038 qepvlfSGTMRYN---LDPF-EQYPDDKLWKALEDVHLKE-------EISELPSGLQSIiseggTNFSVGQRQLVCLARA 1106
Cdd:cd03233 64 ------EGDIHYNgipYKEFaEKYPGEIIYVSEEDVHFPTltvretlDFALRCKGNEFV-----RGISGGERKRVSIAEA 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1107 ILRENRILVMDEATANVDPQTDALIQATIR---NKFKDCTVLTIAHRLNTIMDS-DKVLVMDAGHVVEFG 1172
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDSSTALEILKCIRtmaDVLKTTTFVSLYQASDEIYDLfDKVLVLYEGRQIYYG 202
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
639-925 |
1.26e-06 |
|
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: 51.62 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 639 LVFVVLIMLciGTQILASGGDYFLSYWVKNTASSSTLDIyyftainvglvicallRTLLFFNItmhsstelhntmfQGLS 718
Cdd:cd18544 40 LLLLALLYL--GLLLLSFLLQYLQTYLLQKLGQRIIYDL----------------RRDLFSHI-------------QRLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 719 rtaLYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMMLAFYYWRDFYLKTS 798
Cdd:cd18544 89 ---LSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 799 RDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHssgYYTFVSTSRAFGYY---LDLFCVAYVISV 875
Cdd:cd18544 166 RKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEY---RKANLKSIKLFALFrplVELLSSLALALV 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 876 ILHnFFNPPLHNAGQIGL--AITQALGM-----TGMVQwgmrQSAELENAMTSVERV 925
Cdd:cd18544 243 LWY-GGGQVLSGAVTLGVlyAFIQYIQRffrpiRDLAE----KFNILQSAMASAERI 294
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
973-1136 |
1.35e-06 |
|
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: 50.18 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIdsldtNDIGLHDLRSKIsiipQEPVLFSG---TMR 1048
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLaGRVLL-----NGGPLDFQRDSI----ARGLLYLGhapGIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1049 YNLDPFEQ-------YPDDKLWKALEDVHLkeeiselpSGLQSIISeggTNFSVGQRQLVCLARAILRENRILVMDEATA 1121
Cdd:cd03231 86 TTLSVLENlrfwhadHSDEQVEEALARVGL--------NGFEDRPV---AQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170
....*....|....*
gi 665408680 1122 NVDPQTDALIQATIR 1136
Cdd:cd03231 155 ALDKAGVARFAEAMA 169
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
973-1191 |
1.36e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.33 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFR-LSYNDGAILIDSLDTNDIGLHDLRSKISIIPQE-PVLFSGTMRyN 1050
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRhQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAEGMTVR-E 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1051 LDPFEQYPddklWK-AL-----EDVHLKEEISELpSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVD 1124
Cdd:PRK10575 105 LVAIGRYP----WHgALgrfgaADREKVEEAISL-VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408680 1125 --PQTD--ALIQATIRNkfKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASKAKVFHGMVM 1191
Cdd:PRK10575 180 iaHQVDvlALVHRLSQE--RGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPM 249
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
989-1177 |
1.61e-06 |
|
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: 51.73 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 989 IVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHdLRSkISIIPQEPVLFSG-TMRYNLdpfeQYP-------- 1058
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDsGSIMLDGEDVTNVPPH-LRH-INMVFQSYALFPHmTVEENV----AFGlkmrkvpr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1059 ---DDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQ--- 1132
Cdd:TIGR01187 75 aeiKPRVLEALRLVQLEEFADRKPHQL-----------SGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQlel 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 665408680 1133 ATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYEL 1177
Cdd:TIGR01187 144 KTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
946-1177 |
1.64e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 51.76 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 946 PKSWPKEGKLVTKDLSLRYEPDT-NSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL--FRLSyNDGAILIDSLDTN 1022
Cdd:PRK11607 6 PRPQAKTRKALTPLLEIRNLTKSfDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLagFEQP-TAGQIMLDGVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1023 DIGLHdlRSKISIIPQEPVLFSG-TMRYNLD-PFEQypdDKLWKA---------LEDVHLKEEISELPSGLqsiiseggt 1091
Cdd:PRK11607 85 HVPPY--QRPINMMFQSYALFPHmTVEQNIAfGLKQ---DKLPKAeiasrvnemLGLVHMQEFAKRKPHQL--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1092 nfSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFK--DCTVLTIAHRLNTIMD-SDKVLVMDAGHV 1168
Cdd:PRK11607 151 --SGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTmAGRIAIMNRGKF 228
|
....*....
gi 665408680 1169 VEFGSPYEL 1177
Cdd:PRK11607 229 VQIGEPEEI 237
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
358-542 |
1.84e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYA-SQEPWLFNASV-------RDNILFGLPM 429
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrSPQDGLANGIVyisedrkRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 430 DKQRYRTVLKR-----CALERDLELLHGDGTI-------------VGErgasLSGGQRARICLARAVYRRADVYLLDDPL 491
Cdd:PRK10762 348 KENMSLTALRYfsragGSLKHADEQQAVSDFIrlfniktpsmeqaIGL----LSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 665408680 492 SAVDTHVGRHLFDeCMRGFLGKQL-VILVTHQL-QFLEDADLIVIMDKGHVSA 542
Cdd:PRK10762 424 RGVDVGAKKEIYQ-LINQFKAEGLsIILVSSEMpEVLGMSDRILVMHEGRISG 475
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
912-1174 |
1.99e-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: 52.71 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 912 SAELENAMTSVERVLE-YKDLD-PEGDFNSPAEKQPPKSWPKegkLVTKDLSLRYEPdTNSPCVLKgLSFTIQPMEKVGI 989
Cdd:TIGR01257 887 STREERALEKTEPLTEeMEDPEhPEGINDSFFERELPGLVPG---VCVKNLVKIFEP-SGRPAVDR-LNITFYENQITAF 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 990 VGRTGAGKSSLINALF-RLSYNDGAILIDSLDTnDIGLHDLRSKISIIPQEPVLFSG-TMRYNLDPFEQYPDdklwKALE 1067
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTgLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFYAQLKG----RSWE 1036
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1068 DVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTI 1147
Cdd:TIGR01257 1037 EAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMS 1116
|
250 260
....*....|....*....|....*...
gi 665408680 1148 AHRLNTI-MDSDKVLVMDAGHVVEFGSP 1174
Cdd:TIGR01257 1117 THHMDEAdLLGDRIAIISQGRLYCSGTP 1144
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1094-1177 |
2.43e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 51.26 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1094 SVGQRQLVCLARAILRENRILVMDEATANVdpqtDALIQATIRNKFK------DCTVLTIAH-RLNTIMDSDKVLVMDAG 1166
Cdd:PRK11432 138 SGGQQQRVALARALILKPKVLLFDEPLSNL----DANLRRSMREKIRelqqqfNITSLYVTHdQSEAFAVSDTVIVMNKG 213
|
90
....*....|.
