|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1-1333 |
0e+00 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 1817.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 1 MECVSVEGLDSSFLEGQTFGDILCLPWT-IIKGIReRKNRNKMKIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGE 79
Cdd:TIGR00956 32 YKNLSAYGVAADSDYQPTFPNALLKILTrGFRKLK-KFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 80 TSQFAGGVTtGHISYDGIPQKEMMQHYKPDVIYNGEQDVHFPHLTVKQTLDFAISCKMPAKRVNNVTKEEYITANREFYA 159
Cdd:TIGR00956 111 TDGFHIGVE-GVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKTPQNRPDGVSREEYAKHIADVYM 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 160 KIFGLTHTFDTKVGNDFISGVSGGERKRVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQ 239
Cdd:TIGR00956 190 ATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 240 ASENIYETFDKVIVLYAGRQIFCGKTTEAKDYFENMGYLCPPRQSTAEYLTAITDPNGlHEIKPGFEYQVPHTTDEFEKY 319
Cdd:TIGR00956 270 CSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPDRQTTADFLTSLTSPAE-RQIKPGYEKKVPRTPQEFETY 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 320 WLDSPEYARLKGEIQKYKHEVNTEWTKKTYNESMAQEKSKGTRKKSYYTVSYWEQIRLCTIRGFLRIYGDKSYTVINTCA 399
Cdd:TIGR00956 349 WRNSPEYAQLMKEIDEYLDRCSESDTKEAYRESHVAKQSKRTRPSSPYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 400 AIAQAFITGSLFYQAPSSTLGAFSRSGVLFFSLLYYSLMGLANIS--FEHRPILQKHKVYSLYHPSAEALASTISSFPFR 477
Cdd:TIGR00956 429 NIIMALILSSVFYNLPKNTSDFYSRGGALFFAILFNAFSSLLEIAsmYEARPIVEKHRKYALYHPSADAIASIISEIPFK 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 478 MIGLTFFIIILYFLAGLHRSAGAFFTMYLLLTMCSEAITSLFQMVSSLCDTLSQANSIAGVVMLSIAMYSTYMIQLPSMH 557
Cdd:TIGR00956 509 IIESVVFNIILYFMVNFRRTAGRFFFYLLILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSML 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 558 PWFKWISYILPIRYAFESMLNAEFHGRHMDCGgTLVPSGPGFENILPENQVCAFVGSRPGQSWVLGDDYLRAQYQYEYKN 637
Cdd:TIGR00956 589 GWSKWIYYVNPLAYAFESLMVNEFHGRRFECS-QYVPSGGGYDNLGVTNKVCTVVGAEPGQDYVDGDDYLKLSFQYYNSH 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 638 TWRNFGIMWCFLIGYIVLRAVFTEYKSPVKSGGDALVVKKGT----KNAIQRSWSSKNDEENLNASIATQDMKEIASSND 713
Cdd:TIGR00956 668 KWRNFGIIIGFTVFFFFVYILLTEFNKGAKQKGEILVFRRGSlkraKKAGETSASNKNDIEAGEVLGSTDLTDESDDVND 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 714 DStsaDFEGLESTGVFIWKNVSFTIPHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQR-NVGTIT-GDML 791
Cdd:TIGR00956 748 EK---DMEKESGEDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERvTTGVITgGDRL 824
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 792 VDGLPMDASFKRRTGYVQQQDLHVAELTVKESLQFSARMRRPQSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGLNV 871
Cdd:TIGR00956 825 VNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLNV 904
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 872 EQRKKLSIGVELVGKPDLLLFLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSATLFEQFDRLLLLGKGGQTIY 951
Cdd:TIGR00956 905 EQRKRLTIGVELVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGGQTVY 984
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 952 FGEIGKNSSSVIKYFEKNGARKCQQNENPAEYILEAIGAGATASVQQNWPDIWQKSHEYANINEKINDMIKDLSSTTLHK 1031
Cdd:TIGR00956 985 FGDLGENSHTIINYFEKHGAPKCPEDANPAEWMLEVIGAAPGAHANQDYHEVWRNSSEYQAVKNELDRLEAELSKAEDDN 1064
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 1032 TATRASKYATSYSYQFHHVLKRSSLTFWRNLNYIMAKMMLLMISGLFIGFTFFHVGVNAIGLQNSLFACFMAIVISAPAT 1111
Cdd:TIGR00956 1065 DPDALSKYAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVGTSLQGLQNQMFAVFMATVLFNPLI 1144
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 1112 NQIQERATVAKELYEVRESKSNMFHWSLLLITHYLNELPYHLLFSTIFFVSLYFPLGVFTEASRSS------VFYLNYAI 1185
Cdd:TIGR00956 1145 QQYLPPFVAQRDLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFYWNASKTGqvhergVLFWLLST 1224
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 1186 LFQLYYIGLALMILYMSPNLQSANVIVGFILSFLLSFCGAVQPASLMPGFWTFMWKLSPYTYFLQNLVGLLMHDKPVRCS 1265
Cdd:TIGR00956 1225 MFFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLADVPVTCK 1304
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767243141 1266 KKELSLFNPPVGQTCGEFTKPFFEFGTGYIANPDATADCAYCQYKVGDEYLARINASFSYLWRNFG-FI 1333
Cdd:TIGR00956 1305 VKELLTFNPPSGQTCGEYMKPYLENAGGYLLNPNATDSCSFCQYSYTNDFLEPISSKYSGRWRNFGiFI 1373
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
45-1253 |
2.81e-132 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 443.13 E-value: 2.81e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGgvTTGHISYDGIPQKEMMQhyKPDVIYNGEQDVHFPHLT 124
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLK--VSGEITYNGYRLNEFVP--RKTSAYISQNDVHVGVMT 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 125 VKQTLDFAISCK------------------------------MPAKRVNNVtKEEYITanrEFYAKIFGLTHTFDTKVGN 174
Cdd:PLN03140 256 VKETLDFSARCQgvgtrydllselarrekdagifpeaevdlfMKATAMEGV-KSSLIT---DYTLKILGLDICKDTIVGD 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 175 DFISGVSGGERKRVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQASENIYETFDKVIVL 254
Cdd:PLN03140 332 EMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFDLFDDIILL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 255 YAGRQIFCGKTTEAKDYFENMGYLCPPRQSTAEYLTAITdpnglheikpgfeyqvphTTDEFEKYWLDS---------PE 325
Cdd:PLN03140 412 SEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVT------------------SKKDQEQYWADRnkpyryisvSE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 326 YArlkgeiQKYKH-EVNTewtkKTYNE-SMAQEKSKGTRKK---SYYTVSYWEQIRLCTIRGFLRIYGDKSYTVINTCAA 400
Cdd:PLN03140 474 FA------ERFKSfHVGM----QLENElSVPFDKSQSHKAAlvfSKYSVPKMELLKACWDKEWLLMKRNAFVYVFKTVQI 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 401 IAQAFITGSLFYQAPSSTLGAFSRS---GVLFFSLLYYSLMGLANISF--EHRPILQKHKVYsLYHPS-AEALASTISSF 474
Cdd:PLN03140 544 IIVAAIASTVFLRTEMHTRNEEDGAlyiGALLFSMIINMFNGFAELALmiQRLPVFYKQRDL-LFHPPwTFTLPTFLLGI 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 475 PFRMIGLTFFIIILYFLAGLHRSAGAFFTMYLLLTMCSEAITSLFQMVSSLCDTLSQANSIAGVVMLSIAMYSTYMIQLP 554
Cdd:PLN03140 623 PISIIESVVWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKG 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 555 SMHPWFKWISYILPIRYAFESM-LNAEFHGRHMdcggtlvpsgpgfenilpeNQVCAFVGSRpgqswvLGDDYLRAQYQY 633
Cdd:PLN03140 703 EIPNWWEWAYWVSPLSYGFNALaVNEMFAPRWM-------------------NKMASDNSTR------LGTAVLNIFDVF 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 634 EYKN-TWRNFGIMWCFLIGYIVLRAVFTEYKSPVksGGDALVVKKGTKNAIQRSWSSKNDEENLNASIATQDMKEIASSN 712
Cdd:PLN03140 758 TDKNwYWIGVGALLGFTILFNVLFTLALTYLNPL--GKKQAIISEETAEEMEGEEDSIPRSLSSADGNNTREVAIQRMSN 835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 713 D--DSTSADFEGLESTGV---------FIWKNVSFT-------IPHSSGQR-------KLLDSVSGYCVPGTLTALIGES 767
Cdd:PLN03140 836 PegLSKNRDSSLEAANGVapkrgmvlpFTPLAMSFDdvnyfvdMPAEMKEQgvtedrlQLLREVTGAFRPGVLTALMGVS 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 768 GAGKTTLLNTLAQRNVGT-ITGDMLVDGLP-MDASFKRRTGYVQQQDLHVAELTVKESLQFSARMRRPQSIPDAEKMEYV 845
Cdd:PLN03140 916 GAGKTTLMDVLAGRKTGGyIEGDIRISGFPkKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFV 995
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 846 EKIISILEMQEFSEALVGEIGY-GLNVEQRKKLSIGVELVGKPDLLlFLDEPTSGLDSQSAWAVVKMLKRLALAGQSILC 924
Cdd:PLN03140 996 DEVMELVELDNLKDAIVGLPGVtGLSTEQRKRLTIAVELVANPSII-FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVC 1074
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 925 TIHQPSATLFEQFDRLLLLGKGGQTIYFGEIGKNSSSVIKYFEK-NGARKCQQNENPAEYILEAIGAGATASVQQNWPDI 1003
Cdd:PLN03140 1075 TIHQPSIDIFEAFDELLLMKRGGQVIYSGPLGRNSHKIIEYFEAiPGVPKIKEKYNPATWMLEVSSLAAEVKLGIDFAEH 1154
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 1004 WQKSHEYaninEKINDMIKDLSstTLHKTATR---ASKYATSYSYQFHHVLKRSSLTFWRNLNYIMAKMMLLMISGLFIG 1080
Cdd:PLN03140 1155 YKSSSLY----QRNKALVKELS--TPPPGASDlyfATQYSQSTWGQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVG 1228
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 1081 FTFFHVGV---NAIGLQNSLFACFMAIV-ISAPATNQIQERATVAKELYeVRESKSNMFHWSLLLITHYLNELPYhLLFS 1156
Cdd:PLN03140 1229 TIFWKVGTkrsNANDLTMVIGAMYAAVLfVGINNCSTVQPMVAVERTVF-YRERAAGMYSALPYAIAQVVCEIPY-VLIQ 1306
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 1157 TIFFVSLYFPLGVFtEASRSSVFYLNYAILFQ-LYYIGLALMILYMSPNLQSANVIVGFILSFLLSFCGAVQPASLMPGF 1235
Cdd:PLN03140 1307 TTYYTLIVYAMVAF-EWTAAKFFWFYFISFFSfLYFTYYGMMTVSLTPNQQVAAIFAAAFYGLFNLFSGFFIPRPKIPKW 1385
|
1290
....*....|....*...
gi 767243141 1236 WTFMWKLSPYTYFLQNLV 1253
Cdd:PLN03140 1386 WVWYYWICPVAWTVYGLI 1403
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
727-953 |
6.20e-98 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 311.10 E-value: 6.20e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 727 GVFIWKNVSFTIPHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQR-NVGTITGDMLVDGLPMDASFKRRT 805
Cdd:cd03232 2 SVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRkTAGVITGEILINGRPLDKNFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 806 GYVQQQDLHVAELTVKESLQFSARMRrpqsipdaekmeyvekiisilemqefsealvgeigyGLNVEQRKKLSIGVELVG 885
Cdd:cd03232 82 GYVEQQDVHSPNLTVREALRFSALLR------------------------------------GLSVEQRKRLTIGVELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767243141 886 KPDLLlFLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSATLFEQFDRLLLLGKGGQTIYFG 953
Cdd:cd03232 126 KPSIL-FLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRGGKTVYFG 192
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
34-263 |
3.74e-83 |
|
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: 270.29 E-value: 3.74e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 34 RERKNRNKMKIiLKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGgvTTGHISYDGIPQKEMMQHYKPDVIYN 113
Cdd:cd03233 12 TTGKGRSKIPI-LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS--VEGDIHYNGIPYKEFAEKYPGEIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 114 GEQDVHFPHLTVKQTLDFAISCKmpakrvnnvtkeeyitanrefyakifglthtfdtkvGNDFISGVSGGERKRVSIAEA 193
Cdd:cd03233 89 SEEDVHFPTLTVRETLDFALRCK------------------------------------GNEFVRGISGGERKRVSIAEA 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 194 LAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQASENIYETFDKVIVLYAGRQIFCG 263
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
742-1247 |
3.16e-78 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 271.54 E-value: 3.16e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 742 SGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRNVG--TITGDMLVDGLPMDAS-FKRRTGYVQQQDLHVAEL 818
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvKGSGSVLLNGMPIDAKeMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 819 TVKESLQFSARMRRPQSIPDAEKMEYVEKIISILEMQEFSEALVGEIGY--GLNVEQRKKLSIGVELVGKPdLLLFLDEP 896
Cdd:TIGR00955 115 TVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDP-PLLFCDEP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 897 TSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSATLFEQFDRLLLLGKgGQTIYFGeigkNSSSVIKYFEKNGARkCQQ 976
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAE-GRVAYLG----SPDQAVPFFSDLGHP-CPE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 977 NENPAEYILE--AIGAGATASVQQNWPDIW---QKSHEYANINEKINDMIKDLSSTTLHKTATRASKYATSYSYQFHHVL 1051
Cdd:TIGR00955 268 NYNPADFYVQvlAVIPGSENESRERIEKICdsfAVSDIGRDMLVNTNLWSGKAGGLVKDSENMEGIGYNASWWTQFYALL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 1052 KRSSLTFWRNLNYIMAKMMLLMISGLFIGFTFFHVGVNAIGLQN---SLFAC--FMAIVISAPATNQI-QERATVAkely 1125
Cdd:TIGR00955 348 KRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNingALFLFltNMTFQNVFPVINVFtAELPVFL---- 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 1126 evRESKSNMFHWSLLLITHYLNELPYHLLFSTIFFVSLYFPLGVFTEASRSSVFYLnYAILFQLYYIGLALMILYMSPNL 1205
Cdd:TIGR00955 424 --RETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLF-LVTLVANVATSFGYLISCAFSST 500
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 767243141 1206 QSA-NVIVGFILSFLLsFCGAVQPASLMPGFWTFMWKLSPYTY 1247
Cdd:TIGR00955 501 SMAlTVGPPFVIPFLL-FGGFFINSDSIPVYFKWLSYLSWFRY 542
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
731-953 |
1.25e-68 |
|
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: 228.97 E-value: 1.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 731 WKNVSFTIPH--SSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLA-QRNVGTITGDMLVDGLPMDA-SFKRRTG 806
Cdd:cd03213 6 FRNLTVTVKSspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLGVSGEVLINGRPLDKrSFRKIIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 807 YVQQQDLHVAELTVKESLQFSARMRrpqsipdaekmeyvekiisilemqefsealvgeigyGLNVEQRKKLSIGVELVGK 886
Cdd:cd03213 86 YVPQDDILHPTLTVRETLMFAAKLR------------------------------------GLSGGERKRVSIALELVSN 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767243141 887 PdLLLFLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSATLFEQFDRLLLLGKgGQTIYFG 953
Cdd:cd03213 130 P-SLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQ-GRVIYFG 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
38-581 |
1.09e-62 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 226.08 E-value: 1.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 38 NRNKMKIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSqfAGGVTTGHISYDGIP-QKEMMQhykpdVI--YNG 114
Cdd:TIGR00955 33 RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSP--KGVKGSGSVLLNGMPiDAKEMR-----AIsaYVQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 115 EQDVHFPHLTVKQTLDFAISCKMPakrvNNVTKEEYITANREFYAKIfGLTHTFDTKVGN-DFISGVSGGERKRVSIAEA 193
Cdd:TIGR00955 106 QDDLFIPTLTVREHLMFQAHLRMP----RRVTKKEKRERVDEVLQAL-GLRKCANTRIGVpGRVKGLSGGERKRLAFASE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 194 LAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLlGTTALVTVYQASENIYETFDKVIVLYAGRQIFCGKTTEAKDYFE 273
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 274 NMGYLCPPRQSTAEYL--TAITDPNglHEIKPgfeyqvphtTDEFEKYWLdspeyarlkgeiQKYKHEVNTEWTKKTYNE 351
Cdd:TIGR00955 260 DLGHPCPENYNPADFYvqVLAVIPG--SENES---------RERIEKICD------------SFAVSDIGRDMLVNTNLW 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 352 S-MAQEKSKGTR--KKSYYTVSYWEQIRLCTIRGFLRIYGDKSYTVINTCAAIAQAFITGSLFYQAPSSTLGAFSRSGVL 428
Cdd:TIGR00955 317 SgKAGGLVKDSEnmEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGAL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 429 FFSLL---YYSLMGLANISFEHRPILQKHKVYSLYHPSAEALASTISSFPFRMIGLTFFIIILYFLAGLHRSAGAFFTMY 505
Cdd:TIGR00955 397 FLFLTnmtFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFL 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767243141 506 LLLTMCSEAITSLFQMVSSLCDTLSQANSIAGVVMLSIAMYSTYMIQLPSMHPWFKWISYILPIRYAFESMLNAEF 581
Cdd:TIGR00955 477 FLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQW 552
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
731-953 |
1.35e-52 |
|
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: 184.40 E-value: 1.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 731 WKNVSFTIPHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQR--NVGTITGDMLVDGLPMD-ASFKRRTGY 807
Cdd:cd03234 6 WWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRveGGGTTSGQILFNGQPRKpDQFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 808 VQQQDLHVAELTVKESLQFSARMRRPQSIPDAEKmeyvEKIISILEMQEFSEALVG-EIGYGLNVEQRKKLSIGVELVGK 886
Cdd:cd03234 86 VRQDDILLPGLTVRETLTYTAILRLPRKSSDAIR----KKRVEDVLLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767243141 887 PDLLlFLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSATLFEQFDRLLLLGKGGqTIYFG 953
Cdd:cd03234 162 PKVL-ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGE-IVYSG 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
43-581 |
1.96e-46 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 178.53 E-value: 1.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAG--ETSQFAGGVTTGhisyDGIPQKEMMQHykpdVIYNGEQDVHF 120
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILAN----NRKPTKQILKR----TGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 121 PHLTVKQTLDFAISCKMPakrvNNVTKEEYITANREFYAKIfGLTHTFDTKVGNDFISGVSGGERKRVSIAEALAAKGSI 200
Cdd:PLN03211 153 PHLTVRETLVFCSLLRLP----KSLTKQEKILVAESVISEL-GLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 201 YCWDNATRGLDSSTALEFARAIRTMTNlLGTTALVTVYQASENIYETFDKVIVLYAGRQIFCGKTTEAKDYFENMGYLCP 280
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPS 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 281 PRQSTAEYLTAITdpNGLHEIKPGFEYQVPHTTDEFEKYW--LDSPeyarlkgeiqKYKHEVNTEWTKKTYNESMAQEKS 358
Cdd:PLN03211 307 FPMNPADFLLDLA--NGVCQTDGVSEREKPNVKQSLVASYntLLAP----------KVKAAIEMSHFPQANARFVGSAST 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 359 KGTRKKSYYTVSYW-EQIRLCTIRGfLRIYGDKSYTVINTCAAIAQAFITGSLFYQapSSTLGAFSRSGVLFFSLLYYSL 437
Cdd:PLN03211 375 KEHRSSDRISISTWfNQFSILLQRS-LKERKHESFNTLRVFQVIAAALLAGLMWWH--SDFRDVQDRLGLLFFISIFWGV 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 438 MGLANISF---EHRPILQKHKVYSLYHPSAEALASTISSFPFRMIGLTFFIIILYFLAGLHRSAGAFFTMYLLLTMCSEA 514
Cdd:PLN03211 452 FPSFNSVFvfpQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLV 531
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767243141 515 ITSLFQMVSSLCDTLSQANSIAGVVMLSIAMYSTYMI-QLPSMHPWFKWISYILpirYAFESMLNAEF 581
Cdd:PLN03211 532 SQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYVhKLPSCMAWIKYISTTF---YSYRLLINVQY 596
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
378-579 |
1.06e-44 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 160.90 E-value: 1.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 378 CTIRGFLRIYGDKSYTVINTCAAIAQAFITGSLFYQAPSSTlGAFSRSGVLFFSLL---YYSLMGLANISFEHRPILQKH 454
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQ-GGLNRPGLLFFSILfnaFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 455 KVYSLYHPSAEALASTISSFPFRMIGLTFFIIILYFLAGLHRSAGAFFTMYLLLTMCSEAITSLFQMVSSLCDTLSQANS 534
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767243141 535 IAGVVMLSIAMYSTYMIQLPSMHPWFKWISYILPIRYAFESMLNA 579
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
744-1221 |
1.44e-43 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 169.68 E-value: 1.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 744 QRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRNVGT-ITGDMLVDGLPMDASFKRRTGYVQQQDLHVAELTVKE 822
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 823 SLQFSARMRRPQSIPDAEKMEYVEKIISILEMQEFSEALVGE-IGYGLNVEQRKKLSIGVELVGKPDLLLfLDEPTSGLD 901
Cdd:PLN03211 160 TLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNsFIRGISGGERKRVSIAHEMLINPSLLI-LDEPTSGLD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 902 SQSAWAVVKMLKRLALAGQSILCTIHQPSATLFEQFDRLLLLGKgGQTIYFGEigknSSSVIKYFEKNGARKcQQNENPA 981
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSE-GRCLFFGK----GSDAMAYFESVGFSP-SFPMNPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 982 EYILE-AIGAGATASV-QQNWPDIwqKSHEYANINEKINDMIKDLSSTTLHKTATraSKYATSYSYQFHHVLKRSSLTFW 1059
Cdd:PLN03211 313 DFLLDlANGVCQTDGVsEREKPNV--KQSLVASYNTLLAPKVKAAIEMSHFPQAN--ARFVGSASTKEHRSSDRISISTW 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 1060 RNLNYIMAKMML---------------LMISGLFIGFTFFHVGVNAI----GLqnsLFacFMAIVISA-PATNQI----Q 1115
Cdd:PLN03211 389 FNQFSILLQRSLkerkhesfntlrvfqVIAAALLAGLMWWHSDFRDVqdrlGL---LF--FISIFWGVfPSFNSVfvfpQ 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 1116 ERATVakelyeVRESKSNMFHWSLLLITHYLNELPYHLLFSTIFFVSLYFPLGVFTEAsrsSVFYLNYAILfqLYYI--- 1192
Cdd:PLN03211 464 ERAIF------VKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPEL---GAFLLTLLVL--LGYVlvs 532
|
490 500 510
....*....|....*....|....*....|..
gi 767243141 1193 ---GLALMILYMSPNlQSANVIVGFILSFLLS 1221
Cdd:PLN03211 533 qglGLALGAAIMDAK-KASTIVTVTMLAFVLT 563
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
43-263 |
3.33e-43 |
|
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: 156.17 E-value: 3.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSqfaGGVTTGHISYDGIPQKemMQHYKPDVIYNGEQDVHFPH 122
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRT---GLGVSGEVLINGRPLD--KRSFRKIIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 123 LTVKQTLDFAISCKmpakrvnnvtkeeyitanrefyakifglthtfdtkvgndfisGVSGGERKRVSIAEALAAKGSIYC 202
Cdd:cd03213 97 LTVRETLMFAAKLR------------------------------------------GLSGGERKRVSIALELVSNPSLLF 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767243141 203 WDNATRGLDSSTALEFARAIRTMTNlLGTTALVTVYQASENIYETFDKVIVLYAGRQIFCG 263
Cdd:cd03213 135 LDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PDR_CDR |
pfam06422 |
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters ... |
593-684 |
1.59e-41 |
|
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters comprising extracellular loop 3, transmembrane segment 6 and linker region.
Pssm-ID: 461906 [Multi-domain] Cd Length: 92 Bit Score: 147.22 E-value: 1.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 593 VPSGPGFENILPENQVCAFVGSRPGQSWVLGDDYLRAQYQYEYKNTWRNFGIMWCFLIGYIVLRAVFTEYKSPVKSGGDA 672
Cdd:pfam06422 1 VPSGPGYENVSGANQVCAVVGAVPGQTFVSGDDYLAASYGYSYSHLWRNFGILIAFWIFFLALYLIATEYNSAAKSKGEV 80
|
90
....*....|..
gi 767243141 673 LVVKKGTKNAIQ 684
Cdd:pfam06422 81 LVFKRGKAPKLK 92
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
728-953 |
1.44e-40 |
|
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: 148.95 E-value: 1.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 728 VFIWKNVSFTIPHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRNVGT--ITGDMLVDGLPMD---ASFK 802
Cdd:cd03233 3 TLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsVEGDIHYNGIPYKefaEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 803 RRTGYVQQQDLHVAELTVKESLQFSARMRRPQSIpdaekmeyvekiisilemqefsealvgeigYGLNVEQRKKLSIGVE 882
Cdd:cd03233 83 GEIIYVSEEDVHFPTLTVRETLDFALRCKGNEFV------------------------------RGISGGERKRVSIAEA 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767243141 883 LVGKPDLLLFlDEPTSGLDSQSAWAVVKMLKRLA-LAGQSILCTIHQPSATLFEQFDRLLLLGKGGQtIYFG 953
Cdd:cd03233 133 LVSRASVLCW-DNSTRGLDSSTALEILKCIRTMAdVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQ-IYYG 202
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
25-263 |
4.97e-39 |
|
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: 145.11 E-value: 4.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 25 LPWtiIKGIRERKNRNKMKIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQfaGGVTTGHISYDGIPQK--EM 102
Cdd:cd03234 4 LPW--WDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEG--GGTTSGQILFNGQPRKpdQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 103 MQHykpdVIYNGEQDVHFPHLTVKQTLDFAISCKMPAKRVNnvtkeeyitANREFYAKIFGLTHTFDTKVGNDFISGVSG 182
Cdd:cd03234 80 QKC----VAYVRQDDILLPGLTVRETLTYTAILRLPRKSSD---------AIRKKRVEDVLLRDLALTRIGGNLVKGISG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 183 GERKRVSIAEALAAKGSIYCWDNATRGLDSSTALEFaraIRTMTNLL--GTTALVTVYQASENIYETFDKVIVLYAGRQI 260
Cdd:cd03234 147 GERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL---VSTLSQLArrNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
...
gi 767243141 261 FCG 263
Cdd:cd03234 224 YSG 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
732-946 |
9.13e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 130.57 E-value: 9.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLAqrnvGTIT---GDMLVDGLPMD---ASFKRRT 805
Cdd:COG1131 17 DGVSLTVE-----------------PGEIFGLLGPNGAGKTTTIRMLL----GLLRptsGEVRVLGEDVArdpAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 806 GYVQQQDLHVAELTVKESLQFSARMRRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEI--GyglnveQRKKLSIGVEL 883
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYG---LPRKEARERIDELLELFGLTDAADRKVGTLsgG------MKQRLGLALAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767243141 884 VGKPDLLlFLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSaTLFEQFDRLLLLGKG 946
Cdd:COG1131 147 LHDPELL-ILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLE-EAERLCDRVAIIDKG 207
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
732-946 |
1.79e-31 |
|
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: 122.96 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRNvGTITGDMLVDGLPMDAS----FKRRTGY 807
Cdd:cd03225 3 KNLSFSYPD--GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL-GPTSGEVLVDGKDLTKLslkeLRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 808 V-QQQDLHVAELTVKESLQFSARMRrpqSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGK 886
Cdd:cd03225 80 VfQNPDDQFFGPTVEEEVAFGLENL---GLPEEEIEERVEEALELVGLEGLRDRSPFTLSGG----QKQRVAIAGVLAMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 887 PDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSaTLFEQFDRLLLLGKG 946
Cdd:cd03225 153 PDILL-LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDG 210
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
732-956 |
4.70e-31 |
|
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: 122.66 E-value: 4.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIphssGQRKLLDSVSgYCVP-GTLTALIGESGAGKTTLLNTLAQR---NVGTItgdmLVDGLP---MDASFKRR 804
Cdd:COG4555 5 ENLSKKY----GKVPALKDVS-FTAKdGEITGLLGPNGAGKTTLLRMLAGLlkpDSGSI----LIDGEDvrkEPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 805 TGYVQQQDLHVAELTVKESLQFSARMRRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELV 884
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYG---LFDEELKKRIEELIELLGLEEFLDRRVGELSTG----MKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767243141 885 GKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSaTLFEQFDRLLLLgKGGQTIYFGEIG 956
Cdd:COG4555 149 HDPKVLL-LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQ-EVEALCDRVVIL-HKGKVVAQGSLD 217
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
1050-1254 |
3.29e-29 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 116.22 E-value: 3.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 1050 VLKRSSLTFWRNLNYIMAKMMLLMISGLFIGFTFFHVGVNAIGLQNSLFACFMAIVISAPATNQI-----QERATVAKEL 1124
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQGGLNRPGLLFFSILFNAFSALSGIspvfeKERGVLYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 1125 YevreskSNMFHWSLLLITHYLNELPYHLLFSTIFFVSLYFPLGVFTEASRSSVFYLnYAILFQLYYIGLALMILYMSPN 1204
Cdd:pfam01061 81 A------SPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLL-VLLLTALAASSLGLFISALAPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767243141 1205 LQSANVIVGFILSFLLSFCGAVQPASLMPGFWTFMWKLSPYTYFLQNLVG 1254
Cdd:pfam01061 154 FEDASQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRA 203
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
748-898 |
5.24e-27 |
|
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: 108.12 E-value: 5.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 748 LDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqRNVGTITGDMLVDGLPMD----ASFKRRTGYVQQQDLHVAELTVKES 823
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIA-GLLSPTEGTILLDGQDLTdderKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767243141 824 LQFSARMRRPQSIPDAEKMeyvEKIISILEMQEFSEALVGEIGYGLNVEQRKKLSIGVELVGKPDLLLfLDEPTS 898
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARA---EEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLL-LDEPTA 150
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
45-582 |
3.51e-26 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 117.25 E-value: 3.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSqfaGGVTTGHISYDGIPQKEmmQHYKPDVIYNGEQDVHFPHLT 124
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKT---GGYIEGDIRISGFPKKQ--ETFARISGYCEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 125 VKQTLDFAISCKMPAKrvnnVTKEEYITANREFyAKIFGLTHTFDTKVGNDFISGVSGGERKRVSIAEALAAKGSIYCWD 204
Cdd:PLN03140 970 VRESLIYSAFLRLPKE----VSKEEKMMFVDEV-MELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMD 1044
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 205 NATRGLDSSTALEFARAIRTMTNlLGTTALVTVYQASENIYETFDKVIVLYAGRQIFcgktteakdyfenmgYLCPPRQS 284
Cdd:PLN03140 1045 EPTSGLDARAAAIVMRTVRNTVD-TGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVI---------------YSGPLGRN 1108
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 285 T---AEYLTAItdpnglheikPGfeyqVPHTTdefEKY----WL--DSPEYARLKGEI---QKYKHEVNTEWTKKTYNE- 351
Cdd:PLN03140 1109 ShkiIEYFEAI----------PG----VPKIK---EKYnpatWMleVSSLAAEVKLGIdfaEHYKSSSLYQRNKALVKEl 1171
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 352 SMAQEKSKGTRKKSYYTVSYWEQIRLCTIRGFLRIYGDKSYTVINTCAAIAQAFITGSLFYQAPSSTLGAFSRS---GVL 428
Cdd:PLN03140 1172 STPPPGASDLYFATQYSQSTWGQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFWKVGTKRSNANDLTmviGAM 1251
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 429 FFSLLYyslMGLANISFEH------RPILQKHKVYSLYHPSAEALASTISSFPFRMIGLTFFIIILYFLAGLHRSAGAFF 502
Cdd:PLN03140 1252 YAAVLF---VGINNCSTVQpmvaveRTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFF 1328
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 503 TMYLLLTMCSEAITSLFQMVSSLCDTLSQANSIAGVVMLSIAMYSTYMIQLPSMHPWFKWISYILPIRYAFESMLNAEFH 582
Cdd:PLN03140 1329 WFYFISFFSFLYFTYYGMMTVSLTPNQQVAAIFAAAFYGLFNLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIVSQYG 1408
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
46-207 |
9.94e-26 |
|
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: 104.27 E-value: 9.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 46 LKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSqfaggVTTGHISYDGIP-QKEMMQHYKPDVIYNGEQDVHFPHLT 124
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS-----PTEGTILLDGQDlTDDERKSLRKEIGYVFQDPQLFPRLT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 125 VKQTLDFAISCKMPAKRVNNVTKEEYITAnrefyakiFGLTHTFDTKVGNdFISGVSGGERKRVSIAEALAAKGSIYCWD 204
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREKDARAEEALEK--------LGLGDLADRPVGE-RPGTLSGGQRQRVAIARALLTKPKLLLLD 146
|
...
