|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-1413 |
0e+00 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 1814.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 19 DEAEHALQWAEIQRLPTFKRLRSSLVDKYGEGTEKGK----KVVDVTKLGAMERHLMIEKLIKHIENDNLKLLKKIRRRM 94
Cdd:PLN03140 41 DEDEEALKWAAIEKLPTYSRLRTSIMKSFVENDVYGNqllhKEVDVTKLDGNDRQKFIDMVFKVAEEDNEKFLKKFRNRI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 95 ERVGVEFPSIEVRYEHLGVEAACEVvEGKALPTLWNSLKHVFLDLLKLSGVR-TNEANIKILTDVSGIISPGRLTLLLGP 173
Cdd:PLN03140 121 DRVGIKLPTVEVRFEHLTVEADCYI-GSRALPTLPNAARNIAESALGMLGINlAKKTKLTILKDASGIIKPSRMTLLLGP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 174 PGCGKTTLLKALSGNLENNLKCYGEISYNGHGLNEVVPQKTSAYISQHDLHIAEMTTRETIDFSARCQGVGSRTDIMMEV 253
Cdd:PLN03140 200 PSSGKTTLLLALAGKLDPSLKVSGEITYNGYRLNEFVPRKTSAYISQNDVHVGVMTVKETLDFSARCQGVGTRYDLLSEL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 254 SKREKDGGIIPDPEIDAYMKAISVKGLKRSLQTDYILKILGLDICAETLVGNAMKRGISGGQKKRLTTAEMIVGPTKALF 333
Cdd:PLN03140 280 ARREKDAGIFPEAEVDLFMKATAMEGVKSSLITDYTLKILGLDICKDTIVGDEMIRGISGGQKKRVTTGEMIVGPTKTLF 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 334 MDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSLLQPAPESYDLFDDIVLMAEGKIVYHGPRDDVLKFFEECGFQCPER 413
Cdd:PLN03140 360 MDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFDLFDDIILLSEGQIVYQGPRDHILEFFESCGFKCPER 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 414 KGVADFLQEVISKKDQGQYWLHQNLPHSFVSVDTLSKRFKDLEIGRKIEEALSKPYDISKTHKDALSFNVYSLPKWELFR 493
Cdd:PLN03140 440 KGTADFLQEVTSKKDQEQYWADRNKPYRYISVSEFAERFKSFHVGMQLENELSVPFDKSQSHKAALVFSKYSVPKMELLK 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 494 ACISREFLLMKRNYFVYLFKTFQLVLAAIITMTVFIRTRMDI-DIIHGNSYMSCLFFATVVLLVDGIPELSMTVQRLSVF 572
Cdd:PLN03140 520 ACWDKEWLLMKRNAFVYVFKTVQIIIVAAIASTVFLRTEMHTrNEEDGALYIGALLFSMIINMFNGFAELALMIQRLPVF 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 573 YKQKQLCFYPAWAYAIPATVLKIPLSFFESLVWTCLTYYVIGYTPEPYRFFRQFMILFAVHFTSISMFRCIAAIFQTGVA 652
Cdd:PLN03140 600 YKQRDLLFHPPWTFTLPTFLLGIPISIIESVVWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMII 679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 653 AMTAGSFVMLITFVFAGFAIPYTDMPGWLKWGFWVNPISYAEIGLSVNEFLAPRW-QKMQPTNVT-LGRTILESRGLNYD 730
Cdd:PLN03140 680 ANTGGALVLLLVFLLGGFILPKGEIPNWWEWAYWVSPLSYGFNALAVNEMFAPRWmNKMASDNSTrLGTAVLNIFDVFTD 759
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 731 DYMYWVSLSALLGLTIIFNTIFTLALSFLKSPTSSRPMISQDKLSELQGTKDSSVK-----------------------K 787
Cdd:PLN03140 760 KNWYWIGVGALLGFTILFNVLFTLALTYLNPLGKKQAIISEETAEEMEGEEDSIPRslssadgnntrevaiqrmsnpegL 839
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 788 NKPLDSSIKTNE--DPGK-MILPFKPLTITFQDLNYYVDVPVEMKGQGYNEKKLQLLSEITGAFRPGVLTALMGISGAGK 864
Cdd:PLN03140 840 SKNRDSSLEAANgvAPKRgMVLPFTPLAMSFDDVNYFVDMPAEMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGK 919
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 865 TTLLDVLAGRKTSGYIEGEIRISGFLKVQETFARVSGYCEQTDIHSPSITVEESLIYSAWLRLVPEINPQTKIRFVKQVL 944
Cdd:PLN03140 920 TTLMDVLAGRKTGGYIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVM 999
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 945 ETIELEEIKDALVGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQP 1024
Cdd:PLN03140 1000 ELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQP 1079
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1025 SIHIFEAFDELVLLKRGGRMIYSGPLGQHSSCVIEYFQNIPGVAKIRDKYNPATWMLEVTSESVETELDMDFAKIYNESD 1104
Cdd:PLN03140 1080 SIDIFEAFDELLLMKRGGQVIYSGPLGRNSHKIIEYFEAIPGVPKIKEKYNPATWMLEVSSLAAEVKLGIDFAEHYKSSS 1159
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1105 LYKNNSELVKELSKPDHGSSDLHFKRTFAQNWWEQFKSCLWKMSLSYWRSPSYNLMRIGHTFISSFIFGLLFWNQGKKID 1184
Cdd:PLN03140 1160 LYQRNKALVKELSTPPPGASDLYFATQYSQSTWGQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFWKVGTKRS 1239
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1185 TQQNLFTVLGAIYGLVLFVGINNCTSALQYFETERNVMYRERFAGMYSAFAYALAQVVTEIPYIFIQSAEFVIVIYPMIG 1264
Cdd:PLN03140 1240 NANDLTMVIGAMYAAVLFVGINNCSTVQPMVAVERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVA 1319
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1265 FYASFSKVFWSLYAMFCNLLCFNYLAMFLISITPNFMVAAILQSLFFTTFNIFAGFLIPKPQIPKWWVWFYYITPTSWTL 1344
Cdd:PLN03140 1320 FEWTAAKFFWFYFISFFSFLYFTYYGMMTVSLTPNQQVAAIFAAAFYGLFNLFSGFFIPRPKIPKWWVWYYWICPVAWTV 1399
|
1370 1380 1390 1400 1410 1420 1430
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228112 1345 NLFFSSQYGDIHQKINAFGETK--TVASFLEDYFGFHHDRLMITAIILIAFPIALATMYAFFVAKLNFQKR 1413
Cdd:PLN03140 1400 YGLIVSQYGDVEDTIKVPGGAPdpTIKWYIQDHYGYDPDFMGPVAAVLVGFTVFFAFIFAFCIRTLNFQTR 1470
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
80-1359 |
0e+00 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 1116.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 80 ENDNLKLLKKIRRRMERVGVEFP--SIEVRYEHLGVEAACevVEGKALPTLWNSLKHVFLDLLKLSGVRTNEANIKILTD 157
Cdd:TIGR00956 2 EFNAKAWVKNFRKLIDSDPIYYKpyKLGVAYKNLSAYGVA--ADSDYQPTFPNALLKILTRGFRKLKKFRDTKTFDILKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 158 VSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLKCY-GEISYNGHGLNEVVPQKT--SAYISQHDLHIAEMTTRETI 234
Cdd:TIGR00956 80 MDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVeGVITYDGITPEEIKKHYRgdVVYNAETDVHFPHLTVGETL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 235 DFSARCQGVGSRTDIMMEVSKREKdggiipdpeidaymkaisvkglkrslQTDYILKILGLDICAETLVGNAMKRGISGG 314
Cdd:TIGR00956 160 DFAARCKTPQNRPDGVSREEYAKH--------------------------IADVYMATYGLSHTRNTKVGNDFVRGVSGG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 315 QKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSLLQPAPESYDLFDDIVLMAEGKIVYHG 394
Cdd:TIGR00956 214 ERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 395 PRDDVLKFFEECGFQCPERKGVADFLQEVISKKdQGQYWLHQNLPhSFVSVDTLSKRFKDLEIGRKIEEALSKPYD---- 470
Cdd:TIGR00956 294 PADKAKQYFEKMGFKCPDRQTTADFLTSLTSPA-ERQIKPGYEKK-VPRTPQEFETYWRNSPEYAQLMKEIDEYLDrcse 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 471 -----------ISKTHKDALSFNVYSLPKWELFRACISREFLLMKRNYFVYLFKTFQLVLAAIITMTVFIRTRMDIDiiH 539
Cdd:TIGR00956 372 sdtkeayreshVAKQSKRTRPSSPYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTS--D 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 540 GNSYMSCLFFATVVLLVDGIPELSMTVQRLSVFYKQKQLCFYPAWAYAIPATVLKIPLSFFESLVWTCLTYYVIGYTPEP 619
Cdd:TIGR00956 450 FYSRGGALFFAILFNAFSSLLEIASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTA 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 620 YRFFRQFMILFAVHFTSISMFRCIAAIFQTGVAAMTAGSFVMLITFVFAGFAIPYTDMPGWLKWGFWVNPISYAEIGLSV 699
Cdd:TIGR00956 530 GRFFFYLLILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMV 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 700 NEFLAPRWQKMQP-------TNVTLGRTILESRGL-------NYDDYM----------YWVSLSALLGLTIIFNTIFTLA 755
Cdd:TIGR00956 610 NEFHGRRFECSQYvpsgggyDNLGVTNKVCTVVGAepgqdyvDGDDYLklsfqyynshKWRNFGIIIGFTVFFFFVYILL 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 756 LSFLKSPTSSRPMISQDKLSELQGTKDSSVKKNKPLDssIKTNEDpgkmiLPFKPLTITFQDLNYYVDVPVEMKG----- 830
Cdd:TIGR00956 690 TEFNKGAKQKGEILVFRRGSLKRAKKAGETSASNKND--IEAGEV-----LGSTDLTDESDDVNDEKDMEKESGEdifhw 762
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 831 ------QGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYIEGEIRISGFLKVQETFARVSGYCE 904
Cdd:TIGR00956 763 rnltyeVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRPLDSSFQRSIGYVQ 842
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 905 QTDIHSPSITVEESLIYSAWLRLVPEINPQTKIRFVKQVLETIELEEIKDALVGVAGvSGLSTEQRKRLTVAVELVANP- 983
Cdd:TIGR00956 843 QQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPG-EGLNVEQRKRLTIGVELVAKPk 921
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 984 SIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIHIFEAFDELVLLKRGGRMIYSGPLGQHSSCVIEYFQn 1063
Cdd:TIGR00956 922 LLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGGQTVYFGDLGENSHTIINYFE- 1000
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1064 IPGVAKIRDKYNPATWMLEVTSESVETELDMDFAKIYNESDLYKNNSELVKELSKPDHGSSDLHF---KRTFAQNWWEQF 1140
Cdd:TIGR00956 1001 KHGAPKCPEDANPAEWMLEVIGAAPGAHANQDYHEVWRNSSEYQAVKNELDRLEAELSKAEDDNDpdaLSKYAASLWYQF 1080
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1141 KSCLWKMSLSYWRSPSYNLMRIGHTFISSFIFGLLFWNQGKkidTQQNLFTVLGAIYGLVLFVGINNcTSALQYFETERN 1220
Cdd:TIGR00956 1081 KLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVGT---SLQGLQNQMFAVFMATVLFNPLI-QQYLPPFVAQRD 1156
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1221 VM-YRERFAGMYSAFAYALAQVVTEIPYIFIQSAEFVIVIYPMIGFYASFSKV---------FWSLYAMFcnLLCFNYLA 1290
Cdd:TIGR00956 1157 LYeVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFYWNASKTgqvhergvlFWLLSTMF--FLYFSTLG 1234
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228112 1291 MFLISITPNFMVAAILQSLFFTTFNIFAGFLIPKPQIPKWWVWFYYITPTSWTLNLFFSSQYGDIHQKI 1359
Cdd:TIGR00956 1235 QMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLADVPVTC 1303
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
810-1048 |
4.38e-99 |
|
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: 314.95 E-value: 4.38e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 810 PLTITFQDLNYYVDVPvemkgqgynEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYIEGEIRISGF 889
Cdd:cd03232 1 GSVLTWKNLNYTVPVK---------GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 890 lKVQETFARVSGYCEQTDIHSPSITVEESLIYSAWLRlvpeinpqtkirfvkqvletieleeikdalvgvagvsGLSTEQ 969
Cdd:cd03232 72 -PLDKNFQRSTGYVEQQDVHSPNLTVREALRFSALLR-------------------------------------GLSVEQ 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228112 970 RKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIHIFEAFDELVLLKRGGRMIYSG 1048
Cdd:cd03232 114 RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRGGKTVYFG 192
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
829-1342 |
1.04e-92 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 313.14 E-value: 1.04e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 829 KGQGYNEK-KLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGY-IEGEIRISGFLKVQETFARVSGYCEQT 906
Cdd:TIGR00955 28 RGCFCRERpRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkGSGSVLLNGMPIDAKEMRAISAYVQQD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 907 DIHSPSITVEESLIYSAWLRLVPEINPQTKIRFVKQVLETIELEEIKDALVGVAG-VSGLSTEQRKRLTVAVELVANPSI 985
Cdd:TIGR00955 108 DLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGrVKGLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 986 IFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIHIFEAFDELVLLKrGGRMIYSGPLGQhsscVIEYFQNIP 1065
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMA-EGRVAYLGSPDQ----AVPFFSDLG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1066 gvAKIRDKYNPATWMLEV--TSESVETELDMDFAKIYNE---SDLYKNNSELVKELSKPDHG---SSDLHFKRTFAQNWW 1137
Cdd:TIGR00955 263 --HPCPENYNPADFYVQVlaVIPGSENESRERIEKICDSfavSDIGRDMLVNTNLWSGKAGGlvkDSENMEGIGYNASWW 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1138 EQFKSCLWKMSLSYWRSPSYNLMRIGHTFISSFIFGLLFWNQGKKIDTQQNlftVLGAIYGLVLFVGINNCTSALQYFET 1217
Cdd:TIGR00955 341 TQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQN---INGALFLFLTNMTFQNVFPVINVFTA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1218 ERNVMYRERFAGMYSAFAYALAQVVTEIPYIFIQSAEFVIVIYPMIGFYASFSKVFWSLyamFCNLLCFNY---LAMFLI 1294
Cdd:TIGR00955 418 ELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFL---FLVTLVANVatsFGYLIS 494
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15228112 1295 SITPNFMVAAILQSLFFTTFNIFAGFLIPKPQIPKWWVWFYYItptSW 1342
Cdd:TIGR00955 495 CAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYL---SW 539
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
810-1048 |
1.29e-72 |
|
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: 240.53 E-value: 1.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 810 PLTITFQDLNYYVDVPVemkgqgyNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYIEGEIRISGF 889
Cdd:cd03213 1 GVTLSFRNLTVTVKSSP-------SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 890 LKVQETFARVSGYCEQTDIHSPSITVEESLIYSAWLRlvpeinpqtkirfvkqvletieleeikdalvgvagvsGLSTEQ 969
Cdd:cd03213 74 PLDKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------------GLSGGE 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228112 970 RKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIHIFEAFDELVLLKRgGRMIYSG 1048
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQ-GRVIYFG 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
116-756 |
3.16e-71 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 251.51 E-value: 3.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 116 ACEVVEGKALPTLWNSLKHVFLDLLKLSGVRTNEANIK-ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLK 194
Cdd:TIGR00955 1 LTYSWRNSDVFGRVAQDGSWKQLVSRLRGCFCRERPRKhLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 195 CYGEISYNGHGLNEVVPQKTSAYISQHDLHIAEMTTRETIDFSARCQgvgsrtdimmevskrekdggiipdpeidayMKA 274
Cdd:TIGR00955 81 GSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLR------------------------------MPR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 275 ISVKGLKRsLQTDYILKILGLDICAETLVGNA-MKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSL 353
Cdd:TIGR00955 131 RVTKKEKR-ERVDEVLQALGLRKCANTRIGVPgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 354 QQVAHiTNATVFVSLLQPAPESYDLFDDIVLMAEGKIVYHGPRDDVLKFFEECGFQCPERKGVADFLQEVISkkdqgqyw 433
Cdd:TIGR00955 210 KGLAQ-KGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLA-------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 434 lhqNLPHSFV-SVDTLSK---RFKDLEIGRKIEEALSKPYDISK---THKDALSFNVYSLPKWELFRACISREFLLMKRN 506
Cdd:TIGR00955 281 ---VIPGSENeSRERIEKicdSFAVSDIGRDMLVNTNLWSGKAGglvKDSENMEGIGYNASWWTQFYALLKRSWLSVLRD 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 507 YFVYLFKTFQLVLAAIITMTVFIRTRMD---IDIIHGNSYMSCLF--FATVVLLVDGIPelsmtvQRLSVFYKQKQLCFY 581
Cdd:TIGR00955 358 PLLLKVRLIQTMMTAILIGLIYLGQGLTqkgVQNINGALFLFLTNmtFQNVFPVINVFT------AELPVFLRETRSGLY 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 582 PAWAYAIPATVLKIPLSFFESLVWTCLTYYVIGYTPEPYRFFRQFMILFAVHFTSISMFRCIAAIFQTGVAAMTAGSFVM 661
Cdd:TIGR00955 432 RVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFV 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 662 LITFVFAGFAIPYTDMPGWLKWGFWVNPISYAEIGLSVNEFLAPRWQKMQPTNVTL-----GRTILESRGLNYDDymYWV 736
Cdd:TIGR00955 512 IPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVDNIECTSANTTGpcpssGEVILETLSFRNAD--LYL 589
|
650 660
....*....|....*....|
gi 15228112 737 SLSALLGLTIIFNTIFTLAL 756
Cdd:TIGR00955 590 DLIGLVILIFFFRLLAYFAL 609
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
146-394 |
5.89e-71 |
|
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: 236.01 E-value: 5.89e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 146 RTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLKCYGEISYNGHGLNEV--VPQKTSAYISQHDL 223
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYKEFaeKYPGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 224 HIAEMTTRETIDFSARCQGvgsrtdimmevskrekdggiipdpeidaymkaisvkglkrslqtdyilkilgldicaetlv 303
Cdd:cd03233 94 HFPTLTVRETLDFALRCKG------------------------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 304 gNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSLLQPAPESYDLFDDIV 383
Cdd:cd03233 113 -NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVL 191
|
250
....*....|.
gi 15228112 384 LMAEGKIVYHG 394
Cdd:cd03233 192 VLYEGRQIYYG 202
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
810-1354 |
1.03e-60 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 221.68 E-value: 1.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 810 PLTITFQDLNYYVDVPvEMKGQGYNEKKL-----------------QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLA 872
Cdd:PLN03211 37 PITLKFMDVCYRVKFE-NMKNKGSNIKRIlghkpkisdetrqiqerTILNGVTGMASPGEILAVLGPSGSGKSTLLNALA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 873 GRKTSGYIEGEIRISGFLKVQETFARvSGYCEQTDIHSPSITVEESLIYSAWLRLVPEINPQTKIRFVKQVLETIELEEI 952
Cdd:PLN03211 116 GRIQGNNFTGTILANNRKPTKQILKR-TGFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKC 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 953 KDALVGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIHIFEAF 1032
Cdd:PLN03211 195 ENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1033 DELVLLKRgGRMIYSGPLGQhsscVIEYFQNIPGVAKIrdKYNPATWMLEVT---------SESVETELDMDFAKIYNE- 1102
Cdd:PLN03211 275 DSVLVLSE-GRCLFFGKGSD----AMAYFESVGFSPSF--PMNPADFLLDLAngvcqtdgvSEREKPNVKQSLVASYNTl 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1103 -----------SDLYKNNSELVKELSKPDHGSSDlhfkRTFAQNWWEQFkSCLWKMSLSYWRSPSYNLMRIGHTFISSFI 1171
Cdd:PLN03211 348 lapkvkaaiemSHFPQANARFVGSASTKEHRSSD----RISISTWFNQF-SILLQRSLKERKHESFNTLRVFQVIAAALL 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1172 FGLLFWNQGKKiDTQQNlftvLGAIYGLVLFVGINNCTSALQYFETERNVMYRERFAGMYSAFAYALAQVVTEIPYIFIQ 1251
Cdd:PLN03211 423 AGLMWWHSDFR-DVQDR----LGLLFFISIFWGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELIL 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1252 SAEFVIVIYPMIGFYASFSKVFWSLYAMFCNLLCFNYLAMFLISITPNFMVAAILQSLFFTTFNIFAGFLIPKpqIPKWW 1331
Cdd:PLN03211 498 PTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYVHK--LPSCM 575
|
570 580
....*....|....*....|...