gi 665408680 1167 HVVEFGSPYEL 1177
Cdd:PRK11432 214 KIMQIGSPQEL 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
336-549 |
2.47e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.47 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 336 PDTLvEIKALRArwgqEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPP----ESGSVQVSGKYSYAS-- 409
Cdd:PRK10418 2 PQQI-ELRNIAL----QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCal 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 410 ---------QEPW-LFN------ASVRDNIL-FGLPMDKQRYRTVLKRCALERdlellhgDGTIVGERGASLSGGQRARI 472
Cdd:PRK10418 77 rgrkiatimQNPRsAFNplhtmhTHARETCLaLGKPADDATLTAALEAVGLEN-------AARVLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 473 CLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECM-----RGfLGkqlVILVTHQLQFLED-ADLIVIMDKGHVSACGTY 546
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLEsivqkRA-LG---MLLVTHDMGVVARlADDVAVMSHGRIVEQGDV 225
|
...
gi 665408680 547 EEM 549
Cdd:PRK10418 226 ETL 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
358-541 |
2.62e-06 |
|
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: 51.36 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELP--PESGSVQVSGKYSYAS--------------QEPWLF-NASVR 420
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASnirdteragiviihQELTLVpELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 421 DNILFG----LPMDKQRYRTVLKRC-ALERDLEL-LHGDGTIVGERGaslsGGQRARICLARAVYRRADVYLLDDPLSAV 494
Cdd:TIGR02633 97 ENIFLGneitLPGGRMAYNAMYLRAkNLLRELQLdADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 665408680 495 DTHVGRHLFDeCMRGFLGKQLV-ILVTHQLQFLED-ADLI-VIMDKGHVS 541
Cdd:TIGR02633 173 TEKETEILLD-IIRDLKAHGVAcVYISHKLNEVKAvCDTIcVIRDGQHVA 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
980-1164 |
2.83e-06 |
|
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: 50.10 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 980 TIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDsldtndiglhdlRSKISIIPQE-PVLFSGTMRYNLdpfeqy 1057
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAgVLKPDEGDIEIE------------LDTVSYKPQYiKADYEGTVRDLL------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1058 pDDKLWKALEDVHLKEEISElPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRn 1137
Cdd:cd03237 83 -SSITKDFYTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR- 159
|
170 180 190
....*....|....*....|....*....|.
gi 665408680 1138 KF---KDCTVLTIAHRLNTI-MDSDKVLVMD 1164
Cdd:cd03237 160 RFaenNEKTAFVVEHDIIMIdYLADRLIVFE 190
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1091-1211 |
2.96e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 50.40 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1091 TNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGH 1167
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRyCERIVALRQGH 230
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 665408680 1168 VvefgspyelltaskakVFHGMVMQTGKASFDHLLKVAENTKQN 1211
Cdd:PRK09984 231 V----------------FYDGSSQQFDNERFDHLYRSINRVEEN 258
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
887-1150 |
3.54e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 51.29 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 887 NAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEykDLDpEGDFNSPAEKQPPKS---------WPKEGKLVT 957
Cdd:TIGR00954 371 NNGRLLLKAADALGRLMLAGRDMTRLAGFTARVDTLLQVLD--DVK-SGNFKRPRVEEIESGreggrnsnlVPGRGIVEY 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 958 KDLSLRYEpdtNSPCV-------LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL--SYNdGAILIDSldtndiglhd 1028
Cdd:TIGR00954 448 QDNGIKFE---NIPLVtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpVYG-GRLTKPA---------- 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1029 lRSKISIIPQEPVLFSGTMR----YNLDPFEQ----YPDDKLWKALEDVHLkEEISELPSGLqSIISEGGTNFSVGQRQL 1100
Cdd:TIGR00954 514 -KGKLFYVPQRPYMTLGTLRdqiiYPDSSEDMkrrgLSDKDLEQILDNVQL-THILEREGGW-SAVQDWMDVLSGGEKQR 590
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 665408680 1101 VCLARAILRENRILVMDEATANVDPQTDALIQATIRNkfKDCTVLTIAHR 1150
Cdd:TIGR00954 591 IAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
977-1168 |
4.21e-06 |
|
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: 50.98 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 977 LSFTIQPMEKVGIVGRTGAGKSSLINALFRlSYN---DGAILIDS--LDTNDIgLHDLRSKISIIPQE-------PVL-- 1042
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPgkfEGNVFINGkpVDIRNP-AQAIRAGIAMVPEDrkrhgivPILgv 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1043 -----------FSGTMRYNldpfEQYPDDKLWKALEDVHLKEEISELPSGlqsiiseggtNFSVGQRQLVCLARAILREN 1111
Cdd:TIGR02633 357 gknitlsvlksFCFKMRID----AAAELQIIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 1112 RILVMDEATANVDPQTDALIQATIRNKFKD-CTVLTIAHRLNTIMD-SDKVLVMDAGHV 1168
Cdd:TIGR02633 423 RVLILDEPTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
974-1166 |
4.26e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 974 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTN-DIGLHDLRSKISIIPQE--PVLFSGTM-- 1047
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIyQKDSGSILFQGKEIDfKSSKEALENGISMVHQElnLVLQRSVMdn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1048 ----RYNL-----DPFEQYPDDK-LWKALE-DVHLKEEISELpsglqsiiseggtnfSVGQRQLVCLARAILRENRILVM 1116
Cdd:PRK10982 94 mwlgRYPTkgmfvDQDKMYRDTKaIFDELDiDIDPRAKVATL---------------SVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 665408680 1117 DEATANV-DPQTDALIqaTIRNKFKD--CTVLTIAHRLNTIMD-SDKVLVMDAG 1166
Cdd:PRK10982 159 DEPTSSLtEKEVNHLF--TIIRKLKErgCGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
955-1132 |
4.29e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 49.43 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDI---GLHDLR 1030
Cdd:PRK11629 6 LQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQPMSKLssaAKAELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1031 S-KISIIPQ---------------EPVLFSGTMRynldpfeQYPDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfS 1094
Cdd:PRK11629 86 NqKLGFIYQfhhllpdftalenvaMPLLIGKKKP-------AEINSRALEMLAAVGLEHRANHRPSEL-----------S 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 665408680 1095 VGQRQLVCLARAILRENRILVMDEATANVDPQT-DALIQ 1132
Cdd:PRK11629 148 GGERQRVAIARALVNNPRLVLADEPTGNLDARNaDSIFQ 186
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1081-1177 |
5.04e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 49.22 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1081 GLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQT----DALIqATIRNKFkDCTVLTIAHRLNTIMD 1156
Cdd:PRK11300 142 GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKEtkelDELI-AELRNEH-NVTVLLIEHDMKLVMG 219
|
90 100
....*....|....*....|..