gi 767243141 205 NAT 207
Cdd:pfam00005 147 EPT 149
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
732-946 |
2.83e-25 |
|
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: 105.49 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrnvGTI---TGDMLVDGLPMD----ASFKRR 804
Cdd:COG1122 4 ENLSFSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN----GLLkptSGEVLVDGKDITkknlRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 805 TGYV-QQQDLHVAELTVKESLQFSARMRRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSI-GVe 882
Cdd:COG1122 77 VGLVfQNPDDQLFAPTVEEDVAFGPENLG---LPREEIRERVEEALELVGLEHLADRPPHELSGG----QKQRVAIaGV- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767243141 883 LVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSAtLFEQFDRLLLLGKG 946
Cdd:COG1122 149 LAMEPEVLV-LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDG 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
730-953 |
4.66e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 105.56 E-value: 4.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 730 IWKNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLAqrnvGTI---TGDMLVDGLPMDASfKRRTG 806
Cdd:COG1121 21 VLEDVSLTIP-----------------PGEFVAIVGPNGAGKSTLLKAIL----GLLpptSGTVRLFGKPPRRA-RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 807 YVQQQ---DLHVAeLTVKE--SLQFSARMRRPQSIPDAEKmEYVEKIISILEMQEFSEALVGEI--GyglnveQRKKLSI 879
Cdd:COG1121 79 YVPQRaevDWDFP-ITVRDvvLMGRYGRRGLFRRPSRADR-EAVDEALERVGLEDLADRPIGELsgG------QQQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767243141 880 GVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSaTLFEQFDRLLLLGKGgqTIYFG 953
Cdd:COG1121 151 ARALAQDPDLLL-LDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLG-AVREYFDRVLLLNRG--LVAHG 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
740-927 |
7.55e-25 |
|
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: 104.12 E-value: 7.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 740 HSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRNVGTiTGDMLVDGLPMDASFK---RRTGYVQQQDLHVA 816
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPT-SGTAYINGYSIRTDRKaarQSLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 817 ELTVKESLQFSARMRrpqSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDlLLFLDEP 896
Cdd:cd03263 89 ELTVREHLRFYARLK---GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGG----MKRKLSLAIALIGGPS-VLLLDEP 160
|
170 180 190
....*....|....*....|....*....|....
gi 767243141 897 TSGLDSQS---AWAVVKMLKRlalaGQSILCTIH 927
Cdd:cd03263 161 TSGLDPASrraIWDLILEVRK----GRSIILTTH 190
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
743-944 |
8.86e-25 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 103.33 E-value: 8.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 743 GQRKLLDSVSgYCV-PGTLTALIGESGAGKTTLLNTLAqrnvGTIT---GDMLVDGLPMD---ASFKRRTGYVQQQDLHV 815
Cdd:COG4133 13 GERLLFSGLS-FTLaAGEALALTGPNGSGKTTLLRILA----GLLPpsaGEVLWNGEPIRdarEDYRRRLAYLGHADGLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 816 AELTVKESLQFSARMRrpqsiPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLDE 895
Cdd:COG4133 88 PELTVRENLRFWAALY-----GLRADREAIDEALEAVGLAGLADLPVRQLSAG----QKRRVALARLLLSPAPLWL-LDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767243141 896 PTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPsatLFEQFDRLLLLG 944
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAVLLTTHQP---LELAAARVLDLG 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
732-946 |
8.87e-25 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 102.48 E-value: 8.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIphssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrnvGTIT---GDMLVDGLPM---DASFKRRT 805
Cdd:cd03230 4 RNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIL----GLLKpdsGEIKVLGKDIkkePEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 806 GYVQQQDLHVAELTVKESLQFSARMRRpqsipdaekmeyvekiisilemqefsealvgeigyglnveqrkKLSIGVELVG 885
Cdd:cd03230 76 GYLPEEPSLYENLTVRENLKLSGGMKQ-------------------------------------------RLALAQALLH 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767243141 886 KPDlLLFLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSaTLFEQFDRLLLLGKG 946
Cdd:cd03230 113 DPE-LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILE-EAERLCDRVAILNNG 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
730-953 |
3.42e-24 |
|
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: 102.23 E-value: 3.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 730 IWKNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLA---QRNVGTITgdmlVDGLPMDASfKRRTG 806
Cdd:cd03235 14 VLEDVSFEVK-----------------PGEFLAIVGPNGAGKSTLLKAILgllKPTSGSIR----VFGKPLEKE-RKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 807 YVQQQdlHVAE----LTVKESLQFSA-RMRRPQSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGV 881
Cdd:cd03235 72 YVPQR--RSIDrdfpISVRDVVLMGLyGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGG----QQQRVLLAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767243141 882 ELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSaTLFEQFDRLLLLGKGGqtIYFG 953
Cdd:cd03235 146 ALVQDPDLLL-LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLG-LVLEYFDRVLLLNRTV--VASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
732-954 |
7.21e-24 |
|
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: 102.43 E-value: 7.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIphssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqRNVGTITGDMLVDGLPMDA-SFK---RRTGY 807
Cdd:COG1120 5 ENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALA-GLLKPSSGEVLLDGRDLASlSRRelaRRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 808 VQQQDLHVAELTVKESLQFsARM--RRPQSIPDAEKMEYVEKIISILEMQEFSEALVGEI--GyglnveQRKKLSIGVEL 883
Cdd:COG1120 80 VPQEPPAPFGLTVRELVAL-GRYphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELsgG------ERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767243141 884 VGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLA-LAGQSILCTIHQPS-ATLFeqFDRLLLLgKGGQTIYFGE 954
Cdd:COG1120 153 AQEPPLLL-LDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNlAARY--ADRLVLL-KDGRIVAQGP 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
742-953 |
1.59e-23 |
|
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: 100.13 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 742 SGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrnvGTI---TGDMLVDGL-----PMDAsfKRRTGYVQQQDL 813
Cdd:cd03266 15 KKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLA----GLLepdAGFATVDGFdvvkePAEA--RRRLGFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 814 HVAELTVKESLQFSARMR--RPQSIPDAekmeyVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLL 891
Cdd:cd03266 89 LYDRLTARENLEYFAGLYglKGDELTAR-----LEELADRLGMEELLDRRVGGFSTG----MRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767243141 892 fLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIH--QPSATLfeqFDRLLLLGKgGQTIYFG 953
Cdd:cd03266 160 -LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHimQEVERL---CDRVVVLHR-GRVVYEG 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
732-946 |
1.59e-23 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 100.26 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRNVGTiTGDMLVDGLPMD-------ASFKRR 804
Cdd:cd03255 4 KNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPT-SGEVRVDGTDISklsekelAAFRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 805 T-GYVQQQDLHVAELTVKESLQFSARMRRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVEL 883
Cdd:cd03255 83 HiGFVFQSFNLLPDLTALENVELPLLLAG---VPKKERRERAEELLERVGLGDRLNHYPSELSGG----QQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767243141 884 VGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLA-LAGQSILCTIHQPSatLFEQFDRLLLLGKG 946
Cdd:cd03255 156 ANDPKIIL-ADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPE--LAEYADRIIELRDG 216
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
727-946 |
4.22e-23 |
|
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: 99.20 E-value: 4.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 727 GVFIWKNVSFTIPHSsgQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRNVGTiTGDMLVDGLPMD----ASFK 802
Cdd:cd03245 1 GRIEFRNVSFSYPNQ--EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT-SGSVLLDGTDIRqldpADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 803 RRTGYVQQqDLHVAELTVKESLQFSArmrrpQSIPDAEKMEYVEkIISI----------LEMQefsealVGEIGYGLNVE 872
Cdd:cd03245 78 RNIGYVPQ-DVTLFYGTLRDNITLGA-----PLADDERILRAAE-LAGVtdfvnkhpngLDLQ------IGERGRGLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767243141 873 QRKKLSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLaLAGQSILCTIHQPSatLFEQFDRLLLLGKG 946
Cdd:cd03245 145 QRQAVALARALLNDPPILL-LDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPS--LLDLVDRIIVMDSG 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
732-946 |
1.40e-22 |
|
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: 103.68 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqRNVGTITGDMLVDGLPMD----ASFKRRTGY 807
Cdd:COG4988 340 EDVSFSYP---GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL-GFLPPYSGSILINGVDLSdldpASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 808 VQQQDlHVAELTVKESLqfsaRMRRPQsIPDAEkmeyVEKIISILEMQEFSEAL-------VGEIGYGLNVEQRKKLSIG 880
Cdd:COG4988 416 VPQNP-YLFAGTIRENL----RLGRPD-ASDEE----LEAALEAAGLDEFVAALpdgldtpLGEGGRGLSGGQAQRLALA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767243141 881 VELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLAlAGQS-ILCTiHQPSATlfEQFDRLLLLGKG 946
Cdd:COG4988 486 RALLRDAPLLL-LDEPTAHLDAETEAEILQALRRLA-KGRTvILIT-HRLALL--AQADRILVLDDG 547
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
43-272 |
1.65e-22 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 96.54 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSqfaGGVTTGHISYDGIPQKEMMQHYkpdVIYNGEQDVHFPH 122
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKT---AGVITGEILINGRPLDKNFQRS---TGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 123 LTVKQTLdfaisckmpakrvnnvtkeeyitanrEFYAKIFGLthtfdtkvgndfisgvSGGERKRVSIAEALAAKGSIYC 202
Cdd:cd03232 94 LTVREAL--------------------------RFSALLRGL----------------SVEQRKRLTIGVELAAKPSILF 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 203 WDNATRGLDSSTALEFARAIRTMTNlLGTTALVTVYQASENIYETFDKVIVLYAGrqifcGKTTeakdYF 272
Cdd:cd03232 132 LDEPTSGLDSQAAYNIVRFLKKLAD-SGQAILCTIHQPSASIFEKFDRLLLLKRG-----GKTV----YF 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
732-953 |
1.20e-21 |
|
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: 94.57 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHssgqRKLLDSVSgYCVPGTLTALIGESGAGKTTLLNTLA---QRNVGTITGDMlVDGLPMDASFKRRTGYV 808
Cdd:cd03264 4 ENLTKRYGK----KRALDGVS-LTLGPGMYGLLGPNGAGKTTLMRILAtltPPSSGTIRIDG-QDVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 809 QQQDLHVAELTVKESLQFSARMRRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPD 888
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKG---IPSKEVKARVDEVLELVNLGDRAKKKIGSLSGG----MRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767243141 889 LLLfLDEPTSGLDSQSAWAVVKMLKRLAlAGQSILCTIHQPSATLFeQFDRLLLLgKGGQTIYFG 953
Cdd:cd03264 151 ILI-VDEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVES-LCNQVAVL-NKGKLVFEG 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
714-943 |
2.60e-21 |
|
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: 99.67 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 714 DSTSADFEGLEstgvfiWKNVSFTIPhssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqRNVGTITGDMLVD 793
Cdd:TIGR02857 313 PVTAAPASSLE------FSGVSVAYP---GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLL-GFVDPTEGSIAVN 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 794 GLPMD----ASFKRRTGYVQQQDlHVAELTVKESLQFSArmrrpqsiPDAEKMEyVEKIISILEMQEFSEAL-------V 862
Cdd:TIGR02857 383 GVPLAdadaDSWRDQIAWVPQHP-FLFAGTIAENIRLAR--------PDASDAE-IREALERAGLDEFVAALpqgldtpI 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 863 GEIGYGLNVEQRKKLSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLAlAGQSILCTIHQPSatLFEQFDRLLL 942
Cdd:TIGR02857 453 GEGGAGLSGGQAQRLALARAFLRDAPLLL-LDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLA--LAALADRIVV 528
|
.
gi 767243141 943 L 943
Cdd:TIGR02857 529 L 529
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
732-923 |
3.01e-21 |
|
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: 94.04 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLAqrnvGTIT---GDMLVDG-----LPMDASFKR 803
Cdd:cd03219 17 DDVSFSVR-----------------PGEIHGLIGPNGAGKTTLFNLIS----GFLRptsGSVLFDGeditgLPPHEIARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 804 ---RTgyvqQQDLHV-AELTVKESLQFSARMRRPQSI-------PDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnve 872
Cdd:cd03219 76 gigRT----FQIPRLfPELTVLENVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAGELSYG---- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767243141 873 QRKKLSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSIL 923
Cdd:cd03219 148 QQRRLEIARALATDPKLLL-LDEPAAGLNPEETEELAELIRELRERGITVL 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
732-953 |
4.21e-21 |
|
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: 92.11 E-value: 4.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIphssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqRNVGTITGDMLVDGLPmdasfkrrtgyvqqq 811
Cdd:cd03214 3 ENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA-GLLKPSSGEILLDGKD--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 812 dlhVAELTVKEslqfsarmrrpqsipDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLL 891
Cdd:cd03214 63 ---LASLSPKE---------------LARKIAYVPQALELLGLAHLADRPFNELSGG----ERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767243141 892 fLDEPTSGLDSQSAWAVVKMLKRLALA-GQSILCTIHQPSATLfeQF-DRLLLLgKGGQTIYFG 953
Cdd:cd03214 121 -LDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAA--RYaDRVILL-KDGRIVAQG 180
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
732-949 |
8.71e-21 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 91.93 E-value: 8.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHssgQRKLLDSVSgYCVP-GTLTALIGESGAGKTTLLNTLAqrnvGTI---TGDMLVDGLPMDASFKRRT-G 806
Cdd:cd03226 3 ENISFSYKK---GTEILDDLS-LDLYaGEIIALTGKNGAGKTTLAKILA----GLIkesSGSILLNGKPIKAKERRKSiG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 807 YVQQQ-DLHVAELTVKESLQFSARmrrpqsiPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVG 885
Cdd:cd03226 75 YVMQDvDYQLFTDSVREELLLGLK-------ELDAGNEQAETVLKDLDLYALKERHPLSLSGG----QKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767243141 886 KPDLLLFlDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSaTLFEQFDRLLLLGKGGQT 949
Cdd:cd03226 144 GKDLLIF-DEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYE-FLAKVCDRVLLLANGAIV 205
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
732-946 |
9.17e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 92.41 E-value: 9.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLaqrnvGTI----TGDMLVDGLPMD-------AS 800
Cdd:COG1136 8 RNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIL-----GGLdrptSGEVLIDGQDISslserelAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 801 FKRRT-GYV-QQQDLhVAELTVKESLQFSARMRRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEI--GyglnveQRKK 876
Cdd:COG1136 83 LRRRHiGFVfQFFNL-LPELTALENVALPLLLAG---VSRKERRERARELLERVGLGDRLDHRPSQLsgG------QQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767243141 877 LSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALA-GQSILCTIHQPSatLFEQFDRLLLLGKG 946
Cdd:COG1136 153 VAIARALVNRPKLIL-ADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPE--LAARADRVIRLRDG 220
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
730-946 |
2.32e-20 |
|
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: 97.60 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 730 IWKNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLA---QRNVGTItgdmLVDGLPMD----ASFK 802
Cdd:COG2274 490 VLDNISLTIK-----------------PGERVAIVGRSGSGKSTLLKLLLglyEPTSGRI----LIDGIDLRqidpASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 803 RRTGYVQQQDlhvaEL---TVKESLQFSArmrrpqsiPDAEkMEYVEKIISILEMQEFSEAL-------VGEIGYGLNVE 872
Cdd:COG2274 549 RQIGVVLQDV----FLfsgTIRENITLGD--------PDAT-DEEIIEAARLAGLHDFIEALpmgydtvVGEGGSNLSGG 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767243141 873 QRKKLSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLaLAGQSILCTIHQPSaTLfEQFDRLLLLGKG 946
Cdd:COG2274 616 QRQRLAIARALLRNPRILI-LDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLS-TI-RLADRIIVLDKG 685
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
732-946 |
4.42e-20 |
|
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: 88.46 E-value: 4.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIphssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqRNVGTITGDMLVDGLPMDASF----KRRTGY 807
Cdd:cd00267 3 ENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIA-GLLKPTSGEILIDGKDIAKLPleelRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 808 VqqqdlhvaeltvkesLQFSArmrrpqsipdaekmeyvekiisilemqefsealvgeigyGlnveQRKKLSIGVELVGKP 887
Cdd:cd00267 78 V---------------PQLSG---------------------------------------G----QRQRVALARALLLNP 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767243141 888 DLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSaTLFEQFDRLLLLGKG 946
Cdd:cd00267 100 DLLL-LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPE-LAELAADRVIVLKDG 156
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
732-946 |
4.43e-20 |
|
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: 90.27 E-value: 4.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSftipHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrnvGTIT---GDMLVDG-----LPMDasfKR 803
Cdd:cd03259 4 KGLS----KTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIA----GLERpdsGEILIDGrdvtgVPPE---RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 804 RTGYVQQQDLHVAELTVKESLQFSARMRRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVEL 883
Cdd:cd03259 73 NIGMVFQDYALFPHLTVAENIAFGLKLRG---VPKAEIRARVRELLELVGLEGLLNRYPHELSGG----QQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767243141 884 VGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQ--SILCTIHQPSAtlFEQFDRLLLLGKG 946
Cdd:cd03259 146 AREPSLLL-LDEPLSALDAKLREELREELKELQRELGitTIYVTHDQEEA--LALADRIAVMNEG 207
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
745-946 |
4.89e-20 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 90.62 E-value: 4.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 745 RKLLDSVSGYCVPGTLTALIGESGAGKTTLlNTLAQRNVGTITGDMLVDGLPM----DASFKRRTGYVQQqdlhvaeltv 820
Cdd:cd03252 15 PVILDNISLRIKPGEVVGIVGRSGSGKSTL-TKLIQRFYVPENGRVLVDGHDLaladPAWLRRQVGVVLQ---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 821 kESLQFSARMRRPQSI----PDAEKMEYVEKIIS----ILEMQEFSEALVGEIGYGLNVEQRKKLSIGVELVGKPDLLLF 892
Cdd:cd03252 84 -ENVLFNRSIRDNIALadpgMSMERVIEAAKLAGahdfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767243141 893 lDEPTSGLDSQSAWAVVKMLKRLaLAGQSILCTIHQPSATlfEQFDRLLLLGKG 946
Cdd:cd03252 163 -DEATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRLSTV--KNADRIIVMEKG 212
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
732-953 |
1.46e-18 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 86.47 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHSsgqRKLLDSVSGYCVPGTLTALIGESGAGKTTLL---NTLAQRNVGTITgdmlVDGLPMDA-------SF 801
Cdd:cd03256 4 ENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLrclNGLVEPTSGSVL----IDGTDINKlkgkalrQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 802 KRRTGYVQQQDLHVAELTVKESLQFSARMRRP--QSI----PDAEKmeyvEKIISILE---MQEFSEALVGEIGYGlnve 872
Cdd:cd03256 77 RRQIGMIFQQFNLIERLSVLENVLSGRLGRRStwRSLfglfPKEEK----QRALAALErvgLLDKAYQRADQLSGG---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 873 QRKKLSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALA-GQSILCTIHQPSATLfEQFDRLLLLgKGGQTIY 951
Cdd:cd03256 149 QQQRVAIARALMQQPKLIL-ADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAR-EYADRIVGL-KDGRIVF 225
|
..
gi 767243141 952 FG 953
Cdd:cd03256 226 DG 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
30-258 |
2.92e-18 |
|
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: 83.06 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 30 IKGIRERKNRNKmkiILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSqfaggVTTGHISYDGIP-QKEMMQHYKP 108
Cdd:cd00267 2 IENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK-----PTSGEILIDGKDiAKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 109 DVIYngeqdvhfphltvkqtldfaisckmpakrvnnvtkeeyitanrefyakIFGLthtfdtkvgndfisgvSGGERKRV 188
Cdd:cd00267 74 RIGY------------------------------------------------VPQL----------------SGGQRQRV 89
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 189 SIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNlLGTTALVTVYQASEnIYETFDKVIVLYAGR 258
Cdd:cd00267 90 ALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPEL-AELAADRVIVLKDGK 157
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
732-903 |
2.97e-18 |
|
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: 85.22 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrnvGTIT---GDMLVDGLPMDASfKRRTGYV 808
Cdd:cd03293 4 RNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIA----GLERptsGEVLVDGEPVTGP-GPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 809 QQQDLHVAELTVKESLQFSARMRRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPD 888
Cdd:cd03293 79 FQQDALLPWLTVLDNVALGLELQG---VPKAEARERAEELLELVGLSGFENAYPHQLSGG----MRQRVALARALAVDPD 151
|
170
....*....|....*
gi 767243141 889 LLLfLDEPTSGLDSQ 903
Cdd:cd03293 152 VLL-LDEPFSALDAL 165
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
732-946 |
3.28e-18 |
|
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: 90.21 E-value: 3.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqRNVGTITGDMLVDGLPMD----ASFKRRTGY 807
Cdd:COG4987 337 EDVSFRYPG--AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLL-RFLDPQSGSITLGGVDLRdldeDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 808 VQQqDLHVAELTVKESLQFsARmrrpqsiPDAEKmeyvEKIISILE---MQEFSEAL-------VGEIGYGLNVEQRKKL 877
Cdd:COG4987 414 VPQ-RPHLFDTTLRENLRL-AR-------PDATD----EELWAALErvgLGDWLAALpdgldtwLGEGGRRLSGGERRRL 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767243141 878 SIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRlALAGQSILCTIHQPSAtlFEQFDRLLLLGKG 946
Cdd:COG4987 481 ALARALLRDAPILL-LDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLAG--LERMDRILVLEDG 545
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
732-946 |
8.66e-18 |
|
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: 83.64 E-value: 8.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLAqrnvGTIT---GDMLVDG-----LPMDASFKR 803
Cdd:cd03224 17 FGVSLTVP-----------------EGEIVALLGRNGAGKTTLLKTIM----GLLPprsGSIRFDGrditgLPPHERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 804 RTGYVQQQDLHVAELTVKESLQFSARMRRPQSIPDAekMEYVEKIISILEmqEFSEALVGEIGYGlnveQRKKLSIGVEL 883
Cdd:cd03224 76 GIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKAR--LERVYELFPRLK--ERRKQLAGTLSGG----EQQMLAIARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767243141 884 VGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILctihqpsatLFEQF--------DRLLLLGKG 946
Cdd:cd03224 148 MSRPKLLL-LDEPSEGLAPKIVEEIFEAIRELRDEGVTIL---------LVEQNarfaleiaDRAYVLERG 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
756-953 |
9.96e-18 |
|
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: 83.50 E-value: 9.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 756 VPGTLTALIGESGAGKTTLLNTLA---QRNVGTIT--GDMLVDG-----LPmdaSFKRRTGYVQQQDLHVAELTVKESLQ 825
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAgleKPDGGTIVlnGTVLFDSrkkinLP---PQQRKIGLVFQQYALFPHLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 826 FSARMRRPqsipdAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLDEPTSGLDSQSA 905
Cdd:cd03297 98 FGLKRKRN-----REDRISVDELLDLLGLDHLLNRYPAQLSGG----EKQRVALARALAAQPELLL-LDEPFSALDRALR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767243141 906 WAVVKMLKRLA--LAGQSILCTiHQPSaTLFEQFDRLLLLgKGGQTIYFG 953
Cdd:cd03297 168 LQLLPELKQIKknLNIPVIFVT-HDLS-EAEYLADRIVVM-EDGRLQYIG 214
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
746-927 |
1.05e-17 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 82.47 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 746 KLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrnvGTI---TGDMLVDGLPMDASFK------RRTGYV-QQQDLHV 815
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLN----GLLrpqSGAVLIDGEPLDYSRKgllerrQRVGLVfQDPDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 816 AELTVKESLQFSARmrrPQSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLDE 895
Cdd:TIGR01166 82 FAADVDQDVAFGPL---NLGLSEAEVERRVREALTAVGASGLRERPTHCLSGG----EKKRVAIAGAVAMRPDVLL-LDE 153
|
170 180 190
....*....|....*....|....*....|..
gi 767243141 896 PTSGLDSQSAWAVVKMLKRLALAGQSILCTIH 927
Cdd:TIGR01166 154 PTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
733-923 |
1.51e-17 |
|
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: 83.93 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 733 NVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLA---QRNVGTIT-GDMLVDGLPMDASFKR---RT 805
Cdd:COG0411 22 DVSLEVE-----------------RGEIVGLIGPNGAGKTTLFNLITgfyRPTSGRILfDGRDITGLPPHRIARLgiaRT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 806 GyvqqQDLHV-AELTVKESLQFSARMRRPQSIP------------DAEKMEYVEKIISILEMQEFSEALVGEIGYGlnve 872
Cdd:COG0411 85 F----QNPRLfPELTVLENVLVAAHARLGRGLLaallrlprarreEREARERAEELLERVGLADRADEPAGNLSYG---- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767243141 873 QRKKLSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRL-ALAGQSIL 923
Cdd:COG0411 157 QQRRLEIARALATEPKLLL-LDEPAAGLNPEETEELAELIRRLrDERGITIL 207
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
732-946 |
1.54e-17 |
|
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: 81.66 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhsSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLA---QRNVGTItgdmLVDGLPMD----ASFKRR 804
Cdd:cd03228 4 KNVSFSYP--GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLrlyDPTSGEI----LIDGVDLRdldlESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 805 TGYVQQqdlhvaeltvkESLQFSArmrrpqSIpdaekmeyVEKIISilemqefsealVGeigyglnveQRKKLSIGVELV 884
Cdd:cd03228 78 IAYVPQ-----------DPFLFSG------TI--------RENILS-----------GG---------QRQRIAIARALL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767243141 885 GKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLAlAGQSILCTIHQPSatLFEQFDRLLLLGKG 946
Cdd:cd03228 113 RDPPILI-LDEATSALDPETEALILEALRALA-KGKTVIVIAHRLS--TIRDADRIIVLDDG 170
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
743-927 |
1.97e-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: 82.80 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 743 GQRKLLDSVSGYCVPGTLTALIGESGAGKTT---LLNTLAQRNVG--TITG-DMLVDGlpmdASFKRRTGYVQQQDLHVA 816
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTtikMLTTLLKPTSGraTVAGhDVVREP----REVRRRIGIVFQDLSVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 817 ELTVKESLQFSARMrrpQSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGLnveqRKKLSIGVELVGKPDLLlFLDEP 896
Cdd:cd03265 87 ELTGWENLYIHARL---YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGM----RRRLEIARSLVHRPEVL-FLDEP 158
|
170 180 190
....*....|....*....|....*....|....
gi 767243141 897 TSGLDSQS---AWAVVKMLKRlaLAGQSILCTIH 927
Cdd:cd03265 159 TIGLDPQTrahVWEYIEKLKE--EFGMTILLTTH 190
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
743-951 |
2.66e-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: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 743 GQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLntlaqRNVGTI----TGDMLVDGLPMDASFKRRTGYVQQQDLHVAEL 818
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTI-----RMILGIilpdSGEVLFDGKPLDIAARNRIGYLPEERGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 819 TVKESLQFSAR---MRRPQSIPDAEkmEYVEKiisiLEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLDE 895
Cdd:cd03269 86 KVIDQLVYLAQlkgLKKEEARRRID--EWLER----LELSEYANKRVEELSKG----NQQKVQFIAAVIHDPELLI-LDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767243141 896 PTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQpsATLFEQF-DRLLLLGKGGQTIY 951
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQ--MELVEELcDRVLLLNKGRAVLY 209
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
722-947 |
4.85e-17 |
|
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: 81.89 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 722 GLESTGVFIWKNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLAqRNVGTITGDMLVDGLPMD--- 798
Cdd:cd03251 9 RYPGDGPPVLRDISLDIP-----------------AGETVALVGPSGSGKSTLVNLIP-RFYDVDSGRILIDGHDVRdyt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 799 -ASFKRRTGYVqQQDLHVAELTVKESLQFSARMRRPQSIPDAEKMEYVEKIisILEMQEFSEALVGEIGYGLNVEQRKKL 877
Cdd:cd03251 71 lASLRRQIGLV-SQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEF--IMELPEGYDTVIGERGVKLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 878 SIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLaLAGQSILCTIHQPSAtlFEQFDRLLLLGKGG 947
Cdd:cd03251 148 AIARALLKDPPILI-LDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLST--IENADRIVVLEDGK 213
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
743-927 |
8.76e-17 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 82.82 E-value: 8.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 743 GQRKLLDSVSGYCVPGTLTALIGESGAGKTTL---LNTLAQRNVGTITgdmlVDGLPM---DASFKRRTGYVQQQDLHVA 816
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTirmLTTLLRPTSGTAR----VAGYDVvrePRKVRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 817 ELTVKESLQFSARMrrpQSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLlFLDEP 896
Cdd:TIGR01188 80 DLTGRENLEMMGRL---YGLPKDEAEERAEELLELFELGEAADRPVGTYSGG----MRRRLDIAASLIHQPDVL-FLDEP 151
|
170 180 190
....*....|....*....|....*....|.