gi 15228112 1332 VWFYYITPTSWTLNLFFSSQYGD 1354
Cdd:PLN03211 576 AWIKYISTTFYSYRLLINVQYGE 598
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
1143-1347 |
2.06e-56 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 194.41 E-value: 2.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1143 CLWKMSLSYWRSPSYNLMRIGHTFISSFIFGLLFWNQGkkidTQQNLFTVLGAIYGLVLFVGINNCTSALQYFETERNVM 1222
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG----NQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1223 YRERFAGMYSAFAYALAQVVTEIPYIFIQSAEFVIVIYPMIGFYASFSKVFWSLYAMFCNLLCFNYLAMFLISITPNFMV 1302
Cdd:pfam01061 77 YRELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFED 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15228112 1303 AAILQSLFFTTFNIFAGFLIPKPQIPKWWVWFYYITPTSWTLNLF 1347
Cdd:pfam01061 157 ASQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEAL 201
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
822-1048 |
1.06e-51 |
|
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: 181.70 E-value: 1.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 822 VDVPVEMKGQGyneKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYI-EGEIRISGFLKVQETFARVS 900
Cdd:cd03234 7 WDVGLKAKNWN---KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTtSGQILFNGQPRKPDQFQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 901 GYCEQTDIHSPSITVEESLIYSAWLRLvPEINPQtKIRfvKQVLETIELEEIKDALVGVAGVSGLSTEQRKRLTVAVELV 980
Cdd:cd03234 84 AYVRQDDILLPGLTVRETLTYTAILRL-PRKSSD-AIR--KKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15228112 981 ANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIHIFEAFDELVLLKRgGRMIYSG 1048
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSS-GEIVYSG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
135-394 |
3.55e-48 |
|
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: 170.42 E-value: 3.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 135 VFLDLLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnNLKCYGEISYNGHGLNEVVPQKT 214
Cdd:cd03213 5 SFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRT-GLGVSGEVLINGRPLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 215 SAYISQHDLHIAEMTTRETIDFSARCqgvgsrtdimmevskrekdggiipdpeidaymkaisvkglkrslqtdyilkilg 294
Cdd:cd03213 84 IGYVPQDDILHPTLTVRETLMFAAKL------------------------------------------------------ 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 295 ldicaetlvgnamkRGISGGQKKRLTTA-EMIVGPTkALFMDEITNGLDSSTAFQIIKSLQQVAHiTNATVFVSLLQPAP 373
Cdd:cd03213 110 --------------RGLSGGERKRVSIAlELVSNPS-LLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPSS 173
|
250 260
....*....|....*....|.
gi 15228112 374 ESYDLFDDIVLMAEGKIVYHG 394
Cdd:cd03213 174 EIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
495-700 |
1.30e-42 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 154.74 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 495 CISREFLLMKRNYFVYLFKTFQLVLAAIITMTVFIRTRmdiDIIHGNSYMSCLFFATVVLLVDGIPELS-MTVQRLSVFY 573
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG---NQQGGLNRPGLLFFSILFNAFSALSGISpVFEKERGVLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 574 KQKQLCFYPAWAYAIPATVLKIPLSFFESLVWTCLTYYVIGYTPEPYRFFRQFMILFAVHFTSISMFRCIAAIFQTGVAA 653
Cdd:pfam01061 78 RELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15228112 654 MTAGSFVMLITFVFAGFAIPYTDMPGWLKWGFWVNPISYAEIGLSVN 700
Cdd:pfam01061 158 SQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
153-394 |
1.78e-42 |
|
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: 155.12 E-value: 1.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLKCYGEISYNGHGLNEVVPQKTSAYISQHDLHIAEMTTRE 232
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 233 TIDFSARCQgvgsrtdimmevSKREKDGGIIpdpeidayMKAISVKGLKRslqtdyilkilgldiCAETLVGNAMKRGIS 312
Cdd:cd03234 101 TLTYTAILR------------LPRKSSDAIR--------KKRVEDVLLRD---------------LALTRIGGNLVKGIS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 313 GGQKKRLTTA-EMIVGPtKALFMDEITNGLDSSTAFQIIKSLQQVAHiTNATVFVSLLQPAPESYDLFDDIVLMAEGKIV 391
Cdd:cd03234 146 GGERRRVSIAvQLLWDP-KVLILDEPTSGLDSFTALNLVSTLSQLAR-RNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
...
gi 15228112 392 YHG 394
Cdd:cd03234 224 YSG 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
154-693 |
5.98e-36 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 146.56 E-value: 5.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkCY-GEISYNGHGLNEVVPQKTsAYISQHDLHIAEMTTRE 232
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGN--NFtGTILANNRKPTKQILKRT-GFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 233 TIDFSARCQgvgsrtdIMMEVSKREKdggiipdpeidaymkaisvkglkrSLQTDYILKILGLDICAETLVGNAMKRGIS 312
Cdd:PLN03211 160 TLVFCSLLR-------LPKSLTKQEK------------------------ILVAESVISELGLTKCENTIIGNSFIRGIS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 313 GGQKKRLTTA-EMIVGPTkALFMDEITNGLDSSTAFQIIKSLQQVAHiTNATVFVSLLQPAPESYDLFDDIVLMAEGKIV 391
Cdd:PLN03211 209 GGERKRVSIAhEMLINPS-LLILDEPTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 392 YHGPRDDVLKFFEECGFQCPERKGVADFLQEV---------ISKKDQGQywLHQNLPHSFVSVdtLSKRFKD-LEIGRKI 461
Cdd:PLN03211 287 FFGKGSDAMAYFESVGFSPSFPMNPADFLLDLangvcqtdgVSEREKPN--VKQSLVASYNTL--LAPKVKAaIEMSHFP 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 462 EEalSKPYDISKTHKDALSFNVYSLPKWeLFRACISREFLLMKRNYFVY-LFKTFQLVLAAIITMTVFIRTrmdiDIIHG 540
Cdd:PLN03211 363 QA--NARFVGSASTKEHRSSDRISISTW-FNQFSILLQRSLKERKHESFnTLRVFQVIAAALLAGLMWWHS----DFRDV 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 541 NSYMSCLFFATVVLLVdgIPELSMTV---QRLSVFYKQKQLCFYPAWAYAIPATVLKIPLSFFESLVWTCLTYYVIGYTP 617
Cdd:PLN03211 436 QDRLGLLFFISIFWGV--FPSFNSVFvfpQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKP 513
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228112 618 EPYRFFRQFMILFAVHFTSISMFRCIAAIFQTGVAAMTAGSFVMLITFVFAGFAIpyTDMPGWLKWGFWVNPISYA 693
Cdd:PLN03211 514 ELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYV--HKLPSCMAWIKYISTTFYS 587
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
832-1048 |
2.93e-35 |
|
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: 133.54 E-value: 2.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 832 GYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRkTSGY--IEGEIRISGF--LKVQETFARVSGYCEQTD 907
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR-TEGNvsVEGDIHYNGIpyKEFAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 908 IHSPSITVEESLIYSAWLRlvpeinpqtkirfvkqvletieleeikdalvGVAGVSGLSTEQRKRLTVAVELVANPSIIF 987
Cdd:cd03233 93 VHFPTLTVRETLDFALRCK-------------------------------GNEFVRGISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15228112 988 MDEPTTGLDARAAAIVMRAVKNVA-ETGRTIVCTIHQPSIHIFEAFDELVLLkRGGRMIYSG 1048
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTMAdVLKTTTFVSLYQASDEIYDLFDKVLVL-YEGRQIYYG 202
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
836-1050 |
2.25e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 129.41 E-value: 2.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 836 KKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGFlKVQETFARVS---GYCEQTDIHS 910
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGllRPTSG----EVRVLGE-DVARDPAEVRrriGYVPQEPALY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 911 PSITVEESLIYSAWLRLVPEINPQTKIRfvkQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDE 990
Cdd:COG1131 86 PDLTVRENLRFFARLYGLPRKEARERID---ELLELFGLTDAADRKVG-----TLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228112 991 PTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSihifEA---FDELVLLKRgGRMIYSGPL 1050
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLE----EAerlCDRVAIIDK-GRIVADGTP 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
836-1059 |
2.00e-30 |
|
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: 121.12 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 836 KKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGFLKVQETFARVS--GYCEQTDIHSP 911
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGllKPDSG----SILIDGEDVRKEPREARRqiGVLPDERGLYD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 912 SITVEESLIYSAWLRLVPEINPQTKIrfvKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDEP 991
Cdd:COG4555 88 RLTVRENIRYFAELYGLFDEELKKRI---EELIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15228112 992 TTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRgGRMIYSGPLGQHSSCVIE 1059
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIMQ-EVEALCDRVVILHK-GKVVAQGSLDELREEIGE 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
832-1048 |
2.91e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 116.86 E-value: 2.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 832 GYNEKKLqlLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGFlKVQETFARVsGYCEQT--- 906
Cdd:cd03235 8 SYGGHPV--LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGllKPTSG----SIRVFGK-PLEKERKRI-GYVPQRrsi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 907 DIHSPsITVEESLIYSAWLRLVPeINPQTKIRF--VKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPS 984
Cdd:cd03235 80 DRDFP-ISVRDVVLMGLYGHKGL-FRRLSKADKakVDEALERVGLSELADRQIG-----ELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228112 985 IIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRggRMIYSG 1048
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLG-LVLEYFDRVLLLNR--TVVASG 213
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
145-394 |
7.78e-29 |
|
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: 114.65 E-value: 7.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 145 VRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNlENNLKCYGEISYNGHGLNEVVpQKTSAYISQHDLH 224
Cdd:cd03232 13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGR-KTAGVITGEILINGRPLDKNF-QRSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 225 IAEMTTRETIDFSARCqgvgsrtdimmevskrekdggiipdpeidaymkaisvkglkrslqtdyilkilgldicaetlvg 304
Cdd:cd03232 91 SPNLTVREALRFSALL---------------------------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 305 namkRGISGGQKKRLTTA-EMIVGPTkALFMDEITNGLDSSTAFQIIKSLQQVAHiTNATVFVSLLQPAPESYDLFDDIV 383
Cdd:cd03232 107 ----RGLSVEQRKRLTIGvELAAKPS-ILFLDEPTSGLDSQAAYNIVRFLKKLAD-SGQAILCTIHQPSASIFEKFDRLL 180
|
250
....*....|..
gi 15228112 384 LMAE-GKIVYHG 394
Cdd:cd03232 181 LLKRgGKTVYFG 192
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
833-1048 |
1.00e-28 |
|
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: 115.29 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 833 YNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGFLKVQETFA--RVSGYCEQTDI 908
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGelRPTSG----TAYINGYSIRTDRKAarQSLGYCPQFDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 909 HSPSITVEESLIYSAWLRLVPEinpQTKIRFVKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFM 988
Cdd:cd03263 86 LFDELTVREHLRFYARLKGLPK---SEIKEEVELLLRVLGLTDKANKRAR-----TLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228112 989 DEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHqpSIHIFEAF-DELVLLKRgGRMIYSG 1048
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRK-GRSIILTTH--SMDEAEALcDRIAIMSD-GKLRCIG 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
813-1049 |
1.09e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 113.26 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 813 ITFQDLNYyvdvpvemkgqGYNEKklQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSgyieGEIRISGfL 890
Cdd:COG1121 7 IELENLTV-----------SYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGllPPTS----GTVRLFG-K 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 891 KVQETFARVsGYCEQT---DIHSPsITVEEsLIYSAWLRLVPEINPQTKI--RFVKQVLETIELEEIKDALVGvagvsGL 965
Cdd:COG1121 69 PPRRARRRI-GYVPQRaevDWDFP-ITVRD-VVLMGRYGRRGLFRRPSRAdrEAVDEALERVGLEDLADRPIG-----EL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 966 STEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRggRMI 1045
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLG-AVREYFDRVLLLNR--GLV 217
|
....
gi 15228112 1046 YSGP 1049
Cdd:COG1121 218 AHGP 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
833-1041 |
2.19e-26 |
|
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: 106.56 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 833 YNEKKLqlLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGflkvqetfarvsgyceqtdihsps 912
Cdd:cd00267 9 YGGRTA--LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT--SGEILIDG------------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 913 itveesliysawlrlvpeinpqtkirfvkQVLETIELEEIKDalvGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPT 992
Cdd:cd00267 61 -----------------------------KDIAKLPLEELRR---RIGYVPQLSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15228112 993 TGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIhIFEAFDELVLLKRG 1041
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPEL-AELAADRVIVLKDG 156
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
836-1048 |
2.22e-26 |
|
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: 108.43 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 836 KKLQLLSEITGAFRPGVlTALMGISGAGKTTLLDVLAG-RKTSgyiEGEIRISGF--LKVQETFARVSGYCEQTDIHSPS 912
Cdd:cd03264 11 GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATlTPPS---SGTIRIDGQdvLKQPQKLRRRIGYLPQEFGVYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 913 ITVEESLIYSAWLRlvpEINPQTKIRFVKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDEPT 992
Cdd:cd03264 87 FTVREFLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIG-----SLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 993 TGLDARAAAIVMRAVKNVAETGRTIVCTihqpsiHIFE----AFDELVLLKrGGRMIYSG 1048
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGEDRIVILST------HIVEdvesLCNQVAVLN-KGKLVFEG 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
833-1041 |
8.35e-26 |
|
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: 106.78 E-value: 8.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 833 YNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKtsGYIEGEIRISGFLKVQET---FARVSGYCEQtdih 909
Cdd:cd03225 9 YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL--GPTSGEVLVDGKDLTKLSlkeLRRKVGLVFQ---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 910 SP-----SITVEESLIYSAWLRLVPEinPQTKIRfVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPS 984
Cdd:cd03225 83 NPddqffGPTVEEEVAFGLENLGLPE--EEIEER-VEEALELVGLEGLRDRSP-----FTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15228112 985 IIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRG 1041
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDG 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
832-1049 |
1.91e-25 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 107.05 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 832 GYNEKklQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGEiRISGfLKVQEtFARVSGYCEQTD 907
Cdd:COG1120 10 GYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGllKPSSGevLLDGR-DLAS-LSRRE-LARRIAYVPQEP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 908 IHSPSITVEESLIY------SAWLRLVPEinpqtKIRFVKQVLETIELEEIKDALvgvagVSGLSTEQRKRLTVAVELVA 981
Cdd:COG1120 85 PAPFGLTVRELVALgryphlGLFGRPSAE-----DREAVEEALERTGLEHLADRP-----VDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228112 982 NPSIIFMDEPTTGLDARAAAIVMRAVKN-VAETGRTIVCTIHQPSiHIFEAFDELVLLKrGGRMIYSGP 1049
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRlARERGRTVVMVLHDLN-LAARYADRLVLLK-DGRIVAQGP 221
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
151-405 |
7.46e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 104.76 E-value: 7.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 151 NIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHglnEVVPQKTSA-----YISQHDLHI 225
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT---SGEVRVLGE---DVARDPAEVrrrigYVPQEPALY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 226 AEMTTRETIDFSARCQGVgsrtdimmevskrekdggiiPDPEIDAymkaisvkglkrslQTDYILKILGLDICAETLVGN 305
Cdd:COG1131 86 PDLTVRENLRFFARLYGL--------------------PRKEARE--------------RIDELLELFGLTDAADRKVGT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 306 amkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHiTNATVFVS--LLqpaPESYDLFDDIV 383
Cdd:COG1131 132 -----LSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSthYL---EEAERLCDRVA 202
|
250 260
....*....|....*....|...
gi 15228112 384 LMAEGKIVYHGPRDDVL-KFFEE 405
Cdd:COG1131 203 IIDKGRIVADGTPDELKaRLLED 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
832-1048 |
9.31e-24 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 99.82 E-value: 9.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 832 GYNEKklQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG-RKTSGyieGEIRISGflkvqetfarvsgyceqTDIHS 910
Cdd:cd03214 8 GYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGlLKPSS---GEILLDG-----------------KDLAS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 911 PSItveesliySAWLRlvpeinpqtKIRFVKQVLETIELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDE 990
Cdd:cd03214 66 LSP--------KELAR---------KIAYVPQALELLGLAHLADRPFNE-----LSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15228112 991 PTTGLDARAAAIVMRAVKNVA-ETGRTIVCTIHQPSiHIFEAFDELVLLKrGGRMIYSG 1048
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLN-LAARYADRVILLK-DGRIVAQG 180
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
840-1024 |
2.58e-23 |
|
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: 99.48 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 840 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTsgyiEGEIRISGF--LKVQETFARVSGYCEQTDIHSPSITV 915
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGllPPS----AGEVLWNGEpiRDAREDYRRRLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 916 EESLIYSAWLRLVPEINPQtkirfVKQVLETIELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGL 995
Cdd:COG4133 93 RENLRFWAALYGLRADREA-----IDEALEAVGLAGLADLPVRQ-----LSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180
....*....|....*....|....*....
gi 15228112 996 DARAAAIVMRAVKNVAETGRTIVCTIHQP 1024
Cdd:COG4133 163 DAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
813-1049 |
2.40e-22 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 97.40 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 813 ITFQDLNYYvdvpvemkgqgYNEKKlQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGFL 890
Cdd:COG1122 1 IELENLSFS-----------YPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGllKPTSG----EVLVDGKD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 891 KVQETFARVS---GYCEQ---TDIHSPsiTVEESLIYSawlrlvPE---INPQTKIRFVKQVLETIELEEIKDAlvgvaG 961
Cdd:COG1122 65 ITKKNLRELRrkvGLVFQnpdDQLFAP--TVEEDVAFG------PEnlgLPREEIRERVEEALELVGLEHLADR-----P 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 962 VSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRg 1041
Cdd:COG1122 132 PHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLD-LVAELADRVIVLDD- 209
|
....*...
gi 15228112 1042 GRMIYSGP 1049
Cdd:COG1122 210 GRIVADGT 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
832-1041 |
6.46e-22 |
|
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: 95.40 E-value: 6.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 832 GYNEKKLqLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGFLKVQETFARVSGYCEQT-DI 908
Cdd:cd03226 8 SYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGliKESSG----SILLNGKPIKAKERRKSIGYVMQDvDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 909 HSPSITVEESLIYSawLRLVPEINPQtkirfVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSIIFM 988
Cdd:cd03226 83 QLFTDSVREELLLG--LKELDAGNEQ-----AETVLKDLDLYALKERHP-----LSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15228112 989 DEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIhIFEAFDELVLLKRG 1041
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEF-LAKVCDRVLLLANG 202
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
155-339 |
7.27e-22 |
|
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: 93.48 E-value: 7.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 155 LTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEVVPQKTS---AYISQHDLHIAEMTTR 231
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT---EGTILLDGQDLTDDERKSLRkeiGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 232 ETIDFSARCQGvgsrtdimmeVSKREKDGgiipdpeidaymkaisvkglkrslQTDYILKILGLDICAETLVGNAMKrGI 311
Cdd:pfam00005 78 ENLRLGLLLKG----------LSKREKDA------------------------RAEEALEKLGLGDLADRPVGERPG-TL 122
|
170 180
....*....|....*....|....*...
gi 15228112 312 SGGQKKRLTTAEMIVGPTKALFMDEITN 339
Cdd:pfam00005 123 SGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
834-1041 |
1.46e-21 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 94.48 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 834 NEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGeIRISGFLKVQETFARVS--GYCEQTd 907
Cdd:cd03255 13 GGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGldRPTSGevRVDG-TDISKLSEKELAAFRRRhiGFVFQS- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 908 iHS--PSITVEESLIYSawLRLVPEINPQTKIRfVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSI 985
Cdd:cd03255 91 -FNllPDLTALENVELP--LLLAGVPKKERRER-AEELLERVGLGDRLNHYP-----SELSGGQQQRVAIARALANDPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15228112 986 IFMDEPTTGLDARAAAIVMRAVKNVA-ETGRTIVCTIHQPSihIFEAFDELVLLKRG 1041
Cdd:cd03255 162 ILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPE--LAEYADRIIELRDG 216
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
139-401 |
1.49e-21 |
|
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: 95.31 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 139 LLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNE---------- 208
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD---SGSILIDGEDVRKeprearrqig 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 209 VVPQKTSAYisqhdlhiAEMTTRETIDFSARCQGVgsrtdimmevskrekdggiipdpeidaymkaisvKGLKRSLQTDY 288
Cdd:COG4555 78 VLPDERGLY--------DRLTVRENIRYFAELYGL----------------------------------FDEELKKRIEE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 289 ILKILGLDICAETLVGnamkrGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHiTNATVFVS- 367
Cdd:COG4555 116 LIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKK-EGKTVLFSs 189
|
250 260 270
....*....|....*....|....*....|....*
gi 15228112 368 -LLQpapESYDLFDDIVLMAEGKIVYHGPRDDVLK 401
Cdd:COG4555 190 hIMQ---EVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| PDR_assoc |
pfam08370 |
Plant PDR ABC transporter associated; This domain is found on the C-terminus of ABC-2 type ... |
707-769 |
4.18e-21 |
|
Plant PDR ABC transporter associated; This domain is found on the C-terminus of ABC-2 type transporter domains (pfam01061). It seems to be associated with the plant pleiotropic drug resistance (PDR) protein family of ABC transporters. Like in yeast, plant PDR ABC transporters may also play a role in the transport of antifungal agents [also pfam06422]. The PDR family is characterized by a configuration in which the ABC domain is nearer the N-terminus of the protein than the transmembrane domain.