gi 665408680 1157 -SDKVLVMDAGHVVEFGSPYEL 1177
Cdd:PRK11300 220 iSDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
338-538 |
5.39e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.47 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 338 TLVEIKALRARWGQEQHD-LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPE-----SGSVQVSGKYSYASQE 411
Cdd:PRK15134 4 PLLAIENLSVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 412 PWLfnASVRDN---ILFGLPM---------DKQRYRtVLkrcALERDLELLHGDGTI------VGERGAS---------L 464
Cdd:PRK15134 84 QTL--RGVRGNkiaMIFQEPMvslnplhtlEKQLYE-VL---SLHRGMRREAARGEIlncldrVGIRQAAkrltdyphqL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 465 SGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRH---LFDEcMRGFLGKQLvILVTHQLQFLED-ADLIVIMDKG 538
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQilqLLRE-LQQELNMGL-LFITHNLSIVRKlADRVAVMQNG 233
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
682-925 |
5.85e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 49.43 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 682 AINVGLVICALLRTLLFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLT 761
Cdd:cd18563 51 GAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILM 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 762 LTGIICVLCVTNPWY----LINTFAMMLAFYYWRD----FYLKTSRdvkrleavARSPMYSHFSATLVGLPTIRAMGAQQ 833
Cdd:cd18563 131 IIGIGVVLFSLNWKLallvLIPVPLVVWGSYFFWKkirrLFHRQWR--------RWSRLNSVLNDTLPGIRVVKAFGQEK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 834 TLIGQYDNY-QDLhssgYYTFVSTSRAFGYYLDLFCVAYVISVILHNFFNPPLHNAGQIGL-AITQALGMTGM----VQW 907
Cdd:cd18563 203 REIKRFDEAnQEL----LDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLgTLVAFLSYLGMfygpLQW 278
|
250
....*....|....*...
gi 665408680 908 GMRQSAELENAMTSVERV 925
Cdd:cd18563 279 LSRLNNWITRALTSAERI 296
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
317-498 |
5.93e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.47 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 317 QHLLkEVEKRSYPVGIGKEPDTLVEIKALRARWGQEQ--------HDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI 388
Cdd:PRK15134 254 QKLL-NSEPSGDPVPLPEPASPLLDVEQLQVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLAL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 389 L------GE---------------LPPESGSVQVSGKYSYASQEPWLfnaSVRDNILFGLPMD---------KQRYRTVL 438
Cdd:PRK15134 333 LrlinsqGEiwfdgqplhnlnrrqLLPVRHRIQVVFQDPNSSLNPRL---NVLQIIEEGLRVHqptlsaaqrEQQVIAVM 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 439 KRCALerDLELLHgdgtivgERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHV 498
Cdd:PRK15134 410 EEVGL--DPETRH-------RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTV 460
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
987-1006 |
6.92e-06 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 49.38 E-value: 6.92e-06
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
973-1170 |
7.08e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.42 E-value: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAILIDSLDTNDIGlhdlrSKISIIPQEPVLFSgtmrynld 1052
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFG-----REASLIDAIGRKGD-------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1053 pfeqyPDDKLwKALEDVHLkeeiSELPSGLQSIiseggTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQ 1132
Cdd:COG2401 112 -----FKDAV-ELLNAVGL----SDAVLWLRRF-----KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 665408680 1133 ATIRnkfKDC-----TVLTIAHRLNTI--MDSDKVLVMDAGHVVE 1170
Cdd:COG2401 177 RNLQ---KLArragiTLVVATHHYDVIddLQPDLLIFVGYGGVPE 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
328-542 |
7.95e-06 |
|
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: 49.82 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 328 YPvgigKEP----DTLVEIKALRARWGQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPE-SGSVQVS 402
Cdd:TIGR02633 246 YP----HEPheigDVILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFIN 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 403 GKySYASQEPwlfNASVRDNILFgLPMDKQRY-------------RTVLKRCALERDLELLHGDGTIVGE------RGAS 463
Cdd:TIGR02633 322 GK-PVDIRNP---AQAIRAGIAM-VPEDRKRHgivpilgvgknitLSVLKSFCFKMRIDAAAELQIIGSAiqrlkvKTAS 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 464 -------LSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDecMRGFLGKQ--LVILVTHQL-QFLEDADLIV 533
Cdd:TIGR02633 397 pflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYK--LINQLAQEgvAIIVVSSELaEVLGLSDRVL 474
|
....*....
gi 665408680 534 IMDKGHVSA 542
Cdd:TIGR02633 475 VIGEGKLKG 483
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
358-550 |
9.33e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 48.68 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPEsGSVQVSGK----YSYAS----------QEPWLFNASVRDNI 423
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRplsdWSAAElarhraylsqQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 424 LFGLP---MDKQRYRTVLKRCaleRDLEL---LHgdgtivgeRGAS-LSGG--QRARicLARA---VYRRADVY----LL 487
Cdd:COG4138 91 ALHQPagaSSEAVEQLLAQLA---EALGLedkLS--------RPLTqLSGGewQRVR--LAAVllqVWPTINPEgqllLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 488 DDPLSAVD-THVGrhLFDECMRGFLGKQL-VILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEML 550
Cdd:COG4138 158 DEPMNSLDvAQQA--ALDRLLRELCQQGItVVMSSHDLnHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
973-1169 |
1.44e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 47.95 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF---RLSynDGAILIDSLDTNDIGLHD-LRSKISIIPQEPVLFSG-TM 1047
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCgdpRAT--SGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1048 RYNLDPFEQYPDDKLWKAledvHLKEEISELPSGLQSIISEGGTnFSVGQRQLVCLARAILRENRILVMDEATANVDPQT 1127
Cdd:PRK11614 98 EENLAMGGFFAERDQFQE----RIKWVYELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 665408680 1128 DALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVV 1169
Cdd:PRK11614 173 IQQIFDTIEQlREQGMTIFLVEQNANQALKlADRGYVLENGHVV 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
358-551 |
1.59e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 48.54 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLFNASVrdniLFG--------LP- 428
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGV----VFGqrsqlwwdLPa 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 429 ------------MDKQRYRTVLKRCAlerdlELLHgdgtiVGE------RgaSLSGGQRARICLARAVYRRADVYLLDDP 490
Cdd:COG4586 114 idsfrllkaiyrIPDAEYKKRLDELV-----ELLD-----LGElldtpvR--QLSLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 491 LSAVDTHVGRHLfdecmRGFLgKQL-------VILVTHQLQFLED-ADLIVIMDKGHVSACGTYEEMLK 551
Cdd:COG4586 182 TIGLDVVSKEAI-----REFL-KEYnrergttILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
955-1187 |
1.61e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 48.18 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 955 LVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLI-NALFRLSYNDGAIL-----IDSLDTNDIG-LH 1027
Cdd:COG4152 2 LELKGLTKRFGDKT----AVDDVSFTVPKGEIFGLLGPNGAGKTTTIrIILGILAPDSGEVLwdgepLDPEDRRRIGyLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1028 D---LRSKISIIPQepVLFSGTMRyNLDPFEQYPDDKLWkaLEDVHLKE----EISELpsglqsiiseggtnfSVGQRQL 1100
Cdd:COG4152 78 EergLYPKMKVGEQ--LVYLARLK-GLSKAEAKRRADEW--LERLGLGDrankKVEEL---------------SKGNQQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1101 VCLARAILRENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELL 1178
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRElAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIR 217
|
....*....
gi 665408680 1179 TASKAKVFH 1187
Cdd:COG4152 218 RQFGRNTLR 226
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
986-1006 |
1.67e-05 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 45.30 E-value: 1.67e-05
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
974-1166 |
1.88e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 974 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHDLR-SKISIIPQE----PVL----- 1042
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDaGSILYLGKEVTFNGPKSSQeAGIGIIHQElnliPQLtiaen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1043 -FSGtmRYNLDPF------EQYPD-DKLWKALEDVH-LKEEISELpsglqsiiseggtnfSVGQRQLVCLARAILRENRI 1113
Cdd:PRK10762 100 iFLG--REFVNRFgridwkKMYAEaDKLLARLNLRFsSDKLVGEL---------------SIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 1114 LVMDEAT-ANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAG 1166
Cdd:PRK10762 163 IIMDEPTdALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEiCDDVTVFRDG 217
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
988-1031 |
2.24e-05 |
|
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.
Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 45.41 E-value: 2.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 988 GIVGRTGAGKSSLINALFRLS---------------------YNDGAILIDSLDTNDIGLHDLRS 1031
Cdd:cd11383 1 GLMGKTGAGKSSLCNALFGTEvaavgdrrpttraaqayvwqtGGDGLVLLDLPGVGERGRRDREY 65
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
337-390 |
2.86e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.94 E-value: 2.86e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 665408680 337 DTLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILG 390
Cdd:CHL00131 5 KPILEIKNLHASVNENE---ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1094-1177 |
4.66e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 47.33 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1094 SVGQRQLVCLARAILRENRILVMDEATANVDPqtdAL-----IQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGH 1167
Cdd:PRK11000 135 SGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA---ALrvqmrIEISRLHKRLGRTMIYVTHDQVEAMTlADKIVVLDAGR 211
|
90
....*....|
gi 665408680 1168 VVEFGSPYEL 1177
Cdd:PRK11000 212 VAQVGKPLEL 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
973-1169 |
4.78e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.80 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL------SYNDGAILIDSLDTNDigLHDLRSK-ISIIPQepvlfsg 1045
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLdkptsgTYRVAGQDVATLDADA--LAQLRREhFGFIFQ------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1046 tmRYNLDPF---EQYPD-DKLWKALEDVHLKEEISELPS--GLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEA 1119
Cdd:PRK10535 94 --RYHLLSHltaAQNVEvPAVYAGLERKQRLLRAQELLQrlGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 665408680 1120 TANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVV 1169
Cdd:PRK10535 172 TGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
973-1173 |
5.34e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.17 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYN--DGAILIDSLDTNDIGlHDLRSKISIIP--QEPVLFSGT- 1046
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAgHPAYKilEGDILFKGESILDLE-PEERAHLGIFLafQYPIEIPGVs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1047 ------MRYN----------LDP--FEQYPDDKlwkaLEDVHLKeeiselPSGLQSIISEGgtnFSVGQRQLVCLARAIL 1108
Cdd:CHL00131 101 nadflrLAYNskrkfqglpeLDPleFLEIINEK----LKLVGMD------PSFLSRNVNEG---FSGGEKKRNEILQMAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1109 RENRILVMDEATANVDpqTDAL-IQATIRNKFKDCT--VLTIAH--RLNTIMDSDKVLVMDAGHVVEFGS 1173
Cdd:CHL00131 168 LDSELAILDETDSGLD--IDALkIIAEGINKLMTSEnsIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
358-541 |
5.38e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.23 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELP--PESGSVQVSGKYSYAS--------------QEPWLF-NASVR 420
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASnirdteragiaiihQELALVkELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 421 DNILFG---LPMDKQRYRTVLKRC-ALERDLELLHGDGTIVGErgasLSGGQRARICLARAVYRRADVYLLDDPLSAVDT 496
Cdd:PRK13549 101 ENIFLGneiTPGGIMDYDAMYLRAqKLLAQLKLDINPATPVGN----LGLGQQQLVEIAKALNKQARLLILDEPTASLTE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 665408680 497 HVGRHLFDecmrgfLGKQL------VILVTHQLQFLED-ADLI-VIMDKGHVS 541
Cdd:PRK13549 177 SETAVLLD------IIRDLkahgiaCIYISHKLNEVKAiSDTIcVIRDGRHIG 223
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
341-495 |
5.81e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.19 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 341 EIKALRARWGQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLFNA-SV 419
Cdd:PRK13545 23 KLKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQlTG 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665408680 420 RDNI-LFGLPM--DKQRYRTVLKRCALERDLellhgdGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVD 495
Cdd:PRK13545 103 IENIeLKGLMMglTKEKIKEIIPEIIEFADI------GKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
358-566 |
5.91e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG--KYSYASQEPWLFNA-SVRDNILFGL------- 427
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlIVARLQQDPPRNVEgTVYDFVAEGIeeqaeyl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 428 -------------PMDK---------------------QRYRTVLKRCALERDLELlhgdgtivgergASLSGGQRARIC 473
Cdd:PRK11147 99 kryhdishlvetdPSEKnlnelaklqeqldhhnlwqleNRINEVLAQLGLDPDAAL------------SSLSGGWLRKAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 474 LARAVYRRADVYLLDDPLSavdthvgrHLfD----ECMRGFLG--KQLVILVTHQLQFLED-ADLIVIMDKGH-VSACGT 545
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTN--------HL-DietiEWLEGFLKtfQGSIIFISHDRSFIRNmATRIVDLDRGKlVSYPGN 237
|
250 260
....*....|....*....|.
gi 665408680 546 YEEMLKSGQDfaQLLVESTQN 566
Cdd:PRK11147 238 YDQYLLEKEE--ALRVEELQN 256
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
974-1174 |
6.25e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 46.28 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 974 LKGLSFTIQPMEKVGIVGRTGAGKSS---LINALfrLSYNDGAILIDSLD-TNDIGLHDL---RSKISIIPQ--EPVLFS 1044
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTimqLLNGL--HVPTQGSVRVDDTLiTSTSKNKDIkqiRKKVGLVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1045 GT----MRYNLDPFEQYPDDKLWKALEDVHLKEeISElpsglqSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEAT 1120
Cdd:PRK13649 101 ETvlkdVAFGPQNFGVSQEEAEALAREKLALVG-ISE------SLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 1121 ANVDPQTDALIQATIRNKFKD-CTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSP 1174
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKP 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
342-554 |
6.69e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.16 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 342 IKALRARWGQEQHDL-VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQvsgkysyaSQEPWL------ 414
Cdd:PRK10261 15 VENLNIAFMQEQQKIaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ--------CDKMLLrrrsrq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 415 -------FNASVRD------NILFGLPMD---------KQRYRTVLKRCALERDLELLHGD-----------GTIVGERG 461
Cdd:PRK10261 87 vielseqSAAQMRHvrgadmAMIFQEPMTslnpvftvgEQIAESIRLHQGASREEAMVEAKrmldqvripeaQTILSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 462 ASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDecMRGFLGKQL---VILVTHQLQFLED-ADLIVIMDK 537
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ--LIKVLQKEMsmgVIFITHDMGVVAEiADRVLVMYQ 244
|
250
....*....|....*..