gi 767243141 897 TSGLDSQSAWAVVKMLKRLALAGQSILCTIH 927
Cdd:TIGR01188 152 TTGLDPRTRRAIWDYIRALKEEGVTILLTTH 182
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
743-940 |
9.82e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.55 E-value: 9.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 743 GQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTL---AQRNVGTITgdMLVDGLPMDASFKR-RTGYVQQQDLHVAEL 818
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLlglTHPDAGSIS--LCGEPVPSRARHARqRVGVVPQFDNLDPDF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 819 TVKESLQFSARMRrpqSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGLnveqRKKLSIGVELVGKPDLLLfLDEPTS 898
Cdd:PRK13537 96 TVRENLLVFGRYF---GLSAAAARALVPPLLEFAKLENKADAKVGELSGGM----KRRLTLARALVNDPDVLV-LDEPTT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767243141 899 GLDSQSAWAVVKMLKRLALAGQSILCTIHqpsatLFEQFDRL 940
Cdd:PRK13537 168 GLDPQARHLMWERLRSLLARGKTILLTTH-----FMEEAERL 204
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
732-946 |
9.91e-17 |
|
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: 81.01 E-value: 9.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFtiphSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLaqrnVGTIT---GDMLVDGLPMDA-------SF 801
Cdd:cd03261 4 RGLTK----SFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLI----VGLLRpdsGEVLIDGEDISGlseaelyRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 802 KRRTGYVQQQDLHVAELTVKESLQFSARMRRpqSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGV 881
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENVAFPLREHT--RLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGG----MKKRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767243141 882 ELVGKPDlLLFLDEPTSGLDSQSAWAVVKMLKRL--ALAGQSILCTiHQPSaTLFEQFDRLLLLGKG 946
Cdd:cd03261 150 ALALDPE-LLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVT-HDLD-TAFAIADRIAVLYDG 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
732-946 |
1.33e-16 |
|
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: 80.84 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHssgqrklldsvsgycvpGTLTALIGESGAGKTTLLNTLAqrnvGTIT---GDMLVDGL-PMDAS--FKRRT 805
Cdd:cd03267 38 KGISFTIEK-----------------GEIVGFIGPNGAGKTTTLKILS----GLLQptsGEVRVAGLvPWKRRkkFLRRI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 806 GYVQQQDLHVA-ELTVKESLQFSARMRRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELV 884
Cdd:cd03267 97 GVVFGQKTQLWwDLPVIDSFYLLAAIYD---LPPARFKKRLDELSELLDLEELLDTPVRQLSLG----QRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767243141 885 GKPDLLlFLDEPTSGLDSQSAWAVVKMLKRL-ALAGQSILCTIH--QPSATLfeqFDRLLLLGKG 946
Cdd:cd03267 170 HEPEIL-FLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHymKDIEAL---ARRVLVIDKG 230
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
732-946 |
1.42e-16 |
|
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: 79.15 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIphssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRNVGTiTGDMLVDGLPMDA------SFKRRT 805
Cdd:cd03229 4 KNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD-SGSILIDGEDLTDledelpPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 806 GYVQQQDLHVAELTVKESlqfsarmrrpqsipdaekmeyvekiisilemqefsealvgeIGYGLNVEQRKKLSIGVELVG 885
Cdd:cd03229 79 GMVFQDFALFPHLTVLEN-----------------------------------------IALGLSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767243141 886 KPDLLLfLDEPTSGLDSQSAWAVVKMLKRL-ALAGQSILCTIHQPsATLFEQFDRLLLLGKG 946
Cdd:cd03229 118 DPDVLL-LDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDL-DEAARLADRVVVLRDG 177
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
732-955 |
2.03e-16 |
|
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: 80.51 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFtiphSSGQRKLLDSVSgYCV-PGTLTALIGESGAGKTTLLNTLAQRNVGTITGDMLVDGLPMDAS----FKRRTG 806
Cdd:COG1119 7 RNVTV----RRGGKTILDDIS-WTVkPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGERRGGEdvweLRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 807 YV--QQQDLHVAELTVKESLQ--FSARMRRPQSiPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnvEQRKKLsIGVE 882
Cdd:COG1119 82 LVspALQLRFPRDETVLDVVLsgFFDSIGLYRE-PTDEQRERARELLELLGLAHLADRPFGTLSQG---EQRRVL-IARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767243141 883 LVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAG--QSILCTiHQPSAtLFEQFDRLLLLgKGGQTIYFGEI 955
Cdd:COG1119 157 LVKDPELLI-LDEPTAGLDLGARELLLALLDKLAAEGapTLVLVT-HHVEE-IPPGITHVLLL-KDGRVVAAGPK 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
717-916 |
2.12e-16 |
|
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: 84.18 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 717 SADFEGLESTGVFIWKNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLAqrnvGTIT---GDMLVD 793
Cdd:COG1123 267 SKRYPVRGKGGVRAVDDVSLTLR-----------------RGETLGLVGESGSGKSTLARLLL----GLLRptsGSILFD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 794 GLPMD-------ASFKRRTGYVQQQDLH--VAELTVKESLQFSARMRRPQSIPDAEkmeyvEKIISILEM----QEFSEA 860
Cdd:COG1123 326 GKDLTklsrrslRELRRRVQMVFQDPYSslNPRMTVGDIIAEPLRLHGLLSRAERR-----ERVAELLERvglpPDLADR 400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767243141 861 LVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLA 916
Cdd:COG1123 401 YPHELSGG----QRQRVAIARALALEPKLLI-LDEPTSALDVSVQAQILNLLRDLQ 451
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
732-915 |
3.00e-16 |
|
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: 79.85 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLA--QRNVgtiTGDMLVDGLPM----DASFKRRT 805
Cdd:COG1124 5 RNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAglERPW---SGEVTFDGRPVtrrrRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 806 GYVQQQ---DLH----VAElTVKESLQFSARMRRPQSIpdAEKMEYVEKIISILEMqeFSEALVGeigyGlnveQRKKLS 878
Cdd:COG1124 82 QMVFQDpyaSLHprhtVDR-ILAEPLRIHGLPDREERI--AELLEQVGLPPSFLDR--YPHQLSG----G----QRQRVA 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 767243141 879 IGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRL 915
Cdd:COG1124 149 IARALILEPELLL-LDEPTSALDVSVQAEILNLLKDL 184
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
732-946 |
3.38e-16 |
|
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: 83.41 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQ--RNVGTITGDMLVDGLPMDASFK----RRT 805
Cdd:COG1123 8 RDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllPHGGRISGEVLLDGRDLLELSEalrgRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 806 GYV-QQQDLHVAELTVKESLQFSARMRRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELV 884
Cdd:COG1123 86 GMVfQDPMTQLNPVTVGDQIAEALENLG---LSRAEARARVLELLEAVGLERRLDRYPHQLSGG----QRQRVAIAMALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767243141 885 GKPDLLLfLDEPTSGLDSQSAWAVVKMLKRL-ALAGQSILCTIHQPsATLFEQFDRLLLLGKG 946
Cdd:COG1123 159 LDPDLLI-ADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDL-GVVAEIADRVVVMDDG 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
732-915 |
4.27e-16 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 79.09 E-value: 4.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrNVGTIT-GDMLVDG---LPMDASFKR-RTG 806
Cdd:cd03257 5 KNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAIL--GLLKPTsGSIIFDGkdlLKLSRRLRKiRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 807 YVQQ--QDLHVA---ELTVKESLQFSARMRRPQSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGV 881
Cdd:cd03257 83 EIQMvfQDPMSSlnpRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGG----QRQRVAIAR 158
|
170 180 190
....*....|....*....|....*....|....
gi 767243141 882 ELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRL 915
Cdd:cd03257 159 ALALNPKLLI-ADEPTSALDVSVQAQILDLLKKL 191
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
43-258 |
4.42e-16 |
|
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: 77.61 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAG-ETSqfaggvTTGHISYDGIPQKEMMQHYKP---DVIYNGEQDV 118
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGlEEP------DSGSILIDGEDLTDLEDELPPlrrRIGMVFQDFA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 119 HFPHLTVKQtldfaisckmpakrvnNVTkeeyitanrefyakiFGLthtfdtkvgndfisgvSGGERKRVSIAEALAAKG 198
Cdd:cd03229 87 LFPHLTVLE----------------NIA---------------LGL----------------SGGQQQRVALARALAMDP 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 199 SIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQASEnIYETFDKVIVLYAGR 258
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDE-AARLADRVVVLRDGK 178
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
729-927 |
4.77e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.83 E-value: 4.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 729 FIWKNVSFTIPhssgQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqRNVGTITGDMLVDGLPMDA----SFKRR 804
Cdd:PRK10575 12 FALRNVSFRVP----GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLG-RHQPPSEGEILLDAQPLESwsskAFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 805 TGYVQQQdLHVAE-LTVKEslqFSARMRRPQSIP----DAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSI 879
Cdd:PRK10575 87 VAYLPQQ-LPAAEgMTVRE---LVAIGRYPWHGAlgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGG----ERQRAWI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767243141 880 GVeLVGKPDLLLFLDEPTSGLDSQSAWAVVKMLKRLA-LAGQSILCTIH 927
Cdd:PRK10575 159 AM-LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLH 206
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
743-946 |
5.52e-16 |
|
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: 78.03 E-value: 5.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 743 GQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrnvGTI---TGDMLVDGLPMD--ASFKRRTGYVQQQDLHVAE 817
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIL----GLIkpdSGEITFDGKSYQknIEALRRIGALIEAPGFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 818 LTVKESLQFSARMRRpqsIPDAEkmeyVEKIISILEMQEFSEALVGeiGYGLNVEQRkkLSIGVELVGKPDLLLfLDEPT 897
Cdd:cd03268 87 LTARENLRLLARLLG---IRKKR----IDEVLDVVGLKDSAKKKVK--GFSLGMKQR--LGIALALLGNPDLLI-LDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767243141 898 SGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSAtlFEQF-DRLLLLGKG 946
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQGITVLISSHLLSE--IQKVaDRIGIINKG 202
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
732-916 |
5.70e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 82.91 E-value: 5.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNtLAQR----NVGTItgdmLVDGLPMD----ASFKR 803
Cdd:COG1132 343 ENVSFSYP---GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVN-LLLRfydpTSGRI----LIDGVDIRdltlESLRR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 804 RTGYVqQQDLHVAELTVKESLqfsaRMRRPQsIPDAEkmeyVEKIISILEMQEFSEAL-------VGEIGYGLNVEQRKK 876
Cdd:COG1132 415 QIGVV-PQDTFLFSGTIRENI----RYGRPD-ATDEE----VEEAAKAAQAHEFIEALpdgydtvVGERGVNLSGGQRQR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767243141 877 LSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLA 916
Cdd:COG1132 485 IAIARALLKDPPILI-LDEATSALDTETEALIQEALERLM 523
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
732-903 |
6.77e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 78.98 E-value: 6.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrnvGTIT---GDMLVDGLPMDASFKRRtGYV 808
Cdd:COG1116 11 RGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA----GLEKptsGEVLVDGKPVTGPGPDR-GVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 809 QQQDLhvaeL----TVKESLQFSARMRRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEI--GyglnveQRKKLSIGVE 882
Cdd:COG1116 86 FQEPA----LlpwlTVLDNVALGLELRG---VPKAERRERARELLELVGLAGFEDAYPHQLsgG------MRQRVAIARA 152
|
170 180
....*....|....*....|.
gi 767243141 883 LVGKPDLLLfLDEPTSGLDSQ 903
Cdd:COG1116 153 LANDPEVLL-MDEPFGALDAL 172
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
732-953 |
1.10e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 78.62 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIphssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRNVGTiTGDMLVDGLPMdASF------KRRT 805
Cdd:COG4559 5 ENLSVRL----GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPS-SGEVRLNGRPL-AAWspwelaRRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 806 gyVQQQDLHVA-ELTVKESlqfsARM-RRPQSIPDAEKMEYVEKIISILEMQEFSEALV-----GEigyglnvEQRkkls 878
Cdd:COG4559 79 --VLPQHSSLAfPFTVEEV----VALgRAPHGSSAAQDRQIVREALALVGLAHLAGRSYqtlsgGE-------QQR---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 879 igVEL----------VGKPDLLLFLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSATLfeQF-DRLLLLgKGG 947
Cdd:COG4559 142 --VQLarvlaqlwepVDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAA--QYaDRILLL-HQG 216
|
....*.
gi 767243141 948 QTIYFG 953
Cdd:COG4559 217 RLVAQG 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
732-926 |
1.69e-15 |
|
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: 77.58 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNtLAQRNVGTITGDMLVDGLPMD----ASFKRRTGY 807
Cdd:cd03249 4 KNVSFRYP-SRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVS-LLERFYDPTSGEILLDGVDIRdlnlRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 808 VqQQDLHVAELTVKESLQFSArmrrpqsiPDAEkMEYVEKIISILEMQEFSEAL-------VGEIGYGLNVEQRKKLSIG 880
Cdd:cd03249 82 V-SQEPVLFDGTIAENIRYGK--------PDAT-DEEVEEAAKKANIHDFIMSLpdgydtlVGERGSQLSGGQKQRIAIA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767243141 881 VELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSI-----LCTI 926
Cdd:cd03249 152 RALLRNPKILL-LDEATSALDAESEKLVQEALDRAMKGRTTIviahrLSTI 201
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
732-929 |
2.32e-15 |
|
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: 80.87 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqRNVGTITGDMLVDGLP---MDASFKRRTGYV 808
Cdd:TIGR02868 338 RDLSAGYP---GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLA-GLLDPLQGEVTLDGVPvssLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 809 QQQDLHVAELTVKESLqfsaRMRRPQSiPDAEKMEYVEKI---ISILEMQEFSEALVGEIGYGLNVEQRKKLSIGVELVG 885
Cdd:TIGR02868 414 CAQDAHLFDTTVRENL----RLARPDA-TDEELWAALERVglaDWLRALPDGLDTVLGEGGARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767243141 886 KPDLLLfLDEPTSGLDSQSAWAVVKMLkRLALAGQSILCTIHQP 929
Cdd:TIGR02868 489 DAPILL-LDEPTEHLDAETADELLEDL-LAALSGRTVVLITHHL 530
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
740-916 |
3.00e-15 |
|
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: 76.45 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 740 HSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRNVG----TITGDMLVDGLPMDA------SFKRRTGYVQ 809
Cdd:cd03260 8 VYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgaPDEGEVLLDGKDIYDldvdvlELRRRVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 810 QQdLHVAELTVKESLQFSARMRRpqSIPDAEKMEYVEKIISILEM-QEFSEALVgeiGYGLNVEQRKKLSIGVELVGKPD 888
Cdd:cd03260 88 QK-PNPFPGSIYDNVAYGLRLHG--IKLKEELDERVEEALRKAALwDEVKDRLH---ALGLSGGQQQRLCLARALANEPE 161
|
170 180
....*....|....*....|....*...
gi 767243141 889 LLLfLDEPTSGLDSQSAWAVVKMLKRLA 916
Cdd:cd03260 162 VLL-LDEPTSALDPISTAKIEELIAELK 188
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
732-946 |
3.69e-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: 75.91 E-value: 3.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHSSgqrKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRNVGTiTGDMLVDGLPMD-------ASFKRR 804
Cdd:cd03292 4 INVTKTYPNGT---AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPT-SGTIRVNGQDVSdlrgraiPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 805 TGYVQQQDLHVAELTVKESLQFSARM--RRPQSIPdaekmEYVEKIISILEMQEFSEALVGEIGYGlnvEQrKKLSIGVE 882
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVtgVPPREIR-----KRVPAALELVGLSHKHRALPAELSGG---EQ-QRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767243141 883 LVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHqpSATLFEQFD-RLLLLGKG 946
Cdd:cd03292 151 IVNSPTILI-ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH--AKELVDTTRhRVIALERG 212
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
43-270 |
4.59e-15 |
|
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: 76.00 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQfaggvTTGHISYDGIPQKEMMQHYKPDVIYN-G---EQDV 118
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRP-----DSGEVLIDGEDISGLSEAELYRLRRRmGmlfQSGA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 119 HFPHLTVKQTLDFAIS--CKMPAKRVNNVTKEeyitanrefyaKI--FGLTHTFDTKVGNdfisgVSGGERKRVSIAEAL 194
Cdd:cd03261 88 LFDSLTVFENVAFPLRehTRLSEEEIREIVLE-----------KLeaVGLRGAEDLYPAE-----LSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767243141 195 AAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQASEnIYETFDKVIVLYAGRQIFCGKTTEAKD 270
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDT-AFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
43-258 |
5.28e-15 |
|
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: 75.25 E-value: 5.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAG-ETsqfaggVTTGHISYDG------IPQKE----MMQHYkpdvi 111
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGlER------PDSGEILIDGrdvtgvPPERRnigmVFQDY----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 112 yngeqdVHFPHLTVKQTLDFAIsckmpakRVNNVTKEEyITANREFYAKIFGLTHtfdtkVGNDFISGVSGGERKRVSIA 191
Cdd:cd03259 82 ------ALFPHLTVAENIAFGL-------KLRGVPKAE-IRARVRELLELVGLEG-----LLNRYPHELSGGQQQRVALA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767243141 192 EALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQASEnIYETFDKVIVLYAGR 258
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEE-ALALADRIAVMNEGR 208
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
732-915 |
9.07e-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: 9.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLAqrnvG--TIT-GDMLVDGLPMD--ASFKRRTG 806
Cdd:COG3839 20 KDIDLDIE-----------------DGEFLVLLGPSGCGKSTLLRMIA----GleDPTsGEILIGGRDVTdlPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 807 YV-QQQDL--HvaeLTVKESLQFSARMRRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVEL 883
Cdd:COG3839 79 MVfQSYALypH---MTVYENIAFPLKLRK---VPKAEIDRRVREAAELLGLEDLLDRKPKQLSGG----QRQRVALGRAL 148
|
170 180 190
....*....|....*....|....*....|..
gi 767243141 884 VGKPDLLLFlDEPTSGLDSQSAWAVVKMLKRL 915
Cdd:COG3839 149 VREPKVFLL-DEPLSNLDAKLRVEMRAEIKRL 179
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
732-928 |
9.40e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.51 E-value: 9.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSftipHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLL---NTLAqrnvgTIT-GDMLVDGLPMDAS------F 801
Cdd:PRK09493 5 KNVS----KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKLE-----EITsGDLIVDGLKVNDPkvderlI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 802 KRRTGYVQQQDLHVAELTVKESLQFSARMRRPQSIPDAEKMeyvekiisilemqefSEALVGEIGYG---------LNVE 872
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQ---------------ARELLAKVGLAerahhypseLSGG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767243141 873 QRKKLSIGVELVGKPDLLLFlDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQ 928
Cdd:PRK09493 141 QQQRVAIARALAVKPKLMLF-DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
732-946 |
9.42e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.12 E-value: 9.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHssGQRklldsvsgycvpgtlTALIGESGAGKTTLLNTLaqrnVGTI--TGDMLVDGLPMD----ASFKRRT 805
Cdd:PRK11174 367 GPLNFTLPA--GQR---------------IALVGPSGAGKTSLLNAL----LGFLpyQGSLKINGIELReldpESWRKHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 806 GYVqQQDLHVAELTVKESLqfsaRMRRPQsIPDAEKMEYVEKIisilEMQEFSEAL-------VGEIGYGLNVEQRKKLS 878
Cdd:PRK11174 426 SWV-GQNPQLPHGTLRDNV----LLGNPD-ASDEQLQQALENA----WVSEFLPLLpqgldtpIGDQAAGLSVGQAQRLA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767243141 879 IGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRlALAGQSILCTIHQPSATlfEQFDRLLLLGKG 946
Cdd:PRK11174 496 LARALLQPCQLLL-LDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDL--AQWDQIWVMQDG 559
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
40-258 |
1.01e-14 |
|
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: 74.43 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 40 NKMKIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGEtsqfaGGVTTGHISYDGIPQKEM------------MQHyk 107
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL-----LGPTSGEVLVDGKDLTKLslkelrrkvglvFQN-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 108 PDViyngeQdvhFPHLTVKQtlDFAISCKMpakrvNNVTKEEyITANREFYAKIFGLTHTFDTKvgndfISGVSGGERKR 187
Cdd:cd03225 84 PDD-----Q---FFGPTVEE--EVAFGLEN-----LGLPEEE-IEERVEEALELVGLEGLRDRS-----PFTLSGGQKQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767243141 188 VSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNlLGTTALVtvyqAS---ENIYETFDKVIVLYAGR 258
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIII----VThdlDLLLELADRVIVLEDGK 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
743-928 |
1.14e-14 |
|
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: 74.49 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 743 GQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrNVGTIT-GDMLVDGLPMDASFK------RRTGYV-QQQDLH 814
Cdd:cd03262 11 GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCIN--LLEEPDsGTIIIDGLKLTDDKKninelrQKVGMVfQQFNLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 815 vAELTVKESLQFSARMRRPQSIPDAEK--MEYVEKIisilEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLF 892
Cdd:cd03262 89 -PHLTVLENITLAPIKVKGMSKAEAEEraLELLEKV----GLADKADAYPAQLSGG----QQQRVAIARALAMNPKVMLF 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 767243141 893 lDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQ 928
Cdd:cd03262 160 -DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
732-948 |
2.00e-14 |
|
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: 72.63 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhsSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrnvGTI---TGDMLVDGLPMD----ASFKRR 804
Cdd:cd03246 4 ENVSFRYP--GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLIL----GLLrptSGRVRLDGADISqwdpNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 805 TGYVQQQDlhvaELtvkeslqFSArmrrpqSIPDAekmeyvekIISilemqefsealvGeiGyglnveQRKKLSIGVELV 884
Cdd:cd03246 78 VGYLPQDD----EL-------FSG------SIAEN--------ILS------------G--G------QRQRLGLARALY 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767243141 885 GKPDlLLFLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSatLFEQFDRLLLLGKGGQ 948
Cdd:cd03246 113 GNPR-ILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDGRV 173
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
732-901 |
2.08e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 76.29 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLAqrnvGTIT---GDMLVDGLPMDA--SFKRRTG 806
Cdd:COG3842 22 DDVSLSIE-----------------PGEFVALLGPSGCGKTTLLRMIA----GFETpdsGRILLDGRDVTGlpPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 807 YVQQQDL---HvaeLTVKESLQFSARMRRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEigyglnveqrkkLSIG--- 880
Cdd:COG3842 81 MVFQDYAlfpH---LTVAENVAFGLRMRG---VPKAEIRARVAELLELVGLEGLADRYPHQ------------LSGGqqq 142
|
170 180
....*....|....*....|....*.
gi 767243141 881 -VE----LVGKPDLLLfLDEPTSGLD 901
Cdd:COG3842 143 rVAlaraLAPEPRVLL-LDEPLSALD 167
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
30-258 |
3.17e-14 |
|
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: 73.29 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 30 IKGIRERKNRNKMKI-ILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAG-ETsqfaggVTTGHISYDGIPQKEM----M 103
Cdd:cd03255 3 LKNLSKTYGGGGEKVqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGlDR------PTSGEVRVDGTDISKLsekeL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 104 QHYKPD---VIYngeQDVHF-PHLTVKQTLdfaiscKMPAkRVNNVTKEEYITANREFyAKIFGLTHTFDTKVGNdfisg 179
Cdd:cd03255 77 AAFRRRhigFVF---QSFNLlPDLTALENV------ELPL-LLAGVPKKERRERAEEL-LERVGLGDRLNHYPSE----- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767243141 180 VSGGERKRVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYqaSENIYETFDKVIVLYAGR 258
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTH--DPELAEYADRIIELRDGK 217
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
748-950 |
4.86e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 73.34 E-value: 4.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 748 LDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrnvGTIT--GDMLVDGLPMD----ASFKRRTGYVQQQDLHVAELTVK 821
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMA----GLLPgqGEILLNGRPLSdwsaAELARHRAYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 822 ESLQFSArmrrPQSIPDAEkmeyvekiiSILEMQEFSEALVGEIGYGLNVEQrkkLSIG----VELVGK-----PDL--- 889
Cdd:COG4138 88 QYLALHQ----PAGASSEA---------VEQLLAQLAEALGLEDKLSRPLTQ---LSGGewqrVRLAAVllqvwPTInpe 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767243141 890 --LLFLDEPTSGLD-SQSAwAVVKMLKRLALAGQSILCTIHQPSATLFeQFDRLLLLgKGGQTI 950
Cdd:COG4138 152 gqLLLLDEPMNSLDvAQQA-ALDRLLRELCQQGITVVMSSHDLNHTLR-HADRVWLL-KQGKLV 212
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
732-946 |
4.97e-14 |
|
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: 73.03 E-value: 4.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIphsSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNtLAQRNVGTITGDMLVDGLPMD----ASFKRRTGY 807
Cdd:cd03254 6 ENVNFSY---DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLIN-LLMRFYDPQKGQILIDGIDIRdisrKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 808 VqQQDLHVAELTVKESLqfsaRMRRPQSipdaeKMEYVEKIISILEMQEFSEAL-------VGEIGYGLNVEQRKKLSIG 880
Cdd:cd03254 82 V-LQDTFLFSGTIMENI----RLGRPNA-----TDEEVIEAAKEAGAHDFIMKLpngydtvLGENGGNLSQGERQLLAIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767243141 881 VELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLaLAGQSILCTIHQPSATLFEqfDRLLLLGKG 946
Cdd:cd03254 152 RAMLRDPKILI-LDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKNA--DKILVLDDG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
730-946 |
7.16e-14 |
|
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: 72.70 E-value: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 730 IWKNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLaqrnVGTIT---GDMLVDGLPMDA------- 799
Cdd:COG1127 20 VLDGVSLDVP-----------------RGEILAIIGGSGSGKSVLLKLI----IGLLRpdsGEILVDGQDITGlsekely 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 800 SFKRRTGYVQQQ----DlhvaELTVKESLQFSARMRRpqSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRK 875
Cdd:COG1127 79 ELRRRIGMLFQGgalfD----SLTVFENVAFPLREHT--DLSEAEIRELVLEKLELVGLPGAADKMPSELSGG----MRK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767243141 876 KLSIGVELVGKPDLLlFLDEPTSGLDSQSAWAVVKMLKRL--ALAGQSILCTiHQpSATLFEQFDRLLLLGKG 946
Cdd:COG1127 149 RVALARALALDPEIL-LYDEPTAGLDPITSAVIDELIRELrdELGLTSVVVT-HD-LDSAFAIADRVAVLADG 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
727-946 |
7.68e-14 |
|
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: 72.50 E-value: 7.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 727 GVFIWKNVSFTIPHSSgQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLaQRNVGTITGDMLVDGLPMDAsfkrrtg 806
Cdd:cd03248 10 GIVKFQNVTFAYPTRP-DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALL-ENFYQPQGGQVLLDGKPISQ------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 807 yVQQQDLHVAELTVKESLQFSARMRRP------QSIPDAEKMEYVEKIIS---ILEMQEFSEALVGEIGYGLNVEQRKKL 877
Cdd:cd03248 81 -YEHKYLHSKVSLVGQEPVLFARSLQDniayglQSCSFECVKEAAQKAHAhsfISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767243141 878 SIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLkRLALAGQSILCTIHQPSatLFEQFDRLLLLGKG 946
Cdd:cd03248 160 AIARALIRNPQVLI-LDEATSALDAESEQQVQQAL-YDWPERRTVLVIAHRLS--TVERADQILVLDGG 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
726-946 |
8.01e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 76.30 E-value: 8.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 726 TGVFIWKNVSFTIPHSSGQrKLLDSVSGYCVPGTLTALIGESGAGKTT---LLNTLAQRNVGTItgdmLVDGLPMDA--- 799
Cdd:TIGR00958 476 EGLIEFQDVSFSYPNRPDV-PVLKGLTFTLHPGEVVALVGPSGSGKSTvaaLLQNLYQPTGGQV----LLDGVPLVQydh 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 800 -SFKRRTGYVQQQDLHVAElTVKESLQFSARMRRPQSIPDAEKMEYVEKIISilEMQEFSEALVGEIGYGLNVEQRKKLS 878
Cdd:TIGR00958 551 hYLHRQVALVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAANAHDFIM--EFPNGYDTEVGEKGSQLSGGQKQRIA 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767243141 879 IGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRlalAGQSILCTIHQPSatLFEQFDRLLLLGKG 946
Cdd:TIGR00958 628 IARALVRKPRVLI-LDEATSALDAECEQLLQESRSR---ASRTVLLIAHRLS--TVERADQILVLKKG 689
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
31-258 |
8.90e-14 |
|
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: 72.15 E-value: 8.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 31 KGIRERKNRNKmkiILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGetsqfAGGVTTGHISYDGIP----QKEMMQHY 106
Cdd:cd03257 9 VSFPTGGGSVK---ALDDVSFSIKKGETLGLVGESGSGKSTLARAILG-----LLKPTSGSIIFDGKDllklSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 107 KPDV--IYngeQDVHF---PHLTVKQTLdfaiscKMPAKRVNNVTKEEYITANREFYAKIFGLthtfDTKVGNDFISGVS 181
Cdd:cd03257 81 RKEIqmVF---QDPMSslnPRMTIGEQI------AEPLRIHGKLSKKEARKEAVLLLLVGVGL----PEEVLNRYPHELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 182 GGERKRVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTAL-VT----VyqasenIYETFDKVIVLYA 256
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLfIThdlgV------VAKIADRVAVMYA 221
|
..