Pssm-ID: 462450 [Multi-domain] Cd Length: 65 Bit Score: 87.94 E-value: 4.18e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228112 707 WQKMQP--TNVTLGRTILESRGLNYDDYMYWVSLSALLGLTIIFNTIFTLALSFLKSPTSSRPMI 769
Cdd:pfam08370 1 WMKPTAsnGNTTLGVAVLKSRGLFTEAYWYWIGVGALLGFTILFNILFTLALTYLNPLGKSQAII 65
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
836-1048 |
1.72e-20 |
|
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: 91.12 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 836 KKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIEgeIRISGFLKVQETFARVSGYCEQTDIHsPSI 913
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGliKPDSGEIT--FDGKSYQKNIEALRRIGALIEAPGFY-PNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 914 TVEESLIYSAWLRLVPEINpqtkirfVKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDEPTT 993
Cdd:cd03268 88 TARENLRLLARLLGIRKKR-------IDEVLDVVGLKDSAKKKVK-----GFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15228112 994 GLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLkRGGRMIYSG 1048
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLISSHLLS-EIQKVADRIGII-NKGKLIEEG 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
841-993 |
1.86e-20 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 89.24 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 841 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTsgYIEGEIRISG--FLKVQETFARVS-GYCEQTDIHSPSITVEE 917
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS--PTEGTILLDGqdLTDDERKSLRKEiGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228112 918 SLIYSAWLRLVPEINPQTKirfVKQVLETIELEEIKDALVGVAGvSGLSTEQRKRLTVAVELVANPSIIFMDEPTT 993
Cdd:pfam00005 79 NLRLGLLLKGLSKREKDAR---AEEALEKLGLGDLADRPVGERP-GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
140-401 |
2.33e-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: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGV--RTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNE--------- 208
Cdd:COG2274 474 IELENVsfRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT---SGRILIDGIDLRQidpaslrrq 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 209 --VVPQktsayisqhDLHIAEMTTRETIDFSArcqgvgsrtdimmevskrekdggiiPDPEIDAYMKAISVKGLkrslqT 286
Cdd:COG2274 551 igVVLQ---------DVFLFSGTIRENITLGD-------------------------PDATDEEIIEAARLAGL-----H 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 287 DYILKI-LGLDicaeTLVGNaMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHitNATVF 365
Cdd:COG2274 592 DFIEALpMGYD----TVVGE-GGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVI 664
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15228112 366 V-----SLLQpapesydLFDDIVLMAEGKIVYHGPRDDVLK 401
Cdd:COG2274 665 IiahrlSTIR-------LADRIIVLDKGRIVEDGTHEELLA 698
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
162-394 |
2.64e-20 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 91.03 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 162 ISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlKCYGEISYNGHGLNE--VVPQKTSAYISQHDLHIAEMTTRETIDFSAR 239
Cdd:cd03263 25 VYKGEIFGLLGHNGAGKTTTLKMLTGELR---PTSGTAYINGYSIRTdrKAARQSLGYCPQFDALFDELTVREHLRFYAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 240 CQGVgSRTDIMMEVSKrekdggiipdpeidaymkaisvkglkrslqtdyILKILGLDICAETLVGNamkrgISGGQKKRL 319
Cdd:cd03263 102 LKGL-PKSEIKEEVEL---------------------------------LLRVLGLTDKANKRART-----LSGGMKRKL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228112 320 TTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHitNATVFVSLLQPApESYDLFDDIVLMAEGKIVYHG 394
Cdd:cd03263 143 SLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMD-EAEALCDRIAIMSDGKLRCIG 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
799-1041 |
3.12e-20 |
|
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: 96.37 E-value: 3.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 799 EDPGKMILPFKPLTITFQDLNYyvdvpvemkgqGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKT 876
Cdd:COG4987 320 TEPAEPAPAPGGPSLELEDVSF-----------RYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRflDPQ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 877 SGyiegEIRISGflkV------QETFARVSGYCEQtDIHSPSITVEESLiysawlRLVpeiNPQTKIRFVKQVLETIELE 950
Cdd:COG4987 389 SG----SITLGG---VdlrdldEDDLRRRIAVVPQ-RPHLFDTTLRENL------RLA---RPDATDEELWAALERVGLG 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 951 EIKDAL-------VGVAGvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHQ 1023
Cdd:COG4987 452 DWLAALpdgldtwLGEGG-RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHR 529
|
250
....*....|....*...
gi 15228112 1024 PSIHifEAFDELVLLKRG 1041
Cdd:COG4987 530 LAGL--ERMDRILVLEDG 545
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
810-1041 |
3.13e-20 |
|
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: 96.37 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 810 PLTITFQDLNYyvdvpvemkgqGYNEKKlQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISG- 888
Cdd:COG4988 334 PPSIELEDVSF-----------SYPGGR-PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP--YSGSILINGv 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 889 ---FLKVQETFARVSgYCEQTDiHSPSITVEEsliysaWLRLV-PEINPQTkirfVKQVLETIELEEIKDAL-------V 957
Cdd:COG4988 400 dlsDLDPASWRRQIA-WVPQNP-YLFAGTIRE------NLRLGrPDASDEE----LEAALEAAGLDEFVAALpdgldtpL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 958 GVAGvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAEtGRT-IVCTiHQPsiHIFEAFDELV 1036
Cdd:COG4988 468 GEGG-RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTvILIT-HRL--ALLAQADRIL 542
|
....*
gi 15228112 1037 LLKRG 1041
Cdd:COG4988 543 VLDDG 547
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
850-1048 |
9.08e-20 |
|
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: 89.35 E-value: 9.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 850 PGVLTALMGISGAGKTTLLDVLAG--RKTSGYIEgeirISGFLKVQETFA--RVSGYCEQTDIHSPSITVEESLIYSAWL 925
Cdd:cd03266 30 PGEVTGLLGPNGAGKTTTLRMLAGllEPDAGFAT----VDGFDVVKEPAEarRRLGFVSDSTGLYDRLTARENLEYFAGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 926 RlvpEINPQTKIRFVKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMR 1005
Cdd:cd03266 106 Y---GLKGDELTARLEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALRE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15228112 1006 AVKNVAETGRTIVCTIHqpSIHIFEAF-DELVLLKRgGRMIYSG 1048
Cdd:cd03266 178 FIRQLRALGKCILFSTH--IMQEVERLcDRVVVLHR-GRVVYEG 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
839-1041 |
2.02e-19 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 88.35 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 839 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSgyieGEIRISGflkvqETFARVS------GYCEQTDIHS 910
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGleRPDS----GEILIDG-----RDVTGVPperrniGMVFQDYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 911 PSITVEESLIYSAWLRLVPEinPQTKIRfVKQVLETIELEEIKDALvgvagVSGLSTEQRKRLTVAVELVANPSIIFMDE 990
Cdd:cd03259 85 PHLTVAENIAFGLKLRGVPK--AEIRAR-VRELLELVGLEGLLNRY-----PHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15228112 991 PTTGLDARAAAIVMRAVKNV-AETGRTIVCTIHQPSihifEAF---DELVLLKRG 1041
Cdd:cd03259 157 PLSALDAKLREELREELKELqRELGITTIYVTHDQE----EALalaDRIAVMNEG 207
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
849-1022 |
2.10e-19 |
|
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: 88.58 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 849 RPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGFLKVQET--FARVSGYCEQTDIHSPSITVEESLIYSAW 924
Cdd:cd03265 24 RRGEIFGLLGPNGAGKTTTIKMLTTllKPTSG----RATVAGHDVVREPreVRRRIGIVFQDLSVDDELTGWENLYIHAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 925 LRLVPEINPQTKIRfvkQVLETIELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVM 1004
Cdd:cd03265 100 LYGVPGAERRERID---ELLDFVGLLEAADRLVKT-----YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVW 171
|
170
....*....|....*....
gi 15228112 1005 RAVKN-VAETGRTIVCTIH 1022
Cdd:cd03265 172 EYIEKlKEEFGMTILLTTH 190
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
841-1049 |
6.90e-19 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 87.49 E-value: 6.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 841 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGEiRISGfLKVQE--------TFARVSGYceqtdi 908
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGflRPTSGsvLFDGE-DITG-LPPHEiarlgigrTFQIPRLF------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 909 hsPSITVEE------------SLIYSAWLRLVPEINPQtkirfVKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVA 976
Cdd:cd03219 88 --PELTVLEnvmvaaqartgsGLLLARARREEREARER-----AEELLERVGLADLADRPAG-----ELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228112 977 VELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIhIFEAFDELVLLKRgGRMIYSGP 1049
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDV-VMSLADRVTVLDQ-GRVIAEGT 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
813-1022 |
8.77e-19 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 86.85 E-value: 8.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 813 ITFQDLNYYvdvpvemkgqgYNEKklQLLSEITGAFRPGVLTALMGISGAGKTTLL-------DVLAGRKTSG--YIEGE 883
Cdd:cd03260 1 IELRDLNVY-----------YGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLrllnrlnDLIPGAPDEGevLLDGK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 884 IRISGFLKVQETFARVsGYCEQtdihSPSI---TVEESLIYSAWLRLVPEINPQTKIrfVKQVLETIEL-EEIKDALVGv 959
Cdd:cd03260 68 DIYDLDVDVLELRRRV-GMVFQ----KPNPfpgSIYDNVAYGLRLHGIKLKEELDER--VEEALRKAALwDEVKDRLHA- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228112 960 agvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETgRTIVCTIH 1022
Cdd:cd03260 140 ---LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTH 198
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
833-1041 |
9.55e-19 |
|
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: 85.32 E-value: 9.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 833 YNEKklQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGflkvqETFARVSGYCEQtdihs 910
Cdd:cd03229 10 YGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGleEPDSG----SILIDG-----EDLTDLEDELPP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 911 psitveesliysawlrlvpeinPQTKIRFVKQ---------VLETIELeeikdalvgvagvsGLSTEQRKRLTVAVELVA 981
Cdd:cd03229 74 ----------------------LRRRIGMVFQdfalfphltVLENIAL--------------GLSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228112 982 NPSIIFMDEPTTGLDARAAAIVMRAVKNV-AETGRTIVCTIHQpsihIFEAF---DELVLLKRG 1041
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHD----LDEAArlaDRVVVLRDG 177
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
836-1041 |
1.01e-18 |
|
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: 85.14 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 836 KKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGF--LKVQETFARVSGYCEQTDIHSP 911
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGllKPDSG----EIKVLGKdiKKEPEEVKRRIGYLPEEPSLYE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 912 SITVEESLIYSawlrlvpeinpqtkirfvkqvletieleeikdalvgvagvSGlsteQRKRLTVAVELVANPSIIFMDEP 991
Cdd:cd03230 87 NLTVRENLKLS----------------------------------------GG----MKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15228112 992 TTGLDARAAAIVMRAVKNVAETGRTIVCTIHqpsiHIFEA---FDELVLLKRG 1041
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSH----ILEEAerlCDRVAILNNG 171
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
833-1050 |
1.11e-18 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 87.06 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 833 YNEKKLqlLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGR--KTSGyieGEIRISGflkvqETFARVS--------GY 902
Cdd:COG1119 13 RGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlpPTYG---NDVRLFG-----ERRGGEDvwelrkriGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 903 C--EQTDIHSPSITVEESLI---YSAwLRLVPEINPQTKIRfVKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAV 977
Cdd:COG1119 83 VspALQLRFPRDETVLDVVLsgfFDS-IGLYREPTDEQRER-ARELLELLGLAHLADRPFG-----TLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228112 978 ELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETG-RTIVCTIHQPSIhIFEAFDELVLLKRgGRMIYSGPL 1050
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEE-IPPGITHVLLLKD-GRVVAAGPK 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
841-1049 |
1.18e-18 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 86.85 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 841 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGEIRISGFLKVQETFARVSGYCEQTDIHSPSITVE 916
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGlvEPTSGsvLIDGTDINKLKGKALRQLRRQIGMIFQQFNLIERLSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 917 ESL---------IYSAWLRLVPEinpqtkirfvkqvletielEEIKDAL-----VGVAG-----VSGLSTEQRKRLTVAV 977
Cdd:cd03256 97 ENVlsgrlgrrsTWRSLFGLFPK-------------------EEKQRALaalerVGLLDkayqrADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228112 978 ELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAET-GRTIVCTIHQPSIhIFEAFDELVLLKRgGRMIYSGP 1049
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDL-AREYADRIVGLKD-GRIVFDGP 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
154-400 |
2.33e-18 |
|
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: 86.25 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlKCYGEISYNGHGLNEVVPQ---KTSAYISQHDLHIAEMTT 230
Cdd:COG1120 16 VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK---PSSGEVLLDGRDLASLSRRelaRRIAYVPQEPPAPFGLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 231 RETIdfsarcqGVG--SRTDIMMEVSKREKDggiipdpEIDAYMKAISVKGLK-RSLQTdyilkilgldicaetlvgnam 307
Cdd:COG1120 93 RELV-------ALGryPHLGLFGRPSAEDRE-------AVEEALERTGLEHLAdRPVDE--------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 308 krgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSLlqpapesYDL------FDD 381
Cdd:COG1120 138 ---LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVL-------HDLnlaaryADR 207
|
250
....*....|....*....
gi 15228112 382 IVLMAEGKIVYHGPRDDVL 400
Cdd:COG1120 208 LVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
148-389 |
3.56e-18 |
|
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: 84.83 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 148 NEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlKCYGEISYNGHGLNEVVPQ---KTSAYISQH-DL 223
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLG---PTSGEVLVDGKDLTKLSLKelrRKVGLVFQNpDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 224 HIAEMTTRETIDFSARCQGVgsrtdimmevskrekdggiiPDPEIDAYmkaisvkglkrslqTDYILKILGLDICAETLV 303
Cdd:cd03225 87 QFFGPTVEEEVAFGLENLGL--------------------PEEEIEER--------------VEEALELVGLEGLRDRSP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 304 GNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVS----LLqpapesYDLF 379
Cdd:cd03225 133 FT-----LSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVThdldLL------LELA 201
|
250
....*....|
gi 15228112 380 DDIVLMAEGK 389
Cdd:cd03225 202 DRVIVLEDGK 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
848-1038 |
5.00e-18 |
|
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: 89.27 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 848 FRPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGflkVQETFARVSGYCEQTdihspsitveesliysAWLRL 927
Cdd:TIGR02857 345 VPPGERVALVGPSGAGKSTLLNLLLGFVDPT--EGSIAVNG---VPLADADADSWRDQI----------------AWVPQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 928 VPEINPQT---KIRF---------VKQVLETIELEEIKDAL-------VGVAGvSGLSTEQRKRLTVAVELVANPSIIFM 988
Cdd:TIGR02857 404 HPFLFAGTiaeNIRLarpdasdaeIREALERAGLDEFVAALpqgldtpIGEGG-AGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15228112 989 DEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHQPsiHIFEAFDELVLL 1038
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRL--ALAALADRIVVL 529
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
140-401 |
5.79e-18 |
|
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: 89.43 E-value: 5.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGVR-TNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENnlkcY-GEISYNGHGLNEVVP---QKT 214
Cdd:COG4988 337 IELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP----YsGSILINGVDLSDLDPaswRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 215 SAYISQHDlHIAEMTTRETIDFSARCqgvgsrtdimmevskrekdggiIPDPEIDAYMKAISVKGLKRSLQtdyilkiLG 294
Cdd:COG4988 413 IAWVPQNP-YLFAGTIRENLRLGRPD----------------------ASDEELEAALEAAGLDEFVAALP-------DG 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 295 LDicaeTLVG-NAmkRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHitNATVFV-----SL 368
Cdd:COG4988 463 LD----TPLGeGG--RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILithrlAL 534
|
250 260 270
....*....|....*....|....*....|...
gi 15228112 369 LQPApesydlfDDIVLMAEGKIVYHGPRDDVLK 401
Cdd:COG4988 535 LAQA-------DRILVLDDGRIVEQGTHEELLA 560
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
140-394 |
8.90e-18 |
|
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: 83.72 E-value: 8.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENnlKCYGEISYNGHGLNEVVPQKTS-AYI 218
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAG-LER--PDSGEILIDGRDVTGVPPERRNiGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 219 SQHDLHIAEMTTRETIDFSARCQGVgsrtdimmevskrekdggiiPDPEIDAYMKAisvkglkrslqtdyILKILGLDic 298
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGV--------------------PKAEIRARVRE--------------LLELVGLE-- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 299 aetLVGNAMKRGISGGQKKRLTTAE-MIVGPtKALFMDEITNGLDSSTAFQI---IKSLQQVAHITnaTVFVSLLQpaPE 374
Cdd:cd03259 122 ---GLLNRYPHELSGGQQQRVALARaLAREP-SLLLLDEPLSALDAKLREELreeLKELQRELGIT--TIYVTHDQ--EE 193
|
250 260
....*....|....*....|
gi 15228112 375 SYDLFDDIVLMAEGKIVYHG 394
Cdd:cd03259 194 ALALADRIAVMNEGRIVQVG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
154-342 |
1.37e-17 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 82.91 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNGHGLNEVVPQ--KTSAYISQHDLHIAEMTTR 231
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAG-LLPPSA--GEVLWNGEPIRDAREDyrRRLAYLGHADGLKPELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 232 ETIDFSARCQGVGsrtdimmevskrekdggiIPDPEIDAymkaisvkglkrslqtdyILKILGLDICAETLVGNamkrgI 311
Cdd:COG4133 94 ENLRFWAALYGLR------------------ADREAIDE------------------ALEAVGLAGLADLPVRQ-----L 132
|
170 180 190
....*....|....*....|....*....|.