gi 665408680 538 GHVSACGTYEEMLKSGQ 554
Cdd:PRK10261 245 GEAVETGSVEQIFHAPQ 261
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
3-198 |
7.03e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 46.41 E-value: 7.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 3 GITIAALELGTRATVPLLLAGLIsefsehGNGHSYNAQIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRK 82
Cdd:cd18565 23 GVAIDAVFNGEASFLPLVPASLG------PADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 83 ALRLSRTSLGGTTTGQVVNLLSNDLNRFDRclihfhFL--------WLGPLELLIASYFLYEQIGMASFygisiLVLYLP 154
Cdd:cd18565 97 VQRLDMAFFEDRQTGDLMSVLNNDVNQLER------FLddgansiiRVVVTVLGIGAILFYLNWQLALV-----ALLPVP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 665408680 155 LQTYLSRVTSKL--RLQTALRtdQRVRMMNEI----ISGIQVIKMYTWER 198
Cdd:cd18565 166 LIIAGTYWFQRRiePRYRAVR--EAVGDLNARlennLSGIAVIKAFTAED 213
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
979-1206 |
1.27e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 979 FTIQPMEKVGIVGRTGAGKSSLINALFR-LSYNDGAILIDSldtndiglhDLrsKISIIPQEP---VlfSGTM------- 1047
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGeVLLDDGRIIYEQ---------DL--IVARLQQDPprnV--EGTVydfvaeg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1048 ---------RYN--LDPFEQYPDDKLWKALEdvHLKEEIS-----ELPSGLQSIISEGG-------TNFSVGQRQLVCLA 1104
Cdd:PRK11147 91 ieeqaeylkRYHdiSHLVETDPSEKNLNELA--KLQEQLDhhnlwQLENRINEVLAQLGldpdaalSSLSGGWLRKAALG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1105 RAILRENRILVMDEATANVDPQTDALIQATIRNkFKDCTVLtIAH------RLNT-IMDsdkvlvMDAGHVVEFGSPYEL 1177
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT-FQGSIIF-ISHdrsfirNMATrIVD------LDRGKLVSYPGNYDQ 240
|
250 260
....*....|....*....|....*....
gi 665408680 1178 LTASKAKVFHGMVMQTgkASFDHllKVAE 1206
Cdd:PRK11147 241 YLLEKEEALRVEELQN--AEFDR--KLAQ 265
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
392-552 |
1.99e-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: 45.77 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 392 LPPESGSVQVSGKYSYASQEPWLFNASVRDNILFGLPMDKQRYRTVLKRCaLERdLELLH--GDGTIVGERGA-SLSGGQ 468
Cdd:TIGR00630 416 LKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEI-RER-LGFLIdvGLDYLSLSRAAgTLSGGE 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 469 RARICLARAVYRR--ADVYLLDDP---LSAVDTH----VGRHLFDecmrgfLGKQlVILVTHQLQFLEDADLIVIMDK-- 537
Cdd:TIGR00630 494 AQRIRLATQIGSGltGVLYVLDEPsigLHQRDNRrlinTLKRLRD------LGNT-LIVVEHDEDTIRAADYVIDIGPga 566
|
170
....*....|....*....
gi 665408680 538 ----GHVSACGTYEEMLKS 552
Cdd:TIGR00630 567 gehgGEVVASGTPEEILAN 585
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
640-775 |
2.54e-04 |
|
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: 44.32 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 640 VFVVLIMLCIGTqILASGGDYFLSY----WVKNTASSSTLDIYYFTAINVGLVICALLRTLLFF-------NITMHSSTE 708
Cdd:cd18547 1 LILVIILAIIST-LLSVLGPYLLGKaidlIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYlqnrlmaRVSQRTVYD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 709 LHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPW 775
Cdd:cd18547 80 LRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPL 146
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
365-546 |
2.65e-04 |
|
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: 43.33 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 365 LRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-KYSYASQEpwlfnasvrdnilfglpmdkqryrtvlkrcal 443
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY-------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 444 erdlellhgdgtivgergASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTH-------VGRHLFDEcmrgflGKQLV 516
Cdd:cd03222 70 ------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnaarAIRRLSEE------GKKTA 125
|
170 180 190
....*....|....*....|....*....|
gi 665408680 517 ILVTHQLQFLEDADLIVIMDKGHVSACGTY 546
Cdd:cd03222 126 LVVEHDLAVLDYLSDRIHVFEGEPGVYGIA 155
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
359-542 |
3.55e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.78 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 359 NNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--------------YSYASQ---EPWLF-NASVR 420
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgMAYITEsrrDNGFFpNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 421 DNILFGLPMDKQRYRTVL--------KRCAlERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLS 492
Cdd:PRK09700 360 QNMAISRSLKDGGYKGAMglfhevdeQRTA-ENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 493 AVDT-------HVGRHLFDEcmrgflGKqLVILVTHQL-QFLEDADLIVIMDKGHVSA 542
Cdd:PRK09700 439 GIDVgakaeiyKVMRQLADD------GK-VILMVSSELpEIITVCDRIAVFCEGRLTQ 489
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
337-523 |
3.71e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 44.33 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 337 DTLVEIKALRARWGQEQHDLV-LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPE---SGSVQVSGKYSYASQEP 412
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 413 WLfNASVRDNI--LFGLPMDK---------------QRYRTVLKRCALERDLELLhgDGTIVGERGASL-------SGGQ 468
Cdd:PRK09473 90 EL-NKLRAEQIsmIFQDPMTSlnpymrvgeqlmevlMLHKGMSKAEAFEESVRML--DAVKMPEARKRMkmyphefSGGM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 665408680 469 RARICLARAVYRRADVYLLDDPLSAVDTHVGRH---LFDECMRGFlgKQLVILVTHQL 523
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQimtLLNELKREF--NTAIIMITHDL 222
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
708-841 |
4.55e-04 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 43.56 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 708 ELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPA----VMLDCIQIFLtltgIICVLCVTNPwylINTFAM 783
Cdd:cd18554 80 DIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTglmnIWLDMITIII----AICIMLVLNP---KLTFVS 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665408680 784 MLAFYYW---RDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDN 841
Cdd:cd18554 153 LVIFPFYilaVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDK 213
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
258-496 |
5.14e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 258 CVTAFYNILRRTVSKFFPSGMSQfAELLVSMRRITNFMMR----EEANVIDMSERRDEKAEEEQHLLKEVEKRSYpvgig 333
Cdd:TIGR00956 677 GFTVFFFFVYILLTEFNKGAKQK-GEILVFRRGSLKRAKKagetSASNKNDIEAGEVLGSTDLTDESDDVNDEKD----- 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 334 KEPDTLVEIKALRARWGQEQ----HDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGEL--------------PPE 395
Cdd:TIGR00956 751 MEKESGEDIFHWRNLTYEVKikkeKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVttgvitggdrlvngRPL 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 396 SGSVQVSGKYSyASQEPWLFNASVRDNILFGLPM-------DKQRYRTVLKRCALerdLELLHGDGTIVGERGASLSGGQ 468
Cdd:TIGR00956 831 DSSFQRSIGYV-QQQDLHLPTSTVRESLRFSAYLrqpksvsKSEKMEYVEEVIKL---LEMESYADAVVGVPGEGLNVEQ 906
|
250 260
....*....|....*....|....*....