gi 767243141 257 GR 258
Cdd:cd03257 222 GK 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
726-946 |
1.47e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 71.24 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 726 TGVFIWKNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTL-------------AQRNVGTITGDMLv 792
Cdd:COG2884 13 GGREALSDVSLEIE-----------------KGEFVFLTGPSGAGKSTLLKLLygeerptsgqvlvNGQDLSRLKRREI- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 793 dglpmdASFKRRTGYVqQQDLH-VAELTVKESLQFSARMRRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnv 871
Cdd:COG2884 75 ------PYLRRRIGVV-FQDFRlLPDRTVYENVALPLRVTG---KSRKEIRRRVREVLDLVGLSDKAKALPHELSGG--- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767243141 872 EQrKKLSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSatLFEQFD-RLLLLGKG 946
Cdd:COG2884 142 EQ-QRVAIARALVNRPELLL-ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE--LVDRMPkRVLELEDG 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
45-258 |
1.79e-13 |
|
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: 75.26 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSqfaggVTTGHISYDGIPqkemMQHYKPDVIYN--G--EQDVHF 120
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE-----PTSGRILIDGID----LRQIDPASLRRqiGvvLQDVFL 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 121 PHLTVKQTLDFAisckmpakrVNNVTKEEYITAnrefyAKIFGLtHTF--------DTKVGNDFiSGVSGGERKRVSIAE 192
Cdd:COG2274 561 FSGTIRENITLG---------DPDATDEEIIEA-----ARLAGL-HDFiealpmgyDTVVGEGG-SNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767243141 193 ALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNllGTTALV------TVYQAseniyetfDKVIVLYAGR 258
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIiahrlsTIRLA--------DRIIVLDKGR 686
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
43-258 |
1.99e-13 |
|
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: 71.49 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSaageTSQFAGgVTTGHISYDGIPQKEMMQHYKPDVIYNGEQDVHFPH 122
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRL----LFRFYD-VSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 123 LTVKQTLDFAisckmpakRVNnVTKEEYITANR--EFYAKIFGLTHTFDTKVGNdfiSGV--SGGERKRVSIAEALAAKG 198
Cdd:cd03253 89 DTIGYNIRYG--------RPD-ATDEEVIEAAKaaQIHDKIMRFPDGYDTIVGE---RGLklSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767243141 199 SIYCWDNATRGLDSSTALEFARAIRTMTNllGTTALV------TVYQAseniyetfDKVIVLYAGR 258
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSK--GRTTIViahrlsTIVNA--------DKIIVLKDGR 212
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
55-263 |
2.41e-13 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 70.79 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 55 SGEMVLVLGRPGAGCTSFLKSAAGETSqfaggVTTGHISYDGIP-----QKEMMQHYKPDVIYNGEQDVHFPHLTVKQTL 129
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEK-----PDGGTIVLNGTVlfdsrKKINLPPQQRKIGLVFQQYALFPHLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 130 DFAISCKMPAKRVNNVTKeeyITAnrefyakIFGLTHtfdtkVGNDFISGVSGGERKRVSIAEALAAKGSIYCWDNATRG 209
Cdd:cd03297 97 AFGLKRKRNREDRISVDE---LLD-------LLGLDH-----LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767243141 210 LDSSTALEFARAIRTMTNLLGTTALVTVYQASEnIYETFDKVIVLYAGRQIFCG 263
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNLNIPVIFVTHDLSE-AEYLADRIVVMEDGRLQYIG 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
45-267 |
2.68e-13 |
|
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: 74.17 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQfaGGVTTGHISYDGIPQKEMMQHYKPDVIYNGEQD--VHFPH 122
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPH--GGRISGEVLLDGRDLLELSEALRGRRIGMVFQDpmTQLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 123 LTVKQTLDFAIsckmpakRVNNVTKEEYITANREFYAKIfGLTHTFDtkvgnDFISGVSGGERKRVSIAEALAAKGSIYC 202
Cdd:COG1123 99 VTVGDQIAEAL-------ENLGLSRAEARARVLELLEAV-GLERRLD-----RYPHQLSGGQRQRVAIAMALALDPDLLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767243141 203 WDNATRGLDSSTALEFARAIRTMTNLLGTTALVtVYQASENIYETFDKVIVLYAGRQIFCGKTTE 267
Cdd:COG1123 166 ADEPTTALDVTTQAEILDLLRELQRERGTTVLL-ITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
46-258 |
3.79e-13 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 70.13 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 46 LKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQfaggvTTGHISYDGIPQKEMMQHYKP------DVIYngeQDVH 119
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELP-----TSGTIRVNGQDVSDLRGRAIPylrrkiGVVF---QDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 120 F-PHLTVKQTLDFAISC-----KMPAKRVNNVTKeeyitanrefyakIFGLTHTfdtkvGNDFISGVSGGERKRVSIAEA 193
Cdd:cd03292 89 LlPDRNVYENVAFALEVtgvppREIRKRVPAALE-------------LVGLSHK-----HRALPAELSGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767243141 194 LAAKGSIYCWDNATRGLDSSTALEFARAIRTMtNLLGTTALVTVYQASenIYETFDK-VIVLYAGR 258
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKE--LVDTTRHrVIALERGK 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
29-263 |
5.96e-13 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 69.53 E-value: 5.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 29 IIKGIRERKNRnkmKIILKNVSLLAKSGEMVLvLGRPGAGCTSFLKSAAGETSQfaggvTTGHISYDGIPQKEMMQHYKP 108
Cdd:cd03264 2 QLENLTKRYGK---KRALDGVSLTLGPGMYGL-LGPNGAGKTTLMRILATLTPP-----SSGTIRIDGQDVLKQPQKLRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 109 DVIYNGEQDVHFPHLTVKQTLDF-AISCKMPAKRVnnvtkeeyitanREFYAKIFGLTHTFDtkVGNDFISGVSGGERKR 187
Cdd:cd03264 73 RIGYLPQEFGVYPNFTVREFLDYiAWLKGIPSKEV------------KARVDEVLELVNLGD--RAKKKIGSLSGGMRRR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 188 VSIAEALAAKGSIYCWDNATRGLDSSTALEFaraiRTMTNLLGTTALVTVyqaS----ENIYETFDKVIVLYAGRQIFCG 263
Cdd:cd03264 139 VGIAQALVGDPSILIVDEPTAGLDPEERIRF----RNLLSELGEDRIVIL---SthivEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
726-916 |
6.76e-13 |
|
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: 69.95 E-value: 6.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 726 TGVFIWKNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLAqRNVGTITGDMLVDGLPMD----ASF 801
Cdd:cd03253 12 PGRPVLKDVSFTIP-----------------AGKKVAIVGPSGSGKSTILRLLF-RFYDVSSGSILIDGQDIRevtlDSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 802 KRRTGYVQQqDLHVAELTVKESLQFsARmrrpqsiPDA--EKMEYVEKII----SILEMQEFSEALVGEIGYGLNVEQRK 875
Cdd:cd03253 74 RRAIGVVPQ-DTVLFNDTIGYNIRY-GR-------PDAtdEEVIEAAKAAqihdKIMRFPDGYDTIVGERGLKLSGGEKQ 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767243141 876 KLSIGVELVGKPDLLLFlDEPTSGLDSQSAWAVVKMLKRLA 916
Cdd:cd03253 145 RVAIARAILKNPPILLL-DEATSALDTHTEREIQAALRDVS 184
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
743-946 |
1.05e-12 |
|
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: 69.29 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 743 GQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLA---QRNVGTIT-GDMLVDGLPMDasfKRRTGYVQQqdlHVA-- 816
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAgleRPDSGTILfGGEDATDVPVQ---ERNVGFVFQ---HYAlf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 817 -ELTVKESLQFSARMR-RPQSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLD 894
Cdd:cd03296 87 rHMTVFDNVAFGLRVKpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGG----QRQRVALARALAVEPKVLL-LD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767243141 895 EPTSGLDSQSAWAVVKMLKRL--ALAGQSILCTIHQPSAtlFEQFDRLLLLGKG 946
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLhdELHVTTVFVTHDQEEA--LEVADRVVVMNKG 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
732-946 |
1.13e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 70.14 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLAQrnvgtIT----GDMLVDGLPMDASFKRRTGY 807
Cdd:COG4152 18 DDVSFTVP-----------------KGEIFGLLGPNGAGKTTTIRIILG-----ILapdsGEVLWDGEPLDPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 808 vqqqdlhVAE-------LTVKESLQFSAR---MRRPQSIPDAEkmEYVEKiisiLEMQEFSEALVGEIGYGlnvEQRkKL 877
Cdd:COG4152 76 -------LPEerglypkMKVGEQLVYLARlkgLSKAEAKRRAD--EWLER----LGLGDRANKKVEELSKG---NQQ-KV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767243141 878 SIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQ-PSAtlfEQF-DRLLLLGKG 946
Cdd:COG4152 139 QLIAALLHDPELLI-LDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQmELV---EELcDRIVIINKG 205
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
732-923 |
1.13e-12 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 69.24 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLAqRNVGTITGDMLVDG-----LPMDASFKRRTG 806
Cdd:COG0410 20 HGVSLEVE-----------------EGEIVALLGRNGAGKTTLLKAIS-GLLPPRSGSIRFDGeditgLPPHRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 807 YVqQQDLHV-AELTVKESLQFSARMRRPQSiPDAEKMEYVEKIISILEmqEFSEALVGEIGYGlnveQRKKLSIGVELVG 885
Cdd:COG0410 82 YV-PEGRRIfPSLTVEENLLLGAYARRDRA-EVRADLERVYELFPRLK--ERRRQRAGTLSGG----EQQMLAIGRALMS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767243141 886 KPDLLLfLDEPTSGLdsqsAWAVVK----MLKRLALAGQSIL 923
Cdd:COG0410 154 RPKLLL-LDEPSLGL----APLIVEeifeIIRRLNREGVTIL 190
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
43-258 |
1.26e-12 |
|
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: 67.42 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQfaggvTTGHISYDGIPQKEMMQHYKPDVIYNGEQDVHFPH 122
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKP-----DSGEIKVLGKDIKKEPEEVKRRIGYLPEEPSLYEN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 123 LTVKQTLDFaisckmpakrvnnvtkeeyitanrefyakifglthtfdtkvgndfisgvSGGERKRVSIAEALAAKGSIYC 202
Cdd:cd03230 88 LTVRENLKL-------------------------------------------------SGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767243141 203 WDNATRGLDSSTALEFARAIRTMTNlLGTTALVTvyqaS---ENIYETFDKVIVLYAGR 258
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKK-EGKTILLS----ShilEEAERLCDRVAILNNGR 172
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
37-274 |
1.61e-12 |
|
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: 68.75 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 37 KNRNKMKIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETsqfagGVTTGHISYDGIPQKEMMQHYKPDV------ 110
Cdd:cd03256 8 KTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLV-----EPTSGSVLIDGTDINKLKGKALRQLrrqigm 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 111 IYngeQDVHF-PHLTVKQTLDFAISCKMPAKRV--NNVTKEEYITAnreFYA-KIFGLTHTFDTKVGNdfisgVSGGERK 186
Cdd:cd03256 83 IF---QQFNLiERLSVLENVLSGRLGRRSTWRSlfGLFPKEEKQRA---LAAlERVGLLDKAYQRADQ-----LSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 187 RVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQAsENIYETFDKVIVLYAGRQIFCGKTT 266
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQV-DLAREYADRIVGLKDGRIVFDGPPA 230
|
....*...
gi 767243141 267 EAKDYFEN 274
Cdd:cd03256 231 ELTDEVLD 238
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
29-212 |
1.74e-12 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 68.30 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 29 IIKGIReRKNRNKMKIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSqfaggVTTGHISYDGIPQKEMMQHYKP 108
Cdd:cd03263 2 QIRNLT-KTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELR-----PTSGTAYINGYSIRTDRKAARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 109 DVIYNGEQDVHFPHLTVKQTLDFaiSCkmpakRVNNVTKEEyITANREFYAKIFGLTHTFDTKVGNdfisgVSGGERKRV 188
Cdd:cd03263 76 SLGYCPQFDALFDELTVREHLRF--YA-----RLKGLPKSE-IKEEVELLLRVLGLTDKANKRART-----LSGGMKRKL 142
|
170 180
....*....|....*....|....
gi 767243141 189 SIAEALAAKGSIYCWDNATRGLDS 212
Cdd:cd03263 143 SLAIALIGGPSVLLLDEPTSGLDP 166
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
743-903 |
1.75e-12 |
|
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: 68.42 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 743 GQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrnvGTIT---GDMLVDGLPMDA--SFKRRTGYVQQQDLHVAE 817
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIA----GFETptsGEILLDGKDITNlpPHKRPVNTVFQNYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 818 LTVKESLQFSARMRRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLDEPT 897
Cdd:cd03300 87 LTVFENIAFGLRLKK---LPKAEIKERVAEALDLVQLEGYANRKPSQLSGG----QQQRVAIARALVNEPKVLL-LDEPL 158
|
....*.
gi 767243141 898 SGLDSQ 903
Cdd:cd03300 159 GALDLK 164
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
748-946 |
2.40e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 748 LDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrnvGTIT--GDMLVDGLPMD----ASFKRRTGYVQQQDLHVAELTVK 821
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMA----GLLPgsGSIQFAGQPLEawsaAELARHRAYLSQQQTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 822 ESLQFSarmrRPQSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnvE-QRKKLSiGVELVGKPDL-----LLFLDE 895
Cdd:PRK03695 88 QYLTLH----QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGG---EwQRVRLA-AVVLQVWPDInpagqLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767243141 896 PTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSATLfEQFDRLLLLGKG 946
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTL-RHADRVWLLKQG 209
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
30-257 |
2.88e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 69.73 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 30 IKGIRERKNRNKmkiILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQfaggvTTGHISYDGIPQKEM------- 102
Cdd:PRK10851 5 IANIKKSFGRTQ---VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQ-----TSGHIRFHGTDVSRLhardrkv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 103 ---MQHYkpdviyngeqdVHFPHLTVKQTLDFAISCKMPAKRVNNVTKEEYITANREfyakIFGLTHtfdtkVGNDFISG 179
Cdd:PRK10851 77 gfvFQHY-----------ALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLE----MVQLAH-----LADRYPAQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767243141 180 VSGGERKRVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTAlVTVYQASENIYETFDKVIVLYAG 257
Cdd:PRK10851 137 LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTS-VFVTHDQEEAMEVADRVVVMSQG 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
741-940 |
3.14e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.47 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 741 SSGQRKLLDSVSGYCVPGTLTALIGESGAGKTT---LLNTLAQRNVGTITgdmlVDGLPMDA---SFKRRTGYVQQQDLH 814
Cdd:PRK13536 50 SYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTiarMILGMTSPDAGKIT----VLGVPVPArarLARARIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 815 VAELTVKESLQFSARMRRPQsipdAEKMEYVekIISILE---MQEFSEALVGEIGYGLnveqRKKLSIGVELVGKPDLLL 891
Cdd:PRK13536 126 DLEFTVRENLLVFGRYFGMS----TREIEAV--IPSLLEfarLESKADARVSDLSGGM----KRRLTLARALINDPQLLI 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767243141 892 fLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHqpsatLFEQFDRL 940
Cdd:PRK13536 196 -LDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH-----FMEEAERL 238
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
45-258 |
3.44e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 67.38 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSqfaggVTTGHISYDG-----IPQKEMmqhykPD------VIYn 113
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEER-----PTSGQVLVNGqdlsrLKRREI-----PYlrrrigVVF- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 114 geQDVHF-PHLTVKQTLDFAIsckmpakRVNNVTKEEYITANREFYAKiFGLTHtfdtkVGNDFISGVSGGERKRVSIAE 192
Cdd:COG2884 86 --QDFRLlPDRTVYENVALPL-------RVTGKSRKEIRRRVREVLDL-VGLSD-----KAKALPHELSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767243141 193 ALAAKGSIYCWDNATRGLDSSTALEFARAIRTMtNLLGTTALVTVYqaSENIYETFDK-VIVLYAGR 258
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATH--DLELVDRMPKrVLELEDGR 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
732-915 |
3.54e-12 |
|
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: 67.61 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLL---NTLAQRNVGTItgdmLVDGLPMDA-------SF 801
Cdd:cd03258 5 KNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIrciNGLERPTSGSV----LVDGTDLTLlsgkelrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 802 KRRTGYVQQQDLHVAELTVKESLQFSARMRRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGV 881
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAG---VPKAEIEERVLELLELVGLEDKADAYPAQLSGG----QKQRVGIAR 153
|
170 180 190
....*....|....*....|....*....|....
gi 767243141 882 ELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRL 915
Cdd:cd03258 154 ALANNPKVLL-CDEATSALDPETTQSILALLRDI 186
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
43-224 |
4.07e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.82 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETsqfagGVTTGHISYDGIPQKEmmQHYKPDVIYNGEQDVHFPH 122
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLL-----PPAAGTIKLDGGDIDD--PDVAEACHYLGHRNAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 123 LTVKQTLDFaisckmpAKRVNNvTKEEYITANREFyakiFGLTHTFDTKVGNdfisgVSGGERKRVSIAEALAAKGSIYC 202
Cdd:PRK13539 88 LTVAENLEF-------WAAFLG-GEELDIAAALEA----VGLAPLAHLPFGY-----LSAGQKRRVALARLLVSNRPIWI 150
|
170 180
....*....|....*....|..
gi 767243141 203 WDNATRGLDSSTALEFARAIRT 224
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELIRA 172
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
732-923 |
6.52e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 69.67 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLAqrnvGTIT---GDMLVDGL------PMDAsFK 802
Cdd:COG3845 22 DDVSLTVR-----------------PGEIHALLGENGAGKSTLMKILY----GLYQpdsGEILIDGKpvrirsPRDA-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 803 RRTGYVQQqdlH---VAELTVKESLQFSARmRRPQSIPDAEKMEyvEKIisilemQEFSEAlvgeigYGLNVEQRKK--- 876
Cdd:COG3845 80 LGIGMVHQ---HfmlVPNLTVAENIVLGLE-PTKGGRLDRKAAR--ARI------RELSER------YGLDVDPDAKved 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767243141 877 LSIG----VE----LVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSIL 923
Cdd:COG3845 142 LSVGeqqrVEilkaLYRGARILI-LDEPTAVLTPQEADELFEILRRLAAEGKSII 195
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
738-946 |
6.84e-12 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 66.80 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 738 IPHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLaqrnVGTI---TGDMLVDG-----LPMDASFKRRTGYVQ 809
Cdd:cd03218 6 LSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMI----VGLVkpdSGKILLDGqditkLPMHKRARLGIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 810 QQDLHVAELTVKESLQFSARMRRPqsiPDAEKMeyvEKIISILEmqEFS-EALVGEIGYGLNVEQRKKLSIGVELVGKPD 888
Cdd:cd03218 82 QEASIFRKLTVEENILAVLEIRGL---SKKERE---EKLEELLE--EFHiTHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767243141 889 LLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSATLfEQFDRLLLLGKG 946
Cdd:cd03218 154 FLL-LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETL-SITDRAYIIYEG 209
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
745-933 |
8.16e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.84 E-value: 8.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 745 RKLLDSVSGYCVPGTLTALIGESGAGKTT---LLNTLAQRNVGTIT-GDMLVDGLPMDASFKRRTGYVQQQDLHVAELTV 820
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTtfyMVVGIVPRDAGNIIiDDEDISLLPLHARARRGIGYLPQEASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 821 KESLQFSARMRrpQSIPDAEKMEYVEKIisileMQEFS-EALVGEIGYGLNVEQRKKLSIGVELVGKPDLLLfLDEPTSG 899
Cdd:PRK10895 96 YDNLMAVLQIR--DDLSAEQREDRANEL-----MEEFHiEHLRDSMGQSLSGGERRRVEIARALAANPKFIL-LDEPFAG 167
|
170 180 190
....*....|....*....|....*....|....
gi 767243141 900 LDSQSAWAVVKMLKRLALAGQSILCTIHQPSATL 933
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRDSGLGVLITDHNVRETL 201
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
732-901 |
8.90e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.80 E-value: 8.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLAqrnvGTIT---GDMLVDGL-PmdasFKRRTGY 807
Cdd:COG4586 39 DDISFTIE-----------------PGEIVGFIGPNGAGKSTTIKMLT----GILVptsGEVRVLGYvP----FKRRKEF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 808 V--------QQQDLHvAELTVKESLQFSARMRRpqsIPDAEKMEYVEKIISILEMQEFsealvgeigygLNVEQRKkLSI 879
Cdd:COG4586 94 ArrigvvfgQRSQLW-WDLPAIDSFRLLKAIYR---IPDAEYKKRLDELVELLDLGEL-----------LDTPVRQ-LSL 157
|
170 180 190
....*....|....*....|....*....|
gi 767243141 880 G----VELVG----KPDLLlFLDEPTSGLD 901
Cdd:COG4586 158 GqrmrCELAAallhRPKIL-FLDEPTIGLD 186
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
46-258 |
1.28e-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: 66.21 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 46 LKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTTGHISYDGIPQKE-----MMQHYkpdviyngeqdVHF 120
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErnvgfVFQHY-----------ALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 121 PHLTVKQTLDFAISCKMPAKRVNnvtkEEYITANREFYAKIFGLthtfdTKVGNDFISGVSGGERKRVSIAEALAAKGSI 200
Cdd:cd03296 87 RHMTVFDNVAFGLRVKPRSERPP----EAEIRAKVHELLKLVQL-----DWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767243141 201 YCWDNATRGLDSSTALEFARAIRTMTNLLG-TTALVTVYQasENIYETFDKVIVLYAGR 258
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHvTTVFVTHDQ--EEALEVADRVVVMNKGR 214
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
425-578 |
1.45e-11 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 67.41 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 425 SGVLFFSLLYYSLMGLANISFEHRPILQKHKVYSLYHPSAEALASTISSFpfrMIGLTFFIIILYFLAGLHRSAGAFFTM 504
Cdd:pfam12698 165 GLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDF---LVGLLQLLIILLLLFGIGIPFGNLGLL 241
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767243141 505 YLLLTMCSEAITSLFQMVSSLCDTLSQANSIAGVVMLSIAMYSTYMIQLPSMHPWFKWISYILPIRYAFESMLN 578
Cdd:pfam12698 242 LLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLR 315
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
731-927 |
1.52e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.68 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 731 WKNVSFTI-PHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLL---NTLAQRNVGTI-TGDMLVDGLPMDASFK--- 802
Cdd:PRK13643 4 FEKVNYTYqPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLqhlNGLLQPTEGKVtVGDIVVSSTSKQKEIKpvr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 803 RRTGYVQQ-QDLHVAELTVKESLQFSarmrrPQSIPDAEkmEYVEKIIS-ILEMQEFSEALVGEIGYGLNVEQRKKLSIG 880
Cdd:PRK13643 84 KKVGVVFQfPESQLFEETVLKDVAFG-----PQNFGIPK--EKAEKIAAeKLEMVGLADEFWEKSPFELSGGQMRRVAIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767243141 881 VELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIH 927
Cdd:PRK13643 157 GILAMEPEVLV-LDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
754-915 |
1.80e-11 |
|
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: 65.43 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 754 YCVpgtltaLIGESGAGKTTLLNTLAQRnVGTITGDMLVDG-----LPMDasfKRRTGYVQQQDLHVAELTVKESLQFSA 828
Cdd:cd03299 27 YFV------ILGPTGSGKSVLLETIAGF-IKPDSGKILLNGkditnLPPE---KRDISYVPQNYALFPHMTVYKNIAYGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 829 RMRRpqsipdAEKMEYVEKIISILEMQEFSEAL---VGEIGYGlnveQRKKLSIGVELVGKPDLLLfLDEPTSGLDSQSA 905
Cdd:cd03299 97 KKRK------VDKKEIERKVLEIAEMLGIDHLLnrkPETLSGG----EQQRVAIARALVVNPKILL-LDEPFSALDVRTK 165
|
170
....*....|
gi 767243141 906 WAVVKMLKRL 915
Cdd:cd03299 166 EKLREELKKI 175
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
732-906 |
2.24e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.17 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIphssGQRKLLDSVS-----GYCVpgtltALIGESGAGKTTLLNTLAqrnvGTITGDmlvDGlpmDASFKR--R 804
Cdd:COG0488 2 ENLSKSF----GGRPLLDDVSlsinpGDRI-----GLVGRNGAGKSTLLKILA----GELEPD---SG---EVSIPKglR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 805 TGYVQQQDLHVAELTV--------KESLQFSARMRRPQ---SIPDAEKMEYVEKIISILEMQEFS-EALVGEI--GYGLN 870
Cdd:COG0488 63 IGYLPQEPPLDDDLTVldtvldgdAELRALEAELEELEaklAEPDEDLERLAELQEEFEALGGWEaEARAEEIlsGLGFP 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767243141 871 VE------------QRKKLSIGVELVGKPDLLLfLDEPTSGLDSQS-AW 906
Cdd:COG0488 143 EEdldrpvselsggWRRRVALARALLSEPDLLL-LDEPTNHLDLESiEW 190
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
45-211 |
2.31e-11 |
|
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: 64.86 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAG-ETsqfaggVTTGHISYDGIpqkemmqhykpdVIYNGEQDVH---- 119
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLlEE------PDSGTIIIDGL------------KLTDDKKNINelrq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 120 -----------FPHLTVKQTLDFAIsckmpaKRVNNVTKEEYITANREFYAKIfGLTHtfdtkVGNDFISGVSGGERKRV 188
Cdd:cd03262 77 kvgmvfqqfnlFPHLTVLENITLAP------IKVKGMSKAEAEERALELLEKV-GLAD-----KADAYPAQLSGGQQQRV 144
|
170 180
....*....|....*....|...
gi 767243141 189 SIAEALAAKGSIYCWDNATRGLD 211
Cdd:cd03262 145 AIARALAMNPKVMLFDEPTSALD 167
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
43-270 |
2.96e-11 |
|
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: 65.00 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGetsQFAggVTTGHISYDGipqkemmqhykpdviyngeQDVH--- 119
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIG---LLR--PDSGEILVDG-------------------QDITgls 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 120 --------------------FPHLTVKQTLDFaisckmPAKRVNNVTKEEyITANREFYAKIFGLTHTFDTkvgndFISG 179
Cdd:COG1127 74 ekelyelrrrigmlfqggalFDSLTVFENVAF------PLREHTDLSEAE-IRELVLEKLELVGLPGAADK-----MPSE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 180 VSGGERKRVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQASEnIYETFDKVIVLYAGRQ 259
Cdd:COG1127 142 LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDS-AFAIADRVAVLADGKI 220
|
250
....*....|.
gi 767243141 260 IFCGKTTEAKD 270
Cdd:COG1127 221 IAEGTPEELLA 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
45-258 |
3.92e-11 |
|
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: 64.56 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSaageTSQFAGgVTTGHISYDGIPQKEMMQHYKPDVIYNGEQDVHFPHLT 124
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNL----IPRFYD-VDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 125 VKQTLDFAisckmpakrVNNVTKEEYITANREFYAK--IFGLTHTFDTKVGNdfiSGV--SGGERKRVSIAEALAAKGSI 200
Cdd:cd03251 92 VAENIAYG---------RPGATREEVEEAARAANAHefIMELPEGYDTVIGE---RGVklSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 201 YCWDNATRGLDSSTALEFARAIRTMTNllGTTALVTVYQAS--ENIyetfDKVIVLYAGR 258
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLStiENA----DRIVVLEDGK 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
750-927 |
3.96e-11 |
|
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: 68.12 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 750 SVSGYCV---PGTLTALIGESGAGKTTLLNTLAQRNVGTiTGDMLVDG---LPMDASFKRRTGYVQQQDLHVAELTVKES 823
Cdd:TIGR01257 1954 AVDRLCVgvrPGECFGLLGVNGAGKTTTFKMLTGDTTVT-SGDATVAGksiLTNISDVHQNMGYCPQFDAIDDLLTGREH 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 824 LQFSARMRrpqSIPdAEKMEYVEKI-ISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLDEPTSGLDS 902
Cdd:TIGR01257 2033 LYLYARLR---GVP-AEEIEKVANWsIQSLGLSLYADRLAGTYSGG----NKRKLSTAIALIGCPPLVL-LDEPTTGMDP 2103
|
170 180
....*....|....*....|....*
gi 767243141 903 QSAWAVVKMLKRLALAGQSILCTIH 927
Cdd:TIGR01257 2104 QARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
761-916 |
4.80e-11 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 65.89 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 761 TALIGESGAGKTTLLNTLA---QRNVGTIT--GDMLVDG-----LPMDasfKRRTGYVQQQDLHVAELTVKESLQFSarM 830
Cdd:COG4148 28 TALFGPSGSGKTTLLRAIAgleRPDSGRIRlgGEVLQDSargifLPPH---RRRIGYVFQEARLFPHLSVRGNLLYG--R 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 831 RRpqsIPDAEKMEYVEKIISILEMqefsEALV---------GEigyglnvEQRkkLSIGVELVGKPDLLLfLDEPTSGLD 901
Cdd:COG4148 103 KR---APRAERRISFDEVVELLGI----GHLLdrrpatlsgGE-------RQR--VAIGRALLSSPRLLL-MDEPLAALD 165
|
170
....*....|....*
gi 767243141 902 SQSAWAVVKMLKRLA 916
Cdd:COG4148 166 LARKAEILPYLERLR 180
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
724-946 |
4.89e-11 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 63.64 E-value: 4.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 724 ESTGVFIWKNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNtlaqrnvgTITGDM-LVDGLpmdASFK 802
Cdd:cd03250 14 EQETSFTLKDINLEVP-----------------KGELVAIVGPVGSGKSSLLS--------ALLGELeKLSGS---VSVP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 803 RRTGYVQQQDLHVAElTVKESLQFSARMrrpqsipDAEKMEYV------EKIISILEMQEFSEalVGEIGYGLNVEQRKK 876
Cdd:cd03250 66 GSIAYVSQEPWIQNG-TIRENILFGKPF-------DEERYEKVikacalEPDLEILPDGDLTE--IGEKGINLSGGQKQR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767243141 877 LSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQS--ILCTiHQPSatLFEQFDRLLLLGKG 946
Cdd:cd03250 136 ISLARAVYSDADIYL-LDDPLSAVDAHVGRHIFENCILGLLLNNKtrILVT-HQLQ--LLPHADQIVVLDNG 203
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
743-929 |
5.11e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.74 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 743 GQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLA--QRNV-GTITGDmlvDGLPMDASFKRRTGYVQQQDLHVAELT 819
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAglLPPAaGTIKLD---GGDIDDPDVAEACHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 820 VKESLQFSARMR--RPQSIPDAekmeyvekiisileMQEFSEALVGEIGYG-LNVEQRKKLSIGVELV-GKPdlLLFLDE 895
Cdd:PRK13539 90 VAENLEFWAAFLggEELDIAAA--------------LEAVGLAPLAHLPFGyLSAGQKRRVALARLLVsNRP--IWILDE 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 767243141 896 PTSGLDSqsawAVVKMLKRLALA----GQSILCTIHQP 929
Cdd:PRK13539 154 PTAALDA----AAVALFAELIRAhlaqGGIVIAATHIP 187
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
45-267 |
5.35e-11 |
|
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: 66.85 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAG-ETsqfaggVTTGHISYDGIP----QKEMMQHYKPDV--IYngeQD 117
Cdd:COG1123 280 AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGlLR------PTSGSILFDGKDltklSRRSLRELRRRVqmVF---QD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 118 VH---FPHLTVKQTLDFAIsckmpakRVNNVTKEEYITANREFYAKIFGLthtfDTKVGNDFISGVSGGERKRVSIAEAL 194
Cdd:COG1123 351 PYsslNPRMTVGDIIAEPL-------RLHGLLSRAERRERVAELLERVGL----PPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767243141 195 AAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALV------TVYQASeniyetfDKVIVLYAGRQIFCGKTTE 267
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFishdlaVVRYIA-------DRVAVMYDGRIVEDGPTEE 491
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
46-258 |
5.37e-11 |
|
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: 63.76 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 46 LKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQfaggvTTGHISYDGIPQKEMmqhyKPDVIYNG----EQDVHFP 121
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKP-----TSGSVLLDGTDIRQL----DPADLRRNigyvPQDVTLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 122 HLTVKQTLDFAisckMPAkrvnnVTKEEYITAnrefyAKIFGLT-------HTFDTKVGnDFISGVSGGERKRVSIAEAL 194
Cdd:cd03245 91 YGTLRDNITLG----APL-----ADDERILRA-----AELAGVTdfvnkhpNGLDLQIG-ERGRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767243141 195 AAKGSIYCWDNATRGLDSSTALEFARAIRTMtnLLGTTALVTVYQASenIYETFDKVIVLYAGR 258
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQL--LGDKTLIIITHRPS--LLDLVDRIIVMDSGR 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
732-946 |
5.96e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 64.41 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIphssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQrNVGTITGDMLVDGLPMdASFKRrtgyvQQQ 811
Cdd:PRK13548 6 RNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG-ELSPDSGEVRLNGRPL-ADWSP-----AEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 812 DLHVAELTVKESLQFS------ARM-RRPQSIPDAEKMEYVEKIISILEMQEFSEALV-----GEigyglnvEQRkklsi 879
Cdd:PRK13548 75 ARRRAVLPQHSSLSFPftveevVAMgRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYpqlsgGE-------QQR----- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767243141 880 gVEL---------VGKPDLLLFLDEPTSGLDSQSAWAVVKMLKRLALAGQ-SILCTIHQPS-ATLFEqfDRLLLLGKG 946
Cdd:PRK13548 143 -VQLarvlaqlwePDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGlAVIVVLHDLNlAARYA--DRIVLLHQG 217
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
757-957 |
8.20e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.26 E-value: 8.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 757 PGTLTALIGESGAGKTTLLNTLAqrnvGTI---TGDMLVDGLPMDASfKRRTGYVQQQ--------DLHVAELTVKESLQ 825
Cdd:PRK13638 26 LSPVTGLVGANGCGKSTLFMNLS----GLLrpqKGAVLWQGKPLDYS-KRGLLALRQQvatvfqdpEQQIFYTDIDSDIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 826 FSARmrrPQSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLDEPTSGLDSQSA 905
Cdd:PRK13638 101 FSLR---NLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHG----QKKRVAIAGALVLQARYLL-LDEPTAGLDPAGR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767243141 906 WAVVKMLKRLALAGQSILCTIHQPSaTLFEQFDRLLLLgKGGQTIYFGEIGK 957
Cdd:PRK13638 173 TQMIAIIRRIVAQGNHVIISSHDID-LIYEISDAVYVL-RQGQILTHGAPGE 222
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
40-260 |
1.04e-10 |
|
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: 63.01 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 40 NKMKIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGetsqFAGgVTTGHISYDGIPQKEMMQHYKPDVIYNGEQDVH 119
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMR----FYD-PQKGQILIDGIDIRDISRKSLRSMIGVVLQDTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 120 FPHLTVKQTLDFAisckmpakrVNNVTKEEYITANREFYAKIFG--LTHTFDTKVGNDFiSGVSGGERKRVSIAEALAAK 197
Cdd:cd03254 88 LFSGTIMENIRLG---------RPNATDEEVIEAAKEAGAHDFImkLPNGYDTVLGENG-GNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767243141 198 GSIYCWDNATRGLDSSTALEFARAIRTMTNllGTTALVTVYQASenIYETFDKVIVLYAGRQI 260
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLS--TIKNADKILVLDDGKII 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
45-258 |
1.18e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 65.96 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAG--EtsqfaggVTTGHISYDGIPQKEmmqhYKPDVIYNG----EQDV 118
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfyD-------PTSGRILIDGVDIRD----LTLESLRRQigvvPQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 119 HFPHLTVKQTLDFAisckmpakrVNNVTKEEYITANR-----EFyakIFGLTHTFDTKVGNDfisGV--SGGERKRVSIA 191
Cdd:COG1132 424 FLFSGTIRENIRYG---------RPDATDEEVEEAAKaaqahEF---IEALPDGYDTVVGER---GVnlSGGQRQRIAIA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767243141 192 EALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNllGTTALV------TVYQAseniyetfDKVIVLYAGR 258
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIViahrlsTIRNA--------DRILVLDDGR 551
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
38-254 |
1.20e-10 |
|
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: 62.87 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 38 NRNKMKIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQfaggvTTGHISYDGIPQKEMmqhyKPDVIYNGEQD 117
Cdd:cd03293 12 GGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERP-----TSGEVLVDGEPVTGP----GPDRGYVFQQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 118 VHFPHLTVKQTLDFAIsckmpakRVNNVTKEEyITANREFYAKIFGLTHTfdtkvGNDFISGVSGGERKRVSIAEALAAK 197
Cdd:cd03293 83 ALLPWLTVLDNVALGL-------ELQGVPKAE-ARERAEELLELVGLSGF-----ENAYPHQLSGGMRQRVALARALAVD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767243141 198 GSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTA-LVTvyqasENIYETF---DKVIVL 254
Cdd:cd03293 150 PDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVlLVT-----HDIDEAVflaDRVVVL 205
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
748-903 |
1.24e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 64.86 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 748 LDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRNVGTiTGDMLVDGLPMD--ASFKRRTGYVQQQDLHVAELTVKESLQ 825
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPT-AGQIMLDGVDLShvPPYQRPINMMFQSYALFPHMTVEQNIA 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767243141 826 FSARMRRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLDEPTSGLDSQ 903
Cdd:PRK11607 114 FGLKQDK---LPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGG----QRQRVALARSLAKRPKLLL-LDEPMGALDKK 183
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
743-915 |
1.27e-10 |
|
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: 62.66 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 743 GQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrNVGTIT-GDMLVDGLPM-DASFKRR-TGYVQQQDLHVAELT 819
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIA--GLEEPTsGRIYIGGRDVtDLPPKDRdIAMVFQNYALYPHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 820 VKESLQFSARMRRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLDEPTSG 899
Cdd:cd03301 89 VYDNIAFGLKLRK---VPKDEIDERVREVAELLQIEHLLDRKPKQLSGG----QRQRVALGRAIVREPKVFL-MDEPLSN 160
|
170
....*....|....*.