gi 15228112 312 SGGQKKRLTTAEMIVGPTKALFMDEITNGLD 342
Cdd:COG4133 133 SAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
835-1041 |
2.36e-17 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 82.78 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 835 EKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSgyieGEIRISGflkvqetfarvsgyceqTDIHS-- 910
Cdd:COG1136 18 EGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGldRPTS----GEVLIDG-----------------QDISSls 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 911 ----------------------PSITVEESLIYSAWLRLVPEINPQTKIRfvkQVLETIELEEIKDALvgvagVSGLSTE 968
Cdd:COG1136 77 erelarlrrrhigfvfqffnllPELTALENVALPLLLAGVSRKERRERAR---ELLERVGLGDRLDHR-----PSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228112 969 QRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVA-ETGRTIVCTIHQPsiHIFEAFDELVLLKRG 1041
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDP--ELAARADRVIRLRDG 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
849-1088 |
6.31e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 83.32 E-value: 6.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 849 RPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGF-LKVQETFARVS-GYCEQTDIHSPSITVEESL-IYSAWL 925
Cdd:PRK13537 31 QRGECFGLLGPNGAGKTTTLRMLLGLTHPD--AGSISLCGEpVPSRARHARQRvGVVPQFDNLDPDFTVRENLlVFGRYF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 926 RLvpeiNPQTKIRFVKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMR 1005
Cdd:PRK13537 109 GL----SAAAARALVPPLLEFAKLENKADAKVG-----ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1006 AVKNVAETGRTIVCTIHqpsiHIFEA---FDELVLLKrGGRMIYSGP----LGQHSSC-VIEYFQniPGVAKIRDKYNPA 1077
Cdd:PRK13537 180 RLRSLLARGKTILLTTH----FMEEAerlCDRLCVIE-EGRKIAEGAphalIESEIGCdVIEIYG--PDPVALRDELAPL 252
|
250
....*....|.
gi 15228112 1078 TWMLEVTSESV 1088
Cdd:PRK13537 253 AERTEISGETL 263
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
839-1052 |
8.44e-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: 81.39 E-value: 8.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 839 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGEIRISGFLKVQETFARVSGYCEQTDIHSPSIT 914
Cdd:cd03261 14 TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGllRPDSGevLIDGEDISGLSEAELYRLRRRMGMLFQSGALFDSLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 915 VEESLIYsaWLRlvpE--INPQTKIR-FVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSIIFMDEP 991
Cdd:cd03261 94 VFENVAF--PLR---EhtRLSEEEIReIVLEKLEAVGLRGAEDLYP-----AELSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15228112 992 TTGLDARAAAIVMRAVKNVAET-GRTIVCTIHQPSIhIFEAFDELVLLKRgGRMIYSGPLGQ 1052
Cdd:cd03261 164 TAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDT-AFAIADRIAVLYD-GKIVAEGTPEE 223
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
849-1022 |
1.35e-16 |
|
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: 82.05 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 849 RPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGF--LKVQETFARVSGYCEQTDIHSPSITVEESLIYSAW 924
Cdd:TIGR01188 17 REGEVFGFLGPNGAGKTTTIRMLTTllRPTSG----TARVAGYdvVREPRKVRRSIGIVPQYASVDEDLTGRENLEMMGR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 925 LRLVPEINPQTKIrfvKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVM 1004
Cdd:TIGR01188 93 LYGLPKDEAEERA---EELLELFELGEAADRPVG-----TYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIW 164
|
170
....*....|....*...
gi 15228112 1005 RAVKNVAETGRTIVCTIH 1022
Cdd:TIGR01188 165 DYIRALKEEGVTILLTTH 182
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
813-1041 |
1.44e-16 |
|
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: 78.96 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 813 ITFQDLNYyvdvpvemkgqGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSgyieGEIRISGfl 890
Cdd:cd03228 1 IEFKNVSF-----------SYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRlyDPTS----GEILIDG-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 891 kvqetfarvsgyceqTDIHSPSItveesliysAWLR----LVpeinPQTKIRFVKQVLETIeleeikdalvgvagvsgLS 966
Cdd:cd03228 64 ---------------VDLRDLDL---------ESLRkniaYV----PQDPFLFSGTIRENI-----------------LS 98
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228112 967 TEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHQPSihIFEAFDELVLLKRG 1041
Cdd:cd03228 99 GGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLS--TIRDADRIIVLDDG 170
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
799-1049 |
1.50e-16 |
|
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: 85.27 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 799 EDPGKMILPFKPLTITFQDLNYyvdvpvemkgqGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKT 876
Cdd:COG2274 460 EGRSKLSLPRLKGDIELENVSF-----------RYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGlyEPT 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 877 SGyiegEIRISGF----LKVQETFARVsGYCEQtDIHSPSITVEESLIYSAwlrlvPEINPQTkirfVKQVLETIEL-EE 951
Cdd:COG2274 529 SG----RILIDGIdlrqIDPASLRRQI-GVVLQ-DVFLFSGTIRENITLGD-----PDATDEE----IIEAARLAGLhDF 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 952 IK------DALVGVAGvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHQPS 1025
Cdd:COG2274 594 IEalpmgyDTVVGEGG-SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLS 671
|
250 260
....*....|....*....|....
gi 15228112 1026 ihIFEAFDELVLLKRgGRMIYSGP 1049
Cdd:COG2274 672 --TIRLADRIIVLDK-GRIVEDGT 692
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
850-1048 |
3.58e-16 |
|
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: 78.88 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 850 PGVLTALMGISGAGKTTLLDVLAG--RKTSGYIE------GEIRISGFLKVQEtfaRVSGYCEQTDIHSPSITVEESLIY 921
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGleKPDGGTIVlngtvlFDSRKKINLPPQQ---RKIGLVFQQYALFPHLNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 922 SawlrLVPEINPQTKIRfVKQVLETIELEEIKDAlvgvaGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAA 1001
Cdd:cd03297 99 G----LKRKRNREDRIS-VDELLDLLGLDHLLNR-----YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15228112 1002 IVMRAVKNVAEtgrtivcTIHQPSIHIF----EAF---DELVLLkRGGRMIYSG 1048
Cdd:cd03297 169 QLLPELKQIKK-------NLNIPVIFVThdlsEAEylaDRIVVM-EDGRLQYIG 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
153-405 |
4.26e-16 |
|
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: 78.91 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLennLKCY-GEISYNGhglnEVVPQKTSAYISQH--------DL 223
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNG-L---LKPTsGEVLVDG----KDITKKNLRELRRKvglvfqnpDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 224 HIAEMTTRETIDFSARCQGVgsrtdimmevskrekdggiiPDPEIDAymkaisvkglkrslQTDYILKILGLDICAE--- 300
Cdd:COG1122 87 QLFAPTVEEDVAFGPENLGL--------------------PREEIRE--------------RVEEALELVGLEHLADrpp 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 301 -TLvgnamkrgiSGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTA---FQIIKSLQQvAHITnaTVFVS----LLqpa 372
Cdd:COG1122 133 hEL---------SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRrelLELLKRLNK-EGKT--VIIVThdldLV--- 197
|
250 260 270
....*....|....*....|....*....|...
gi 15228112 373 pesYDLFDDIVLMAEGKIVYHGPRDDVLKFFEE 405
Cdd:COG1122 198 ---AELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
841-1044 |
4.94e-16 |
|
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: 78.60 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 841 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGF----LKVQET--FARVSGYCEQTDIHSPSIT 914
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELP--TSGTIRVNGQdvsdLRGRAIpyLRRKIGVVFQDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 915 VEESLIYSawLRLVpEINPQTKIRFVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTG 994
Cdd:cd03292 95 VYENVAFA--LEVT-GVPPREIRKRVPAALELVGLSHKHRALP-----AELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15228112 995 LDARAAAIVMRAVKNVAETGRTIVCTIHQPSihIFEAFDELVLLKRGGRM 1044
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTTVVVATHAKE--LVDTTRHRVIALERGKL 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
154-394 |
5.27e-16 |
|
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: 78.34 E-value: 5.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlKCYGEISYNGHGLNEV------VPQKTSAyisQHDLHIae 227
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK---PTSGSIRVFGKPLEKErkrigyVPQRRSI---DRDFPI-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 228 mTTRETIdfsarCQGVGSRTDIMMEVSKREKDggiipdpeidaymKAisvkglkrslqtDYILKILGLDICAETLVGNAm 307
Cdd:cd03235 86 -SVRDVV-----LMGLYGHKGLFRRLSKADKA-------------KV------------DEALERVGLSELADRQIGEL- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 308 krgiSGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVaHITNATVFVSL--LQPAPesyDLFDDIVLM 385
Cdd:cd03235 134 ----SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVThdLGLVL---EYFDRVLLL 205
|
....*....
gi 15228112 386 AeGKIVYHG 394
Cdd:cd03235 206 N-RTVVASG 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
140-394 |
6.39e-16 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 78.00 E-value: 6.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGVRTNEANIKILTDVSGIISPGrLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHglnEVVPQKTSA--- 216
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPS---SGTIRIDGQ---DVLKQPQKLrrr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 217 --YISQHDLHIAEMTTRETIDFSARCQGvgsrtdimmevskrekdggiIPDPEIDAymkaisvkglkrslQTDYILKILG 294
Cdd:cd03264 74 igYLPQEFGVYPNFTVREFLDYIAWLKG--------------------IPSKEVKA--------------RVDEVLELVN 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 295 LDICAETLVGnamkrGISGGQKKRLTTAEMIVGPTKALFMDEITNGLD--SSTAFQIIksLQQVAhiTNATVFVS--LLQ 370
Cdd:cd03264 120 LGDRAKKKIG-----SLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDpeERIRFRNL--LSELG--EDRIVILSthIVE 190
|
250 260
....*....|....*....|....
gi 15228112 371 PAPESYdlfDDIVLMAEGKIVYHG 394
Cdd:cd03264 191 DVESLC---NQVAVLNKGKLVFEG 211
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
851-1048 |
8.37e-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: 78.53 E-value: 8.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 851 GVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGFL--KVQETF-ARVSGYCEQTDIHSPSITVEESLiysAWL 925
Cdd:cd03267 47 GEIVGFIGPNGAGKTTTLKILSGllQPTSG----EVRVAGLVpwKRRKKFlRRIGVVFGQKTQLWWDLPVIDSF---YLL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 926 RLVPEINPQTKIRFVKQVLETIELEEIKDAlvgvaGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMR 1005
Cdd:cd03267 120 AAIYDLPPARFKKRLDELSELLDLEELLDT-----PVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15228112 1006 AVKN-VAETGRTIVCTIHqpSIHIFEAFDELVLLKRGGRMIYSG 1048
Cdd:cd03267 195 FLKEyNRERGTTVLLTSH--YMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
840-1041 |
1.10e-15 |
|
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: 76.49 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 840 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGflkvqetfarvsgyceqTDIHSpsitvee 917
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGllRPTSG----RVRLDG-----------------ADISQ------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 918 sliysawlrlvpeINPQTKIRFVKQVLETIELEE--IKDALvgvagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGL 995
Cdd:cd03246 69 -------------WDPNELGDHVGYLPQDDELFSgsIAENI--------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15228112 996 DARAAAIVMRAVKNVAETGRTIVCTIHQPSihIFEAFDELVLLKRG 1041
Cdd:cd03246 128 DVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDG 171
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
833-1052 |
1.11e-15 |
|
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: 81.87 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 833 YNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGR-KTSGYIEGEIRISGF----LKVQETFARVSGYCEQTD 907
Cdd:COG1123 14 YPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlPHGGRISGEVLLDGRdlleLSEALRGRRIGMVFQDPM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 908 IHSPSITVEESLIYSAWLRLVPeinPQTKIRFVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSIIF 987
Cdd:COG1123 94 TQLNPVTVGDQIAEALENLGLS---RAEARARVLELLEAVGLERRLDRYP-----HQLSGGQRQRVAIAMALALDPDLLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228112 988 MDEPTTGLDARAAAIVMRAVKNV-AETGRTIVCTIHQPSIhIFEAFDELVLLKRgGRMIYSGPLGQ 1052
Cdd:COG1123 166 ADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGV-VAEIADRVVVMDD-GRIVEDGPPEE 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
151-391 |
1.35e-15 |
|
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: 76.91 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 151 NIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlKCYGEISYNGHGLNEVVPQKTSAYISQH-DLHIAEMT 229
Cdd:cd03226 12 GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK---ESSGSILLNGKPIKAKERRKSIGYVMQDvDYQLFTDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 230 TRETIDFSArcqgvgsrtdimmevskrekdggiipdPEIDAYMKaisvkglkrslQTDYILKILGLDICAEtlvgnAMKR 309
Cdd:cd03226 89 VREELLLGL---------------------------KELDAGNE-----------QAETVLKDLDLYALKE-----RHPL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 310 GISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVS----LLqpapesYDLFDDIVLM 385
Cdd:cd03226 126 SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVIThdyeFL------AKVCDRVLLL 199
|
....*.
gi 15228112 386 AEGKIV 391
Cdd:cd03226 200 ANGAIV 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
153-394 |
2.81e-15 |
|
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: 75.16 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlKCYGEISYNGHGLNEVVPQKTS---AYISQhdlhiaemt 229
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK---PSSGEILLDGKDLASLSPKELArkiAYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 230 tretidfsarcqgvgsrtdimmevskrekdggiipdpeidaYMKAISVKGLK-RSLQTdyilkilgldicaetlvgnamk 308
Cdd:cd03214 81 -----------------------------------------ALELLGLAHLAdRPFNE---------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 309 rgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSLlqpapesYDL------FDDI 382
Cdd:cd03214 98 --LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVL-------HDLnlaaryADRV 168
|
250
....*....|..
gi 15228112 383 VLMAEGKIVYHG 394
Cdd:cd03214 169 ILLKDGRIVAQG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
137-400 |
3.75e-15 |
|
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: 80.33 E-value: 3.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 137 LDLLKLSgVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLKCYGEISYNGH---GLNEVVPQK 213
Cdd:COG1123 5 LEVRDLS-VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRdllELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 214 TSAYISQH-DLHIAEMTTRETIDFSARCQGVgSRTDIMMEVSKrekdggiipdpeidaymkaisvkglkrslqtdyILKI 292
Cdd:COG1123 84 RIGMVFQDpMTQLNPVTVGDQIAEALENLGL-SRAEARARVLE---------------------------------LLEA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 293 LGLDicaetlvgNAMKRGI---SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATV-FVSl 368
Cdd:COG1123 130 VGLE--------RRLDRYPhqlSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVlLIT- 200
|
250 260 270
....*....|....*....|....*....|..
gi 15228112 369 lQPAPESYDLFDDIVLMAEGKIVYHGPRDDVL 400
Cdd:COG1123 201 -HDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
140-399 |
4.88e-15 |
|
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: 76.22 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNGHGLNEVVPQKTS-AYI 218
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG-LERPDS--GTILFGGEDATDVPVQERNvGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 219 SQHDLHIAEMTTRETIDFSARCQGVGSRTdimmevskrekdggiiPDPEIDAYMKAisvkglkrslqtdyILKILGLDic 298
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSERP----------------PEAEIRAKVHE--------------LLKLVQLD-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 299 aetLVGNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQV---AHITnaTVFVSLLQpaPES 375
Cdd:cd03296 128 ---WLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLhdeLHVT--TVFVTHDQ--EEA 200
|
250 260
....*....|....*....|....
gi 15228112 376 YDLFDDIVLMAEGKIVYHGPRDDV 399
Cdd:cd03296 201 LEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
164-394 |
6.05e-15 |
|
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: 75.41 E-value: 6.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 164 PGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNGHGLNEvvpQKTSAYISQHDLHIA----------EMTTRET 233
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAG-LEKPDG--GTIVLNGTVLFD---SRKKINLPPQQRKIGlvfqqyalfpHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 234 IDFSARCQGVGSRTDimmevskrekdggiipdpeidaymkaisvkglkrslQTDYILKILGLDicaetLVGNAMKRGISG 313
Cdd:cd03297 96 LAFGLKRKRNREDRI------------------------------------SVDELLDLLGLD-----HLLNRYPAQLSG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 314 GQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATV-FVSllQPAPESYDLFDDIVLMAEGKIVY 392
Cdd:cd03297 135 GEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPViFVT--HDLSEAEYLADRIVVMEDGRLQY 212
|
..
gi 15228112 393 HG 394
Cdd:cd03297 213 IG 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
832-1018 |
7.52e-15 |
|
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: 75.16 E-value: 7.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 832 GYneKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYI--EGEiRISGflkvQETFARVS---GYCE 904
Cdd:cd03224 9 GY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGllPPRSGSIrfDGR-DITG----LPPHERARagiGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 905 QTDIHSPSITVEESLIYSAWLRlvpeinpqtKIRFVKQVLETI-----ELEEIKDALVGVagvsgLSTEQRKRLTVAVEL 979
Cdd:cd03224 82 EGRRIFPELTVEENLLLGAYAR---------RRAKRKARLERVyelfpRLKERRKQLAGT-----LSGGEQQMLAIARAL 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 15228112 980 VANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIV 1018
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTIL 186
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
141-389 |
8.58e-15 |
|
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: 73.43 E-value: 8.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 141 KLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlKCYGEISYNGHGLNEVVPQKTSAYIsq 220
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK---PTSGEILIDGKDIAKLPLEELRRRI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 221 hdlhiaemttretidfsarcqgvgsrtdimmevskrekdgGIIPdpeidaymkaisvkglkrslqtdyilkilgldicae 300
Cdd:cd00267 76 ----------------------------------------GYVP------------------------------------ 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 301 tlvgnamkrGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAhITNATVFVSLLQPaPESYDLFD 380
Cdd:cd00267 80 ---------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELA-EEGRTVIIVTHDP-ELAELAAD 148
|
....*....
gi 15228112 381 DIVLMAEGK 389
Cdd:cd00267 149 RVIVLKDGK 157
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
840-1024 |
1.10e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 74.32 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 840 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISG--FLKVQETFARVSGYCEQTDIHSPSITVEE 917
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP--DSGEVRWNGtpLAEQRDEPHENILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 918 SLIYsaWLRLVpeinpQTKIRFVKQVLETIELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDA 997
Cdd:TIGR01189 93 NLHF--WAAIH-----GGAQRTIEDALAAVGLTGFEDLPAAQ-----LSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*..
gi 15228112 998 RAAAIVMRAVKNVAETGRTIVCTIHQP 1024
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
841-1041 |
2.02e-14 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 72.46 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 841 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGflkvqetfarvsgycEQTDIHSPsitvees 918
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGlyKPDSG----EILVDG---------------KEVSFASP------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 919 liysawlrlvpeinpqtkirfvkqvletieleeiKDAL-VGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDA 997
Cdd:cd03216 70 ----------------------------------RDARrAGIAMVYQLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15228112 998 RAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRG 1041
Cdd:cd03216 116 AEVERLFKVIRRLRAQGVAVIFISHRLD-EVFEIADRVTVLRDG 158
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
152-400 |
2.09e-14 |
|
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: 77.64 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 152 IKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNGHGLNEVVPQKTSA------YISQHDLH- 224
Cdd:COG1123 278 VRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG-LLRPTS--GSILFDGKDLTKLSRRSLRElrrrvqMVFQDPYSs 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 225 -IAEMTTRETIDFSARCQGVGSRTDImmevskREKdggiipdpeIDAYMKAIsvkGLKRSLQTDYIlkilgldicaetlv 303
Cdd:COG1123 355 lNPRMTVGDIIAEPLRLHGLLSRAER------RER---------VAELLERV---GLPPDLADRYP-------------- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 304 gnamkRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNAT-VFVSllqpapesYDL---- 378
Cdd:COG1123 403 -----HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTyLFIS--------HDLavvr 469
|
250 260
....*....|....*....|....