gi 665408680 469 RARICLARAVYRRADVYL-LDDPLSAVDT 496
Cdd:TIGR00956 907 RKRLTIGVELVAKPKLLLfLDEPTSGLDS 935
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
234-404 |
5.28e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 44.46 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 234 RIAIFVSLLGFVLGGGELTAERAFCVTAFYNILRRTVSKFFPSGMSQFAELLVSMRRITNFMMREEAnviDMSERRDEKA 313
Cdd:COG3899 187 LALRALLLLVLLLLLLLLLLGLLLAAAAALAAAAAAAAAAAPAAPVVLVAALLLALAALLALLLLAA---RLLGLAGAAA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 314 EEEQHLLKEVEKRSYPVGIGKEPDTLV----EIKALRARWGQeqhdlvlnnvnMSLRRGQLVAVIGPVGSGKSSLIQAIL 389
Cdd:COG3899 264 LLLLGLLAAAAAGRRLLARRLIPQPLVgreaELAALLAALER-----------ARAGRGELVLVSGEAGIGKSRLVRELA 332
|
170
....*....|....*
gi 665408680 390 GELPPESGSVqVSGK 404
Cdd:COG3899 333 RRARARGGRV-LRGK 346
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
974-1170 |
5.78e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.13 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 974 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALfrlSYN----DGAILIDSLDTNDIGLHD-LRSKISIIPQE----PVLfs 1044
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKIL---SGNyqpdAGSILIDGQEMRFASTTAaLAAGVAIIYQElhlvPEM-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1045 gTMRYNLdPFEQYP------DDKLWKA-----LEdvHLKEEIS-ELPSGlqsiiseggtNFSVGQRQLVCLARAILRENR 1112
Cdd:PRK11288 95 -TVAENL-YLGQLPhkggivNRRLLNYeareqLE--HLGVDIDpDTPLK----------YLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1113 ILVMDEATANVD-PQTDALIQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVE 1170
Cdd:PRK11288 161 VIAFDEPTSSLSaREIEQLFRVIRELRAEGRVILYVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
328-499 |
6.99e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.76 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 328 YPvgigKEPDTLVEIkALRAR----WGQEQ-HDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPpesgsvqvs 402
Cdd:PRK13549 248 YP----REPHTIGEV-ILEVRnltaWDPVNpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP--------- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 403 GKYsyaSQEPWLFNASV-----RDNILFGLPM---DKQRYRTVL-----------------KRCALERDLELlhgdGTIV 457
Cdd:PRK13549 314 GRW---EGEIFIDGKPVkirnpQQAIAQGIAMvpeDRKRDGIVPvmgvgknitlaaldrftGGSRIDDAAEL----KTIL 386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 458 GE-------------RGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDthVG 499
Cdd:PRK13549 387 ESiqrlkvktaspelAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID--VG 439
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
669-851 |
8.09e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 42.96 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 669 TASSSTLdiyYFTAINVGLVICA-----LLRTLLFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFaNDLGQ 743
Cdd:cd18566 35 NESIPTL---QVLVIGVVIAILLesllrLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 744 VDEV----MPAVMLDC--IQIFLTLTGIIcvlcvtNPWYLINTFAMMLAFYYWRDFYLKTSRDV--KRLEAVARSpmYSH 815
Cdd:cd18566 111 IREFltgqALLALLDLpfVLIFLGLIWYL------GGKLVLVPLVLLGLFVLVAILLGPILRRAlkERSRADERR--QNF 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 665408680 816 FSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYY 851
Cdd:cd18566 183 LIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGF 218
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
653-808 |
8.90e-04 |
|
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: 42.68 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 653 ILASGGDYFLSYW---------VKNTASSSTLDIYYFTAINVGLVICALLRTLLFfNITMHSST-ELHNTMFQGLSRTAL 722
Cdd:cd18784 6 LAAAVGEIFIPYYtgqvidgivIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLF-TLAMARLNiRIRNLLFRSIVSQEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 723 YFFHTNPSGRILNRFANDLgqvdEVMPAVMLDCIQIFL--TLTGI-ICVLCVTNPWYL-INTFA----MMLAFYYWRDFY 794
Cdd:cd18784 85 GFFDTVKTGDITSRLTSDT----TTMSDTVSLNLNIFLrsLVKAIgVIVFMFKLSWQLsLVTLIglplIAIVSKVYGDYY 160
|
170
....*....|....
gi 665408680 795 LKTSRDVKRLEAVA 808
Cdd:cd18784 161 KKLSKAVQDSLAKA 174
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
356-551 |
1.00e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 42.23 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 356 LVLNNVNMS---------LRRGQLVAVIGPVGSGKSSLIQAILGeLPPESGSVQVSGK-------YSYASQEPWLfnaSV 419
Cdd:PRK03695 1 MQLNDVAVStrlgplsaeVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQpleawsaAELARHRAYL---SQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 420 RDNILFGLPM------------DKQRYRTVLKR-CALERDLELLHgdgtivgeRGAS-LSGGQRARICLARA---VYRRA 482
Cdd:PRK03695 77 QQTPPFAMPVfqyltlhqpdktRTEAVASALNEvAEALGLDDKLG--------RSVNqLSGGEWQRVRLAAVvlqVWPDI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408680 483 DVY----LLDDPLSAVDthVGRH-LFDECMRGFLGKQLVILVT-HQL-QFLEDADLIVIMDKGHVSACGTYEEMLK 551
Cdd:PRK03695 149 NPAgqllLLDEPMNSLD--VAQQaALDRLLSELCQQGIAVVMSsHDLnHTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
680-841 |
1.06e-03 |
|
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: 42.45 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 680 FTAINVGLVICALLRTLLFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIF 759
Cdd:cd18545 46 FLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 760 LTLTGIICVLCVTNPWYLINTFA----MMLAFYYWRDFYLKTSRDVKRleavARSPMYSHFSATLVGLPTIRAMGAQQTL 835
Cdd:cd18545 126 LTLVGIVIIMFSLNVRLALVTLAvlplLVLVVFLLRRRARKAWQRVRK----KISNLNAYLHESISGIRVIQSFAREDEN 201
|
....*.
gi 665408680 836 IGQYDN 841
Cdd:cd18545 202 EEIFDE 207
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
974-1001 |
1.07e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 42.77 E-value: 1.07e-03
10 20
....*....|....*....|....*...
gi 665408680 974 LKGLSFTIQPMEKVGIVGRTGAGKSSLI 1001
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTI 65
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
677-871 |
1.09e-03 |
|
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: 42.55 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 677 IYYFTAINVGLVICALLRTLLFfNITMHS-STELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDC 755
Cdd:cd18557 39 ALILLAIYLLQSVFTFVRYYLF-NIAGERiVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 756 IQIFLTLTGIICVLCVTNPwyliNTFAMMLAF---------YYWRdFYLKTSRDVkrLEAVARSPmySHFSATLVGLPTI 826
Cdd:cd18557 118 LRNILQVIGGLIILFILSW----KLTLVLLLVipllliaskIYGR-YIRKLSKEV--QDALAKAG--QVAEESLSNIRTV 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 665408680 827 RAMGAQQTLIGQYDNYQD------LHSSGYYTFVSTSRAFGYYLDLFCVAY 871
Cdd:cd18557 189 RSFSAEEKEIRRYSEALDrsyrlaRKKALANALFQGITSLLIYLSLLLVLW 239
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
463-554 |
1.13e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 463 SLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLfdecmRGFLGK--QLVILVTHQLQFLED--ADLIVIMDKG 538
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL-----ETYLLKwpKTFIVVSHAREFLNTvvTDILHLHGQK 418
|
90 100
....*....|....*....|...