gi 767243141 900 LDSQSAWAVVKMLKRL 915
Cdd:cd03301 161 LDAKLRVQMRAELKRL 176
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
45-267 |
1.56e-10 |
|
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: 62.89 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGctsflKSAAGETSQFAGGVTTGHISYDGIPQKEM-MQHYKPDVIYNGEQDVHFphl 123
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSG-----KSTLTKLIQRFYVPENGRVLVDGHDLALAdPAWLRRQVGVVLQENVLF--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 124 tvKQTLDFAISCKMPAKRVNNVTKEEYITANREFyakIFGLTHTFDTKVGNDFiSGVSGGERKRVSIAEALAAKGSIYCW 203
Cdd:cd03252 89 --NRSIRDNIALADPGMSMERVIEAAKLAGAHDF---ISELPEGYDTIVGEQG-AGLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767243141 204 DNATRGLDSstalEFARAI-RTMTNLL-GTTALVTVYQASenIYETFDKVIVLYAGRQIFCGKTTE 267
Cdd:cd03252 163 DEATSALDY----ESEHAImRNMHDICaGRTVIIIAHRLS--TVKNADRIIVMEKGRIVEQGSHDE 222
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
732-916 |
1.59e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.18 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIphssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqRNVGTITGDMLVDGLPMDASFKR---RTGYV 808
Cdd:COG4604 5 KNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIS-RLLPPDSGEVLVDGLDVATTPSRelaKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 809 QQQDLHV-AELTVKESLQFSarmRRPQS--IPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVG 885
Cdd:COG4604 80 LRQENHInSRLTVRELVAFG---RFPYSkgRLTAEDREIIDEAIAYLDLEDLADRYLDELSGG----QRQRAFIAMVLAQ 152
|
170 180 190
....*....|....*....|....*....|.
gi 767243141 886 KPDLLLfLDEPTSGLDSQSAWAVVKMLKRLA 916
Cdd:COG4604 153 DTDYVL-LDEPLNNLDMKHSVQMMKLLRRLA 182
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
743-928 |
2.01e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.06 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 743 GQRKLLDSVSGYCVPGTLTALIGESGAGKTTLL---NTLAQRNVGTIT-------------GDMLVDGLPMDASFKRRTG 806
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLrciNFLEKPSEGSIVvngqtinlvrdkdGQLKVADKNQLRLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 807 YVQQQDLHVAELTVKESLqfsarMRRPQSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGLNVEQRKKLSIGVELVGK 886
Cdd:PRK10619 96 MVFQHFNLWSHMTVLENV-----MEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767243141 887 PDLLLFlDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQ 928
Cdd:PRK10619 171 PEVLLF-DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
45-270 |
2.65e-10 |
|
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: 61.68 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSqfaggVTTGHISYDG-----IPQKEMMQH---YKPDviyngEQ 116
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP-----PRSGSIRFDGrditgLPPHERARAgigYVPE-----GR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 117 DVhFPHLTVKQTLDFAISCKMPAKRvnnvtkeeyitanREFYAKIFGLthtF-------DTKVGNdfisgVSGGERKRVS 189
Cdd:cd03224 85 RI-FPELTVEENLLLGAYARRRAKR-------------KARLERVYEL---FprlkerrKQLAGT-----LSGGEQQMLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 190 IAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMtNLLGTTALVtVYQASENIYETFDKVIVLYAGRQIFCGKTTEAK 269
Cdd:cd03224 143 IARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILL-VEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
.
gi 767243141 270 D 270
Cdd:cd03224 221 A 221
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
426-576 |
3.14e-10 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 60.98 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 426 GVLFFSLLYYSLMGLA-NISFEHRpilqkHKVYSLY-----HPSAEALASTISSFPFRMIGLTFFIIILYFLAGLHRSAG 499
Cdd:COG0842 8 GLLAMSLLFTALMLTAlSIARERE-----QGTLERLlvtpvSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767243141 500 AFFTMYLLLTMCSEAITSLFQMVSSLCDTLSQANSIAGVVMLSIAMYSTYMIQLPSMHPWFKWISYILPIRYAFESM 576
Cdd:COG0842 83 SLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEAL 159
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
732-927 |
3.20e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.45 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTipHSSG---QRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRNVGTiTGDMLVDGLPMDA--------S 800
Cdd:PRK13649 6 QNVSYT--YQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPT-QGSVRVDDTLITStsknkdikQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 801 FKRRTGYVQQ-QDLHVAELTVKESLQFSarmrrPQ----SIPDAEKMEYvEKiisiLEMQEFSEALVGEIGYGLNVEQRK 875
Cdd:PRK13649 83 IRKKVGLVFQfPESQLFEETVLKDVAFG-----PQnfgvSQEEAEALAR-EK----LALVGISESLFEKNPFELSGGQMR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767243141 876 KLSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIH 927
Cdd:PRK13649 153 RVAIAGILAMEPKILV-LDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
45-289 |
3.51e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.07 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTTGHISYDGI----PQKEMMQHYKPDVIYNGEQDVHF 120
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsQQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 121 PHLTVkqtLDFAISCKMPAKRVnnvTKEEYITANREFYAKIfGLTHTFDTkvgndFISGVSGGERKRVSIAEALAAKGSI 200
Cdd:PRK11264 98 PHRTV---LENIIEGPVIVKGE---PKEEATARARELLAKV-GLAGKETS-----YPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 201 YCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQASENiyETFDKVIVLYAGRQIFCGkttEAKDYFENmgylcP 280
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFAR--DVADRAIFMDQGRIVEQG---PAKALFAD-----P 235
|
....*....
gi 767243141 281 PRQSTAEYL 289
Cdd:PRK11264 236 QQPRTRQFL 244
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
45-267 |
5.16e-10 |
|
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: 63.63 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSqfaggVTTGHISYDGIPqkemMQHYKPDVIYNG----EQDVHF 120
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD-----PQSGSITLGGVD----LRDLDEDDLRRRiavvPQRPHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 121 PHLTVKQTLDFAisckmpakrVNNVTKEEYITANR-----EFYAkifGLTHTFDTKVGNDFiSGVSGGERKRVSIAEALA 195
Cdd:COG4987 421 FDTTLRENLRLA---------RPDATDEELWAALErvglgDWLA---ALPDGLDTWLGEGG-RRLSGGERRRLALARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767243141 196 AKGSIYCWDNATRGLDSSTalefARAIrtMTNLLGTTA-----LVTvYQASENiyETFDKVIVLYAGRQIFCGKTTE 267
Cdd:COG4987 488 RDAPILLLDEPTEGLDAAT----EQAL--LADLLEALAgrtvlLIT-HRLAGL--ERMDRILVLEDGRIVEQGTHEE 555
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
43-254 |
6.13e-10 |
|
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: 60.62 E-value: 6.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQfaggvTTGHISYDGIPQKEMMQH--YKPDviyNGEQDVHF 120
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKP-----TSGSIRVFGKPLEKERKRigYVPQ---RRSIDRDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 121 PhLTVKQTLDFAISCKM-PAKRVNNVTKEEYITAnrefyAKIFGLTHtfdtkVGNDFISGVSGGERKRVSIAEALAAKGS 199
Cdd:cd03235 84 P-ISVRDVVLMGLYGHKgLFRRLSKADKAKVDEA-----LERVGLSE-----LADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767243141 200 IYCWDNATRGLDSSTALEFARAIRTMtNLLGTTALVTVY--QASENIyetFDKVIVL 254
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHdlGLVLEY---FDRVLLL 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
43-260 |
6.74e-10 |
|
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: 60.35 E-value: 6.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAG-ETsqfaggVTTGHISYDG-----IPQKE-----MMQHYkpdVI 111
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGlEE------PTSGRIYIGGrdvtdLPPKDrdiamVFQNY---AL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 112 YngeqdvhfPHLTVKQTLDFAIsckmpakRVNNVTKEEyITANREFYAKIFGLTHTFDTKVgndfiSGVSGGERKRVSIA 191
Cdd:cd03301 84 Y--------PHMTVYDNIAFGL-------KLRKVPKDE-IDERVREVAELLQIEHLLDRKP-----KQLSGGQRQRVALG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767243141 192 EALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTAL-VTVYQAseniyETF---DKVIVLYAGR--QI 260
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIyVTHDQV-----EAMtmaDRIAVMNDGQiqQI 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
732-946 |
1.06e-09 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 60.39 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHSsgqRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLaQRNVGTITGDMLVDGLPMDA----SFKRRTGY 807
Cdd:cd03295 4 ENVTKRYGGG---KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI-NRLIEPTSGEIFIDGEDIREqdpvELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 808 VQQQDLHVAELTVKE------SLQFSARMRRPQSIpdAEKMEYVEkiisiLEMQEFSEALVGEIGYGlnveQRKKLSIGV 881
Cdd:cd03295 80 VIQQIGLFPHMTVEEnialvpKLLKWPKEKIRERA--DELLALVG-----LDPAEFADRYPHELSGG----QQQRVGVAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767243141 882 ELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRL-ALAGQSILCTIHQpsatLFEQF---DRLLLLGKG 946
Cdd:cd03295 149 ALAADPPLLL-MDEPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHD----IDEAFrlaDRIAIMKNG 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
735-949 |
1.28e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.97 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 735 SFTIPHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRnvgtitgdmlvdglpmdASFKRRTGYVQQQDLH 814
Cdd:COG2401 33 AFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA-----------------LKGTPVAGCVDVPDNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 815 VA-ELTVKESLQfsarmrRPQSIPDAekmeyvekiISILEMQEFSEA-----LVGEIGYGlnveQRKKLSIGVELVGKPD 888
Cdd:COG2401 96 FGrEASLIDAIG------RKGDFKDA---------VELLNAVGLSDAvlwlrRFKELSTG----QKFRFRLALLLAERPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767243141 889 LLLfLDEPTSGLDSQSAWAVVKMLKRLA--LAGQSILCTiHQPSATLFEQFDRLLLLGKGGQT 949
Cdd:COG2401 157 LLV-IDEFCSHLDRQTAKRVARNLQKLArrAGITLVVAT-HHYDVIDDLQPDLLIFVGYGGVP 217
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
741-929 |
1.55e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 59.04 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 741 SSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLA--QRnvgTITGDMLVDGLPMD---ASFKRRTGYVQQQDLHV 815
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAglSP---PLAGRVLLNGGPLDfqrDSIARGLLYLGHAPGIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 816 AELTVKESLQFSARMRRPQSIPDAekmeyvekiISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLDE 895
Cdd:cd03231 86 TTLSVLENLRFWHADHSDEQVEEA---------LARVGLNGFEDRPVAQLSAG----QQRRVALARLLLSGRPLWI-LDE 151
|
170 180 190
....*....|....*....|....*....|....
gi 767243141 896 PTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQP 929
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
732-927 |
1.61e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.48 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHSSgqrKLLDSVSGYCVPGTLTALIGESGAGKTTL---LNTLAQRNVGTItgdmLVDGLPMDASFK-----R 803
Cdd:PRK13639 5 RDLKYSYPDGT---EALKGINFKAEKGEMVALLGPNGAGKSTLflhFNGILKPTSGEV----LIKGEPIKYDKKsllevR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 804 RT-GYV-QQQDLHVAELTVKESLQFSarmrrPQSIpdAEKMEYVEKIISilemqefsEAL--VGEIGYG------LNVEQ 873
Cdd:PRK13639 78 KTvGIVfQNPDDQLFAPTVEEDVAFG-----PLNL--GLSKEEVEKRVK--------EALkaVGMEGFEnkpphhLSGGQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767243141 874 RKKLSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIH 927
Cdd:PRK13639 143 KKRVAIAGILAMKPEIIV-LDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
732-954 |
1.70e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.87 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTI-PHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTL---LNTLAQRNVGTI------------------TGD 789
Cdd:PRK13651 6 KNIVKIFnKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALLLPDTGTIewifkdeknkkktkekekVLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 790 MLVDGLPMDASFK------RRTGYVQQ-QDLHVAELTVKESLQFSARmrrPQSIPDAEKMEYVEKIIsilEMQEFSEALV 862
Cdd:PRK13651 86 KLVIQKTRFKKIKkikeirRRVGVVFQfAEYQLFEQTIEKDIIFGPV---SMGVSKEEAKKRAAKYI---ELVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 863 GEIGYGLNVEQRKKLSIGVELVGKPDLLlFLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSATLfEQFDRLLL 942
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFL-VFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVL-EWTKRTIF 237
|
250
....*....|..
gi 767243141 943 LgKGGQTIYFGE 954
Cdd:PRK13651 238 F-KDGKIIKDGD 248
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
732-964 |
1.72e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 62.05 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTL-------------AQRNVGTITGDMLvdglpmd 798
Cdd:PRK10535 8 KDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptsgtyrvAGQDVATLDADAL------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 799 ASFKRRT-GYVQQQDLHVAELTVKESLQFSArmrrpqsipdaekmeyVEKIISILEMQEFSEALVGEIGYGLNVE----- 872
Cdd:PRK10535 81 AQLRREHfGFIFQRYHLLSHLTAAQNVEVPA----------------VYAGLERKQRLLRAQELLQRLGLEDRVEyqpsq 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 873 ----QRKKLSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPsaTLFEQFDRLLllgkggq 948
Cdd:PRK10535 145 lsggQQQRVSIARALMNGGQVIL-ADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP--QVAAQAERVI------- 214
|
250
....*....|....*.
gi 767243141 949 TIYFGEIGKNSSSVIK 964
Cdd:PRK10535 215 EIRDGEIVRNPPAQEK 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
755-919 |
2.04e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 59.64 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 755 CVPGTLTALIGESGAGKTTLLNTLaqrNVGTI--TGDMLVDGLPMDAS----------FKRRTGYV-QQQDL--HvaeLT 819
Cdd:PRK11124 25 CPQGETLVLLGPSGAGKSSLLRVL---NLLEMprSGTLNIAGNHFDFSktpsdkaireLRRNVGMVfQQYNLwpH---LT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 820 VKESLqFSARMrRPQSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLFlDEPTSG 899
Cdd:PRK11124 99 VQQNL-IEAPC-RVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGG----QQQRVAIARALMMEPQVLLF-DEPTAA 171
|
170 180
....*....|....*....|
gi 767243141 900 LDSQSAWAVVKMLKRLALAG 919
Cdd:PRK11124 172 LDPEITAQIVSIIRELAETG 191
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
743-927 |
2.25e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 59.64 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 743 GQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqRNVGTITGDMLVDGLPM----DASFKRRTGYVQQQDLHVAEL 818
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RLLTPQSGTVFLGDKPIsmlsSRQLARRLALLPQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 819 TVKESLQFSarmRRPQ-------SIPDAEKmeyVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLL 891
Cdd:PRK11231 92 TVRELVAYG---RSPWlslwgrlSAEDNAR---VNQAMEQTRINHLADRRLTDLSGG----QRQRAFLAMVLAQDTPVVL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 767243141 892 fLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIH 927
Cdd:PRK11231 162 -LDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLH 196
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
727-915 |
2.63e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 61.57 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 727 GVFIWKNVSFTIPhssGQRKL-LDSVSGYCVPGTLTALIGESGAGKTTLLNtLAQRNVGTITGDMLVDGLPMD----ASF 801
Cdd:PRK11176 340 GDIEFRNVTFTYP---GKEVPaLRNINFKIPAGKTVALVGRSGSGKSTIAN-LLTRFYDIDEGEILLDGHDLRdytlASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 802 KRRTGYVQQQdLHVAELTVKESLQFSARMR--RPQsIPDAEKMEYVEKIISilEMQEFSEALVGEIGYGLNVEQRKKLSI 879
Cdd:PRK11176 416 RNQVALVSQN-VHLFNDTIANNIAYARTEQysREQ-IEEAARMAYAMDFIN--KMDNGLDTVIGENGVLLSGGQRQRIAI 491
|
170 180 190
....*....|....*....|....*....|....*.
gi 767243141 880 GVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRL 915
Cdd:PRK11176 492 ARALLRDSPILI-LDEATSALDTESERAIQAALDEL 526
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
732-923 |
2.96e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.19 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLAqrnvGTIT---GDMLVDGL------PMDAsfk 802
Cdd:COG1129 21 DGVSLELR-----------------PGEVHALLGENGAGKSTLMKILS----GVYQpdsGEILLDGEpvrfrsPRDA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 803 RRTG-YVQQQDLH-VAELTVKESLqFSARMRRPQSIPDAEKMEyvekiisilemqEFSEALVGEIGYGLNVEQR-KKLSI 879
Cdd:COG1129 77 QAAGiAIIHQELNlVPNLSVAENI-FLGREPRRGGLIDWRAMR------------RRARELLARLGLDIDPDTPvGDLSV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767243141 880 G----VE----LVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSIL 923
Cdd:COG1129 144 AqqqlVEiaraLSRDARVLI-LDEPTASLTEREVERLFRIIRRLKAQGVAII 194
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
46-263 |
3.12e-09 |
|
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: 58.53 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 46 LKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTTghisyDGIPQKEMMQHYKPDVIYNGEQDVHFPHLTV 125
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV-----DGFDVVKEPAEARRRLGFVSDSTGLYDRLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 126 KQTLDFAisckmpaKRVNNVTKEEyITANREFYAKIFGLTHTFDTKVGndfisGVSGGERKRVSIAEALAAKGSIYCWDN 205
Cdd:cd03266 96 RENLEYF-------AGLYGLKGDE-LTARLEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767243141 206 ATRGLD---SSTALEFARAIRTmtnlLGTTALVTVYQASEnIYETFDKVIVLYAGRQIFCG 263
Cdd:cd03266 163 PTTGLDvmaTRALREFIRQLRA----LGKCILFSTHIMQE-VERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
732-953 |
3.21e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 59.36 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHSSgqrKLLDSVSGYCVPGTLTALIGESGAGKTTLL---N--TLAQRnvgtitGDMLVDGLPMDAS----FK 802
Cdd:PRK13647 8 EDLHFRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLlhlNgiYLPQR------GRVKVMGREVNAEnekwVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 803 RRTGYV-QQQDLHVAELTVKESLQFSArmrRPQSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGV 881
Cdd:PRK13647 79 SKVGLVfQDPDDQVFSSTVWDDVAFGP---VNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYG----QKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767243141 882 ELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSATLfEQFDRLLLLgKGGQTIYFG 953
Cdd:PRK13647 152 VLAMDPDVIV-LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVL-KEGRVLAEG 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
758-927 |
3.37e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 59.48 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 758 GTLTALIGESGAGKTTLLNTLaQRNVGTITGDMLVDGLPMDASFK------RRTGYV-QQQDLHVAELTVKESLQFSARM 830
Cdd:PRK13636 32 GEVTAILGGNGAGKSTLFQNL-NGILKPSSGRILFDGKPIDYSRKglmklrESVGMVfQDPDNQLFSASVYQDVSFGAVN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 831 RRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVK 910
Cdd:PRK13636 111 LK---LPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFG----QKKRVAIAGVLVMEPKVLV-LDEPTAGLDPMGVSEIMK 182
|
170
....*....|....*...
gi 767243141 911 MLKRLALA-GQSILCTIH 927
Cdd:PRK13636 183 LLVEMQKElGLTIIIATH 200
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
727-902 |
3.53e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.13 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 727 GVFIWKNVSFTIPhssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLaQRNVGTITGDMLVDGlpMD------AS 800
Cdd:PRK13657 333 GAVEFDDVSFSYD---NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL-QRVFDPQSGRILIDG--TDirtvtrAS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 801 FKRRTGYVQQQDLHVAElTVKESLQF------SARMRRPQSIpdAEKMEYVEKIISILemqefsEALVGEIGYGLNVEQR 874
Cdd:PRK13657 407 LRRNIAVVFQDAGLFNR-SIEDNIRVgrpdatDEEMRAAAER--AQAHDFIERKPDGY------DTVVGERGRQLSGGER 477
|
170 180
....*....|....*....|....*...
gi 767243141 875 KKLSIGVELVGKPDLLLfLDEPTSGLDS 902
Cdd:PRK13657 478 QRLAIARALLKDPPILI-LDEATSALDV 504
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
732-923 |
3.79e-09 |
|
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: 57.05 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLAqrnvGTIT---GDMLVDGlpmdasfkrrtgyv 808
Cdd:cd03216 17 DGVSLSVR-----------------RGEVHALLGENGAGKSTLMKILS----GLYKpdsGEILVDG-------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 809 qqqdlhvaeltvkeslqfsarmrRPQSIPdaekmeyvekiiSILEMQEFSEALVgeigYGLNVEQRKKLSIGVELVGKPD 888
Cdd:cd03216 62 -----------------------KEVSFA------------SPRDARRAGIAMV----YQLSVGERQMVEIARALARNAR 102
|
170 180 190
....*....|....*....|....*....|....*
gi 767243141 889 LLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSIL 923
Cdd:cd03216 103 LLI-LDEPTAALTPAEVERLFKVIRRLRAQGVAVI 136
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
758-946 |
4.38e-09 |
|
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: 57.89 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 758 GTLTALIGESGAGKTTLLNTLAQRNVGTiTGDMLVDGLPMDAS--FKRRTGYVQQQDLHVAELTVKESLQFSarmRRPQS 835
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQ-SGRVLINGVDVTAAppADRPVSMLFQENNLFAHLTVEQNVGLG---LSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 836 IPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELV-GKPDLLlfLDEPTSGLDSQSAWAVVKMLKR 914
Cdd:cd03298 100 KLTAEDRQAIEVALARVGLAGLEKRLPGELSGG----ERQRVALARVLVrDKPVLL--LDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|...
gi 767243141 915 L-ALAGQSILCTIHQPSATLfEQFDRLLLLGKG 946
Cdd:cd03298 174 LhAETKMTVLMVTHQPEDAK-RLAQRVVFLDNG 205
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
746-927 |
4.54e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.70 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 746 KLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRNVGTiTGDMLVDGLPMdaSFKRRTGYVQQ------QDLH-VAEL 818
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD-AGSILIDGQEM--RFASTTAALAAgvaiiyQELHlVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 819 TVKESL---QFSARMrrpqsipdaekmeyveKIISILEMQEFSEALVGEIGYGLNVEQR-KKLSIG----VElVGKPDLL 890
Cdd:PRK11288 95 TVAENLylgQLPHKG----------------GIVNRRLLNYEAREQLEHLGVDIDPDTPlKYLSIGqrqmVE-IAKALAR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767243141 891 ----LFLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIH 927
Cdd:PRK11288 158 narvIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
741-929 |
4.87e-09 |
|
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: 57.75 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 741 SSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLA--QRNVGtitGDMLVDGLPMD---ASFKRRTGYVQQQDLHV 815
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAglLRPDS---GEVRWNGTPLAeqrDEPHENILYLGHLPGLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 816 AELTVKESLQFSARMRRPQSIPDAEKMEYVekiisilEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLDE 895
Cdd:TIGR01189 86 PELSALENLHFWAAIHGGAQRTIEDALAAV-------GLTGFEDLPAAQLSAG----QQRRLALARLWLSRRPLWI-LDE 153
|
170 180 190
....*....|....*....|....*....|....
gi 767243141 896 PTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQP 929
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
29-267 |
5.04e-09 |
|
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: 58.32 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 29 IIKGIRERKnrnkmkiILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSqfaggVTTGHISYDG--IPQKEMMQHY 106
Cdd:cd03218 6 LSKRYGKRK-------VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVK-----PDSGKILLDGqdITKLPMHKRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 107 KPDVIYNGEQDVHFPHLTVKQTLdfaisckMPAKRVNNVTKEEyITANREFYAKIFGLTHTFDTKVgndfiSGVSGGERK 186
Cdd:cd03218 74 RLGIGYLPQEASIFRKLTVEENI-------LAVLEIRGLSKKE-REEKLEELLEEFHITHLRKSKA-----SSLSGGERR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 187 RVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNlLGTTALVTVYQASENIyETFDKVIVLYAGRQIFCGKTT 266
Cdd:cd03218 141 RVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETL-SITDRAYIIYEGKVLAEGTPE 218
|
.
gi 767243141 267 E 267
Cdd:cd03218 219 E 219
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
46-258 |
5.13e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.42 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 46 LKNVSLLAKSGEMVLVLGRPGAGctsflKSA-AGETSQFAGgVTTGHISYDGIPqkemMQHYKPDVIYNG----EQDVHF 120
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSG-----KSTiANLLTRFYD-IDEGEILLDGHD----LRDYTLASLRNQvalvSQNVHL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 121 PHLTVKQTLDFAisckmpakRVNNVTKEEYITANREFYAKIF--GLTHTFDTKVGNDFISgVSGGERKRVSIAEALAAKG 198
Cdd:PRK11176 429 FNDTIANNIAYA--------RTEQYSREQIEEAARMAYAMDFinKMDNGLDTVIGENGVL-LSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767243141 199 SIYCWDNATRGLDSstalEFARAIRTMTNLL--GTTALVTVYQASenIYETFDKVIVLYAGR 258
Cdd:PRK11176 500 PILILDEATSALDT----ESERAIQAALDELqkNRTSLVIAHRLS--TIEKADEILVVEDGE 555
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
740-901 |
6.65e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.40 E-value: 6.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 740 HSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQR---NVGTITGDM----LVDGLPMDASFKR---RT--GY 807
Cdd:PRK11701 14 KLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARlapDAGEVHYRMrdgqLRDLYALSEAERRrllRTewGF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 808 VQQQDLHVAELTVKESLQFSARM-----RRPQSIPD--AEKMEYVEkiISILEMQEFSEALVGeigyGLnveqRKKLSIG 880
Cdd:PRK11701 94 VHQHPRDGLRMQVSAGGNIGERLmavgaRHYGDIRAtaGDWLERVE--IDAARIDDLPTTFSG----GM----QQRLQIA 163
|
170 180
....*....|....*....|.
gi 767243141 881 VELVGKPDlLLFLDEPTSGLD 901
Cdd:PRK11701 164 RNLVTHPR-LVFMDEPTGGLD 183
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
732-946 |
7.01e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 60.22 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqRNVGTITGDMLVDGLPMDA---SFKRRTGYV 808
Cdd:PRK11160 342 NNVSFTYPD--QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT-RAWDPQQGEILLNGQPIADyseAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 809 QQQDLHVAELTVKESLQFSArmrrPQSIpDAEKMEYVEKI--ISILEMQEFSEALVGEIGYGLNVEQRKKLSIGVELVGK 886
Cdd:PRK11160 419 VSQRVHLFSATLRDNLLLAA----PNAS-DEALIEVLQQVglEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHD 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 887 PDLLLfLDEPTSGLDSQSAWAVVKMLKRLAlAGQSILCTIHQpsATLFEQFDRLLLLGKG 946
Cdd:PRK11160 494 APLLL-LDEPTEGLDAETERQILELLAEHA-QNKTVLMITHR--LTGLEQFDRICVMDNG 549
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
43-263 |
8.32e-09 |
|
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: 56.67 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSqfaggVTTGHISYDGIPqkemMQHYKPDVIyngeqdvhfph 122
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK-----PSSGEILLDGKD----LASLSPKEL----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 123 ltvkqtldfaisckmpAKRVNNVTkeeyiTANREFyakifGLTHtFDTKvgndFISGVSGGERKRVSIAEALAAKGSIYC 202
Cdd:cd03214 72 ----------------ARKIAYVP-----QALELL-----GLAH-LADR----PFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767243141 203 WDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVY---QASenIYetFDKVIVLYAGRQIFCG 263
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHdlnLAA--RY--ADRVILLKDGRIVAQG 180
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
737-927 |
8.35e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 58.36 E-value: 8.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 737 TIPHSSGQRKLLDSVsgYCVP-GTLTALIGESGAGKTTLLNTLAQRnVGTITGDMLVDGLPMDASFKRR-TGYVQQQD-- 812
Cdd:PRK15056 13 TVTWRNGHTALRDAS--FTVPgGSIAALVGVNGSGKSTLFKALMGF-VRLASGKISILGQPTRQALQKNlVAYVPQSEev 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 813 -----LHVAELTVKESLQFSARMRRPQsipdAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKP 887
Cdd:PRK15056 90 dwsfpVLVEDVVMMGRYGHMGWLRRAK----KRDRQIVTAALARVDMVEFRHRQIGELSGG----QKKRVFLARAIAQQG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767243141 888 DLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIH 927
Cdd:PRK15056 162 QVIL-LDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
738-946 |
8.68e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 58.94 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 738 IPHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLA---QRNVGTIT-GDMLVDGLpmdASFKRRTGYVQQqdl 813
Cdd:PRK10851 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAgleHQTSGHIRfHGTDVSRL---HARDRKVGFVFQ--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 814 HVA---ELTVKESLQFSARM--RRPQsiPDAEKMEYveKIISILEMQEFSEaLVGEIGYGLNVEQRKKLSIGVELVGKPD 888
Cdd:PRK10851 82 HYAlfrHMTVFDNIAFGLTVlpRRER--PNAAAIKA--KVTQLLEMVQLAH-LADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767243141 889 LLLfLDEPTSGLDSQsawaVVKMLKRL------ALAGQSILCTIHQPSATlfEQFDRLLLLGKG 946
Cdd:PRK10851 157 ILL-LDEPFGALDAQ----VRKELRRWlrqlheELKFTSVFVTHDQEEAM--EVADRVVVMSQG 213
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
732-946 |
1.01e-08 |
|
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: 57.12 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLaQRNVGTITGDMLVDGLPMdasfkrrtgyvQQQ 811
Cdd:cd03244 21 KNISFSIK-----------------PGEKVGIVGRTGSGKSSLLLAL-FRLVELSSGSILIDGVDI-----------SKI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 812 DLHV--AELTV--KESLQFSARMRrpQSI-PDAEKMEyvEKIISILE---MQEFSEALVG-------EIGYGLNVEQRKK 876
Cdd:cd03244 72 GLHDlrSRISIipQDPVLFSGTIR--SNLdPFGEYSD--EELWQALErvgLKEFVESLPGgldtvveEGGENLSVGQRQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 877 LSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLkRLALAGQSILCTIHQPSATLfeQFDRLLLLGKG 946
Cdd:cd03244 148 LCLARALLRKSKILV-LDEATASVDPETDALIQKTI-REAFKDCTVLTIAHRLDTII--DSDRILVLDKG 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
741-945 |
1.41e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 57.23 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 741 SSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLaQRNV-----GTITGDMLVDG---LPMDAS-FKRRTGYVQQQ 811
Cdd:PRK14247 12 SFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-NRLIelypeARVSGEVYLDGqdiFKMDVIeLRRRVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 812 DLHVAELTVKESLQFSARMRRPQSipdaEKMEYVEKIISILEMQEFSEALVGEIGY---GLNVEQRKKLSIGVELVGKPD 888
Cdd:PRK14247 91 PNPIPNLSIFENVALGLKLNRLVK----SKKELQERVRWALEKAQLWDEVKDRLDApagKLSGGQQQRLCIARALAFQPE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767243141 889 LLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSATLFEQFDRLLLLGK 945
Cdd:PRK14247 167 VLL-ADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQ 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
760-946 |
1.48e-08 |
|
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: 59.64 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 760 LTALIGESGAGKTTLLNTLAQRNVGTiTGDMLVDGLPMDASF---KRRTGYVQQQDLHVAELTVKESLQFSARMRrPQSI 836
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPPT-SGTVLVGGKDIETNLdavRQSLGMCPQHNILFHHLTVAEHILFYAQLK-GRSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 837 PDAEkmeyvekiisiLEMqefsEALVGEIG--YGLNVEQR-------KKLSIGVELVGKPDLLLfLDEPTSGLDSQSAWA 907
Cdd:TIGR01257 1036 EEAQ-----------LEM----EAMLEDTGlhHKRNEEAQdlsggmqRKLSVAIAFVGDAKVVV-LDEPTSGVDPYSRRS 1099
|
170 180 190
....*....|....*....|....*....|....*....