gi 15228112 379 --FDDIVLMAEGKIVYHGPRDDVL 400
Cdd:COG1123 470 yiADRVAVMYDGRIVEDGPTEEVF 493
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
850-1088 |
2.31e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.02 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 850 PGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGF-LKVQETFARVS-GYCEQTDIHSPSITVEESLI-YSAWLR 926
Cdd:PRK13536 66 SGECFGLLGPNGAGKSTIARMILGMTSPD--AGKITVLGVpVPARARLARARiGVVPQFDNLDLEFTVRENLLvFGRYFG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 927 LvpeiNPQTKIRFVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRA 1006
Cdd:PRK13536 144 M----STREIEAVIPSLLEFARLESKADARV-----SDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWER 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1007 VKNVAETGRTIVCTihqpsIHIFEAF----DELVLLKRGGRMIYSGP---LGQHSSC-VIEYFQNIPgvAKIRDKYNPAT 1078
Cdd:PRK13536 215 LRSLLARGKTILLT-----THFMEEAerlcDRLCVLEAGRKIAEGRPhalIDEHIGCqVIEIYGGDP--HELSSLVKPYA 287
|
250
....*....|
gi 15228112 1079 WMLEVTSESV 1088
Cdd:PRK13536 288 RRIEVSGETL 297
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
849-1022 |
2.57e-14 |
|
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: 78.90 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 849 RPGVLTALMGISGAGKTTLLDVLAGRK--TSG--YIEGEIRISGFLKVQETFarvsGYCEQTDIHSPSITVEESLIYSAW 924
Cdd:TIGR01257 1963 RPGECFGLLGVNGAGKTTTFKMLTGDTtvTSGdaTVAGKSILTNISDVHQNM----GYCPQFDAIDDLLTGREHLYLYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 925 LRLVP--EINpqtkiRFVKQVLETIELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAI 1002
Cdd:TIGR01257 2039 LRGVPaeEIE-----KVANWSIQSLGLSLYADRLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
170 180
....*....|....*....|
gi 15228112 1003 VMRAVKNVAETGRTIVCTIH 1022
Cdd:TIGR01257 2109 LWNTIVSIIREGRAVVLTSH 2128
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
841-1024 |
2.60e-14 |
|
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: 77.40 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 841 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAG-RKTSGyieGEIRISGF----LKVQETFARVSgYCEQtDIHSPSITV 915
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGlLDPLQ---GEVTLDGVpvssLDQDEVRRRVS-VCAQ-DAHLFDTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 916 EESLIYSAwlrlvPEINPQTkirfVKQVLETIELEEIKDALVG------VAGVSGLSTEQRKRLTVAVELVANPSIIFMD 989
Cdd:TIGR02868 426 RENLRLAR-----PDATDEE----LWAALERVGLADWLRALPDgldtvlGEGGARLSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|....*
gi 15228112 990 EPTTGLDARAAAIVMRAVkNVAETGRTIVCTIHQP 1024
Cdd:TIGR02868 497 EPTEHLDAETADELLEDL-LAALSGRTVVLITHHL 530
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
155-366 |
2.68e-14 |
|
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: 77.33 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 155 LTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEVVP---QKTSAYISQHDlHIAEMTTR 231
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT---EGSIAVNGVPLADADAdswRDQIAWVPQHP-FLFAGTIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 232 ETIDFSarcQGVGSRTDImmevskrekdggiipdpeIDAYMKAisvkGLKRSLQTdyilkiLGLDIcaETLVGNAmKRGI 311
Cdd:TIGR02857 414 ENIRLA---RPDASDAEI------------------REALERA----GLDEFVAA------LPQGL--DTPIGEG-GAGL 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15228112 312 SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAhiTNATVFV 366
Cdd:TIGR02857 460 SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLL 512
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
140-389 |
2.70e-14 |
|
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: 72.42 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGV--RTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEVVPQ---KT 214
Cdd:cd03228 1 IEFKNVsfSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT---SGEILIDGVDLRDLDLEslrKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 215 SAYISQHDlHIAEMTTRETIdfsarcqgvgsrtdimmevskrekdggiipdpeidaymkaisvkglkrslqtdyilkilg 294
Cdd:cd03228 78 IAYVPQDP-FLFSGTIRENI------------------------------------------------------------ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 295 ldicaetlvgnamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHitNATVFV-----SLL 369
Cdd:cd03228 97 ----------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIViahrlSTI 158
|
250 260
....*....|....*....|
gi 15228112 370 QpapesydLFDDIVLMAEGK 389
Cdd:cd03228 159 R-------DADRIIVLDDGR 171
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
849-1092 |
3.43e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 74.76 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 849 RPGVLTALMGISGAGKTTL----LDVLAgrKTSGyiegEIRISGFLKVQETFARVsGYceqtdihsPSITVEESLIYSAW 924
Cdd:COG4152 25 PKGEIFGLLGPNGAGKTTTiriiLGILA--PDSG----EVLWDGEPLDPEDRRRI-GYlpeerglyPKMKVGEQLVYLAR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 925 LRLVPEinPQTKIRfVKQVLETIELEEIKDALVgvagvSGLS-TEQRKrLTVAVELVANPSIIFMDEPTTGLDARAAAIV 1003
Cdd:COG4152 98 LKGLSK--AEAKRR-ADEWLERLGLGDRANKKV-----EELSkGNQQK-VQLIAALLHDPELLILDEPFSGLDPVNVELL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1004 MRAVKNVAETGRTIVCTIHQpsIHIFEAF-DELVLLKRgGRMIYSGPLGQ------------HSSCVIEYFQNIPGVAKI 1070
Cdd:COG4152 169 KDVIRELAAKGTTVIFSSHQ--MELVEELcDRIVIINK-GRKVLSGSVDEirrqfgrntlrlEADGDAGWLRALPGVTVV 245
|
250 260
....*....|....*....|..
gi 15228112 1071 RDkyNPATWMLEVTSESVETEL 1092
Cdd:COG4152 246 EE--DGDGAELKLEDGADAQEL 265
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
849-1048 |
4.14e-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: 73.31 E-value: 4.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 849 RPGVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGEIRISGFLKVQETFARVSGYCEQTDIHS--PSITVEESLIYS 922
Cdd:cd03257 29 KKGETLGLVGESGSGKSTLARAILGllKPTSGsiIFDGKDLLKLSRRLRKIRRKEIQMVFQDPMSSlnPRMTIGEQIAEP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 923 AWLRLvPEINPQTKIRFVKQVLETIEL-EEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAA 1001
Cdd:cd03257 109 LRIHG-KLSKKEARKEAVLLLLVGVGLpEEVLNRYP-----HELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQA 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15228112 1002 IVMRAVKNV-AETGRTIVCTIHQPSIHIFEAfDELVLLKrGGRMIYSG 1048
Cdd:cd03257 183 QILDLLKKLqEELGLTLLFITHDLGVVAKIA-DRVAVMY-AGKIVEEG 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
153-390 |
5.98e-14 |
|
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: 71.27 E-value: 5.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEVVPQ--KTSAYISQHDLHIAEMTT 230
Cdd:cd03230 14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD---SGEIKVLGKDIKKEPEEvkRRIGYLPEEPSLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 231 RETIDFsarcqgvgsrtdimmevskrekdggiipdpeidaymkaisvkglkrslqtdyilkilgldicaetlvgnamkrg 310
Cdd:cd03230 91 RENLKL-------------------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 311 iSGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTA---FQIIKSLQQvahiTNATVFVS--LLQPAPEsydLFDDIVLM 385
Cdd:cd03230 97 -SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRrefWELLRELKK----EGKTILLSshILEEAER---LCDRVAIL 168
|
....*
gi 15228112 386 AEGKI 390
Cdd:cd03230 169 NNGRI 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
140-399 |
6.37e-14 |
|
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: 72.60 E-value: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSG--NLENNLKCYGEISYNGHGLNEV-------- 209
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlnDLIPGAPDEGEVLLDGKDIYDLdvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 210 -----VPQKTSAYisqhdlhiaEMTTRETIDFSARCQGVGSRTDimmevskrekdggiipdpeidayMKAISVKGLKRSL 284
Cdd:cd03260 81 rrvgmVFQKPNPF---------PGSIYDNVAYGLRLHGIKLKEE-----------------------LDERVEEALRKAA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 285 QTDYILKilgldicaetlvgNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQI---IKSLQQVAHItn 361
Cdd:cd03260 129 LWDEVKD-------------RLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIeelIAELKKEYTI-- 193
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15228112 362 atVFVS--LLQPAPESydlfDDIVLMAEGKIVYHGPRDDV 399
Cdd:cd03260 194 --VIVThnMQQAARVA----DRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
833-1048 |
6.82e-14 |
|
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: 72.24 E-value: 6.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 833 YNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRktsgYI--EGEIRISGF----LKVQETFARVsGYCEQt 906
Cdd:cd03245 12 YPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL----YKptSGSVLLDGTdirqLDPADLRRNI-GYVPQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 907 DIHSPSITVEESLIYSAwlrlvPEINPQtkirfvkQVLETIELEEIK----------DALVGVAGvSGLSTEQRKRLTVA 976
Cdd:cd03245 86 DVTLFYGTLRDNITLGA-----PLADDE-------RILRAAELAGVTdfvnkhpnglDLQIGERG-RGLSGGQRQAVALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228112 977 VELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHQPSihifeaFDELV---LLKRGGRMIYSG 1048
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPS------LLDLVdriIVMDSGRIVADG 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
839-1046 |
8.14e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 71.93 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 839 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGrktsgyI----EGEIRISGFLKVQETFARVsGYCEQTDIHSPSIT 914
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILG------IilpdSGEVLFDGKPLDIAARNRI-GYLPEERGLYPKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 915 VEESLIYSAWLRlvpEINPQTKIRFVKQVLETIELEEIKDAlvgvaGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTG 994
Cdd:cd03269 87 VIDQLVYLAQLK---GLKKEEARRRIDEWLERLELSEYANK-----RVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15228112 995 LDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRGGRMIY 1046
Cdd:cd03269 159 LDPVNVELLKDVIRELARAGKTVILSTHQME-LVEELCDRVLLLNKGRAVLY 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
153-399 |
1.08e-13 |
|
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: 72.22 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEVVPQKT------SAYISQHDLHIA 226
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT---SGSVLIDGTDINKLKGKALrqlrrqIGMIFQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 227 EMTTRETIdFSARcqgVGSRT---DIMMEVSKREKDGGIipdpeidaymkaisvkglkrslqtdYILKILGLDICAETLV 303
Cdd:cd03256 92 RLSVLENV-LSGR---LGRRStwrSLFGLFPKEEKQRAL-------------------------AALERVGLLDKAYQRA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 304 GNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSLLQPapesyDL----F 379
Cdd:cd03256 143 DQ-----LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQV-----DLareyA 212
|
250 260
....*....|....*....|
gi 15228112 380 DDIVLMAEGKIVYHGPRDDV 399
Cdd:cd03256 213 DRIVGLKDGRIVFDGPPAEL 232
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
847-1018 |
1.30e-13 |
|
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: 72.38 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 847 AFRPGVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGEiRISGfLKVQE--------TFARVSGYceqtdihsPSIT 914
Cdd:COG0411 26 EVERGEIVGLIGPNGAGKTTLFNLITGfyRPTSGriLFDGR-DITG-LPPHRiarlgiarTFQNPRLF--------PELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 915 VEESL-----------IYSAWLRLVPEINPQTKIR-FVKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVAN 982
Cdd:COG0411 96 VLENVlvaaharlgrgLLAALLRLPRARREEREAReRAEELLERVGLADRADEPAG-----NLSYGQQRRLEIARALATE 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 15228112 983 PSIIFMDEPTTGLDARAAAIVMRAVKNV-AETGRTIV 1018
Cdd:COG0411 171 PKLLLLDEPAAGLNPEETEELAELIRRLrDERGITIL 207
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
832-1048 |
1.36e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 72.35 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 832 GYNEKKLqlLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIE-GEIRISGFLKVQetFARVSGYCEQTDI 908
Cdd:PRK11231 11 GYGTKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARllTPQSGTVFlGDKPISMLSSRQ--LARRLALLPQHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 909 HSPSITVEESLIY--SAWLRLVPEINPQTKIRfVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSII 986
Cdd:PRK11231 87 TPEGITVRELVAYgrSPWLSLWGRLSAEDNAR-VNQAMEQTRINHLADRRL-----TDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228112 987 FMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIH---QPSIHIfeafDELVLLKrGGRMIYSG 1048
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQASRYC----DHLVVLA-NGHVMAQG 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
140-391 |
1.59e-13 |
|
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: 71.13 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNGHGLNEVVPQKTS-AYI 218
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAG-LEEPTS--GRIYIGGRDVTDLPPKDRDiAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 219 SQHDLHIAEMTTRETIDFSARCQGVgsrtdimmevskrekdggiiPDPEIDaymkaisvkglKRSLQTDYILKIlgldic 298
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKV--------------------PKDEID-----------ERVREVAELLQI------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 299 aETLVGNAMKRgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQI---IKSLQQVAHITnaTVFVSLLQpaPES 375
Cdd:cd03301 121 -EHLLDRKPKQ-LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMraeLKRLQQRLGTT--TIYVTHDQ--VEA 194
|
250
....*....|....*.
gi 15228112 376 YDLFDDIVLMAEGKIV 391
Cdd:cd03301 195 MTMADRIAVMNDGQIQ 210
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
832-1048 |
1.86e-13 |
|
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: 71.49 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 832 GYNEKKlQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEG----EIRISGFLK-----VQETFAR 898
Cdd:cd03254 11 SYDEKK-PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfyDPQKGqiLIDGidirDISRKSLRSmigvvLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 899 VSGYCEQTDIHSPSITVEEsliysaWLRLVPEINPQTKIRFVKQVLETIeleeikdalVGVAGvSGLSTEQRKRLTVAVE 978
Cdd:cd03254 90 SGTIMENIRLGRPNATDEE------VIEAAKEAGAHDFIMKLPNGYDTV---------LGENG-GNLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 979 LVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHQPSIhIFEAfDELVLLKRgGRMIYSG 1048
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLST-IKNA-DKILVLDD-GKIIEEG 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
154-400 |
3.10e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 71.34 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEVVPQ---KTSAYISQHdlhiaemtT 230
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD---SGEVRLNGRPLADWSPAelaRRRAVLPQH--------S 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 231 RETIDFSARcqgvgsrtdimmEV----------SKREKdggiipDPEIDAYMKAISVKGLK-RSLQTdyilkilgldica 299
Cdd:PRK13548 86 SLSFPFTVE------------EVvamgraphglSRAED------DALVAAALAQVDLAHLAgRDYPQ------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 300 etlvgnamkrgISGGQKKRLTTAEMIV------GPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSLlqpap 373
Cdd:PRK13548 135 -----------LSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVL----- 198
|
250 260 270
....*....|....*....|....*....|...
gi 15228112 374 esYDL------FDDIVLMAEGKIVYHGPRDDVL 400
Cdd:PRK13548 199 --HDLnlaaryADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
832-1042 |
3.41e-13 |
|
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: 70.72 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 832 GYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAgrKTSGYIEGEIRISGfLKVQE----TFARVSGYCEQtD 907
Cdd:cd03251 9 RYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIP--RFYDVDSGRILIDG-HDVRDytlaSLRRQIGLVSQ-D 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 908 IHSPSITVEESLIYSAwlrlvPEINPQTKIRFVKQV--LETI-ELEEIKDALVGVAGVSgLSTEQRKRLTVAVELVANPS 984
Cdd:cd03251 85 VFLFNDTVAENIAYGR-----PGATREEVEEAARAAnaHEFImELPEGYDTVIGERGVK-LSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15228112 985 IIFMDEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHQPSIhIFEAfDELVLLKRGG 1042
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLST-IENA-DRIVVLEDGK 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
140-390 |
3.87e-13 |
|
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: 70.21 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGVR----TNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNGHGLNEVVPQKTS 215
Cdd:cd03255 1 IELKNLSktygGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG-LDRPTS--GEVRVDGTDISKLSEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 216 AY----IS----QHDLhIAEMTTRETIDFSARCQGVGSRtdimmevskrekdggiipdpeiDAYMKAISVkglkrslqtd 287
Cdd:cd03255 78 AFrrrhIGfvfqSFNL-LPDLTALENVELPLLLAGVPKK----------------------ERRERAEEL---------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 288 yiLKILGLDICAETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNAT-VFV 366
Cdd:cd03255 125 --LERVGLGDRLNHYPSE-----LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTiVVV 197
|
250 260
....*....|....*....|....
gi 15228112 367 SllqPAPESYDLFDDIVLMAEGKI 390
Cdd:cd03255 198 T---HDPELAEYADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
142-401 |
4.05e-13 |
|
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: 70.61 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 142 LSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlkcygeisynghglnevvPQKTSAYISQH 221
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR--------------------PDSGEVLIDGE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 222 DlhIAEMTTRETIDFSARC----QGVGSRTDimMEVSK------REKdgGIIPDPEIDaymkaisvkglkrslqtdyilk 291
Cdd:cd03261 63 D--ISGLSEAELYRLRRRMgmlfQSGALFDS--LTVFEnvafplREH--TRLSEEEIR---------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 292 ilglDICAETL--VG-----NAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLD--SSTAF-QIIKSLQQVAHITn 361
Cdd:cd03261 115 ----EIVLEKLeaVGlrgaeDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDpiASGVIdDLIRSLKKELGLT- 189
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15228112 362 aTVFVSllQPAPESYDLFDDIVLMAEGKIVYHGPRDDVLK 401
Cdd:cd03261 190 -SIMVT--HDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
839-1024 |
6.27e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 70.33 E-value: 6.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 839 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLaGRKTSGYIEGEIRISGFLKVQETFA--------RVSgYCEQTDIHS 910
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-NRLIELYPEARVSGEVYLDGQDIFKmdvielrrRVQ-MVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 911 PSITVEESLIYSAWLRLVPEINPQTKIRfVKQVLETIEL-EEIKDALVGVAGvsGLSTEQRKRLTVAVELVANPSIIFMD 989
Cdd:PRK14247 95 PNLSIFENVALGLKLNRLVKSKKELQER-VRWALEKAQLwDEVKDRLDAPAG--KLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 15228112 990 EPTTGLD----ARAAAIVMRAVKNVaetgrTIVCTIHQP 1024
Cdd:PRK14247 172 EPTANLDpentAKIESLFLELKKDM-----TIVLVTHFP 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
157-394 |
8.68e-13 |
|
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: 69.32 E-value: 8.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 157 DVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlkcygeisynghglnevvPQKTSAYISQHDLhiaemtTRETIDF 236
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLK--------------------PTSGRATVAGHDV------VREPREV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 237 SARCQGVGSRTDIMMEVSKREkdggiipdpeiDAYMKA--ISVKGLKRSLQTDYILKILGLDICAETLVGNamkrgISGG 314
Cdd:cd03265 72 RRRIGIVFQDLSVDDELTGWE-----------NLYIHArlYGVPGAERRERIDELLDFVGLLEAADRLVKT-----YSGG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 315 QKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSlLQPAPESYDLFDDIVLMAEGKIVYHG 394
Cdd:cd03265 136 MRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLT-THYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
841-1041 |
8.83e-13 |
|
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: 69.68 E-value: 8.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 841 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGEiRISGfLKVQEtfaRVSGYCEQTDIHSPSITVE 916
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGleRPDSGtiLFGGE-DATD-VPVQE---RNVGFVFQHYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 917 ESLIYSAWLRLVPEINPQTKIRF-VKQVLETIELEEIKDALvgvagVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGL 995
Cdd:cd03296 93 DNVAFGLRVKPRSERPPEAEIRAkVHELLKLVQLDWLADRY-----PAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15228112 996 DARAAAIVMRAVKNVA-ETGRTIVCTIHQPSiHIFEAFDELVLLKRG 1041
Cdd:cd03296 168 DAKVRKELRRWLRRLHdELHVTTVFVTHDQE-EALEVADRVVVMNKG 213
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
808-1041 |
9.24e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 9.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 808 FKPLTITFQ---DLNYYVDVPVEMKGQGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYIEGEI 884
Cdd:COG2401 10 LMRVTKVYSsvlDLSERVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 885 risgflkvqetfarvsgyceqtDIHSPSITVEESLIYSAWlrlvpeinpqtKIRFVKQVLETIELEEIKDALVGVAGVSG 964
Cdd:COG2401 90 ----------------------DVPDNQFGREASLIDAIG-----------RKGDFKDAVELLNAVGLSDAVLWLRRFKE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 965 LSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVA-ETGRT-IVCTIH-------QPSIHIFEAFDEL 1035
Cdd:COG2401 137 LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLArRAGITlVVATHHydviddlQPDLLIFVGYGGV 216
|
....*.