gi 665408680 539 HVSACGTY-------EEMLKSGQ 554
Cdd:PLN03073 419 LVTYKGDYdtfertrEEQLKNQQ 441
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
988-1006 |
1.24e-03 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 40.69 E-value: 1.24e-03
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
358-545 |
1.41e-03 |
|
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: 41.83 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAIL-----------GELPPESGSV---QVSGKYSYASQEPwlFNASVRDN- 422
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlkKEQPGNHDRIeglEHIDKVIVIDQSP--IGRTPRSNp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 423 -----------ILFGLPMDKQRY-RTVL------KRCA-------------------LERDLELLH--GDGTI-VGERGA 462
Cdd:cd03271 89 atytgvfdeirELFCEVCKGKRYnRETLevrykgKSIAdvldmtveealeffenipkIARKLQTLCdvGLGYIkLGQPAT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 463 SLSGGQRARICLARAVYRRAD---VYLLDDPLSAVDTHVGRHLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIM---- 535
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLgpeg 248
|
250
....*....|..
gi 665408680 536 -DK-GHVSACGT 545
Cdd:cd03271 249 gDGgGQVVASGT 260
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
974-1170 |
1.54e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 974 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL----SYnDGAILidsLDTNDIGLHDLRSK----ISIIPQE----PV 1041
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgSY-EGEIL---FDGEVCRFKDIRDSealgIVIIHQElaliPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1042 L------FSGTMRYN---LDPFEQYPDDKlwKALEDVHLKEEiselPsglQSIISEGGtnfsVGQRQLVCLARAILRENR 1112
Cdd:NF040905 93 LsiaeniFLGNERAKrgvIDWNETNRRAR--ELLAKVGLDES----P---DTLVTDIG----VGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1113 ILVMDEATANV-DPQTDALIQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVE 1170
Cdd:NF040905 160 LLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
669-774 |
1.75e-03 |
|
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: 41.70 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 669 TASSSTLDIYYFTAINVGLVI----CALLRTLLFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQV 744
Cdd:cd18576 27 LGGGDTASLNQIALLLLGLFLlqavFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQI 106
|
90 100 110
....*....|....*....|....*....|
gi 665408680 745 DEVMPAVMLDCIQIFLTLTGIICVLCVTNP 774
Cdd:cd18576 107 QDTLTTTLAEFLRQILTLIGGVVLLFFISW 136
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
358-389 |
2.29e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 2.29e-03
10 20 30
....*....|....*....|....*....|..
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAIL 389
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINDTL 655
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
362-402 |
2.38e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 2.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 665408680 362 NMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVS 402
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ 63
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
983-1156 |
2.61e-03 |
|
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: 39.66 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 983 PMEKVGIVGRTGAGKSSLINALFR-LSYNDGAILIDSLDTNDIGLHDLRSKIsiipqepvlfsgtmrynldpfeqypddk 1061
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLI---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1062 lwkaledvhlkeeiselpsglqsIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIR----- 1136
Cdd:smart00382 53 -----------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlll 109
|
170 180
....*....|....*....|..
gi 665408680 1137 --NKFKDCTVLTIAHRLNTIMD 1156
Cdd:smart00382 110 llKSEKNLTVILTTNDEKDLGP 131
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
980-1164 |
2.78e-03 |
|
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: 41.69 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 980 TIQPMEKVGIVGRTGAGKSSLINALfrlsynDGAILIDSldtndiGLHDLRSKISIIPQEPV-LFSGTMRYNLdpFEQYP 1058
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKIL------AGVLKPDE------GEVDEDLKISYKPQYISpDYDGTVEEFL--RSANT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1059 DDklwkaLEDVHLKEEISElPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDP----QTDALIQAT 1134
Cdd:COG1245 428 DD-----FGSSYYKTEIIK-PLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRRF 501
|
170 180 190
....*....|....*....|....*....|.
gi 665408680 1135 IRNkfKDCTVLTIAHRLNTI-MDSDKVLVMD 1164
Cdd:COG1245 502 AEN--RGKTAMVVDHDIYLIdYISDRLMVFE 530
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
339-552 |
2.88e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 41.27 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 339 LVEIKALRARWGQEQHDL-VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGeLPPESGSVQVSgKYSYASQEPWLFNA 417
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMG-LIDYPGRVMAE-KLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 418 SVRDNI-------LFGLPMdkqryrTVLKRC---------AL------------ERDLELLhgdgTIVG-ERGAS----- 463
Cdd:PRK11022 81 KERRNLvgaevamIFQDPM------TSLNPCytvgfqimeAIkvhqggnkktrrQRAIDLL----NQVGiPDPASrldvy 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 464 ---LSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFD--------ECMRgflgkqlVILVTHQLQFL-EDADL 531
Cdd:PRK11022 151 phqLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIElllelqqkENMA-------LVLITHDLALVaEAAHK 223
|
250 260
....*....|....*....|.
gi 665408680 532 IVIMDKGHVSACGTYEEMLKS 552
Cdd:PRK11022 224 IIVMYAGQVVETGKAHDIFRA 244
|
|
| YlqF_related_GTPase |
cd01849 |
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ... |
986-1031 |
3.12e-03 |
|
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, and archaea. They all exhibit a circular permutation of the GTPase signature motifs so that the order of the conserved G box motifs is G4-G5-G1-G2-G3, with G4 and G5 being permuted from the C-terminal region of proteins in the Ras superfamily to the N-terminus of YlqF-related GTPases.
Pssm-ID: 206746 [Multi-domain] Cd Length: 146 Bit Score: 39.29 E-value: 3.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 665408680 986 KVGIVGRTGAGKSSLINAL---FRLSYNDGAIL----IDSLDTNDIGLHDLRS 1031
Cdd:cd01849 93 RVGVVGLPNVGKSSFINALlnkFKLKVGSIPGTtklqQDVKLDKEIYLYDTPG 145
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
41-253 |
3.19e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 40.96 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 41 IYAVLLIACILASVLLT--HPYMMG--MMHLAMKMRVAVssaiYRKALRLSRTSLGGTTTGQVVNLLSNDLNRfdrclIH 116
Cdd:cd18563 44 LLVLGLAGAYVLSALLGilRGRLLArlGERITADLRRDL----YEHLQRLSLSFFDKRQTGSLMSRVTSDTDR-----LQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 117 fHFLWLGPLELLIasyflyeQIGMasFYGISILVLYL------------PLQTYLSRVTSKlRLQTA-LRTDQRVRMMN- 182
Cdd:cd18563 115 -DFLSDGLPDFLT-------NILM--IIGIGVVLFSLnwklallvlipvPLVVWGSYFFWK-KIRRLfHRQWRRWSRLNs 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 183 ---EIISGIQVIKMYTWERP----FGKLIGQMRRSEMSSIRqMNLLRGILLSFEITLGriAIFVSLLG--FVLGG----G 249
Cdd:cd18563 184 vlnDTLPGIRVVKAFGQEKReikrFDEANQELLDANIRAEK-LWATFFPLLTFLTSLG--TLIVWYFGgrQVLSGtmtlG 260
|
....