gi 767243141 908 VVKMLKRLALAGQSILCTIHQPSATLFEqfDRLLLLGKG 946
Cdd:TIGR01257 1100 IWDLLLKYRSGRTIIMSTHHMDEADLLG--DRIAIISQG 1136
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
744-928 |
1.57e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 57.33 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 744 QRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrnvGTITGDMLVDG--------------LPMDASFKR-RTGYV 808
Cdd:PRK09984 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLS----GLITGDKSAGShiellgrtvqregrLARDIRKSRaNTGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 809 QQQDLHVAELTVKESLQFSARMRRP------QSIPDAEKMEYVEKIISIlEMQEFSEALVGEIGYGlnveQRKKLSIGVE 882
Cdd:PRK09984 92 FQQFNLVNRLSVLENVLIGALGSTPfwrtcfSWFTREQKQRALQALTRV-GMVHFAHQRVSTLSGG----QQQRVAIARA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767243141 883 LVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALA-GQSILCTIHQ 928
Cdd:PRK09984 167 LMQQAKVIL-ADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQ 212
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
732-915 |
1.70e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.50 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHSsgQRKLLDSVSGYCVPGTLTALIGESGAGKTT---LLNTLA---QRNVGTITgdmlVDGLPMDA----SF 801
Cdd:PRK13640 9 KHVSFTYPDS--KKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLlpdDNPNSKIT----VDGITLTAktvwDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 802 KRRTGYV-QQQDLHVAELTVKESLQFSARMRrpqSIPDAEKMEYVEKIISILEMQEFSEAlvgEIGYgLNVEQRKKLSIG 880
Cdd:PRK13640 83 REKVGIVfQNPDNQFVGATVGDDVAFGLENR---AVPRPEMIKIVRDVLADVGMLDYIDS---EPAN-LSGGQKQRVAIA 155
|
170 180 190
....*....|....*....|....*....|....*
gi 767243141 881 VELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRL 915
Cdd:PRK13640 156 GILAVEPKIII-LDESTSMLDPAGKEQILKLIRKL 189
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
732-953 |
3.27e-08 |
|
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: 54.63 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHSSGQrkLLDSVSGYCVPGTLTALIGESGAGKTTLLntlaqrnvGTITGDMlvdglpmdasfKRRTGYVQQQ 811
Cdd:cd03247 4 NNVSFSYPEQEQQ--VLKNLSLELKQGEKIALLGRSGSGKSTLL--------QLLTGDL-----------KPQQGEITLD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 812 DLHVAELTvkeslqfsarmrrpqsipdaekmEYVEKIISILEMQE--FSEALVGEIGYGLNVEQRKKLSIGVELVGKPDL 889
Cdd:cd03247 63 GVPVSDLE-----------------------KALSSLISVLNQRPylFDTTLRNNLGRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767243141 890 LLfLDEPTSGLDSQSAWAVVKMLKRlALAGQSILCTIHQPSAtlFEQFDRLLLLgKGGQTIYFG 953
Cdd:cd03247 120 VL-LDEPTVGLDPITERQLLSLIFE-VLKDKTLIWITHHLTG--IEHMDKILFL-ENGKIIMQG 178
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
743-905 |
3.35e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.94 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 743 GQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRN----VGTITGDMLVDGLPMDA------SFKRRTGYVQQQD 812
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpEVTITGSIVYNGHNIYSprtdtvDLRKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 813 lHVAELTVKESLQFSARMRrpqSIPDAEKM-EYVEKIISILEMQEFSEALVGEIGYGLNVEQRKKLSIGVELVGKPDLLL 891
Cdd:PRK14239 96 -NPFPMSIYENVVYGLRLK---GIKDKQVLdEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170
....*....|....
gi 767243141 892 fLDEPTSGLDSQSA 905
Cdd:PRK14239 172 -LDEPTSALDPISA 184
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
731-927 |
3.66e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 56.38 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 731 WKNVSFTI-PHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLL---NTLAQRNVGTITgdmlVDGLPMDAS------ 800
Cdd:PRK13641 5 FENVDYIYsPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMqhfNALLKPSSGTIT----IAGYHITPEtgnknl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 801 --FKRRTGYV-QQQDLHVAELTVKESLQFSarmrrPQSIPDAEKmEYVEKIISILEMQEFSEALVGEIGYGLNVEQRKKL 877
Cdd:PRK13641 81 kkLRKKVSLVfQFPEAQLFENTVLKDVEFG-----PKNFGFSED-EAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767243141 878 SIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIH 927
Cdd:PRK13641 155 AIAGVMAYEPEILC-LDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
30-263 |
5.31e-08 |
|
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: 55.42 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 30 IKGIRERKNRNKmkIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTTGHIsydgIPQKEMMQHYKPD 109
Cdd:cd03267 23 LKSLFKRKYREV--EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKRRKKFLRRI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 110 VIYNGEQDVHFPHLTVKQTLDFAisckmpaKRVNNVTKEEYiTANREFYAKIFGLTHTFDTKVGNdfisgVSGGERKRVS 189
Cdd:cd03267 97 GVVFGQKTQLWWDLPVIDSFYLL-------AAIYDLPPARF-KKRLDELSELLDLEELLDTPVRQ-----LSLGQRMRAE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767243141 190 IAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQAsENIYETFDKVIVLYAGRQIFCG 263
Cdd:cd03267 164 IAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYM-KDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
56-258 |
5.98e-08 |
|
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: 54.81 E-value: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 56 GEMVLVLGRPGAGCTSFLKSAAG-ETSQFaGGVTTGHISYDGIPQKEmmqhyKPDVIYNGEQDVhFPHLTVKQTLDFAIS 134
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGfETPQS-GRVLINGVDVTAAPPAD-----RPVSMLFQENNL-FAHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 135 ckmPAKRVNNVTKEEYITANREfyakiFGLTHTFDTKVGNdfisgVSGGERKRVSIAEALAAKGSIYCWDNATRGLDSST 214
Cdd:cd03298 97 ---PGLKLTAEDRQAIEVALAR-----VGLAGLEKRLPGE-----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767243141 215 ALEFARAIRTMTNLLGTTALVTVYQASEnIYETFDKVIVLYAGR 258
Cdd:cd03298 164 RAEMLDLVLDLHAETKMTVLMVTHQPED-AKRLAQRVVFLDNGR 206
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
730-929 |
7.92e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 54.69 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 730 IWKNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTLAQRNVGTIT-GDMLVDG-----LPMDASFKR 803
Cdd:COG0396 15 ILKGVNLTIK-----------------PGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTsGSILLDGedileLSPDERARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 804 RTGYVQQQDLHVAELTVKESLQFSARMRRPQSIPDAEKMEYVEKIISILEM-QEFSEAlvgeigyGLNVE----QRKKLS 878
Cdd:COG0396 78 GIFLAFQYPVEIPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLdEDFLDR-------YVNEGfsggEKKRNE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767243141 879 IGVELVGKPDLLLfLDEPTSGLDsqsAWA---VVKMLKRLALAGQSILCTIHQP 929
Cdd:COG0396 151 ILQMLLLEPKLAI-LDETDSGLD---IDAlriVAEGVNKLRSPDRGILIITHYQ 200
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
743-915 |
8.34e-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: 8.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 743 GQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTL-AQRNVGTITGDMLVDGLPMDASFKRRT-----GYVQQQDLHVA 816
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILsGVYPHGTWDGEIYWSGSPLKASNIRDTeragiVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 817 ELTVKESLQFSARMRRPQSIPDAEKMEY-VEKIISILEMQEFSEAL-VGEIGYGlnveQRKKLSIGVELvGKPDLLLFLD 894
Cdd:TIGR02633 92 ELSVAENIFLGNEITLPGGRMAYNAMYLrAKNLLRELQLDADNVTRpVGDYGGG----QQQLVEIAKAL-NKQARLLILD 166
|
170 180
....*....|....*....|.
gi 767243141 895 EPTSGLDSQSAWAVVKMLKRL 915
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDL 187
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
41-249 |
8.54e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.90 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 41 KMKIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTtghISYDGIPQKEMMQHYKPDVIYNGEQDVHF 120
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNII---IDDEDISLLPLHARARRGIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 121 PHLTVKQTLDFAISCKmpakrvNNVTKEEYITANREFYAKiFGLTHtfdtkVGNDFISGVSGGERKRVSIAEALAAKGSI 200
Cdd:PRK10895 91 RRLSVYDNLMAVLQIR------DDLSAEQREDRANELMEE-FHIEH-----LRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767243141 201 YCWDNATRGLDSSTALEFARAIRTMTNlLGTTALVTvyqaSENIYETFD 249
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRD-SGLGVLIT----DHNVRETLA 202
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
748-942 |
8.89e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 54.71 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 748 LDSVSGYCVPGTLTALIGESGAGKTTLLNTLA---QRNVGTITgdmlVDGLPMDASFKRRtGYVQQQDLHVAELTVKESL 824
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAgfvPYQHGSIT----LDGKPVEGPGAER-GVVFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 825 QFSARMRrpqSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLDEPTSGLDSQS 904
Cdd:PRK11248 92 AFGLQLA---GVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGG----QRQRVGIARALAANPQLLL-LDEPFGALDAFT 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 767243141 905 AWAVVKMLKRL-ALAGQSILCTIHQPSATLFEQFDRLLL 942
Cdd:PRK11248 164 REQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLL 202
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
56-235 |
1.00e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.33 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 56 GEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTTG-HISYdgipqkemmqhyKPDVIyngEQDVHfphLTVKQTLDFAIS 134
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlKISY------------KPQYI---SPDYD---GTVEEFLRSANT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 135 CKMPAKRVnnvtKEEYItanrefyaKIFGLTHTFDTKVgndfiSGVSGGERKRVSIAEALAAKGSIYCWDNATRGLDSST 214
Cdd:COG1245 428 DDFGSSYY----KTEII--------KPLGLEKLLDKNV-----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
170 180
....*....|....*....|.
gi 767243141 215 ALEFARAIRTMTNLLGTTALV 235
Cdd:COG1245 491 RLAVAKAIRRFAENRGKTAMV 511
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
741-947 |
1.04e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 56.00 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 741 SSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrnvGTIT---GDMLVDGLPMDA----SFKRRTGYVQQQDL 813
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAIN----GTLTptaGTVLVAGDDVEAlsarAASRRVASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 814 HVAELTVKESLQFSarmRRPQ----SIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDL 889
Cdd:PRK09536 88 LSFEFDVRQVVEMG---RTPHrsrfDTWTETDRAAVERAMERTGVAQFADRPVTSLSGG----ERQRVLLARALAQATPV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767243141 890 LLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHqpSATLFEQF-DRLLLLGKGG 947
Cdd:PRK09536 161 LL-LDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIH--DLDLAARYcDELVLLADGR 216
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
758-998 |
1.20e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 758 GTLTALIGESGAGKTTLLNTlaqrnvgtitgdMLVDGLPMDAS---FKRRTGYVQQQDLhVAELTVKESLQFSARMrRPQ 834
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISA------------MLGELSHAETSsvvIRGSVAYVPQVSW-IFNATVRENILFGSDF-ESE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 835 SIPDAEKMEYVEKIISILEMQEFSEalVGEIGYGLNVEQRKKLSIGVELVGKPDLLLFlDEPTSGLDSQSAWAVVKMLKR 914
Cdd:PLN03232 709 RYWRAIDVTALQHDLDLLPGRDLTE--IGERGVNISGGQKQRVSMARAVYSNSDIYIF-DDPLSALDAHVAHQVFDSCMK 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 915 LALAGQSILCTIHQpsATLFEQFDRLLLLGKG--GQTIYFGEIGKNSSSVIKYFEKNGARKCQQNENPAEYILEAIGAGA 992
Cdd:PLN03232 786 DELKGKTRVLVTNQ--LHFLPLMDRIILVSEGmiKEEGTFAELSKSGSLFKKLMENAGKMDATQEVNTNDENILKLGPTV 863
|
....*.
gi 767243141 993 TASVQQ 998
Cdd:PLN03232 864 TIDVSE 869
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
37-258 |
1.33e-07 |
|
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: 53.63 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 37 KNRNKMKIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTT-GHISYdgIPQKEMMQhykpdviyNGe 115
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVpGSIAY--VSQEPWIQ--------NG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 116 qdvhfphlTVKQTLDFAisckmpakrvnnvtkEEYitaNREFYAKIF---GLTHTFD-------TKVGNDFISgVSGGER 185
Cdd:cd03250 81 --------TIRENILFG---------------KPF---DEERYEKVIkacALEPDLEilpdgdlTEIGEKGIN-LSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767243141 186 KRVSIAEALAAKGSIYCWDNATRGLDSSTALE-FARAIRTMTNLLGTTALVT--VYQASEniyetFDKVIVLYAGR 258
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHiFENCILGLLLNNKTRILVThqLQLLPH-----ADQIVVLDNGR 204
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
757-930 |
1.36e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 54.37 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 757 PGTLTALIGESGAGKTTLL---NTLAQRNVGTIT-GDMLVDGlpmDASFKRRTGYVQQQDLHVA----------ELTVKE 822
Cdd:PRK11264 28 PGEVVAIIGPSGSGKTTLLrciNLLEQPEAGTIRvGDITIDT---ARSLSQQKGLIRQLRQHVGfvfqnfnlfpHRTVLE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 823 SLqfsarMRRPQSIPDAEKMEYVEKIISILemqefseALVG----EIGYG--LNVEQRKKLSIGVELVGKPDLLLFlDEP 896
Cdd:PRK11264 105 NI-----IEGPVIVKGEPKEEATARARELL-------AKVGlagkETSYPrrLSGGQQQRVAIARALAMRPEVILF-DEP 171
|
170 180 190
....*....|....*....|....*....|....
gi 767243141 897 TSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPS 930
Cdd:PRK11264 172 TSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
46-278 |
1.51e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 54.74 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 46 LKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTTGHISYDGIPQKEMMQ--HYKPDVIYNGEQDVHFPHL 123
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKpvRKKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 124 TVKQTL----DFAIScKMPAKRVNnVTKEEYITANREFYAKifgltHTFDtkvgndfisgVSGGERKRVSIAEALAAKGS 199
Cdd:PRK13643 102 VLKDVAfgpqNFGIP-KEKAEKIA-AEKLEMVGLADEFWEK-----SPFE----------LSGGQMRRVAIAGILAMEPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767243141 200 IYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTvyQASENIYETFDKVIVLYAGRQIFCGKTTeakDYFENMGYL 278
Cdd:PRK13643 165 VLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVT--HLMDDVADYADYVYLLEKGHIISCGTPS---DVFQEVDFL 238
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
732-915 |
1.75e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 54.25 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHSSgqRKLLDSVSGYCVPGTLTALIGESGAGKTTL---LNTLAQRNVGTITgdmlVDGLPMDAS----FKRR 804
Cdd:PRK13635 9 EHISFRYPDAA--TYALKDVSFSVYEGEWVAIVGHNGSGKSTLaklLNGLLLPEAGTIT----VGGMVLSEEtvwdVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 805 TGYV-QQQDLHVAELTVKESLQFSArmrRPQSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVEL 883
Cdd:PRK13635 83 VGMVfQNPDNQFVGATVQDDVAFGL---ENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGG----QKQRVAIAGVL 155
|
170 180 190
....*....|....*....|....*....|..
gi 767243141 884 VGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRL 915
Cdd:PRK13635 156 ALQPDIII-LDEATSMLDPRGRREVLETVRQL 186
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
40-263 |
1.77e-07 |
|
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: 52.70 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 40 NKMKIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTtghisydgipqkemmqhykpdviYNGeqdvh 119
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT-----------------------LDG----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 120 FPHLTVKQTLDFAISCkmpakrvnnVTKEEYItanrefyakifglthtFDTKVGNDFISGVSGGERKRVSIAEALAAKGS 199
Cdd:cd03247 64 VPVSDLEKALSSLISV---------LNQRPYL----------------FDTTLRNNLGRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767243141 200 IYCWDNATRGLDSSTALE----FARAIRTMTNLLGTTALVTVyqaseniyETFDKVIVLYAGRQIFCG 263
Cdd:cd03247 119 IVLLDEPTVGLDPITERQllslIFEVLKDKTLIWITHHLTGI--------EHMDKILFLENGKIIMQG 178
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
743-900 |
2.03e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.73 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 743 GQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRNVGTiTGDMLVDGlpmdasfKRRTGYVQQQDLHVAELTVKE 822
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRAT-SGRIVFDG-------KDITDWQTAKIMREAVAIVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 823 SLQFSARMRRPQSIPD----AEKMEYVEKIISILE----MQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLD 894
Cdd:PRK11614 88 GRRVFSRMTVEENLAMggffAERDQFQERIKWVYElfprLHERRIQRAGTMSGG----EQQMLAIGRALMSQPRLLL-LD 162
|
....*.
gi 767243141 895 EPTSGL 900
Cdd:PRK11614 163 EPSLGL 168
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
757-912 |
2.05e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.24 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 757 PGTLTALIGESGAGKTTLLNTLAQRNVGTiTGDMLVDGLP---MD----ASFK-RRTGYVQQQDLHVAELTVKESLQFSA 828
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDGS-SGEVSLVGQPlhqMDeearAKLRaKHVGFVFQSFMLIPTLNALENVELPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 829 RMRRPQsipDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnvEQrKKLSIGVELVGKPDlLLFLDEPTSGLDSQSAWAV 908
Cdd:PRK10584 114 LLRGES---SRQSRNGAKALLEQLGLGKRLDHLPAQLSGG---EQ-QRVALARAFNGRPD-VLFADEPTGNLDRQTGDKI 185
|
....
gi 767243141 909 VKML 912
Cdd:PRK10584 186 ADLL 189
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
758-902 |
2.35e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 54.34 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 758 GTLTALIGESGAGKTTLLNTLAQRNVGTiTGDMLVDGlpMDASfKRRtgyVQQQDLHVA--------ELTVKESLQFSAR 829
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRLVAGLEKPT-EGQIFIDG--EDVT-HRS---IQQRDICMVfqsyalfpHMSLGENVGYGLK 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767243141 830 MrrpQSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLFlDEPTSGLDS 902
Cdd:PRK11432 105 M---LGVPKEERKQRVKEALELVDLAGFEDRYVDQISGG----QQQRVALARALILKPKVLLF-DEPLSNLDA 169
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
761-901 |
2.70e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.11 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 761 TALIGESGAGKTTLLNTLA-----QRNVGTITGDMLVDG-----LPMDasfKRRTGYVQQQdlhvAEL----TVKESLQF 826
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISgltrpQKGRIVLNGRVLFDAekgicLPPE---KRRIGYVFQD----ARLfphyKVRGNLRY 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767243141 827 SarMrrpqsipdAEKM-EYVEKIISILEMqefsEALVGEIGYGLNVEQRKKLSIGVELVGKPDLLLfLDEPTSGLD 901
Cdd:PRK11144 100 G--M--------AKSMvAQFDKIVALLGI----EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLL-MDEPLASLD 160
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
43-214 |
3.09e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.16 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTTGHISYDGiPQKEMmqhykpDVIYngEQDVHFPH 122
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAER------GVVF--QNEGLLPW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 123 LTVKQTLDFAIsckmpakRVNNVTKEEYITANREFYAKIfGLThtfdtKVGNDFISGVSGGERKRVSIAEALAAKGSIYC 202
Cdd:PRK11248 85 RNVQDNVAFGL-------QLAGVEKMQRLEIAHQMLKKV-GLE-----GAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170
....*....|..
gi 767243141 203 WDNATRGLDSST 214
Cdd:PRK11248 152 LDEPFGALDAFT 163
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
764-901 |
4.29e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.75 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 764 IGESGAGKTTLLNTLaqrnvgtiTGdmLVD---------GLPMDA---SFKRRTGYVQQQ-DLHvAELTVKESLQFSARM 830
Cdd:NF033858 298 LGSNGCGKSTTMKML--------TG--LLPasegeawlfGQPVDAgdiATRRRVGYMSQAfSLY-GELTVRQNLELHARL 366
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767243141 831 RRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGLnveqRKKLSIGVELVGKPDLLLfLDEPTSGLD 901
Cdd:NF033858 367 FH---LPAAEIAARVAEMLERFDLADVADALPDSLPLGI----RQRLSLAVAVIHKPELLI-LDEPTSGVD 429
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
45-236 |
4.63e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 52.40 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSA-AGETsqfaggVTTGHISYDGIPqkemmqhykpdvIYNGEQDVH---- 119
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInKLEE------ITSGDLIVDGLK------------VNDPKVDERlirq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 120 -----------FPHLTVKQTLDFAisckmpAKRVNNVTKEEYITANREFYAKIfGLTHTfdtkvGNDFISGVSGGERKRV 188
Cdd:PRK09493 78 eagmvfqqfylFPHLTALENVMFG------PLRVRGASKEEAEKQARELLAKV-GLAER-----AHHYPSELSGGQQQRV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767243141 189 SIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVT 236
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVT 193
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
45-267 |
5.40e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 54.34 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGctsflKSAAGETSQFAGGVTTGHISYDGIPQKEMMQHY-KPDVIYNGEQDVHFPHl 123
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSG-----KSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYlHRQVALVGQEPVLFSG- 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 124 TVKQTLDFAIsckmpakrvNNVTKEEYITANREFYAKIF--GLTHTFDTKVGNDFiSGVSGGERKRVSIAEALAAKGSIY 201
Cdd:TIGR00958 570 SVRENIAYGL---------TDTPDEEIMAAAKAANAHDFimEFPNGYDTEVGEKG-SQLSGGQKQRIAIARALVRKPRVL 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767243141 202 CWDNATRGLD--SSTALEFARAIRTMTNLLGTTALVTVYQAseniyetfDKVIVLYAGRQIFCGKTTE 267
Cdd:TIGR00958 640 ILDEATSALDaeCEQLLQESRSRASRTVLLIAHRLSTVERA--------DQILVLKKGSVVEMGTHKQ 699
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
56-235 |
5.60e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 56 GEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTTG-HISYDgiPQkemmqhY-KPDviyngeqdvhfPHLTVKQTLDfai 133
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElKISYK--PQ------YiKPD-----------YDGTVEDLLR--- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 134 scKMPAKRVNNVTKEEYItanrefyaKIFGLTHTFDTKVGNdfisgVSGGERKRVSIAEALAAKGSIYCWDNATRGLDSS 213
Cdd:PRK13409 423 --SITDDLGSSYYKSEII--------KPLQLERLLDKNVKD-----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180
....*....|....*....|..
gi 767243141 214 TALEFARAIRTMTNLLGTTALV 235
Cdd:PRK13409 488 QRLAVAKAIRRIAEEREATALV 509
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
37-267 |
5.83e-07 |
|
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: 52.20 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 37 KNRNKMKIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAG-ETSqfaggvTTGHISYDG-----IPQKEM-------- 102
Cdd:cd03258 12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlERP------TSGSVLVDGtdltlLSGKELrkarrrig 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 103 M--QHY----KPDVIYNgeqdVHFPhltvkqtLDFAisckmpakrvnNVTKEEYITANREFYaKIFGLTHTfdtkvGNDF 176
Cdd:cd03258 86 MifQHFnllsSRTVFEN----VALP-------LEIA-----------GVPKAEIEERVLELL-ELVGLEDK-----ADAY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 177 ISGVSGGERKRVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQAsENIYETFDKVIVLYA 256
Cdd:cd03258 138 PAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEM-EVVKRICDRVAVMEK 216
|
250
....*....|.
gi 767243141 257 GRQIFCGKTTE 267
Cdd:cd03258 217 GEVVEEGTVEE 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
758-902 |
5.98e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 53.49 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 758 GTLTALIGESGAGKTTLLNTLAqrNVGTIT-GDMLVDGLPMD--ASFKRRTGYVQQQDLHVAELTVKESLQFSARMrrpQ 834
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIA--GLEDITsGDLFIGEKRMNdvPPAERGVGMVFQSYALYPHLSVAENMSFGLKL---A 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767243141 835 SIPDAEKMEYVEKIISILEMQEFSE----ALVGEigyglnveQRKKLSIGVELVGKPDLLLfLDEPTSGLDS 902
Cdd:PRK11000 104 GAKKEEINQRVNQVAEVLQLAHLLDrkpkALSGG--------QRQRVAIGRTLVAEPSVFL-LDEPLSNLDA 166
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
732-957 |
5.98e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 52.35 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFtiphSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRNvgTITGDMLVDGlpmDASFKRRTGYvqQQ 811
Cdd:PRK14258 11 NNLSF----YYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMN--ELESEVRVEG---RVEFFNQNIY--ER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 812 DLHVAELTVKESLQFSARMRRPQSI--------------PDAEKMEYVEKIISILEMQEFSEALVGEIGYGLNVEQRKKL 877
Cdd:PRK14258 80 RVNLNRLRRQVSMVHPKPNLFPMSVydnvaygvkivgwrPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 878 SIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQ--SILCTIHQPSATLFEQFDRLLLLGKG--GQTIYFG 953
Cdd:PRK14258 160 CIARALAVKPKVLL-MDEPCFGLDPIASMKVESLIQSLRLRSEltMVIVSHNLHQVSRLSDFTAFFKGNENriGQLVEFG 238
|
....
gi 767243141 954 EIGK 957
Cdd:PRK14258 239 LTKK 242
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
43-260 |
6.86e-07 |
|
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: 51.85 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTTGHISYDGIPQKE-----MMQHYkpdviyngeqd 117
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKrpvntVFQNY----------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 118 VHFPHLTVKQTLDFAIsckmpakRVNNVTKEEyITANREFYAKIFGLthtfdTKVGNDFISGVSGGERKRVSIAEALAAK 197
Cdd:cd03300 82 ALFPHLTVFENIAFGL-------RLKKLPKAE-IKERVAEALDLVQL-----EGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767243141 198 GSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQASENIYETfDKVIVLYAGR--QI 260
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMS-DRIAVMNKGKiqQI 212
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
738-955 |
7.22e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.63 E-value: 7.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 738 IPHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLA---QRNVGTIT-GDMLVDGLPMDASFKRRTGYVQQQDL 813
Cdd:PRK09700 11 IGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSgihEPTKGTITiNNINYNKLDHKLAAQLGIGIIYQELS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 814 HVAELTVKESLqFSARM--RRPQSIP--DAEKM-EYVEKIISILEMQEFSEALVGEigygLNVEQRKKLSIGVELVGKPD 888
Cdd:PRK09700 91 VIDELTVLENL-YIGRHltKKVCGVNiiDWREMrVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767243141 889 LLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQpSATLFEQFDRLLLLgKGGQTIYFGEI 955
Cdd:PRK09700 166 VII-MDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK-LAEIRRICDRYTVM-KDGSSVCSGMV 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
46-260 |
8.70e-07 |
|
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: 51.67 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 46 LKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSqfaggVTTGHISYDGipqkEMMQHYKPDVIYNGE-----QDVH- 119
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLR-----PTSGSVLFDG----EDITGLPPHEIARLGigrtfQIPRl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 120 FPHLTVKQTLDFAISCKMPAKRVNNVTKEEYITANR--EFYAKIFGLTHTFDTKVGNdfisgVSGGERKRVSIAEALAAK 197
Cdd:cd03219 87 FPELTVLENVMVAAQARTGSGLLLARARREEREAREraEELLERVGLADLADRPAGE-----LSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767243141 198 GSIYCWDNATRGLDSSTALEFARAIRTMtNLLGTTALVT------VYQASeniyetfDKVIVLYAGRQI 260
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVehdmdvVMSLA-------DRVTVLDQGRVI 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
46-274 |
9.71e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.00 E-value: 9.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 46 LKNVSLLAKSGEMVLVLGRPGAG-CTSFLksaagetsQFAGGV--TTGHISYDGIP----QKEMMQHYKPD--VIYNGEQ 116
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGkSTLFL--------HFNGILkpTSGEVLIKGEPikydKKSLLEVRKTVgiVFQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 117 DVHFPhlTVKQTLDFA-ISCKMPAKRVNNVTKEEYITANREFYAKifglthtfdtKVGNDFisgvSGGERKRVSIAEALA 195
Cdd:PRK13639 90 QLFAP--TVEEDVAFGpLNLGLSKEEVEKRVKEALKAVGMEGFEN----------KPPHHL----SGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 196 AKGSIYCWDNATRGLDSSTALEFARAI-----RTMTNLLGT--TALVTVYQaseniyetfDKVIVLYAGRQIfcgKTTEA 268
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLydlnkEGITIIISThdVDLVPVYA---------DKVYVMSDGKII---KEGTP 221
|
....*.
gi 767243141 269 KDYFEN 274
Cdd:PRK13639 222 KEVFSD 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
746-900 |
1.06e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.01 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 746 KLLDSVSGYCVPGTLTALIGESGAGKTTLLNTL-AQRNVGTITGDMLVDGLPMDASFKRRT---GYV--QQQDLHVAELT 819
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsGVYPHGTYEGEIIFEGEELQASNIRDTeraGIAiiHQELALVKELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 820 VKESLqFSARMRRPQSIPDAEKMeYVEkiisilemqefSEALVGEIGYGLNVEQR-KKLSIG----VEL---VGKPDLLL 891
Cdd:PRK13549 99 VLENI-FLGNEITPGGIMDYDAM-YLR-----------AQKLLAQLKLDINPATPvGNLGLGqqqlVEIakaLNKQARLL 165
|
....*....
gi 767243141 892 FLDEPTSGL 900
Cdd:PRK13549 166 ILDEPTASL 174
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
732-901 |
1.15e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 52.76 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIphssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrnvGTITgdmlvdglPMDASFKR----RTGY 807
Cdd:COG0488 319 EGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA----GELE--------PDSGTVKLgetvKIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 808 V-QQQD-LHVaELTVKESLQfsarmrrpQSIPDAEKMEyvekIISILEMQEFSealvGEigyglnvEQRKK---LSIGvE 882
Cdd:COG0488 383 FdQHQEeLDP-DKTVLDELR--------DGAPGGTEQE----VRGYLGRFLFS----GD-------DAFKPvgvLSGG-E 437
|
170 180
....*....|....*....|....*...