gi 15228112 1036 VLLKRG 1041
Cdd:COG2401 217 PEEKRR 222
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
841-1022 |
1.64e-12 |
|
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: 67.83 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 841 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIE---GEIRIS--GFLKVQETFARVSGYCEQtDIHSPsi 913
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGllRPQSGAVLidgEPLDYSrkGLLERRQRVGLVFQDPDD-QLFAA-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 914 TVEESLIYSAwLRLVpeinpqtkirfvkqvLETIELEE-IKDALVGVaGVSG--------LSTEQRKRLTVAVELVANPS 984
Cdd:TIGR01166 85 DVDQDVAFGP-LNLG---------------LSEAEVERrVREALTAV-GASGlrerpthcLSGGEKKRVAIAGAVAMRPD 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 15228112 985 IIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIH 1022
Cdd:TIGR01166 148 VLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
850-1024 |
2.17e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.59 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 850 PGVLTALMGISGAGKTTLLDVLAG--RKTSGYIEGEIRISGFLKVQEtfarVSGYCEQTDIHSPSITVEESLiysawlrl 927
Cdd:PRK13539 27 AGEALVLTGPNGSGKTTLLRLIAGllPPAAGTIKLDGGDIDDPDVAE----ACHYLGHRNAMKPALTVAENL-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 928 vpeinpqtkiRFVKQVLETIELEeIKDAL--VGVAGVSG-----LSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAA 1000
Cdd:PRK13539 95 ----------EFWAAFLGGEELD-IAAALeaVGLAPLAHlpfgyLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170 180
....*....|....*....|....
gi 15228112 1001 AIVMRAVKNVAETGRTIVCTIHQP 1024
Cdd:PRK13539 164 ALFAELIRAHLAQGGIVIAATHIP 187
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
140-401 |
2.48e-12 |
|
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: 68.23 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEVVPQKTSAY-I 218
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT---SGSVLFDGEDITGLPPHEIARLgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 219 S---QHDLHIAEMTTRETIDFSARCQgvgSRTDIMMEVSKREKdggiipdPEIDAymkaisvkglkrslQTDYILKILGL 295
Cdd:cd03219 78 GrtfQIPRLFPELTVLENVMVAAQAR---TGSGLLLARARREE-------REARE--------------RAEELLERVGL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 296 DICAETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFV----SLLqp 371
Cdd:cd03219 134 ADLADRPAGE-----LSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVehdmDVV-- 206
|
250 260 270
....*....|....*....|....*....|
gi 15228112 372 apesYDLFDDIVLMAEGKIVYHGPRDDVLK 401
Cdd:cd03219 207 ----MSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
154-389 |
2.68e-12 |
|
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: 67.49 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlKCYGEISYNGhglnevvpqkTSAYISQHDLhIAEMTTRET 233
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE---KLSGSVSVPG----------SIAYVSQEPW-IQNGTIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 234 IDFSArcqgvgsrtdimmevskrekdggiipdpEIDA--YMKAISVKGLKRslqtDyiLKIL-GLDicaETLVGnamKRG 310
Cdd:cd03250 86 ILFGK----------------------------PFDEerYEKVIKACALEP----D--LEILpDGD---LTEIG---EKG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 311 I--SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVF-----VSLLQPApesydlfDDIV 383
Cdd:cd03250 126 InlSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRIlvthqLQLLPHA-------DQIV 198
|
....*.
gi 15228112 384 LMAEGK 389
Cdd:cd03250 199 VLDNGR 204
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
849-1018 |
2.74e-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: 68.08 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 849 RPGVLTALMGISGAGKTTLLDVLAG--RKTSGYI--EGEiRISGflkvQETFARVS---GYCEQT-DIHsPSITVEESLI 920
Cdd:COG0410 27 EEGEIVALLGRNGAGKTTLLKAISGllPPRSGSIrfDGE-DITG----LPPHRIARlgiGYVPEGrRIF-PSLTVEENLL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 921 YSAWLRlvpeinpqTKIRFVKQVLETI-----ELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGL 995
Cdd:COG0410 101 LGAYAR--------RDRAEVRADLERVyelfpRLKERRRQRAGT-----LSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
170 180
....*....|....*....|...
gi 15228112 996 DARAAAIVMRAVKNVAETGRTIV 1018
Cdd:COG0410 168 APLIVEEIFEIIRRLNREGVTIL 190
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
140-420 |
2.99e-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: 68.03 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEVVPQK-TSAYI 218
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPT---SGEILLDGKDITNLPPHKrPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 219 SQHDLHIAEMTTRETIDFSARCQGVgSRTDIMMEVSKrekdggiipdpeidaYMKAISVKGLkrslqtdyilkilgldic 298
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKL-PKAEIKERVAE---------------ALDLVQLEGY------------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 299 aetlvGNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSS--TAFQI-IKSLQQVAHITnaTVFVSLLQpaPES 375
Cdd:cd03300 124 -----ANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKlrKDMQLeLKRLQKELGIT--FVFVTHDQ--EEA 194
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 15228112 376 YDLFDDIVLMAEGKIVYHG-PRDdvlkFFEEcgfqcPERKGVADFL 420
Cdd:cd03300 195 LTMSDRIAVMNKGKIQQIGtPEE----IYEE-----PANRFVADFI 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
841-1041 |
3.46e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.71 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 841 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISG----FLKVQETFArvSG----YCEqtdIH-SP 911
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD--AGSILIDGqemrFASTTAALA--AGvaiiYQE---LHlVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 912 SITVEESLiysaWLRLVPE----INPQTKIRFVKQvletiELEEIKDALVGVAGVSGLSTEQRKRLTVAVELVANPSIIF 987
Cdd:PRK11288 93 EMTVAENL----YLGQLPHkggiVNRRLLNYEARE-----QLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15228112 988 MDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRG 1041
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRME-EIFALCDAITVFKDG 216
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
154-401 |
4.20e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.31 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNL-----ENNLKCYGEISYNGHGLNEVVPQKTS---AYISQHDLHI 225
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaPRGARVTGDVTLNGEPLAAIDAPRLArlrAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 226 AEMTTRETIDFS----ARCQGVGSRtdimmevskreKDGGIIpdpeidayMKAISVKGlkrslqtdyilkilgldicAET 301
Cdd:PRK13547 96 FAFSAREIVLLGryphARRAGALTH-----------RDGEIA--------WQALALAG-------------------ATA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 302 LVGNAMKRgISGGQKKRLTTAEMI---------VGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSLLQPA 372
Cdd:PRK13547 138 LVGRDVTT-LSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPN 216
|
250 260
....*....|....*....|....*....
gi 15228112 373 PESYDLfDDIVLMAEGKIVYHGPRDDVLK 401
Cdd:PRK13547 217 LAARHA-DRIAMLADGAIVAHGAPADVLT 244
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
823-1049 |
4.34e-12 |
|
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: 67.70 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 823 DVPVEMKG--QGYNEKklQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGflkvqETFAR 898
Cdd:COG1127 3 EPMIEVRNltKSFGDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGllRPDSG----EILVDG-----QDITG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 899 VSGYcEQTDIHSP------------SITVEESLIYsaWLRLVPEINPQTKIRFVKQVLEtieleeikdaLVGVAGV---- 962
Cdd:COG1127 72 LSEK-ELYELRRRigmlfqggalfdSLTVFENVAF--PLREHTDLSEAEIRELVLEKLE----------LVGLPGAadkm 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 963 -SGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAET-GRTIVCTIHQ-PSihIFEAFDELVLLK 1039
Cdd:COG1127 139 pSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDlDS--AFAIADRVAVLA 216
|
250
....*....|
gi 15228112 1040 RgGRMIYSGP 1049
Cdd:COG1127 217 D-GKIIAEGT 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
140-365 |
6.73e-12 |
|
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: 66.73 E-value: 6.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGV----RTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNGHGLNEVVPQKts 215
Cdd:cd03293 1 LEVRNVsktyGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAG-LERPTS--GEVLVDGEPVTGPGPDR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 216 AYISQHDLHIAEMTTRETIDFSARCQGvgsrtdimmeVSKREKdggiipDPEIDAYMKAIsvkGLKRSLqtdyilkilgl 295
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLELQG----------VPKAEA------RERAEELLELV---GLSGFE----------- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228112 296 dicaetlvgNAMKRGISGGQKKRLTTAE-MIVGPtKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVF 365
Cdd:cd03293 126 ---------NAYPHQLSGGMRQRVALARaLAVDP-DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVL 186
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
151-401 |
1.47e-11 |
|
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: 66.02 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 151 NIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALsgnlennLKCY----GEISYNGHGLNEVVPQKTS---AYISQhDL 223
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL-------ERFYdptsGEILLDGVDIRDLNLRWLRsqiGLVSQ-EP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 224 HIAEMTTRETIDFsarcqGVGSRTDIMMEVSKREKdggiipdpEIDAYmkaisvkglkrslqtdyilkILGLDICAETLV 303
Cdd:cd03249 87 VLFDGTIAENIRY-----GKPDATDEEVEEAAKKA--------NIHDF--------------------IMSLPDGYDTLV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 304 GNamkRG--ISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVahITNATVFV-----SLLQPApesy 376
Cdd:cd03249 134 GE---RGsqLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA--MKGRTTIViahrlSTIRNA---- 204
|
250 260
....*....|....*....|....*
gi 15228112 377 dlfDDIVLMAEGKIVYHGPRDDVLK 401
Cdd:cd03249 205 ---DLIAVLQNGQVVEQGTHDELMA 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
139-397 |
2.08e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 67.28 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 139 LLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNGHGLNEVVPQK----T 214
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAG-FETPDS--GRIMLDGQDITHVPAENrhvnT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 215 sayISQHDLHIAEMTTRETIDFSARCQGVgsrtdimmevskrekdggiiPDPEIDaymkaisvkglKRSLQTdyiLKILG 294
Cdd:PRK09452 91 ---VFQSYALFPHMTVFENVAFGLRMQKT--------------------PAAEIT-----------PRVMEA---LRMVQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 295 LDICAETLVgnamkRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQI---IKSLQQVAHITnaTVFVSLLQp 371
Cdd:PRK09452 134 LEEFAQRKP-----HQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMqneLKALQRKLGIT--FVFVTHDQ- 205
|
250 260
....*....|....*....|....*..
gi 15228112 372 aPESYDLFDDIVLMAEGKIVYHG-PRD 397
Cdd:PRK09452 206 -EEALTMSDRIVVMRDGRIEQDGtPRE 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
851-1048 |
3.12e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.42 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 851 GVLTALMGISGAGKTTLLdvlagRKTSGYIEG----EIRISGFLKVQETFARVSGYCEQTDIHSPSI----------TVE 916
Cdd:PRK09984 30 GEMVALLGPSGSGKSTLL-----RHLSGLITGdksaGSHIELLGRTVQREGRLARDIRKSRANTGYIfqqfnlvnrlSVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 917 ESLIYSA------WLRLVPEINPQTKIRFVKQvletieLEEIKDALVGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDE 990
Cdd:PRK09984 105 ENVLIGAlgstpfWRTCFSWFTREQKQRALQA------LTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15228112 991 PTTGLDARAAAIVMRAVKNVAET-GRTIVCTIHQPSIHIfeAFDELVLLKRGGRMIYSG 1048
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYAL--RYCERIVALRQGHVFYDG 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
153-365 |
3.23e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 65.18 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALS--GNLENNLKCYGEISYNGHGL-----NEVVPQKTSAYISQHDlHI 225
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEVTITGSIVYNGHNIysprtDTVDLRKEIGMVFQQP-NP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 226 AEMTTRETIDFSARCQGVgsrtdimmevskreKDggiipdpeidaymKAISVKGLKRSLQTDYIlkilgLDICAETLVGN 305
Cdd:PRK14239 98 FPMSIYENVVYGLRLKGI--------------KD-------------KQVLDEAVEKSLKGASI-----WDEVKDRLHDS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228112 306 AMkrGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQI----------------IKSLQQVAHITNATVF 365
Cdd:PRK14239 146 AL--GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIeetllglkddytmllvTRSMQQASRISDRTGF 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
839-1049 |
3.30e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.41 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 839 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYI--EGE---IRISGFLKVQETFARVSGYCEQ----TD 907
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGllRPQKGAVlwQGKpldYSKRGLLALRQQVATVFQDPEQqifyTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 908 IHSpsitveeSLIYSAWLRLVPEinpQTKIRFVKQVLETIELEEIKDAlvgvaGVSGLSTEQRKRLTVAVELVANPSIIF 987
Cdd:PRK13638 95 IDS-------DIAFSLRNLGVPE---AEITRRVDEALTLVDAQHFRHQ-----PIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15228112 988 MDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIhIFEAFDELVLLKRGGRMIYSGP 1049
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHGAP 220
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
840-1024 |
3.51e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 64.05 E-value: 3.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 840 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIEGEIRISGFlkVQETFARVSGYCEQTDIHSPSITVEE 917
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGlsPPLAGRVLLNGGPLDF--QRDSIARGLLYLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 918 SLiysawlRLVPEINPQTKIrfvKQVLETIELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDA 997
Cdd:cd03231 93 NL------RFWHADHSDEQV---EEALARVGLNGFEDRPVAQ-----LSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180
....*....|....*....|....*..
gi 15228112 998 RAAAIVMRAVKNVAETGRTIVCTIHQP 1024
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
840-1041 |
3.53e-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: 64.03 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 840 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAgrktsgyieGEI-RISGFLKVQETFArvsgYCEQTdihsPSI---TV 915
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALL---------GELeKLSGSVSVPGSIA----YVSQE----PWIqngTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 916 EESLIYSAwlrlvpEINPQtkirFVKQVLETIELEEIKDAL-------VGVAGVSgLSTEQRKRLTVAVELVANPSIIFM 988
Cdd:cd03250 83 RENILFGK------PFDEE----RYEKVIKACALEPDLEILpdgdlteIGEKGIN-LSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15228112 989 DEPTTGLDAR-AAAIVMRAVKNVAETGRTIVCTIHQpsIHIFEAFDELVLLKRG 1041
Cdd:cd03250 152 DDPLSAVDAHvGRHIFENCILGLLLNNKTRILVTHQ--LQLLPHADQIVVLDNG 203
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
848-1018 |
3.60e-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: 67.62 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 848 FRPGVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGEiRISGFLKVQ-ETFARVSGYCEQTDIHS--PSITVEESLi 920
Cdd:COG1123 288 LRRGETLGLVGESGSGKSTLARLLLGllRPTSGsiLFDGK-DLTKLSRRSlRELRRRVQMVFQDPYSSlnPRMTVGDII- 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 921 ySAWLRLVPEINPQTKIRFVKQVLETIEL-EEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARA 999
Cdd:COG1123 366 -AEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPH-----ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSV 439
|
170 180
....*....|....*....|
gi 15228112 1000 AAIVMRAVKNV-AETGRTIV 1018
Cdd:COG1123 440 QAQILNLLRDLqRELGLTYL 459
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
1190-1354 |
4.05e-11 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 63.68 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1190 FTVLGAIYGLVLFVGINNCTSALqYFETERNVMYRERFAGMySAFAYALAQVVTEIPYIFIQSAEFVIVIYPMIGFYASF 1269
Cdd:COG0842 4 FLVPGLLAMSLLFTALMLTALSI-AREREQGTLERLLVTPV-SRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1270 SKVFWSLYAMFCNLLCFNYLAMFLISITPNFMVAAILQSLFFTTFNIFAGFLIPKPQIPKWWVWFYYITPTSWTLNLFFS 1349
Cdd:COG0842 82 LSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRA 161
|
....*
gi 15228112 1350 SQYGD 1354
Cdd:COG0842 162 LFLGG 166
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
849-1045 |
4.39e-11 |
|
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: 64.03 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 849 RPGVLTALMGISGAGKTTLLDVLAG--RKTSgyieGEIRISGfLKVQETFARVsGYCEQTDIHSPSITVEESLIysawlr 926
Cdd:cd03293 28 EEGEFVALVGPSGCGKSTLLRIIAGleRPTS----GEVLVDG-EPVTGPGPDR-GYVFQQDALLPWLTVLDNVA------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 927 LVPEINPQTKIRFVKQVLETIEleeikdaLVGVAGVSG-----LSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAA 1001
Cdd:cd03293 96 LGLELQGVPKAEARERAEELLE-------LVGLSGFENayphqLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTRE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15228112 1002 IVMRAVKNV-AETGRTIVCTIHQpsihIFEAF---DELVLL-KRGGRMI 1045
Cdd:cd03293 169 QLQEELLDIwRETGKTVLLVTHD----IDEAVflaDRVVVLsARPGRIV 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
145-367 |
4.84e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 63.97 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 145 VRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnleNNLKCYGEISYNGHGLNEvVPQKTSAYISQH--- 221
Cdd:cd03292 7 TKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYK---EELPTSGTIRVNGQDVSD-LRGRAIPYLRRKigv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 222 ----DLHIAEMTTRETIDFSARCQGVGSRtdimmEVSKREKDggiipdpeidaymkaisvkglkrslqtdyILKILGLDI 297
Cdd:cd03292 83 vfqdFRLLPDRNVYENVAFALEVTGVPPR-----EIRKRVPA-----------------------------ALELVGLSH 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 298 CAetlvgNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVaHITNATVFVS 367
Cdd:cd03292 129 KH-----RALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVA 192
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
139-394 |
5.04e-11 |
|
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: 64.06 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 139 LLKLSGV----RTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNGHGLNEVVPQ-- 212
Cdd:cd03257 1 LLEVKNLsvsfPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILG-LLKPTS--GSIIFDGKDLLKLSRRlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 213 ----KTSAYISQhDLHIA---EMTTRETIDFSARCQGVGSRTDIMMEVSKREKDGgiIPDPEIDAYMKAisvkglkrslq 285
Cdd:cd03257 78 kirrKEIQMVFQ-DPMSSlnpRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVG--VGLPEEVLNRYP----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 286 tdyilkilgldicaetlvgnamkRGISGGQKKRLTTAE-MIVGPtKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATV 364
Cdd:cd03257 144 -----------------------HELSGGQRQRVAIARaLALNP-KLLIADEPTSALDVSVQAQILDLLKKLQEELGLTL 199
|
250 260 270
....*....|....*....|....*....|....*
gi 15228112 365 -FVS----LLQpapesyDLFDDIVLMAEGKIVYHG 394
Cdd:cd03257 200 lFIThdlgVVA------KIADRVAVMYAGKIVEEG 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
148-394 |
6.42e-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: 6.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 148 NEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEVVPQKTSA---YISQhDLH 224
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT---SGSVLLDGTDIRQLDPADLRRnigYVPQ-DVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 225 IAEMTTRETIDFSArcqgvgsrtdimmevskrekdgGIIPDPEIdayMKAISVKGLkrslqTDYILKI-LGLDicaeTLV 303
Cdd:cd03245 89 LFYGTLRDNITLGA----------------------PLADDERI---LRAAELAGV-----TDFVNKHpNGLD----LQI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 304 GNAmKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQV-AHITN--ATVFVSLLqpapesyDLFD 380
Cdd:cd03245 135 GER-GRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlGDKTLiiITHRPSLL-------DLVD 206
|
250
....*....|....