gi 665408680 250 ELTA 253
Cdd:cd18563 261 TLVA 264
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
358-556 |
3.30e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 358 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLfNASVR--DNILFG-LPMDKQRY 434
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGL-SGQLTgiENIEFKmLCMGFKRK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 435 RTVLKRCALERDLELlhgdGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQ 514
Cdd:PRK13546 119 EIKAMTPKIIEFSEL----GEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNK 194
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 665408680 515 LVILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEMLKSGQDF 556
Cdd:PRK13546 195 TIFFVSHNLgQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEAF 237
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
340-403 |
3.37e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.65 E-value: 3.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665408680 340 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG 403
Cdd:NF033858 2 ARLEGVSHRYGKTV---ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG 62
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
973-1174 |
3.76e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.76 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLS--YNDGAILIDSL--------------DTNDIglHDlrskisi 1035
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgRKTggYIEGDIRISGFpkkqetfarisgycEQNDI--HS------- 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1036 iPQ----EPVLFSGTMRYnldPFEQYPDDKL------WKALEDVHLKEEISELPsglqsiiseGGTNFSVGQRQLVCLAR 1105
Cdd:PLN03140 966 -PQvtvrESLIYSAFLRL---PKEVSKEEKMmfvdevMELVELDNLKDAIVGLP---------GVTGLSTEQRKRLTIAV 1032
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408680 1106 AILRENRILVMDEATANVDPQTDALIQATIRNKFKD--CTVLTIAHRLNTIMDS-DKVLVMDAGHVVEFGSP 1174
Cdd:PLN03140 1033 ELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTgrTVVCTIHQPSIDIFEAfDELLLMKRGGQVIYSGP 1104
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
352-395 |
3.99e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 40.54 E-value: 3.99e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 665408680 352 EQHDLVLNNVNMSLRRGQ-LVAVIGPVGSGKSSLIQAILGELPPE 395
Cdd:COG3267 26 PSHREALARLEYALAQGGgFVVLTGEVGTGKTTLLRRLLERLPDD 70
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
986-1006 |
4.10e-03 |
|
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 39.40 E-value: 4.10e-03
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
363-397 |
5.90e-03 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 39.41 E-value: 5.90e-03
10 20 30
....*....|....*....|....*....|....*
gi 665408680 363 MSlRRGQLVAVIGPVGSGKSSLIQAILGELPPESG 397
Cdd:COG3709 1 MS-GPGRLIYVVGPSGAGKDSLLAAARARLAADPR 34
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
372-399 |
6.59e-03 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 38.59 E-value: 6.59e-03
10 20
....*....|....*....|....*...
gi 665408680 372 AVIGPVGSGKSSLIQAILGELPPESGSV 399
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEVSDV 28
|
|
| Dynamin_N |
pfam00350 |
Dynamin family; |
371-397 |
7.13e-03 |
|
Dynamin family;
Pssm-ID: 459775 [Multi-domain] Cd Length: 168 Bit Score: 38.75 E-value: 7.13e-03
10 20
....*....|....*....|....*....
gi 665408680 371 VAVIGPVGSGKSSLIQAILGE--LPPESG 397
Cdd:pfam00350 1 IAVVGDQSSGKSSVLNALLGRdiLPRGPG 29
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
988-1005 |
7.31e-03 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 38.59 E-value: 7.31e-03
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
973-1172 |
7.42e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 40.63 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 973 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYND--GAILIDsldtNDIGLHDLRSKISIIPQEPVLFSG-TMR 1048
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNftGTILAN----NRKPTKQILKRTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1049 YNLD-------PFEQYPDDKLWKAlEDVhlkeeISELpsGL----QSIIsegGTNF----SVGQRQLVCLARAILRENRI 1113
Cdd:PLN03211 159 ETLVfcsllrlPKSLTKQEKILVA-ESV-----ISEL--GLtkceNTII---GNSFirgiSGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 1114 LVMDEATANVDpQTDA--LIQ--ATIRNKFKdcTVLTIAH----RLNTIMDSdkVLVMDAGHVVEFG 1172
Cdd:PLN03211 228 LILDEPTSGLD-ATAAyrLVLtlGSLAQKGK--TIVTSMHqpssRVYQMFDS--VLVLSEGRCLFFG 289
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
986-1004 |
9.05e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 40.03 E-value: 9.05e-03
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
942-1164 |
9.17e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.18 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 942 EKQPPKSWPKEGKLV-----TKDL---SLRYEPdtnspcvlkGlsfTIQPMEKVGIVGRTGAGKSSLINALfrlsynDGA 1013
Cdd:PRK13409 327 EERPPRDESERETLVeypdlTKKLgdfSLEVEG---------G---EIYEGEVIGIVGPNGIGKTTFAKLL------AGV 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 1014 ILIDSldtndiGLHDLRSKISIIPQE-PVLFSGTMRYNLdpfEQYPDDklwkaLEDVHLKEEISElPSGLQSIISEGGTN 1092
Cdd:PRK13409 389 LKPDE------GEVDPELKISYKPQYiKPDYDGTVEDLL---RSITDD-----LGSSYYKSEIIK-PLQLERLLDKNVKD 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408680 1093 FSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN--KFKDCTVLTIAHRLNTI-MDSDKVLVMD 1164
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRiaEEREATALVVDHDIYMIdYISDRLMVFE 528
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
987-1006 |
9.22e-03 |
|
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.
Pssm-ID: 206665 [Multi-domain] Cd Length: 170 Bit Score: 38.26 E-value: 9.22e-03
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
3-268 |
9.40e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 39.44 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 3 GITIAALELGTRA--TVPLLLAGLISEFSEHGNGHSYNAQIyAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIY 80
Cdd:cd18778 2 ILTLLCALLSTLLglVPPWLIRELVDLVTIGSKSLGLLLGL-ALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 81 RKALRLSRTSLGGTTTGQVVNLLSNDLNRFDRCLIHfhflwlgPLELLIASYFlyeqigmaSFYGISILVLY-------- 152
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIAD-------GIPQGITNVL--------TLVGVAIILFSinpklall 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408680 153 ----LPLQTYLSRVTSKlRLQTALRTDQRVR-----MMNEIISGIQVIKMYTWERP----FGKLIGQMRRSEMSSIRQMN 219
Cdd:cd18778 146 tlipIPFLALGAWLYSK-KVRPRYRKVREALgelnaLLQDNLSGIREIQAFGREEEeakrFEALSRRYRKAQLRAMKLWA 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 665408680 220 LLRGiLLSFEITLGriaiFVSLLGF----VLGG----GELTAERAFcVTAFYNILRR 268
Cdd:cd18778 225 IFHP-LMEFLTSLG----TVLVLGFggrlVLAGeltiGDLVAFLLY-LGLFYEPITS 275
|
|
| |