gi 767243141 883 ---------LVGKPDLLLfLDEPTSGLD 901
Cdd:COG0488 438 karlalaklLLSPPNVLL-LDEPTNHLD 464
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
43-277 |
1.19e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 50.60 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQfagGVTTGHISYDGIPQKEMMqhykpdviyngeqdvhfPH 122
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKY---EVTEGEILFKGEDITDLP-----------------PE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 123 LTVKqtLDFAISCKMPAkRVNNVTKEEYItanREFyakifglthtfdtkvgNDfisGVSGGERKRVSIAEALAAKGSIYC 202
Cdd:cd03217 73 ERAR--LGIFLAFQYPP-EIPGVKNADFL---RYV----------------NE---GFSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767243141 203 WDNATRGLDsSTALE-FARAIRTMTNLLGTTALVTVYQaseNI--YETFDKVIVLYAGRQIFCGKTTEAKDyFENMGY 277
Cdd:cd03217 128 LDEPDSGLD-IDALRlVAEVINKLREEGKSVLIITHYQ---RLldYIKPDRVHVLYDGRIVKSGDKELALE-IEKKGY 200
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
30-257 |
1.22e-06 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 50.72 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 30 IKGIRERKNRNKMkiILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQfaggvTTGHISYDG--IPQKE------ 101
Cdd:cd03226 2 IENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE-----SSGSILLNGkpIKAKErrksig 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 102 -MMQHykPDVIYNGEqdvhfphlTVKQTLDfaISCKMPAKRvnNVTKEEYItanREFYAKIFGLTHTFDtkvgndfisgV 180
Cdd:cd03226 75 yVMQD--VDYQLFTD--------SVREELL--LGLKELDAG--NEQAETVL---KDLDLYALKERHPLS----------L 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767243141 181 SGGERKRVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLlgTTALVTVYQASENIYETFDKVIVLYAG 257
Cdd:cd03226 128 SGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ--GKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
735-947 |
1.22e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.79 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 735 SFTIPHSsgQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLnTLAQRNVGTITGDMLVDGLPMDA----SFKRRTGYVQQ 810
Cdd:PRK10789 320 QFTYPQT--DHPALENVNFTLKPGQMLGICGPTGSGKSTLL-SLIQRHFDVSEGDIRFHDIPLTKlqldSWRSRLAVVSQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 811 QDLHVAElTVKESLQFSarmrRPQSIPdaEKMEYVEKIIS----ILEMQEFSEALVGEIGYGLNVEQRKKLSIGVELVGK 886
Cdd:PRK10789 397 TPFLFSD-TVANNIALG----RPDATQ--QEIEHVARLASvhddILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767243141 887 PDLLLfLDEPTSGLDSQSAWAVVKMLKRLAlAGQSILCTIHQPSAtLFEQfDRLLLLGKGG 947
Cdd:PRK10789 470 AEILI-LDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLSA-LTEA-SEILVMQHGH 526
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
731-927 |
1.34e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 51.70 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 731 WKNVSFTIPHSSG-QRKLLDSVSGYCVPGTLTALIGESGAGKTTL---LNTLAQRNVGTITgdmlVDGLPMDASFK---- 802
Cdd:PRK13646 5 FDNVSYTYQKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLiqnINALLKPTTGTVT----VDDITITHKTKdkyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 803 ----RRTGYV-QQQDLHVAELTVKESLQFSarmrrpqsiPDAEKMEyvekiisILEMQEFSEALVGEIGYGLNV------ 871
Cdd:PRK13646 81 rpvrKRIGMVfQFPESQLFEDTVEREIIFG---------PKNFKMN-------LDEVKNYAHRLLMDLGFSRDVmsqspf 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767243141 872 ----EQRKKLSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLAL-AGQSILCTIH 927
Cdd:PRK13646 145 qmsgGQMRKIAIVSILAMNPDIIV-LDEPTAGLDPQSKRQVMRLLKSLQTdENKTIILVSH 204
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
43-267 |
1.52e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.20 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTT-GHISYDGipqKEMMQ----HYKPDVIYNGEQD 117
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdGKVLYFG---KDIFQidaiKLRKEVGMVFQQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 118 VHFPHLTVKQTLDFaisckmPAKRVNNVTKEEYITANREFYAKIFGLTHTFDTKvgNDFISGVSGGERKRVSIAEALAAK 197
Cdd:PRK14246 100 NPFPHLSIYDNIAY------PLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRL--NSPASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767243141 198 GSIYCWDNATRGLD--SSTALEfaraiRTMTNLLGTTALVTVYQASENIYETFDKVIVLYAGRQIFCGKTTE 267
Cdd:PRK14246 172 PKVLLMDEPTSMIDivNSQAIE-----KLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNE 238
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
45-258 |
1.91e-06 |
|
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: 52.13 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGctsflKSAAG-------EtsqfaggVTTGHISYDGIPQKEMMQHYKPDVIynG--E 115
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAG-----KSTLArllfrfyD-------VTSGRILIDGQDIRDVTQASLRAAI--GivP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 116 QDvhfphlTV--KQTLDFAISCKMPakrvnNVTKEEYITANR-----EFyakIFGLTHTFDTKVGNdfiSGV--SGGERK 186
Cdd:COG5265 439 QD------TVlfNDTIAYNIAYGRP-----DASEEEVEAAARaaqihDF---IESLPDGYDTRVGE---RGLklSGGEKQ 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767243141 187 RVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNllGTTALV------TVYQAseniyetfDKVIVLYAGR 258
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLViahrlsTIVDA--------DEILVLEAGR 569
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
29-258 |
2.24e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 51.26 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 29 IIKGIRERKNRNkmkIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQfaggvTTGHISYDG-------IPQKE 101
Cdd:PRK11432 8 VLKNITKRFGSN---TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKP-----TEGQIFIDGedvthrsIQQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 102 M---MQHYkpdviyngeqdVHFPHLTVKQTLDFAIscKMpakrvNNVTKEEYITANREFYAKIfglthtfDTK-VGNDFI 177
Cdd:PRK11432 80 IcmvFQSY-----------ALFPHMSLGENVGYGL--KM-----LGVPKEERKQRVKEALELV-------DLAgFEDRYV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 178 SGVSGGERKRVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQASEnIYETFDKVIVLYAG 257
Cdd:PRK11432 135 DQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSE-AFAVSDTVIVMNKG 213
|
.
gi 767243141 258 R 258
Cdd:PRK11432 214 K 214
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
757-945 |
2.26e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.23 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 757 PGTLTALIGESGAGKTTLLNTLAqrnvGTI---TGDMLVDGLPM-DASFKRRTGYVQQQDLHVAELTVKESLQFSARM-- 830
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLA----GLLhveSGQIQIDGKTAtRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLhg 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 831 RRPQSIPDAEkmeyvekiISILEMQEFSEALVGEIGYGlnveQRKKLSIGvELVGKPDLLLFLDEPTSGLDSQSAWAVVK 910
Cdd:PRK13543 112 RRAKQMPGSA--------LAIVGLAGYEDTLVRQLSAG----QKKRLALA-RLWLSPAPLWLLDEPYANLDLEGITLVNR 178
|
170 180 190
....*....|....*....|....*....|....*
gi 767243141 911 MLKRLALAGQSILCTIHQPSATLFEQfDRLLLLGK 945
Cdd:PRK13543 179 MISAHLRGGGAALVTTHGAYAAPPVR-TRMLTLEA 212
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
45-215 |
2.60e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.20 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQfaggvTTGHISYDGIPQKEMMQHYKPDV-------IYngeqd 117
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTP-----TSGDVIFNGQPMSKLSSAAKAELrnqklgfIY----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 118 vHFPHLTVkqtlDFAI--SCKMPAkRVNNVTKEEYITANREFYAKIfGLTHTfdtkvGNDFISGVSGGERKRVSIAEALA 195
Cdd:PRK11629 94 -QFHHLLP----DFTAleNVAMPL-LIGKKKPAEINSRALEMLAAV-GLEHR-----ANHRPSELSGGERQRVAIARALV 161
|
170 180
....*....|....*....|
gi 767243141 196 AKGSIYCWDNATRGLDSSTA 215
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNA 181
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
732-901 |
4.25e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 49.73 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIphssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNT---LAQRNVGTITGDmlvDGLpmdasfkrRTGYV 808
Cdd:PRK09544 8 ENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVvlgLVAPDEGVIKRN---GKL--------RIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 809 QQQdLHV---AELTVKESLQFSARMRRPQSIPDAEKMEYVEKIISilEMQEFSEalvGEIgyglnveQRKKLSIGveLVG 885
Cdd:PRK09544 73 PQK-LYLdttLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDA--PMQKLSG---GET-------QRVLLARA--LLN 137
|
170
....*....|....*.
gi 767243141 886 KPDLLLfLDEPTSGLD 901
Cdd:PRK09544 138 RPQLLV-LDEPTQGVD 152
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
760-901 |
4.31e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 50.72 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 760 LTaLIGESGAGKTTLLNTLA---QRNVGTIT-GDMLVDGLPMDasfKRRTGYVQQQDLHVAELTVKESLQFSARMrrpQS 835
Cdd:PRK09452 43 LT-LLGPSGCGKTTVLRLIAgfeTPDSGRIMlDGQDITHVPAE---NRHVNTVFQSYALFPHMTVFENVAFGLRM---QK 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767243141 836 IPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLDEPTSGLD 901
Cdd:PRK09452 116 TPAAEITPRVMEALRMVQLEEFAQRKPHQLSGG----QQQRVAIARAVVNKPKVLL-LDESLSALD 176
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
745-799 |
4.93e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.83 E-value: 4.93e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767243141 745 RKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLA-------QRNVGTITGDMLVDGLPMDA 799
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltgggAPRGARVTGDVTLNGEPLAA 75
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
45-258 |
5.12e-06 |
|
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: 48.95 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAagetsqF-AGGVTTGHISYDGIPQKEMMQHYKPDVIYNGEQDvhfPHL 123
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILAL------FrFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQD---PTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 124 ---TVKQTLDfaisckmpakRVNNVTKEEYITANREfyakifglthtfdTKVGNDFisgvSGGERKRVSIAEALAAKGSI 200
Cdd:cd03369 94 fsgTIRSNLD----------PFDEYSDEEIYGALRV-------------SEGGLNL----SQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767243141 201 YCWDNATRGLDSSTALEFARAIRTMTNllGTTALVTVYQASENIyeTFDKVIVLYAGR 258
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTII--DYDKILVMDAGE 200
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
157-267 |
5.53e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 49.85 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 157 FYAKIFGLTHTFDTKvgNDFisGVSGGERKRVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTmTNLLGTTALVT 236
Cdd:PRK13631 158 FYLNKMGLDDSYLER--SPF--GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVI 232
|
90 100 110
....*....|....*....|....*....|.
gi 767243141 237 VYQAsENIYETFDKVIVLYAGRQIFCGKTTE 267
Cdd:PRK13631 233 THTM-EHVLEVADEVIVMDKGKILKTGTPYE 262
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
757-903 |
5.65e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 49.22 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 757 PGTLTALIGESGAGKTTLLNTLA---QRNVGTIT-GDMLVDGLPmdaSFK-RRTGYVQQ-QdlHV---AELTVKESLqFS 827
Cdd:PRK11300 30 EQEIVSLIGPNGAGKTTVFNCLTgfyKPTGGTILlRGQHIEGLP---GHQiARMGVVRTfQ--HVrlfREMTVIENL-LV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 828 ARMRRPQS--------IP-----DAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLD 894
Cdd:PRK11300 104 AQHQQLKTglfsgllkTPafrraESEALDRAATWLERVGLLEHANRQAGNLAYG----QQRRLEIARCMVTQPEILM-LD 178
|
....*....
gi 767243141 895 EPTSGLDSQ 903
Cdd:PRK11300 179 EPAAGLNPK 187
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
732-946 |
5.92e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 49.60 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHSSgqrKLLDSVSGYCVPGTLTALIGESGAGKTTL---LNTLAQRNVGTItgdmLVDGlpMDA-------SF 801
Cdd:PRK13644 5 ENVSYSYPDGT---PALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLRPQKGKV----LVSG--IDTgdfsklqGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 802 KRRTGYV-QQQDLHVAELTVKESLQFSarmrrPQSI--PDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLS 878
Cdd:PRK13644 76 RKLVGIVfQNPETQFVGRTVEEDLAFG-----PENLclPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGG----QGQCVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767243141 879 IGVELVGKPDLLLFlDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSAtlFEQFDRLLLLGKG 946
Cdd:PRK13644 147 LAGILTMEPECLIF-DEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE--LHDADRIIVMDRG 211
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
726-915 |
6.79e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.62 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 726 TGVFIWKNVSFTIPHSSG-QRKLLDSVSGYCVPGTLTALIGESGAGKTTLL---NTLAQRNVG-TITGDMLVDG----LP 796
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIqltNGLIISETGqTIVGDYAIPAnlkkIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 797 MDASFKRRTGYVQQ-QDLHVAELTVKESLQFSarmrrPQSIpDAEKMEYVEKIISILEMQEFSEALVGEIGYGLNVEQRK 875
Cdd:PRK13645 84 EVKRLRKEIGLVFQfPEYQLFQETIEKDIAFG-----PVNL-GENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767243141 876 KLSIG--VELVGKPdllLFLDEPTSGLDSQSAWAVVKMLKRL 915
Cdd:PRK13645 158 RVALAgiIAMDGNT---LVLDEPTGGLDPKGEEDFINLFERL 196
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
758-915 |
7.40e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 49.21 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 758 GTLTALIGESGAGKTTLLNTLAqRNVGTITGDMLVDGLPMD--AS--FKRRTGYVQQQDLHVAELTVKEslqFSARMRRP 833
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLS-RLMTPAHGHVWLDGEHIQhyASkeVARRIGLLAQNATTPGDITVQE---LVARGRYP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 834 -QSIPDAEKMEYVEKIISILEMQEFSEaLVGEIGYGLNVEQRKKLSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKML 912
Cdd:PRK10253 109 hQPLFTRWRKEDEEAVTKAMQATGITH-LADQSVDTLSGGQRQRAWIAMVLAQETAIML-LDEPTTWLDISHQIDLLELL 186
|
...
gi 767243141 913 KRL 915
Cdd:PRK10253 187 SEL 189
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
45-258 |
7.89e-06 |
|
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: 48.62 E-value: 7.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGctsflKSAAGETSQFAGGVTTGHISYDGIPQKEMMQHYKPDVIYNGEQDvhfPHLT 124
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSG-----KSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQE---PVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 125 VKQTLDfAISCKMPAKRVNNVTkEEYITANREFYakIFGLTHTFDTKVGNDFiSGVSGGERKRVSIAEALAAKGSIYCWD 204
Cdd:cd03248 101 ARSLQD-NIAYGLQSCSFECVK-EAAQKAHAHSF--ISELASGYDTEVGEKG-SQLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767243141 205 NATRGLDSSTALEFARAI----RTMTNLLGTTALVTVYQAseniyetfDKVIVLYAGR 258
Cdd:cd03248 176 EATSALDAESEQQVQQALydwpERRTVLVIAHRLSTVERA--------DQILVLDGGR 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
43-98 |
9.96e-06 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 48.61 E-value: 9.96e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSqfaggVTTGHISYDGIP 98
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELS-----PDSGEVRLNGRP 65
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
732-915 |
1.02e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 48.86 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTI-PHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTL---LNTLAQRNVGTIT-GDMLVDGLPMDASFK---R 803
Cdd:PRK13634 6 QKVEHRYqYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLlqhLNGLLQPTSGTVTiGERVITAGKKNKKLKplrK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 804 RTGYVQQQDLH-VAELTVKESLQFSarmrrPQS--IPDAEKMEYVEKIIsilEMQEFSEALVGEIGYGLNVEQRKKLSIG 880
Cdd:PRK13634 86 KVGIVFQFPEHqLFEETVEKDICFG-----PMNfgVSEEDAKQKAREMI---ELVGLPEELLARSPFELSGGQMRRVAIA 157
|
170 180 190
....*....|....*....|....*....|....*
gi 767243141 881 VELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRL 915
Cdd:PRK13634 158 GVLAMEPEVLV-LDEPTAGLDPKGRKEMMEMFYKL 191
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
754-946 |
1.27e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 48.69 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 754 YCVpgtltalIGESGAGKTTLL---NTLAQRNVGTITGDMLVDGlpMDASFKRRTGYVQQQDL-HVAEL--TVKESLQFS 827
Cdd:PRK13631 55 YFI-------IGNSGSGKSTLVthfNGLIKSKYGTIQVGDIYIG--DKKNNHELITNPYSKKIkNFKELrrRVSMVFQFP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 828 ARMRRPQSI-------PDA---EKMEYVEKIISILEMQEFSEALVGEIGYGLNVEQRKKLSIGVELVGKPDLLLFlDEPT 897
Cdd:PRK13631 126 EYQLFKDTIekdimfgPVAlgvKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIF-DEPT 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767243141 898 SGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSATLfEQFDRLLLLGKG 946
Cdd:PRK13631 205 AGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVL-EVADEVIVMDKG 252
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
48-211 |
1.45e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 49.06 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 48 NVSLLAKSGEMVLVLGRPGAGCTSFLKSAAG-ETSqfaggvTTGHISYDGI----------PQKEMMQHYkpdviyngeq 116
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQP------TAGQIMLDGVdlshvppyqrPINMMFQSY---------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 117 dVHFPHLTVKQTLDFAISC-KMPAKRVNNVTKEeyitanrefyakIFGLTHTfdtkvgNDFIS----GVSGGERKRVSIA 191
Cdd:PRK11607 101 -ALFPHMTVEQNIAFGLKQdKLPKAEIASRVNE------------MLGLVHM------QEFAKrkphQLSGGQRQRVALA 161
|
170 180
....*....|....*....|
gi 767243141 192 EALAAKGSIYCWDNATRGLD 211
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALD 181
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
745-916 |
1.47e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.55 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 745 RKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRNVGT----ITGDMLVDGLPM----DA-SFKRRTGYVQQQDlHV 815
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVsgyrYSGDVLLGGRSIfnyrDVlEFRRRVGMLFQRP-NP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 816 AELTVKESLQfsARMRRPQSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGLNVEQRKKLSIGVELVGKPDLLLfLDE 895
Cdd:PRK14271 113 FPMSIMDNVL--AGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL-LDE 189
|
170 180
....*....|....*....|.
gi 767243141 896 PTSGLDSQSAWAVVKMLKRLA 916
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLA 210
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
744-946 |
1.54e-05 |
|
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: 49.05 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 744 QRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRNVGTITGDMLVDGLPMDASF---------------KRRTGYV 808
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDIRNpaqairagiamvpedRKRHGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 809 QqqDLHVAELTVKESLQ-FSARMRrpqsIPDAEKMEYVEKIISILEMQEFSEALvgEIGyGLNVEQRKKLSIGVELVGKP 887
Cdd:TIGR02633 352 P--ILGVGKNITLSVLKsFCFKMR----IDAAAELQIIGSAIQRLKVKTASPFL--PIG-RLSGGNQQKAVLAKMLLTNP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767243141 888 DLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILcTIHQPSATLFEQFDRLLLLGKG 946
Cdd:TIGR02633 423 RVLI-LDEPTRGVDVGAKYEIYKLINQLAQEGVAII-VVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
120-290 |
1.58e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.91 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 120 FPHLTVKQTLdfAISCKMpakrvNNVTK-EEYITANREFYAKIFGLTHTFDTKVgNDFISGVSGGERKRVSIAEALAAKG 198
Cdd:PRK14267 97 FPHLTIYDNV--AIGVKL-----NGLVKsKKELDERVEWALKKAALWDEVKDRL-NDYPSNLSGGQRQRLVIARALAMKP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 199 SIYCWDNATRGLDSSTALEFARAIRTMTNLLgTTALVTVYQASENiyETFDKVIVLYAGRQIFCGKTTEAkdyFENmgyl 278
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKEY-TIVLVTHSPAQAA--RVSDYVAFLYLGKLIEVGPTRKV---FEN---- 238
|
170
....*....|..
gi 767243141 279 cPPRQSTAEYLT 290
Cdd:PRK14267 239 -PEHELTEKYVT 249
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
742-928 |
1.58e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 48.26 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 742 SGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrnvGTIT---GDMLVDGLPMDAS----FKRRTGYV-QQQDL 813
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFN----GILKptsGSVLIRGEPITKEnireVRKFVGLVfQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 814 HVAELTVKESLQFSarmrrPQSIP-DAEKMEY-VEKIISILEMQEFSEalvgEIGYGLNVEQRKKLSIGVELVGKPDLLL 891
Cdd:PRK13652 90 QIFSPTVEQDIAFG-----PINLGlDEETVAHrVSSALHMLGLEELRD----RVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 767243141 892 fLDEPTSGLDSQSAWAVVKMLKRLALA-GQSILCTIHQ 928
Cdd:PRK13652 161 -LDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQ 197
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
44-258 |
1.72e-05 |
|
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: 47.53 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 44 IILKNVSLLAKSGEMVLVLGRPGAGctsflKSAAGETSQFAGGVTTGHISYDGIPQKEMMQHYKPDVIYNGEQDvhfPHL 123
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCG-----KSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQE---PVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 124 ---TVKQTLDFAIsckmpakrvNNVTKEEYITANREFYAK--IFGLTHTFDTKVGnDFISGVSGGERKRVSIAEALAAKG 198
Cdd:cd03249 89 fdgTIAENIRYGK---------PDATDEEVEEAAKKANIHdfIMSLPDGYDTLVG-ERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767243141 199 SIYCWDNATRGLDSST------ALEfaRAIRTMTNLLGTTALVTVYQAseniyetfDKVIVLYAGR 258
Cdd:cd03249 159 KILLLDEATSALDAESeklvqeALD--RAMKGRTTIVIAHRLSTIRNA--------DLIAVLQNGQ 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
180-267 |
2.14e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 47.74 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 180 VSGGERKRVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTaLVTVYQASENIYETFDKVIVLYAGRQ 259
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMT-IILVSHSMEDVAKLADRIIVMNKGKC 223
|
....*...
gi 767243141 260 IFCGKTTE 267
Cdd:PRK13637 224 ELQGTPRE 231
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
732-901 |
2.18e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 47.74 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFT-IPHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTL---LNTLAQRNVGTItgdmLVDGL-PMDASFK---- 802
Cdd:PRK13637 6 ENLTHIyMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLiqhLNGLLKPTSGKI----IIDGVdITDKKVKlsdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 803 -RRTGYV-QQQDLHVAELTVKESLQFSARMRrpqSIPDAEKMEYVEKIISI--LEMQEFSEALVGEIGYGlnveQRKKLS 878
Cdd:PRK13637 82 rKKVGLVfQYPEYQLFEETIEKDIAFGPINL---GLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGG----QKRRVA 154
|
170 180
....*....|....*....|...
gi 767243141 879 IGVELVGKPDLLLfLDEPTSGLD 901
Cdd:PRK13637 155 IAGVVAMEPKILI-LDEPTAGLD 176
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
927-988 |
2.35e-05 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 48.36 E-value: 2.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767243141 927 HQPSATLFEQFDRLLLLGKGGQTIYFGEIGKnsssVIKYFEKNGArKCQQNENPAEY---ILEAI 988
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLTVYHGPVKK----VEEYFAGLGI-NVPERVNPPDHfidILEGI 60
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
743-929 |
2.54e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 46.72 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 743 GQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqrnvGTI---TGDMLVDGLPMdasfkRRTGYVQQQDL----HV 815
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILA----GLArpdAGEVLWQGEPI-----RRQRDEYHQDLlylgHQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 816 A----ELTVKESLQFSARMRRPQSipdaekmeyVEKIISILE---MQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPD 888
Cdd:PRK13538 83 PgiktELTALENLRFYQRLHGPGD---------DEALWEALAqvgLAGFEDVPVRQLSAG----QQRRVALARLWLTRAP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767243141 889 LLLfLDEPTSGLDSQSawavVKMLKRL----ALAGQSILCTIHQP 929
Cdd:PRK13538 150 LWI-LDEPFTAIDKQG----VARLEALlaqhAEQGGMVILTTHQD 189
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
44-274 |
2.80e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 48.10 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 44 IILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTTGHISYDGIPQKE-----MMQHYkpdVIYngeqdv 118
Cdd:PRK11000 17 VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAErgvgmVFQSY---ALY------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 119 hfPHLTVKQTLDFAISCKMPAK-----RVNNVtkeeyitanrefyAKIFGLTHTFDTKVgndfiSGVSGGERKRVSIAEA 193
Cdd:PRK11000 88 --PHLSVAENMSFGLKLAGAKKeeinqRVNQV-------------AEVLQLAHLLDRKP-----KALSGGQRQRVAIGRT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 194 LAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTAlvtvyqasenIYETFD---------KVIVLYAGRQIFCGK 264
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTM----------IYVTHDqveamtladKIVVLDAGRVAQVGK 217
|
250
....*....|
gi 767243141 265 TTEAKDYFEN 274
Cdd:PRK11000 218 PLELYHYPAN 227
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
762-946 |
4.77e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 47.79 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 762 ALIGESGAGKTTLLNTLAQRNVGTiTGDMLVDGLPMD----ASFKRRTGYVQQQDLHVAEltvkeslQFSARMRRPQSIP 837
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMGYYPLT-EGEIRLDGRPLSslshSVLRQGVAMVQQDPVVLAD-------TFLANVTLGRDIS 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 838 DA---EKMEYVEKIISILEMQEFSEALVGEIGYGLNVEQRKKLSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKr 914
Cdd:PRK10790 443 EEqvwQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILI-LDEATANIDSGTEQAIQQALA- 520
|
170 180 190
....*....|....*....|....*....|..
gi 767243141 915 lALAGQSILCTIHQPSATLFEQfDRLLLLGKG 946
Cdd:PRK10790 521 -AVREHTTLVVIAHRLSTIVEA-DTILVLHRG 550
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
732-913 |
5.28e-05 |
|
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: 44.75 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIphssGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQR---NVGTITgdmlvdglpmdASFKRRTGYV 808
Cdd:cd03221 4 ENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGElepDEGIVT-----------WGSTVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 809 QqqdlhvaeltvkeslQFSArmrrpqsipdaekmeyvekiisilemqefsealvGEigyglnveqRKKLSIGVELVGKPD 888
Cdd:cd03221 69 E---------------QLSG----------------------------------GE---------KMRLALAKLLLENPN 90
|
170 180
....*....|....*....|....*
gi 767243141 889 LLLfLDEPTSGLDSQSAWAVVKMLK 913
Cdd:cd03221 91 LLL-LDEPTNHLDLESIEALEEALK 114
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
757-901 |
6.17e-05 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 45.90 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 757 PGTLTALIGESGAGKTTLLNTLAqrnvGTIT---GDMLVDGLPMDAS----------FkrrtgyvQQQDL--HvaeLTVK 821
Cdd:COG3840 24 AGERVAILGPSGAGKSTLLNLIA----GFLPpdsGRILWNGQDLTALppaerpvsmlF-------QENNLfpH---LTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 822 E--SLQFSARMRrpqsIPDAEKmeyvEKIISILE---MQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLDEP 896
Cdd:COG3840 90 QniGLGLRPGLK----LTAEQR----AQVEQALErvgLAGLLDRLPGQLSGG----QRQRVALARCLVRKRPILL-LDEP 156
|
....*
gi 767243141 897 TSGLD 901
Cdd:COG3840 157 FSALD 161
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
43-215 |
8.57e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.97 E-value: 8.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGE--TSQFAGGVT-TGHISYDGIP------------QKEMMQHYK 107
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltGGGAPRGARvTGDVTLNGEPlaaidaprlarlRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 108 PDVIYNGEQDV---HFPHltvkqtldfaisckmpAKRVNNVTKEEyitanREFYAKIFGLTHTfDTKVGNDfISGVSGGE 184
Cdd:PRK13547 94 PAFAFSAREIVllgRYPH----------------ARRAGALTHRD-----GEIAWQALALAGA-TALVGRD-VTTLSGGE 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 767243141 185 RKRVSIAEALAakgSIYCWDNATRG-----LDSSTA 215
Cdd:PRK13547 151 LARVQFARVLA---QLWPPHDAAQPpryllLDEPTA 183
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
748-783 |
8.65e-05 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 46.47 E-value: 8.65e-05
10 20 30
....*....|....*....|....*....|....*.
gi 767243141 748 LDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRNV 783
Cdd:PRK01889 185 LDVLAAWLSGGKTVALLGSSGVGKSTLVNALLGEEV 220
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1063-1257 |
9.30e-05 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 46.23 E-value: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 1063 NYIMAKMMLLMISGLFIGFTFFHVGVNAIGLQNS-----------LFACFMAIVISAPATNQIQERATVAKELYEVresk 1131
Cdd:pfam12698 122 SLLQQLNASALVLLLEALSTSAPIPVESTPLFNPqsgyayylvglILMIIILIGAAIIAVSIVEEKESRIKERLLV---- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 1132 SNMFHWSLLLIthylNELPYHLLFSTIFFVSLYFPLGVFTEASRSSVFYLNYaILFQLYYIGLALMILYMSPNLQSANVI 1211
Cdd:pfam12698 198 SGVSPLQYWLG----KILGDFLVGLLQLLIILLLLFGIGIPFGNLGLLLLLF-LLYGLAYIALGYLLGSLFKNSEDAQSI 272
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767243141 1212 VGFILSFLLSFCGAVQPASLMPGFWTFMWKLSPYTYFLQNLVGLLM 1257
Cdd:pfam12698 273 IGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLRLIY 318
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
745-928 |
1.01e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.08 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 745 RKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTL-AQRNVGtiTGDMLVDglpmdasfkRRTGYVQQQDLhVAELTVKES 823
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLlSQFEIS--EGRVWAE---------RSIAYVPQQAW-IMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 824 LQFSARmRRPQSIPDAEKMEYVEKiisilEMQEFSEALVGEIG-YGLNVE--QRKKLSIGVELVGKPDLLLfLDEPTSGL 900
Cdd:PTZ00243 741 ILFFDE-EDAARLADAVRVSQLEA-----DLAQLGGGLETEIGeKGVNLSggQKARVSLARAVYANRDVYL-LDDPLSAL 813
|
170 180
....*....|....*....|....*...
gi 767243141 901 DSQSAWAVVKMLKRLALAGQSILCTIHQ 928
Cdd:PTZ00243 814 DAHVGERVVEECFLGALAGKTRVLATHQ 841
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
40-290 |
1.02e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 45.54 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 40 NKMKIiLKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTTGHISYDG----IP-------QKEM-MQHYK 107
Cdd:PRK14239 16 NKKKA-LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGhniySPrtdtvdlRKEIgMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 108 PD---------VIY----NGEQDvhfphltvKQTLDFAISCKMPAKRVNNVTKEeyitanrefyakifgltHTFDTKVGn 174
Cdd:PRK14239 95 PNpfpmsiyenVVYglrlKGIKD--------KQVLDEAVEKSLKGASIWDEVKD-----------------RLHDSALG- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 175 dfisgVSGGERKRVSIAEALAAKGSIYCWDNATRGLDSSTAlefARAIRTMTNLLGTTALVTVYQASENIYETFDKVIVL 254
Cdd:PRK14239 149 -----LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISA---GKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFF 220
|
250 260 270
....*....|....*....|....*....|....*.
gi 767243141 255 YAGRQIFCGKTteaKDYFENmgylcPPRQSTAEYLT 290
Cdd:PRK14239 221 LDGDLIEYNDT---KQMFMN-----PKHKETEDYIS 248
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
732-904 |
1.08e-04 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 45.41 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhssgqrklldsvsgycvPGTLTALIGESGAGKTTLLNTL-----AQRNVgTITGDMLVDGLP-----MD-AS 800
Cdd:COG1117 28 KDINLDIP-----------------ENKVTALIGPSGCGKSTLLRCLnrmndLIPGA-RVEGEILLDGEDiydpdVDvVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 801 FKRRTGYVQQQ---------DlHVAeltvkeslqFSARMRRPQSipDAEKMEYVEkiisilemqefsEALVG-----EI- 865
Cdd:COG1117 90 LRRRVGMVFQKpnpfpksiyD-NVA---------YGLRLHGIKS--KSELDEIVE------------ESLRKaalwdEVk 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767243141 866 ------GYGLNVEQRKKLSIGVELVGKPDLLLfLDEPTSGLDSQS 904
Cdd:COG1117 146 drlkksALGLSGGQQQRLCIARALAVEPEVLL-MDEPTSALDPIS 189
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
732-915 |
1.69e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 45.11 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIpHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTT---LLNTLAQRNvgtiTGDMLVDGLPMDAS----FKRR 804
Cdd:PRK13650 8 KNLTFKY-KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLEAE----SGQIIIDGDLLTEEnvwdIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 805 TGYV-QQQDLHVAELTVKESLQFSArmrRPQSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVEL 883
Cdd:PRK13650 83 IGMVfQNPDNQFVGATVEDDVAFGL---ENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGG----QKQRVAIAGAV 155
|
170 180 190
....*....|....*....|....*....|..
gi 767243141 884 VGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRL 915
Cdd:PRK13650 156 AMRPKIII-LDEATSMLDPEGRLELIKTIKGI 186
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
743-933 |
1.77e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 44.63 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 743 GQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLaqrnVGTIT---GDMLVDG-----LPMdasFKR-RTG--YVQQQ 811
Cdd:COG1137 14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMI----VGLVKpdsGRIFLDGedithLPM---HKRaRLGigYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 812 -----DLHVAE--LTVKESLQFSARMRRpqsipdaEKMEyvekiiSILEmqEFS-EALVGEIGYGLNVEQRKKLSIGVEL 883
Cdd:COG1137 87 asifrKLTVEDniLAVLELRKLSKKERE-------ERLE------ELLE--EFGiTHLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767243141 884 VGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSATL 933
Cdd:COG1137 152 ATNPKFIL-LDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETL 200
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
748-915 |
2.22e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 44.70 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 748 LDSVSGYCVPGTLTALIGESGAGKTT---LLNTLAQRNVGTITgdmlVDGLPMDA----SFKRRTGYV-QQQDLHVAELT 819
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLFEEFEGKVK----IDGELLTAenvwNLRRKIGMVfQNPDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 820 VKESLQFSArmrRPQSIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLDEPTSG 899
Cdd:PRK13642 99 VEDDVAFGM---ENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGG----QKQRVAVAGIIALRPEIII-LDESTSM 170
|
170
....*....|....*.