gi 15228112 381 DIVLMAEGKIVYHG 394
Cdd:cd03245 207 RIIVMDSGRIVADG 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
140-400 |
8.19e-11 |
|
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: 63.22 E-value: 8.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlKCYGEISYNGHGLNEVVPQKTS---- 215
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP---PRSGSIRFDGRDITGLPPHERAragi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 216 AYISQHDLHIAEMTTRETIDFSARCQGVGSRTDIMMEVSkrekdgGIIPDpeidaymkaisvkgLKRSLQTDyilkilgl 295
Cdd:cd03224 78 GYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVY------ELFPR--------------LKERRKQL-------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 296 dicAETLvgnamkrgiSGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHiTNATVfvsLL--QPAP 373
Cdd:cd03224 130 ---AGTL---------SGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTI---LLveQNAR 193
|
250 260
....*....|....*....|....*..
gi 15228112 374 ESYDLFDDIVLMAEGKIVYHGPRDDVL 400
Cdd:cd03224 194 FALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
144-401 |
8.92e-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: 63.40 E-value: 8.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 144 GVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSgnlennlKCY----GEISYNGHGLNEVVPQ---KTSA 216
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIP-------RFYdvdsGRILIDGHDVRDYTLAslrRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 217 YISQhDLHIAEMTTRETIDFSARcqgvgsrtdimmevskrekdggiipdpeiDAYMKAIsVKGLKRSLQTDYILKI-LGL 295
Cdd:cd03251 80 LVSQ-DVFLFNDTVAENIAYGRP-----------------------------GATREEV-EEAARAANAHEFIMELpEGY 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 296 DicaeTLVGnamKRGI--SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAhiTNATVFV-----SL 368
Cdd:cd03251 129 D----TVIG---ERGVklSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLM--KNRTTFViahrlST 199
|
250 260 270
....*....|....*....|....*....|...
gi 15228112 369 LQPApesydlfDDIVLMAEGKIVYHGPRDDVLK 401
Cdd:cd03251 200 IENA-------DRIVVLEDGKIVERGTHEELLA 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
813-1048 |
1.00e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 64.48 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 813 ITFQDLNY-YVDVPVEMKGQGYNEKKlqllseitgafrpGVLTALMGISGAGKTTLLDVLAG--RKTSGYI-----EGEI 884
Cdd:PRK13636 6 LKVEELNYnYSDGTHALKGININIKK-------------GEVTAILGGNGAGKSTLFQNLNGilKPSSGRIlfdgkPIDY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 885 RISGFLKVQETFARVSgycEQTDIHSPSITVEESLIYSAWLRLVPEINPQTKIRfvkQVLETIELEEIKDAlvgvaGVSG 964
Cdd:PRK13636 73 SRKGLMKLRESVGMVF---QDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVD---NALKRTGIEHLKDK-----PTHC 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 965 LSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVA-ETGRTIVCTIHqpSIHIFEAFDELVLLKRGGR 1043
Cdd:PRK13636 142 LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQkELGLTIIIATH--DIDIVPLYCDNVFVMKEGR 219
|
....*
gi 15228112 1044 MIYSG 1048
Cdd:PRK13636 220 VILQG 224
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
848-1048 |
1.17e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 63.55 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 848 FRPGVLTALMGISGAGKTTLLDVLAGRKtsGY--IEGEIRISG----FLKVQETFARVSGYCEQTDIHSPSITVEESLIY 921
Cdd:COG0396 23 IKPGEVHAIMGPNGSGKSTLAKVLMGHP--KYevTSGSILLDGedilELSPDERARAGIFLAFQYPVEIPGVSVSNFLRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 922 SAWLRLVPEINPQTKIRFVKQVLETIELEEikDAL---VGVagvsGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDAR 998
Cdd:COG0396 101 ALNARRGEELSAREFLKLLKEKMKELGLDE--DFLdryVNE----GFSGGEKKRNEILQMLLLEPKLAILDETDSGLDID 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15228112 999 AAAIVMRAVKNVAETGRTIVCTIHQPSI--HIfEAfDELVLLKrGGRMIYSG 1048
Cdd:COG0396 175 ALRIVAEGVNKLRSPDRGILIITHYQRIldYI-KP-DFVHVLV-DGRIVKSG 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
848-1018 |
1.27e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.42 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 848 FRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGflkvqetfarvsgycEQTDIHSPS------ItveeSL 919
Cdd:COG1129 27 LRPGEVHALLGENGAGKSTLMKILSGvyQPDSG----EILLDG---------------EPVRFRSPRdaqaagI----AI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 920 IYSAwLRLVPEI---------NPQTKIRFV---------KQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVA 981
Cdd:COG1129 84 IHQE-LNLVPNLsvaeniflgREPRRGGLIdwramrrraRELLARLGLDIDPDTPVG-----DLSVAQQQLVEIARALSR 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 15228112 982 NPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIV 1018
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLFRIIRRLKAQGVAII 194
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
847-1048 |
1.29e-10 |
|
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: 62.51 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 847 AFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYieGEIRISGflkVQETFAR-----VSGYCEQTDIHsPSITVEESLIY 921
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQS--GRVLING---VDVTAAPpadrpVSMLFQENNLF-AHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 922 SawlrlvpeINPQTKIRFVKQvletielEEIKDAL--VGVAGV-----SGLSTEQRKRLTVAVELVANPSIIFMDEPTTG 994
Cdd:cd03298 94 G--------LSPGLKLTAEDR-------QAIEVALarVGLAGLekrlpGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15228112 995 LD-ARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRgGRMIYSG 1048
Cdd:cd03298 159 LDpALRAEMLDLVLDLHAETKMTVLMVTHQPE-DAKRLAQRVVFLDN-GRIAAQG 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
140-420 |
1.32e-10 |
|
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: 63.12 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGVRTNEANIKiLTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEVVPQKTS-AYI 218
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD---SGKILLNGKDITNLPPEKRDiSYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 219 SQHDLHIAEMTTRETIDFSarcqgvgsrtdimMEVSKREKdggiipdPEIDAYMKAISvkglkRSLQTDYILkilgldic 298
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYG-------------LKKRKVDK-------KEIERKVLEIA-----EMLGIDHLL-------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 299 aetlvgNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVfVSLLQPAPESYDL 378
Cdd:cd03299 124 ------NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTV-LHVTHDFEEAWAL 196
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15228112 379 FDDIVLMAEGKIVYHGPRDDVLKffeecgfqCPERKGVADFL 420
Cdd:cd03299 197 ADKVAIMLNGKLIQVGKPEEVFK--------KPKNEFVAEFL 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
153-342 |
1.61e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.47 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNghglnevvPQKTSAYISQHDLHIAEMTTRE 232
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPD---SGEVSIP--------KGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 233 TIdfsarCQGVGSRTDIMMEVSKREKDGGiIPDPEIDAYMKaisvkglkrsLQTDY--------------ILKILGLDIC 298
Cdd:COG0488 81 TV-----LDGDAELRALEAELEELEAKLA-EPDEDLERLAE----------LQEEFealggweaearaeeILSGLGFPEE 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15228112 299 -AETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLD 342
Cdd:COG0488 145 dLDRPVSE-----LSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
146-394 |
1.83e-10 |
|
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: 62.39 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 146 RTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNE----------VVPQKTS 215
Cdd:cd03266 12 RDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD---AGFATVDGFDVVKepaearrrlgFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 216 AYisqhdlhiAEMTTRETIDFSARcqgvgsrtdimmevskrekdggiipdpeidaymkaisVKGLKRSLQTDYILKILGL 295
Cdd:cd03266 89 LY--------DRLTARENLEYFAG-------------------------------------LYGLKGDELTARLEELADR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 296 DICAETLvgNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLD---SSTAFQIIKSLQQVAHitnATVFVSLLQPA 372
Cdd:cd03266 124 LGMEELL--DRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDvmaTRALREFIRQLRALGK---CILFSTHIMQE 198
|
250 260
....*....|....*....|..
gi 15228112 373 PESydLFDDIVLMAEGKIVYHG 394
Cdd:cd03266 199 VER--LCDRVVVLHRGRVVYEG 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
139-400 |
2.22e-10 |
|
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: 62.79 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 139 LLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNlenNLKCYG-EISYNGHGL-NEVVPQ-KTS 215
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGD---LPPTYGnDVRLFGERRgGEDVWElRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 216 -AYISQ--HDLHIAEMTTRETIdFSARCQGVGsrtdIMMEVSKREKDggiipdpeidaymkaisvkglkrslQTDYILKI 292
Cdd:COG1119 80 iGLVSPalQLRFPRDETVLDVV-LSGFFDSIG----LYREPTDEQRE-------------------------RARELLEL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 293 LGLDICAETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITN-ATVFVS-LLQ 370
Cdd:COG1119 130 LGLAHLADRPFGT-----LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVThHVE 204
|
250 260 270
....*....|....*....|....*....|
gi 15228112 371 PAPESydlFDDIVLMAEGKIVYHGPRDDVL 400
Cdd:COG1119 205 EIPPG---ITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
840-1025 |
2.25e-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: 62.50 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 840 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRktsgYI--EGEIRISGF---LKVQETFARVSGYCEQtdihspsit 914
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF----YVpeNGRVLVDGHdlaLADPAWLRRQVGVVLQ--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 915 veESLIYSAWLR----LVPEINPQTKIRFVKQVLET----IELEEIKDALVGVAGVsGLSTEQRKRLTVAVELVANPSII 986
Cdd:cd03252 84 --ENVLFNRSIRdniaLADPGMSMERVIEAAKLAGAhdfiSELPEGYDTIVGEQGA-GLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 15228112 987 FMDEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHQPS 1025
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLS 198
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
151-423 |
2.49e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 63.95 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 151 NIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENnlKCYGEISYNGHGLNEV-VPQKTSAYISQHDLHIAEMT 229
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG-LEH--QTSGHIRFHGTDVSRLhARDRKVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 230 TRETIDFSARCqgvgsrtdimmeVSKREKdggiiPDpeidayMKAISVKGLKrslqtdyILKILGLDICAetlvgNAMKR 309
Cdd:PRK10851 91 VFDNIAFGLTV------------LPRRER-----PN------AAAIKAKVTQ-------LLEMVQLAHLA-----DRYPA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 310 GISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNAT-VFVSLLQpaPESYDLFDDIVLMAEG 388
Cdd:PRK10851 136 QLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTsVFVTHDQ--EEAMEVADRVVVMSQG 213
|
250 260 270
....*....|....*....|....*....|....*
gi 15228112 389 KIVYHGPRDDVlkffeecgFQCPERKGVADFLQEV 423
Cdd:PRK10851 214 NIEQAGTPDQV--------WREPATRFVLEFMGEV 240
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
841-1049 |
2.52e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.55 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 841 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAGrKTSGyiEGEIRISGF----LKVQEtFARVSGYCEQTDIHSPSITVE 916
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPG--QGEILLNGRplsdWSAAE-LARHRAYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 917 EsliYSAwLRLVPEINPQTKIRFVKQVLETIELEeikDALvgVAGVSGLS-TE-QRKRLtVAVEL----VANPS--IIFM 988
Cdd:COG4138 88 Q---YLA-LHQPAGASSEAVEQLLAQLAEALGLE---DKL--SRPLTQLSgGEwQRVRL-AAVLLqvwpTINPEgqLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228112 989 DEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIHIFEAfDELVLLKRgGRMIYSGP 1049
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHA-DRVWLLKQ-GKLVASGE 216
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
142-345 |
2.59e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.81 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 142 LSGVRTNEAnikILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlKCYGEISYNGHGLNEVVPQKTSAYISQH 221
Cdd:PRK13539 8 LACVRGGRV---LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP---PAAGTIKLDGGDIDDPDVAEACHYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 222 DLHIAEMTTRETIDFSARCQGVGsrtdimmevskrekdggiipDPEIDAYMKAISVKGLkrslqtdyilkilgLDICAET 301
Cdd:PRK13539 82 NAMKPALTVAENLEFWAAFLGGE--------------------ELDIAAALEAVGLAPL--------------AHLPFGY 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15228112 302 LvgnamkrgiSGGQKKRLTTAEMIVGPTKALFMDEITNGLDSST 345
Cdd:PRK13539 128 L---------SAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
840-1049 |
2.70e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.09 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 840 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGflkvqetfarvsgyceqTDIHSPSITVEESL 919
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT--AGTVLVAG-----------------DDVEALSARAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 920 IYSawlrlVPEinpQTKIRF---VKQVLE-----------------TIELEEIKDAlVGVAG-----VSGLSTEQRKRLT 974
Cdd:PRK09536 79 VAS-----VPQ---DTSLSFefdVRQVVEmgrtphrsrfdtwtetdRAAVERAMER-TGVAQfadrpVTSLSGGERQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228112 975 VAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHqpSIHIFEAF-DELVLLKrGGRMIYSGP 1049
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIH--DLDLAARYcDELVLLA-DGRVRAAGP 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
851-1022 |
2.77e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 62.79 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 851 GVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGE-IRIS--GFLKVQETFARVSgycEQTD--IHSPsiTVEESLIY 921
Cdd:PRK13639 28 GEMVALLGPNGAGKSTLFLHFNGilKPTSGevLIKGEpIKYDkkSLLEVRKTVGIVF---QNPDdqLFAP--TVEEDVAF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 922 SAWLRLVPEinpqtkirfvkqvlETIElEEIKDALVGVaGVSG--------LSTEQRKRLTVAVELVANPSIIFMDEPTT 993
Cdd:PRK13639 103 GPLNLGLSK--------------EEVE-KRVKEALKAV-GMEGfenkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180
....*....|....*....|....*....
gi 15228112 994 GLDARAAAIVMRAVKNVAETGRTIVCTIH 1022
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
154-356 |
4.03e-10 |
|
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: 64.30 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEVVPQKTSAYIS--QHDLHIAEMTTR 231
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL---QGEVTLDGVPVSSLDQDEVRRRVSvcAQDAHLFDTTVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 232 ETIDFSArcqgvgsrtdimmevskrekdggiiPDPEIDAYMKAISVKGLKRSLQtdyilkilGLDICAETLVGnAMKRGI 311
Cdd:TIGR02868 427 ENLRLAR-------------------------PDATDEELWAALERVGLADWLR--------ALPDGLDTVLG-EGGARL 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15228112 312 SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQV 356
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA 517
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
139-391 |
4.11e-10 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 61.60 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 139 LLKLSGV----RTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGH---GLNE--- 208
Cdd:COG1136 4 LLELRNLtksyGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPT---SGEVLIDGQdisSLSErel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 209 ---------VVPQktsayisQHDLhIAEMTTRETIDFSARCQGVGSRtdimmevskrekdggiipdpeiDAYMKAisvkg 279
Cdd:COG1136 81 arlrrrhigFVFQ-------FFNL-LPELTALENVALPLLLAGVSRK----------------------ERRERA----- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 280 lkrslqtDYILKILGLDICAETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHI 359
Cdd:COG1136 126 -------RELLERVGLGDRLDHRPSQ-----LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRE 193
|
250 260 270
....*....|....*....|....*....|....*
gi 15228112 360 TNATVFVsllqpA---PESYDLFDDIVLMAEGKIV 391
Cdd:COG1136 194 LGTTIVM-----VthdPELAARADRVIRLRDGRIV 223
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
791-1018 |
4.98e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 64.03 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 791 LDSSIKTNEDPGKMILPFKPLTITFQDLNYyvdvpvemkgqGYNEKKlQLLSEITGAFRPGVLTALMGISGAGKTTLLDV 870
Cdd:COG1132 318 LDEPPEIPDPPGAVPLPPVRGEIEFENVSF-----------SYPGDR-PVLKDISLTIPPGETVALVGPSGSGKSTLVNL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 871 LAGRktsgY--IEGEIRISGflkvqetfarvsgyceqTDIHSpsITVEEsliysawLR----LVPE--------I--Npq 934
Cdd:COG1132 386 LLRF----YdpTSGRILIDG-----------------VDIRD--LTLES-------LRrqigVVPQdtflfsgtIreN-- 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 935 tkIRF---------VKQVLETIELEE-IK------DALVGVAGVSgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDAR 998
Cdd:COG1132 434 --IRYgrpdatdeeVEEAAKAAQAHEfIEalpdgyDTVVGERGVN-LSGGQRQRIAIARALLKDPPILILDEATSALDTE 510
|
250 260
....*....|....*....|
gi 15228112 999 AAAIVMRAVKNVAEtGRTIV 1018
Cdd:COG1132 511 TEALIQEALERLMK-GRTTI 529
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
833-1003 |
5.23e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 61.72 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 833 YNEKKLqlLSEITGAFRPGVLTALMGISGAGKTTLLDVLagrKTSGYIEGEIRISGFLKvqetFARVSGYCEQTD----- 907
Cdd:PRK14239 15 YNKKKA--LNSVSLDFYPNEITALIGPSGSGKSTLLRSI---NRMNDLNPEVTITGSIV----YNGHNIYSPRTDtvdlr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 908 ------IHSPS---ITVEESLIYSawLRLVPEINPQTKIRFVKQVLETIEL-EEIKDALVGVAgvSGLSTEQRKRLTVAV 977
Cdd:PRK14239 86 keigmvFQQPNpfpMSIYENVVYG--LRLKGIKDKQVLDEAVEKSLKGASIwDEVKDRLHDSA--LGLSGGQQQRVCIAR 161
|
170 180
....*....|....*....|....*.
gi 15228112 978 ELVANPSIIFMDEPTTGLDARAAAIV 1003
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKI 187
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
140-394 |
6.48e-10 |
|
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: 60.31 E-value: 6.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGL--NEVVPQKTSAY 217
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD---SGEITFDGKSYqkNIEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 218 ISQHDLHiAEMTTRETIDFSARCQGvgsrtdimmevskrekdggiIPDPEIDAymkaisvkglkrslqtdyILKILGLDI 297
Cdd:cd03268 78 IEAPGFY-PNLTARENLRLLARLLG--------------------IRKKRIDE------------------VLDVVGLKD 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 298 CAETLVGnamkrGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDS---STAFQIIKSLQQvahiTNATVFVS--LLQpa 372
Cdd:cd03268 119 SAKKKVK-----GFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPdgiKELRELILSLRD----QGITVLISshLLS-- 187
|
250 260
....*....|....*....|..
gi 15228112 373 pESYDLFDDIVLMAEGKIVYHG 394
Cdd:cd03268 188 -EIQKVADRIGIINKGKLIEEG 208
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
153-401 |
6.61e-10 |
|
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: 61.15 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEvvpqktsayISQHDLHIAE----- 227
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPD---SGEILVDGQDITG---------LSEKELYELRrrigm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 228 ----------MTTRETIDFSarcqgvgsrtdiMMEVSKrekdggiIPDPEID--AYMKaisvkglkrslqtdyiLKILGL 295
Cdd:COG1127 87 lfqggalfdsLTVFENVAFP------------LREHTD-------LSEAEIRelVLEK----------------LELVGL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 296 DicaetLVGNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLD--SSTAF-QIIKSLQQVAHITnaTVFVS--Llq 370
Cdd:COG1127 132 P-----GAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDpiTSAVIdELIRELRDELGLT--SVVVThdL-- 202
|
250 260 270
....*....|....*....|....*....|.