gi 767243141 900 LDSQSAWAVVKMLKRL 915
Cdd:PRK13642 171 LDPTGRQEIMRVIHEI 186
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
180-255 |
2.30e-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: 2.30e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767243141 180 VSGGERKRVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQASENIYETfDKVIVLY 255
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLS-DRIHVFE 146
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
43-275 |
2.69e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 45.22 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGetsqFAGgvTTGHISYDGIPQKEM-MQHYKPDVIYNGeQDVHFP 121
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG----FLP--YQGSLKINGIELRELdPESWRKHLSWVG-QNPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 122 HLTVKQTLDFAIScKMPAKRVNNVTKEEYITanrEFYAKifgLTHTFDTKVGnDFISGVSGGERKRVSIAEALAAKGSIY 201
Cdd:PRK11174 436 HGTLRDNVLLGNP-DASDEQLQQALENAWVS---EFLPL---LPQGLDTPIG-DQAAGLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 202 CWDNATRGLDS------STALEfaRAIRTMTNLLGTTALvtvyqasENIyETFDKVIVLYAGRQIFCGKTTE---AKDYF 272
Cdd:PRK11174 508 LLDEPTASLDAhseqlvMQALN--AASRRQTTLMVTHQL-------EDL-AQWDQIWVMQDGQIVQQGDYAElsqAGGLF 577
|
...
gi 767243141 273 ENM 275
Cdd:PRK11174 578 ATL 580
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
46-267 |
2.93e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 44.45 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 46 LKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQfaggvTTGHISYDGIP----QKEMMQHYKPDVIYNGEQDVHFP 121
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP-----SSGRILFDGKPidysRKGLMKLRESVGMVFQDPDNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 122 HLTVKQTLDF-AISCKMPA----KRVNNVTKEEyitanrefyakifGLTHTFDTKVgndfiSGVSGGERKRVSIAEALAA 196
Cdd:PRK13636 97 SASVYQDVSFgAVNLKLPEdevrKRVDNALKRT-------------GIEHLKDKPT-----HCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767243141 197 KGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQAseNIYETF-DKVIVLYAGRQIFCGKTTE 267
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDI--DIVPLYcDNVFVMKEGRVILQGNPKE 228
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
1153-1256 |
2.94e-04 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 43.65 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 1153 LLFSTIFFVSLYFPLGVFTEASRSSVFYLnYAILFQLYYIGLALMILYMSPNLQSANVIVGFILSFLLSFCGAVQPASLM 1232
Cdd:COG0842 61 LLQALLVLLVALLFFGVPLRGLSLLLLLL-VLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESL 139
|
90 100
....*....|....*....|....
gi 767243141 1233 PGFWTFMWKLSPYTYFLQNLVGLL 1256
Cdd:COG0842 140 PGWLQAIAYLNPLTYFVEALRALF 163
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
730-929 |
2.96e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 44.27 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 730 IWKNVSFTIPHSSgqrklldsvsgycvpgtLTALIGESGAGKTTLLNTLaQRNVGTITGDMLVDG---------LPMDA- 799
Cdd:PRK14246 25 ILKDITIKIPNNS-----------------IFGIMGPSGSGKSTLLKVL-NRLIEIYDSKIKVDGkvlyfgkdiFQIDAi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 800 SFKRRTGYVQQQDLHVAELTVKESLQFSARMRRPQSIPDAEKM--EYVEKIISILEMQEFSEALVGEIGYGlnveQRKKL 877
Cdd:PRK14246 87 KLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIveECLRKVGLWKEVYDRLNSPASQLSGG----QQQRL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767243141 878 SIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLAlAGQSILCTIHQP 929
Cdd:PRK14246 163 TIARALALKPKVLL-MDEPTSMIDIVNSQAIEKLITELK-NEIAIVIVSHNP 212
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
760-915 |
3.59e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.00 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 760 LTALIGESGAGKTTLL------NTLAQ--RNVGTIT--GDMLVDGLPMDASFKRRTGYVQQQDLHVAElTVKESLQFSAR 829
Cdd:PRK14243 38 ITAFIGPSGCGKSTILrcfnrlNDLIPgfRVEGKVTfhGKNLYAPDVDPVEVRRRIGMVFQKPNPFPK-SIYDNIAYGAR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 830 MRRPQSIPDaekmEYVEKIISILEMQEFSEALVGEIGYGLNVEQRKKLSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVV 909
Cdd:PRK14243 117 INGYKGDMD----ELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVIL-MDEPCSALDPISTLRIE 191
|
....*.
gi 767243141 910 KMLKRL 915
Cdd:PRK14243 192 ELMHEL 197
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
46-266 |
3.83e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 44.02 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 46 LKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTtghISYDGIPQKEM--MQHYKPDVIYNGEQDVHFPhl 123
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVL---IRGEPITKENIreVRKFVGLVFQNPDDQIFSP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 124 TVKQTLDFAisckmpakRVNNVTKEEYITANREFYAKIFGLTHTFDtKVGNDfisgVSGGERKRVSIAEALAAKGSIYCW 203
Cdd:PRK13652 95 TVEQDIAFG--------PINLGLDEETVAHRVSSALHMLGLEELRD-RVPHH----LSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767243141 204 DNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQAsENIYETFDKVIVLYAGRqiFCGKTT 266
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQL-DLVPEMADYIYVMDKGR--IVAYGT 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
32-236 |
3.89e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 43.41 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 32 GIRERKNRnkmKIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQfaggvttghisydgipqkemmqhyKPDVI 111
Cdd:COG2401 35 GVELRVVE---RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKG------------------------TPVAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 112 YNGEQDVHFPhltvkqtldfaisckmpakrvNNVTKEEYITANREFYAKIFGLThtfdtKVG-NDFI------SGVSGGE 184
Cdd:COG2401 88 CVDVPDNQFG---------------------REASLIDAIGRKGDFKDAVELLN-----AVGlSDAVlwlrrfKELSTGQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767243141 185 RKRVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVT 236
Cdd:COG2401 142 KFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVA 193
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
46-260 |
4.22e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 44.57 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 46 LKNVSLLAKSGEMVLVLGRPGAGctsflKSAAGETSQFAGGVTTGHISYDGIPQKEM----MQHYKPDVIyngeQDVHFP 121
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAG-----KSTLINLLQRVFDPQSGRILIDGTDIRTVtrasLRRNIAVVF----QDAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 122 HLTVKQTLdfaisckmpakRVN--NVTKEEYITANREFYAKIFGLTHT--FDTKVGNDFiSGVSGGERKRVSIAEALAAK 197
Cdd:PRK13657 422 NRSIEDNI-----------RVGrpDATDEEMRAAAERAQAHDFIERKPdgYDTVVGERG-RQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767243141 198 GSIYCWDNATRGLDSSTALEFARAIRTMTNllGTTALV------TVYQAseniyetfDKVIVLYAGRQI 260
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDELMK--GRTTFIiahrlsTVRNA--------DRILVFDNGRVV 548
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
43-194 |
4.34e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 44.17 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAG-ETsqfaggVTTGHISYDGipqkEMMQHYKPDviyngEQDVH-- 119
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGfET------PDSGRIMLDG----QDITHVPAE-----NRHVNtv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 120 ------FPHLTVKQTLDFAISCKmpakrvnNVTKEEyiTANREFYA-KIFGLTHTFDTKvgndfISGVSGGERKRVSIAE 192
Cdd:PRK09452 92 fqsyalFPHMTVFENVAFGLRMQ-------KTPAAE--ITPRVMEAlRMVQLEEFAQRK-----PHQLSGGQQQRVAIAR 157
|
..
gi 767243141 193 AL 194
Cdd:PRK09452 158 AV 159
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-89 |
4.84e-04 |
|
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: 43.29 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 4 VSVEGLDSSFLEGQTFGDILCLpwtiiKGIRERKNRNKMKIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQF 83
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKK-----LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPD 75
|
....*.
gi 767243141 84 AGGVTT 89
Cdd:cd03220 76 SGTVTV 81
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
757-946 |
6.07e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.59 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 757 PGTLTALIGESGAGKTTLLNTLAQrnvgtitgdmlvdglpmdasfkrrtgyvqqqdlhvaeltvkeslqfsarmrrpQSI 836
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAR-----------------------------------------------------ELG 27
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 837 PDAEKMEYVEkIISILEMQEFSEALVGEIGYGLNVEQRKKLSIGVELVGKPDL-LLFLDEPTSGLDSQSAWAVVKMLKRL 915
Cdd:smart00382 28 PPGGGVIYID-GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPdVLILDEITSLLDAEQEALLLLLEELR 106
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767243141 916 AL------AGQSILCTIHQP----SATLFEQFDRLLLLGKG 946
Cdd:smart00382 107 LLlllkseKNLTVILTTNDEkdlgPALLRRRFDRRIVLLLI 147
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
46-211 |
6.42e-04 |
|
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: 42.70 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 46 LKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTTGHISYDGIPQKEMMQHYKPDVIYnGEQDVHFPHLTV 125
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAY-AAQKPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 126 KQTLDFAisckmpakrvNNVTKEEY--ITANREFYAKIFGLTHTFDTKVGNDFISgVSGGERKRVSIAEALAAKGSIYCW 203
Cdd:cd03290 96 EENITFG----------SPFNKQRYkaVTDACSLQPDIDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFL 164
|
....*...
gi 767243141 204 DNATRGLD 211
Cdd:cd03290 165 DDPFSALD 172
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
732-915 |
6.47e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.93 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKT----TLLNTLAQRNVGTITGDMLVDGLPM-DASFKRRTG 806
Cdd:PRK15134 9 ENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVYPSGDIRFHGESLlHASEQTLRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 807 -------------YVQQQDLHVAELTVKESLQFSARMRRpqsipDAEKMEyvekIISILE----------MQEFSEALVG 863
Cdd:PRK15134 89 vrgnkiamifqepMVSLNPLHTLEKQLYEVLSLHRGMRR-----EAARGE----ILNCLDrvgirqaakrLTDYPHQLSG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767243141 864 eigyglnvEQRKKLSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRL 915
Cdd:PRK15134 160 --------GERQRVMIAMALLTRPELLI-ADEPTTALDVSVQAQILQLLREL 202
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
181-272 |
6.57e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 43.56 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 181 SGGERKRVSIAEALAAKGSIYCWDNATRGLDSS------TAL-----EFARAIRTMTNLLGTTALVTvyqaseniyetfD 249
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTvqaqimTLLnelkrEFNTAIIMITHDLGVVAGIC------------D 230
|
90 100
....*....|....*....|...
gi 767243141 250 KVIVLYAGRQIFCGKtteAKDYF 272
Cdd:PRK09473 231 KVLVMYAGRTMEYGN---ARDVF 250
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
43-267 |
6.85e-04 |
|
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: 42.55 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTTGHISYDGipqkemmqhykpDVIYNGEQDVH--- 119
Cdd:cd03260 13 KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDG------------KDIYDLDVDVLelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 120 ------------FPhLTVKQTLDFAisckmpaKRVNNVTKEEYITANREFYAKIFGLTHTFDTKVGNdfiSGVSGGERKR 187
Cdd:cd03260 81 rrvgmvfqkpnpFP-GSIYDNVAYG-------LRLHGIKLKEELDERVEEALRKAALWDEVKDRLHA---LGLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 188 VSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLgTTALVT--VYQASeniyETFDKVIVLYAGRQIFCGKT 265
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY-TIVIVThnMQQAA----RVADRTAFLLNGRLVEFGPT 224
|
..
gi 767243141 266 TE 267
Cdd:cd03260 225 EQ 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
45-259 |
7.67e-04 |
|
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: 41.82 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 45 ILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSqfaggVTTGHISYDGIP-QKEMMQHYKPDVIYNgEQDVHFphl 123
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR-----PTSGRVRLDGADiSQWDPNELGDHVGYL-PQDDEL--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 124 tvkqtldFAISckmpakrvnnvtkeeyITANrefyakIFglthtfdtkvgndfisgvSGGERKRVSIAEALAAKGSIYCW 203
Cdd:cd03246 88 -------FSGS----------------IAEN------IL------------------SGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767243141 204 DNATRGLDSSTALEFARAIRTMtNLLGTTALVTVYQASenIYETFDKVIVLYAGRQ 259
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPE--TLASADRILVLEDGRV 173
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
724-916 |
9.42e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 42.39 E-value: 9.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 724 ESTGVFIWKNVSFtiphSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRnVGTITGDMLVDGLPMDA---- 799
Cdd:PRK10247 3 ENSPLLQLQNVGY----LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASL-ISPTSGTLLFEGEDISTlkpe 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 800 SFKRRTGYVQQQDLHVAElTVKESLQFSARMRRPQSIPDA--EKMEYVEKIISILEmQEFSEALVGEigyglnvEQRKKL 877
Cdd:PRK10247 78 IYRQQVSYCAQTPTLFGD-TVYDNLIFPWQIRNQQPDPAIflDDLERFALPDTILT-KNIAELSGGE-------KQRISL 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 767243141 878 SIGVELVgkPDLLLfLDEPTSGLDSQSAWAVVKMLKRLA 916
Cdd:PRK10247 149 IRNLQFM--PKVLL-LDEITSALDESNKHNVNEIIHRYV 184
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
758-960 |
9.45e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.42 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 758 GTLTALIGESGAGKTT---LLNTLAQrnvgTITGDMLVDGLPMDAsfKRRTGYVQqqdlhvaeltvkeslQFSA------ 828
Cdd:PRK10522 349 GELLFLIGGNGSGKSTlamLLTGLYQ----PQSGEILLDGKPVTA--EQPEDYRK---------------LFSAvftdfh 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 829 ---RMRRPQSIPDAEKMeyVEKIISILEMQEFSEALVGEIgygLNVE----QRKKLSIGVELVGKPDLLLfLDEptsgld 901
Cdd:PRK10522 408 lfdQLLGPEGKPANPAL--VEKWLERLKMAHKLELEDGRI---SNLKlskgQKKRLALLLALAEERDILL-LDE------ 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 902 sqsaWAV-----------VKMLKRLALAGQSILCTIHQPSatLFEQFDRLLLLGKGGQTIYFGEIGKNSS 960
Cdd:PRK10522 476 ----WAAdqdphfrrefyQVLLPLLQEMGKTIFAISHDDH--YFIHADRLLEMRNGQLSELTGEERDAAS 539
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
760-889 |
1.05e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 40.40 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 760 LTALIGESGAGKTTLLNTLA----QRNVGTITGDMLVDGLPMDasfkRRTGYVQQqdLHVAELTVKESLQFSARMRRpqs 835
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRLLeqlpEVRDSVVFVDLPSGTSPKD----LLRALLRA--LGLPLSGRLSKEELLAALQQ--- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 767243141 836 ipdAEKMEYVEKIISILEMQEFSEALVGEIGYGLNVEQRkklSIGVELVGKPDL 889
Cdd:pfam13401 78 ---LLLALAVAVVLIIDEAQHLSLEALEELRDLLNLSSK---LLQLILVGTPEL 125
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
746-913 |
1.07e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.07 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 746 KLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLA---QRNVGTIT--GDMLVDGLPMDaSFKRRTGYVQQQDLHVAELTV 820
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTgiyTRDAGSILylGKEVTFNGPKS-SQEAGIGIIHQELNLIPQLTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 821 KESLQFSARMRRPQSIPDAEKMeYVE--KIISILEMQEFSEALVGE--IGYGLNVEQRKKLSIGVELVgkpdlllFLDEP 896
Cdd:PRK10762 97 AENIFLGREFVNRFGRIDWKKM-YAEadKLLARLNLRFSSDKLVGElsIGEQQMVEIAKVLSFESKVI-------IMDEP 168
|
170 180
....*....|....*....|
gi 767243141 897 TSGL---DSQSAWAVVKMLK 913
Cdd:PRK10762 169 TDALtdtETESLFRVIRELK 188
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
181-269 |
1.20e-03 |
|
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: 41.97 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 181 SGGERKRVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQASEnIYETFDKVIVLYAGRQI 260
Cdd:cd03265 133 SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEE-AEQLCDRVAIIDHGRII 211
|
....*....
gi 767243141 261 FCGKTTEAK 269
Cdd:cd03265 212 AEGTPEELK 220
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
747-928 |
1.38e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.47 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 747 LLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQRnVGTITGDMLVDGLPMDasfKRRTGYvQQQDLHVAE-------LT 819
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGL-LNPEKGEILFERQSIK---KDLCTY-QKQLCFVGHrsginpyLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 820 VKESLQFSARMrrpqsipDAEKMEyVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVGKPDLLLfLDEPTSG 899
Cdd:PRK13540 91 LRENCLYDIHF-------SPGAVG-ITELCRLFSLEHLIDYPCGLLSSG----QKRQVALLRLWMSKAKLWL-LDEPLVA 157
|
170 180
....*....|....*....|....*....
gi 767243141 900 LDSQSAWAVVKMLKRLALAGQSILCTIHQ 928
Cdd:PRK13540 158 LDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
757-945 |
1.55e-03 |
|
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: 40.81 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 757 PGTLTALIGESGAGKTTLLntlaqRNVGTITGdmlvdglpMDASFKRRTGYVQQQdlhvaeltvkeslQFSARmrrpqsi 836
Cdd:cd03227 20 EGSLTIITGPNGSGKSTIL-----DAIGLALG--------GAQSATRRRSGVKAG-------------CIVAA------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 837 pdaekmEYVEKIISILEMQEfsealvGEIgyglnveQRKKLSIGVELV-GKPDLLLFLDEPTSGLDSQSAWAVVKMLKRL 915
Cdd:cd03227 67 ------VSAELIFTRLQLSG------GEK-------ELSALALILALAsLKPRPLYILDEIDRGLDPRDGQALAEAILEH 127
|
170 180 190
....*....|....*....|....*....|
gi 767243141 916 ALAGQSILCTIHQPsaTLFEQFDRLLLLGK 945
Cdd:cd03227 128 LVKGAQVIVITHLP--ELAELADKLIHIKK 155
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
732-953 |
1.61e-03 |
|
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: 41.36 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTIPhssgqrklldsvSGYCVpgtltALIGESGAGKTTLLNTLA---QRNVGTITGDMLVDGLPmdasfkrrtgyv 808
Cdd:cd03220 39 KDVSFEVP------------RGERI-----GLIGRNGAGKSTLLRLLAgiyPPDSGTVTVRGRVSSLL------------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 809 qqqDLHVA---ELTVKESLQFSARMRRpqsIPDAEKMEYVEKIISILEMQEFSEALVGEIGYGlnveQRKKLSIGVELVG 885
Cdd:cd03220 90 ---GLGGGfnpELTGRENIYLNGRLLG---LSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSG----MKARLAFAIATAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767243141 886 KPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSatLFEQF-DRLLLLgKGGQTIYFG 953
Cdd:cd03220 160 EPDILL-IDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPS--SIKRLcDRALVL-EKGKIRFDG 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
762-945 |
1.85e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 41.75 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 762 ALIGESGAGKTTLL---NTLAQRN-VGTITGDMLVDGL-----PMDA-SFKRRTGYVQQQDLHVAELTVKESLQFSARMR 831
Cdd:PRK14267 34 ALMGPSGCGKSTLLrtfNRLLELNeEARVEGEVRLFGRniyspDVDPiEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 832 ---RPQSIPDaEKMEYVEKIISILEmqEFSEALVGEIGyGLNVEQRKKLSIGVELVGKPDLLLfLDEPTSGLDSQSAWAV 908
Cdd:PRK14267 114 glvKSKKELD-ERVEWALKKAALWD--EVKDRLNDYPS-NLSGGQRQRLVIARALAMKPKILL-MDEPTANIDPVGTAKI 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 767243141 909 VKMLKRLALAGQSILCTiHQPS-ATLFEQFDRLLLLGK 945
Cdd:PRK14267 189 EELLFELKKEYTIVLVT-HSPAqAARVSDYVAFLYLGK 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
30-258 |
1.87e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 41.64 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 30 IKGIRERKNRNKMKIILKNVSLLAKSGEMVLVLGRPGAGctsflKSAageTSQFAGGV---TTGHISYDG---------- 96
Cdd:PRK13650 7 VKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSG-----KST---TVRLIDGLleaESGQIIIDGdllteenvwd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 97 IPQKEMMQHYKPDVIYNG---EQDVHF-------PHLTVKQTLDFAISCkmpakrvnnVTKEEYitANREfyakifglth 166
Cdd:PRK13650 79 IRHKIGMVFQNPDNQFVGatvEDDVAFglenkgiPHEEMKERVNEALEL---------VGMQDF--KERE---------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 167 tfdtkvgndfISGVSGGERKRVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQASENIYE 246
Cdd:PRK13650 138 ----------PARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALS 207
|
250
....*....|..
gi 767243141 247 tfDKVIVLYAGR 258
Cdd:PRK13650 208 --DRVLVMKNGQ 217
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
158-227 |
1.94e-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: 42.46 E-value: 1.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 158 YAKIFGLTHTFDTKVGNdfisgVSGGERKRVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTN 227
Cdd:COG1245 196 LAEKLGLENILDRDISE-----LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAE 260
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
732-905 |
2.14e-03 |
|
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: 42.63 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFTipHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLaqrnvgtiTGDMlvDGLPMDASFKRRTGYVQQQ 811
Cdd:TIGR00957 640 HNATFT--WARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--------LAEM--DKVEGHVHMKGSVAYVPQQ 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 812 DLhVAELTVKESLQFSARMRRPQS---------IPDAEkmeyvekiisILEMQEFSEalVGEIGYGLNVEQRKKLSIGVE 882
Cdd:TIGR00957 708 AW-IQNDSLRENILFGKALNEKYYqqvleacalLPDLE----------ILPSGDRTE--IGEKGVNLSGGQKQRVSLARA 774
|
170 180
....*....|....*....|...
gi 767243141 883 LVGKPDLLLFlDEPTSGLDSQSA 905
Cdd:TIGR00957 775 VYSNADIYLF-DDPLSAVDAHVG 796
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
43-195 |
2.16e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 40.94 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQfaggvTTGHISYDGIPQKEMMQHYKPDVIYNGeqdvhfpH 122
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARP-----DAGEVLWQGEPIRRQRDEYHQDLLYLG-------H 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 123 LT-VKQTLdfaisckmpakrvnnvTKEEyitaNREFYAKIFGLTHTFDT-----KVGndfISGV--------SGGERKRV 188
Cdd:PRK13538 82 QPgIKTEL----------------TALE----NLRFYQRLHGPGDDEALwealaQVG---LAGFedvpvrqlSAGQQRRV 138
|
....*..
gi 767243141 189 siaeALA 195
Cdd:PRK13538 139 ----ALA 141
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
43-99 |
2.19e-03 |
|
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: 39.74 E-value: 2.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTTGH---ISYdgIPQ 99
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGStvkIGY--FEQ 70
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
46-263 |
2.25e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.08 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 46 LKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTTGHISYDGIPQKEMMQhYKPDVIYNgEQDVhFPHLTV 125
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQ-LGIGIIYQ-ELSV-IDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 126 KQTLDFAiscKMPAKRVNNVTKEEY--ITANREFYAKIFGLTHTFDTKVGNDFISgvsggERKRVSIAEALAAKGSIYCW 203
Cdd:PRK09700 98 LENLYIG---RHLTKKVCGVNIIDWreMRVRAAMMLLRVGLKVDLDEKVANLSIS-----HKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767243141 204 DNATRGLdssTALEFARAIRTMTNLLGT-TALVTVYQASENIYETFDKVIVLYAGRQIFCG 263
Cdd:PRK09700 170 DEPTSSL---TNKEVDYLFLIMNQLRKEgTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
732-915 |
2.71e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 41.23 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 732 KNVSFT-IPHSSGQRKL-LDSVSGYCVPGTLTALIGESGAGKTTL---LNTLAQRNVGTitgdMLVDGlpMDAS------ 800
Cdd:PRK13633 8 KNVSYKyESNEESTEKLaLDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIPSEGK----VYVDG--LDTSdeenlw 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 801 -FKRRTGYV-QQQDLHVAELTVKESLQFSarmrrPQS--IPDAEKMEYVEKIISILEMQEFSEalvgEIGYGLNVEQRKK 876
Cdd:PRK13633 82 dIRNKAGMVfQNPDNQIVATIVEEDVAFG-----PENlgIPPEEIRERVDESLKKVGMYEYRR----HAPHLLSGGQKQR 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 767243141 877 LSIGVELVGKPDLLLFlDEPTSGLDSQSAWAVVKMLKRL 915
Cdd:PRK13633 153 VAIAGILAMRPECIIF-DEPTAMLDPSGRREVVNTIKEL 190
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
736-933 |
2.86e-03 |
|
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: 42.20 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 736 FTIPHSSGQRKLLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAQrnVGTITGDMLVDGLPMDA----SFKRRTGYVQQQ 811
Cdd:TIGR01271 1223 LTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLR--LLSTEGEIQIDGVSWNSvtlqTWRKAFGVIPQK 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 812 dLHVAELTVKESLQFSARMRrpqsipDAEKMEYVEKIISILEMQEFSEAL---VGEIGYGLNVEQRKKLSIGVELVGKPD 888
Cdd:TIGR01271 1301 -VFIFSGTFRKNLDPYEQWS------DEEIWKVAEEVGLKSVIEQFPDKLdfvLVDGGYVLSNGHKQLMCLARSILSKAK 1373
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767243141 889 LLLfLDEPTSGLDSQSAWAVVKMLKRlALAGQSILCTIHQPSATL 933
Cdd:TIGR01271 1374 ILL-LDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEHRVEALL 1416
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
43-264 |
2.99e-03 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 41.35 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTTGHISydgIPQKEMMQHYKPDVIynGEQDVHFPH 122
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP---VPARARLARARIGVV--PQFDNLDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 123 LTVKQTL-DFAISCKMPAKRVnnvtkEEYITANREFyAKifgLTHTFDTKVgndfiSGVSGGERKRVSIAEALAAKGSIY 201
Cdd:PRK13536 129 FTVRENLlVFGRYFGMSTREI-----EAVIPSLLEF-AR---LESKADARV-----SDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767243141 202 CWDNATRGLDSSTALEFARAIRTMTNlLGTTALVTVYqASENIYETFDKVIVLYAGRQIFCGK 264
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLA-RGKTILLTTH-FMEEAERLCDRLCVLEAGRKIAEGR 255
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
876-923 |
3.74e-03 |
|
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: 39.72 E-value: 3.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767243141 876 KLSIGVELVGKPDLLLfLDEPTSGLDSQSAWAVVKMLKRLALAGQSIL 923
Cdd:cd03215 112 KVVLARWLARDPRVLI-LDEPTRGVDVGAKAEIYRLIRELADAGKAVL 158
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
747-946 |
4.21e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.50 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 747 LLDSVSGYCVPGTLTALIGESGAGKTTLLNTLAqRNVGTITGDMLVDGLPMdASFK----RRTGYVQQQDLHVAELTVKE 822
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALF-RIVELEKGRIMIDDCDV-AKFGltdlRRVLSIIPQSPVLFSGTVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 823 SLQ-FSARmrrpqsiPDAEKMEYVEK--IISILEMQEFS-EALVGEIGYGLNVEQRKKLSIGVELVGKPDlLLFLDEPTS 898
Cdd:PLN03232 1329 NIDpFSEH-------NDADLWEALERahIKDVIDRNPFGlDAEVSEGGENFSVGQRQLLSLARALLRRSK-ILVLDEATA 1400
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767243141 899 GLDSQSAwAVVKMLKRLALAGQSILCTIHQPSATLfeQFDRLLLLGKG 946
Cdd:PLN03232 1401 SVDVRTD-SLIQRTIREEFKSCTMLVIAHRLNTII--DCDKILVLSSG 1445
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
181-269 |
4.27e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.87 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 181 SGGERKRVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQasENIYETFDKVIVLYAGRQI 260
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYM--EEAEQLAHELTVIDRGRVI 223
|
....*....
gi 767243141 261 FCGKTTEAK 269
Cdd:NF000106 224 ADGKVDELK 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
145-278 |
4.80e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 40.50 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 145 VTKEEYITANREFYAkIFGLTHTFDTKvgNDFisGVSGGERKRVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRT 224
Cdd:PRK13649 116 VSQEEAEALAREKLA-LVGISESLFEK--NPF--ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKK 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 767243141 225 MTNLLGTTALVTvyQASENIYETFDKVIVLYAGRQIFCGKtteAKDYFENMGYL 278
Cdd:PRK13649 191 LHQSGMTIVLVT--HLMDDVANYADFVYVLEKGKLVLSGK---PKDIFQDVDFL 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
43-191 |
5.19e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 41.20 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 43 KIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTTGH---ISYdgIPQkemmqhykpdviyngEQDVH 119
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGEtvkIGY--FDQ---------------HQEEL 390
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767243141 120 FPHLTVKQTLdfaisckmpaKRVNNVTKEEYITAnrefYAKIFGLT-HTFDTKVGNdfisgVSGGERKRVSIA 191
Cdd:COG0488 391 DPDKTVLDEL----------RDGAPGGTEQEVRG----YLGRFLFSgDDAFKPVGV-----LSGGEKARLALA 444
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
874-996 |
6.04e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.49 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 874 RKKLSIGVELVGKPdLLLFLDEPTSGLDSQSAWAVVKMLKRLALAGQSILCTIHQPSATlfEQFDRLLLLGKGGQTIYFG 953
Cdd:NF000106 150 RRRLDLAASMIGRP-AVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEA--EQLAHELTVIDRGRVIADG 226
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 767243141 954 EIGKNSSSVikyfeknGARKCQQNENPAEYILEAIGAGATASV 996
Cdd:NF000106 227 KVDELKTKV-------GGRTLQIRPAHAAELDRMVGAIAQAGL 262
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
741-779 |
6.74e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.69 E-value: 6.74e-03
10 20 30
....*....|....*....|....*....|....*....
gi 767243141 741 SSGQRKLLDSVSGYCVPGTlTALIGESGAGKTTLLNTLA 779
Cdd:cd01854 69 SAKTGEGLDELRELLKGKT-SVLVGQSGVGKSTLLNALL 106
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
761-797 |
6.87e-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: 38.63 E-value: 6.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767243141 761 TALIGESGAGKTTLLNTLAQRNV-------GT----ITGDMLVDGLPM 797
Cdd:cd04164 6 VVIAGKPNVGKSSLLNALAGRDRaivsdiaGTtrdvIEEEIDLGGIPV 53
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
702-859 |
7.13e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 39.68 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 702 TQDMKEIASSNDDSTSADFEGLestgvfiwKNVSFTIPHssgqrklldsvsGYCVpgtltALIGESGAGKTTLLNTLAqr 781
Cdd:COG1134 21 SRSLKELLLRRRRTRREEFWAL--------KDVSFEVER------------GESV-----GIIGRNGAGKSTLLKLIA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 782 nvGTI---TGDMLVDG-----LPMDASFkrrtgyvqqqdlhVAELTVKESLQFSARMrrpQSIPDAEKMEYVEKIIsile 853
Cdd:COG1134 74 --GILeptSGRVEVNGrvsalLELGAGF-------------HPELTGRENIYLNGRL---LGLSRKEIDEKFDEIV---- 131
|
....*.
gi 767243141 854 mqEFSE 859
Cdd:COG1134 132 --EFAE 135
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
29-305 |
8.11e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 40.40 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 29 IIKGIRERK--NRNKMKIILKNVSLLAKSGEMVLVLGRPGAGCTSFLKSAAGETSQFAGGVTTGHISYDGIPQKEMMQHY 106
Cdd:PRK10070 25 IEQGLSKEQilEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 107 KPDVIYNGEQDVHFPHLTVKQTLDFAIS-CKMPAKRvnnvTKEEYITANREFyakifGLTHtfdtkVGNDFISGVSGGER 185
Cdd:PRK10070 105 RKKIAMVFQSFALMPHMTVLDNTAFGMElAGINAEE----RREKALDALRQV-----GLEN-----YAHSYPDELSGGMR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243141 186 KRVSIAEALAAKGSIYCWDNATRGLDSSTALEFARAIRTMTNLLGTTALVTVYQASENIyETFDKVIVLYAGRQIFCGKT 265
Cdd:PRK10070 171 QRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAM-RIGDRIAIMQNGEVVQVGTP 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 767243141 266 TE-----AKDYFENMGYLCPPRQSTAEYLTAITDPNGLHEIKPGF 305
Cdd:PRK10070 250 DEilnnpANDYVRTFFRGVDISQVFSAKDIARRTPNGLIRKTPGF 294
|
|
| |