gi 15228112 371 paPESYDLFDDIVLMAEGKIVYHGPRDDVLK 401
Cdd:COG1127 203 --DSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
139-400 |
7.95e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 63.31 E-value: 7.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 139 LLKLSGV--RTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEVvpqktsa 216
Cdd:PRK11160 338 SLTLNNVsfTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQ---QGEILLNGQPIADY------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 217 yisqhdlhiAEMTTRETIDFsarcqgVGSRTDIMmevSKREKDGGIIPDPEI-DAYMKAISVK-GLKRSLQTDyilkiLG 294
Cdd:PRK11160 408 ---------SEAALRQAISV------VSQRVHLF---SATLRDNLLLAAPNAsDEALIEVLQQvGLEKLLEDD-----KG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 295 LDicaeTLVGNAmKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQvaHITNATV-FVSLLQPAP 373
Cdd:PRK11160 465 LN----AWLGEG-GRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE--HAQNKTVlMITHRLTGL 537
|
250 260
....*....|....*....|....*..
gi 15228112 374 ESydlFDDIVLMAEGKIVYHGPRDDVL 400
Cdd:PRK11160 538 EQ---FDRICVMDNGQIIEQGTHQELL 561
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
151-401 |
8.20e-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: 60.70 E-value: 8.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 151 NIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNG---HGLNEVVPQKTSAYISQhDLHIAE 227
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ---KGQILIDGidiRDISRKSLRSMIGVVLQ-DTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 228 MTTRETIDFSarcqgvgsrtdimmevskrekdGGIIPDPEIDAYMKAISVKGLKRSLQTDYilkilgldicaETLVGNAM 307
Cdd:cd03254 91 GTIMENIRLG----------------------RPNATDEEVIEAAKEAGAHDFIMKLPNGY-----------DTVLGENG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 308 KrGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHitNATVFV-----SLLQPApesydlfDDI 382
Cdd:cd03254 138 G-NLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIiahrlSTIKNA-------DKI 207
|
250
....*....|....*....
gi 15228112 383 VLMAEGKIVYHGPRDDVLK 401
Cdd:cd03254 208 LVLDDGKIIEEGTHDELLA 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
162-401 |
1.03e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 62.04 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 162 ISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNGhglnEVVpqkTSAYISQHDLHIA--------EMTTRET 233
Cdd:PRK11432 29 IKQGTMVTLLGPSGCGKTTVLRLVAG-LEKPTE--GQIFIDG----EDV---THRSIQQRDICMVfqsyalfpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 234 IDFSARCQGVGSRtdimmEVSKREKDGgiipdpeidaymkaisvkglkrslqtdyiLKILGLDICAETLVGNamkrgISG 313
Cdd:PRK11432 99 VGYGLKMLGVPKE-----ERKQRVKEA-----------------------------LELVDLAGFEDRYVDQ-----ISG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 314 GQKKRLTTAEMIVGPTKALFMDEITNGLDSS---TAFQIIKSLQQVAHITnaTVFVSLLQpaPESYDLFDDIVLMAEGKI 390
Cdd:PRK11432 140 GQQQRVALARALILKPKVLLFDEPLSNLDANlrrSMREKIRELQQQFNIT--SLYVTHDQ--SEAFAVSDTVIVMNKGKI 215
|
250
....*....|.
gi 15228112 391 VYHGPRDDVLK 401
Cdd:PRK11432 216 MQIGSPQELYR 226
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
139-394 |
1.07e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.81 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 139 LLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLkCYGEISYNGHGLNEVVPQKTS--- 215
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKI-LEGDILFKGESILDLEPEERAhlg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 216 ---AYisQHDLHIAemttretidfsarcqGVgSRTDIMMEV--SKREKDGgiipDPEIDA--YMKAISVKglkrslqtdy 288
Cdd:CHL00131 86 iflAF--QYPIEIP---------------GV-SNADFLRLAynSKRKFQG----LPELDPleFLEIINEK---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 289 iLKILGLDicaETLVGNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSL 368
Cdd:CHL00131 134 -LKLVGMD---PSFLSRNVNEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
250 260
....*....|....*....|....*.
gi 15228112 369 LQPAPEsYDLFDDIVLMAEGKIVYHG 394
Cdd:CHL00131 210 YQRLLD-YIKPDYVHVMQNGKIIKTG 234
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
140-420 |
1.15e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 61.63 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNGHGLNEVVPQKTS-AYI 218
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG-LEDPTS--GEILIGGRDVTDLPPKDRNiAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 219 SQ------HdlhiaeMTTRETIDFSARCQGVgsrtdimmevskrekdggiiPDPEIDAymkaisvkglkrslQTDYILKI 292
Cdd:COG3839 81 FQsyalypH------MTVYENIAFPLKLRKV--------------------PKAEIDR--------------RVREAAEL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 293 LGLDicaETLvgNAMKRGISGGQKKRLTTAEMIVGPTKALFMDE-ITNgLDSSTAFQI---IKSLQQVAHITnaTVFVsl 368
Cdd:COG3839 121 LGLE---DLL--DRKPKQLSGGQRQRVALGRALVREPKVFLLDEpLSN-LDAKLRVEMraeIKRLHRRLGTT--TIYV-- 190
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 15228112 369 lqpapeSYD------LFDDIVLMAEGKIVYHGPRDDVlkffeecgFQCPERKGVADFL 420
Cdd:COG3839 191 ------THDqveamtLADRIAVMNDGRIQQVGTPEEL--------YDRPANLFVAGFI 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
833-1048 |
1.21e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.40 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 833 YNEK---KLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYieGEIRISGF-LKVQETFARVSGYCEQTDI 908
Cdd:PRK13631 31 FDEKqenELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKY--GTIQVGDIyIGDKKNNHELITNPYSKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 909 HS--------------PSI-----TVEESLIYSawlrlvPEINPQTKIRFVKQVLETIELEEIKDALVGVAGVsGLSTEQ 969
Cdd:PRK13631 109 KNfkelrrrvsmvfqfPEYqlfkdTIEKDIMFG------PVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPF-GLSGGQ 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228112 970 RKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRgGRMIYSG 1048
Cdd:PRK13631 182 KRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME-HVLEVADEVIVMDK-GKILKTG 258
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
838-1023 |
1.25e-09 |
|
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: 60.04 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 838 LQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGFLKVQETFARV---SGYCEQTDIHSP--- 911
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQT--LEGKVHWSNKNESEPSFEATrsrNRYSVAYAAQKPwll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 912 SITVEESLIYSAwlrlvpeinPQTKIRFvKQVLETIELEEIKDAL-------VGVAGVSgLSTEQRKRLTVAVELVANPS 984
Cdd:cd03290 92 NATVEENITFGS---------PFNKQRY-KAVTDACSLQPDIDLLpfgdqteIGERGIN-LSGGQRQRICVARALYQNTN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15228112 985 IIFMDEPTTGLDARAAAIVMRA--VKNVAETGRTIVCTIHQ 1023
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHK 201
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
851-1049 |
1.44e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.67 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 851 GVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGFLKVQETFARVSGYC---EQTDIHSPsITVEESLI----- 920
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGfvRLASG----KISILGQPTRQALQKNLVAYVpqsEEVDWSFP-VLVEDVVMmgryg 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 921 YSAWLRLVPEINPQTkirfVKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAA 1000
Cdd:PRK15056 108 HMGWLRRAKKRDRQI----VTAALARVDMVEFRHRQIG-----ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15228112 1001 AIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKrgGRMIYSGP 1049
Cdd:PRK15056 179 ARIISLLRELRDEGKTMLVSTHNLG-SVTEFCDYTVMVK--GTVLASGP 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
836-1022 |
1.47e-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: 59.86 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 836 KKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIE-GEIRISGfLKVQETfARVS-GYCEQtdihSP 911
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGlvKPDSGKILlDGQDITK-LPMHKR-ARLGiGYLPQ----EA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 912 SI----TVEESLiysawlRLVPEINPQTK---IRFVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPS 984
Cdd:cd03218 85 SIfrklTVEENI------LAVLEIRGLSKkerEEKLEELLEEFHITHLRKSKA-----SSLSGGERRRVEIARALATNPK 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 15228112 985 IIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIH 1022
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDH 191
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
155-423 |
1.78e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 61.32 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 155 LTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNGhglnEVVPQKTSA------YISQH-DL--Hi 225
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAG-LETPDS--GRIVLNG----RDLFTNLPPrerrvgFVFQHyALfpH- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 226 aeMTTRETIDFSARCQGVgSRTDImmevskREKdggiipdpeidaymkaisVKGLkrslqtdyiLKILGLDICAETLVGN 305
Cdd:COG1118 90 --MTVAENIAFGLRVRPP-SKAEI------RAR------------------VEEL---------LELVQLEGLADRYPSQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 306 amkrgISGGQKKRLTTAEM-IVGPtKALFMDEITNGLDSSTAFQIIKSLQQV---AHITnaTVFVS--LLqpapESYDLF 379
Cdd:COG1118 134 -----LSGGQRQRVALARAlAVEP-EVLLLDEPFGALDAKVRKELRRWLRRLhdeLGGT--TVFVThdQE----EALELA 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15228112 380 DDIVLMAEGKIVYHGPRDDVlkffeecgFQCPERKGVADFLQEV 423
Cdd:COG1118 202 DRVVVMNQGRIEQVGTPDEV--------YDRPATPFVARFLGCV 237
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
170-423 |
1.83e-09 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 60.97 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 170 LLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEVVPQKTS-AYISQHDLHIAEMTTRETIDFSARCQGVgsrtd 248
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPD---SGSIMLDGEDVTNVPPHLRHiNMVFQSYALFPHMTVEENVAFGLKMRKV----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 249 immevskrekdggiiPDPEIDAymkaiSVKGLKRSLQtdyilkilgldicaetLVGNAMKRGI--SGGQKKRLTTAEMIV 326
Cdd:TIGR01187 73 ---------------PRAEIKP-----RVLEALRLVQ----------------LEEFADRKPHqlSGGQQQRVALARALV 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 327 GPTKALFMDEITNGLDSSTAFQI---IKSLQQVAHITnaTVFVSLLQpaPESYDLFDDIVLMAEGKIVYHG-PRDdvlkF 402
Cdd:TIGR01187 117 FKPKILLLDEPLSALDKKLRDQMqleLKTIQEQLGIT--FVFVTHDQ--EEAMTMSDRIAIMRKGKIAQIGtPEE----I 188
|
250 260
....*....|....*....|.
gi 15228112 403 FEEcgfqcPERKGVADFLQEV 423
Cdd:TIGR01187 189 YEE-----PANLFVARFIGEI 204
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
839-1025 |
2.24e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 59.76 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 839 QLLSEITGAFRPGVLTALMGISGAGKTTLLDV--LAGRKTSGYIE-GEIRISGF--LKVQETFARV----SGYCEQTDIH 909
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinLLEQPEAGTIRvGDITIDTArsLSQQKGLIRQlrqhVGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 910 SPSITVEESLIYSAwlRLVPEINPQTKIRFVKQVLetieleeikdALVGVAGVSG-----LSTEQRKRLTVAVELVANPS 984
Cdd:PRK11264 97 FPHRTVLENIIEGP--VIVKGEPKEEATARARELL----------AKVGLAGKETsyprrLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15228112 985 IIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPS 1025
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
153-401 |
2.79e-09 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 61.33 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNlennlkcY----GEISYNGHGLNEVVPQ---KTSAYISQhDLHI 225
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF-------YdptsGRILIDGVDIRDLTLEslrRQIGVVPQ-DTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 226 AEMTTRETIDFSarcqgvgsRTDImmevskrekdggiiPDPEIDAYMKAISVkglkrslqTDYILKiL--GLDicaeTLV 303
Cdd:COG1132 426 FSGTIRENIRYG--------RPDA--------------TDEEVEEAAKAAQA--------HEFIEA-LpdGYD----TVV 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 304 GnamKRGI--SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHitNATVFV-----SLLQPApesy 376
Cdd:COG1132 471 G---ERGVnlSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIViahrlSTIRNA---- 541
|
250 260
....*....|....*....|....*
gi 15228112 377 dlfDDIVLMAEGKIVYHGPRDDVLK 401
Cdd:COG1132 542 ---DRILVLDDGRIVEQGTHEELLA 563
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
791-1041 |
3.02e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.40 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 791 LDSSIKTNEDPGKMILPFKPLTITFQDLnyyvdVPVEMKGQgynekklQLLSEITGAFRPGVLTALMGISGAGKTTLLDV 870
Cdd:PRK11174 328 LETPLAHPQQGEKELASNDPVTIEAEDL-----EILSPDGK-------TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 871 LagrktSGYI--EGEIRISGflkvqetfarvsgyCEQTDI----------------HSPSITVEESLIYSAwlrlvPEIN 932
Cdd:PRK11174 396 L-----LGFLpyQGSLKING--------------IELRELdpeswrkhlswvgqnpQLPHGTLRDNVLLGN-----PDAS 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 933 PQTkirfVKQVLETIELEEIKDALV-GVA-----GVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRA 1006
Cdd:PRK11174 452 DEQ----LQQALENAWVSEFLPLLPqGLDtpigdQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
250 260 270
....*....|....*....|....*....|....*
gi 15228112 1007 VKNVAETGRTIVCTiHQpsIHIFEAFDELVLLKRG 1041
Cdd:PRK11174 528 LNAASRRQTTLMVT-HQ--LEDLAQWDQIWVMQDG 559
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
833-1000 |
3.36e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 59.06 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 833 YNEKKLQ--LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISG-FLKVQETFARVS------GYC 903
Cdd:PRK11629 15 YQEGSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTP--TSGDVIFNGqPMSKLSSAAKAElrnqklGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 904 EQTDIHSPSITVEESLiysAWLRLVPEINPQTKIRFVKQVLETIELEEikdalVGVAGVSGLSTEQRKRLTVAVELVANP 983
Cdd:PRK11629 93 YQFHHLLPDFTALENV---AMPLLIGKKKPAEINSRALEMLAAVGLEH-----RANHRPSELSGGERQRVAIARALVNNP 164
|
170
....*....|....*..
gi 15228112 984 SIIFMDEPTTGLDARAA 1000
Cdd:PRK11629 165 RLVLADEPTGNLDARNA 181
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
153-400 |
3.46e-09 |
|
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: 58.78 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALsgnlennLKCY----GEISYNGHGLNE-----------VVPQKTSAY 217
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL-------FRFYdvssGSILIDGQDIREvtldslrraigVVPQDTVLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 218 isqHDlhiaemTTRETIDFsarcqGVGSRTDImmEVSKREKDGGIipDPEI----DAYmkaisvkglkrslqtdyilkil 293
Cdd:cd03253 88 ---ND------TIGYNIRY-----GRPDATDE--EVIEAAKAAQI--HDKImrfpDGY---------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 294 gldicaETLVGnamKRG--ISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQ---------VAH---- 358
Cdd:cd03253 128 ------DTIVG---ERGlkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDvskgrttivIAHrlst 198
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15228112 359 ITNAtvfvsllqpapesydlfDDIVLMAEGKIVYHGPRDDVL 400
Cdd:cd03253 199 IVNA-----------------DKIIVLKDGRIVERGTHEELL 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
848-1041 |
3.77e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 60.09 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 848 FRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGflkvqetfARVsgyceqTDIHS--------------- 910
Cdd:COG3839 26 IEDGEFLVLLGPSGCGKSTLLRMIAGleDPTSG----EILIGG--------RDV------TDLPPkdrniamvfqsyaly 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 911 PSITVEESLIYSAWLRLVP--EINPQtkirfVKQVLETIELEEIKDALVgvagvSGLSTEQRKRltVAV--ELVANPSII 986
Cdd:COG3839 88 PHMTVYENIAFPLKLRKVPkaEIDRR-----VREAAELLGLEDLLDRKP-----KQLSGGQRQR--VALgrALVREPKVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15228112 987 FMDEPTTGLDA--RAAaivMRA--VKNVAETGRTIVCTIHQPSihifEAF---DELVLLKRG 1041
Cdd:COG3839 156 LLDEPLSNLDAklRVE---MRAeiKRLHRRLGTTTIYVTHDQV----EAMtlaDRIAVMNDG 210
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
813-1048 |
3.83e-09 |
|
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: 57.71 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 813 ITFQDLNYyvdvpvemkgqGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGF--L 890
Cdd:cd03247 1 LSINNVSF-----------SYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ--QGEITLDGVpvS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 891 KVQETFARVSGYCEQTdIHSPSITVEESLiysawlrlvpeinpqtKIRFvkqvletieleeikdalvgvagvsglSTEQR 970
Cdd:cd03247 68 DLEKALSSLISVLNQR-PYLFDTTLRNNL----------------GRRF--------------------------SGGER 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 971 KRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHqpsiHI--FEAFDELVLLKRgGRMIYSG 1048
Cdd:cd03247 105 QRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITH----HLtgIEHMDKILFLEN-GKIIMQG 178
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
840-999 |
4.57e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.85 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 840 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTsgYIEGEIRISGFLKVqetfarvsGYCEQTDIHSPSITVEESL 919
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELE--PDSGEVSIPKGLRI--------GYLPQEPPLDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 920 I--YSAWLRLVPEIN-PQTKIRFVKQVLETI-ELEE-------------IKDALVGV--------AGVSGLSTEQRKRLT 974
Cdd:COG0488 83 LdgDAELRALEAELEeLEAKLAEPDEDLERLaELQEefealggweaearAEEILSGLgfpeedldRPVSELSGGWRRRVA 162
|
170 180
....*....|....*....|....*
gi 15228112 975 VAVELVANPSIIFMDEPTTGLDARA 999
Cdd:COG0488 163 LARALLSEPDLLLLDEPTNHLDLES 187
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
154-400 |
5.53e-09 |
|
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: 58.27 E-value: 5.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLennlkcygeisynghglnevVPQKTSAYISQHDLHIAEMTtret 233
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFY--------------------VPENGRVLVDGHDLALADPA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 234 idfSARCQ-GVGSRTDIMMEVSKREKDGGIIPDPEIDAYMKAISVKGLKrslqtDYILKI-LGLDicaeTLVGNaMKRGI 311
Cdd:cd03252 73 ---WLRRQvGVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAH-----DFISELpEGYD----TIVGE-QGAGL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 312 SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAhiTNATVFV-----SLLQPApesydlfDDIVLMA 386
Cdd:cd03252 140 SGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIiahrlSTVKNA-------DRIIVME 210
|
250
....*....|....
gi 15228112 387 EGKIVYHGPRDDVL 400
Cdd:cd03252 211 KGRIVEQGSHDELL 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
813-1003 |
6.12e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 58.51 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 813 ITFQDLNYYvdvpvemkgqgYNEKklQLLSEITGAFRPGVLTALMGISGAGKTTLL-------DVLAGRKtsgyIEGEIR 885
Cdd:COG1117 12 IEVRNLNVY-----------YGDK--QALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPGAR----VEGEIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 886 ISGflkvqetfarvsgyceqTDIHSPSITVEEsliysawLR----LV---PeiNPqtkirFVKQVLETI----------- 947
Cdd:COG1117 75 LDG-----------------EDIYDPDVDVVE-------LRrrvgMVfqkP--NP-----FPKSIYDNVayglrlhgiks 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 948 --ELEEI-KDALVGVA-----------GVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIV 1003
Cdd:COG1117 124 ksELDEIvEESLRKAAlwdevkdrlkkSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKI 193
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
840-1024 |
6.50e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.51 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 840 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIE--GE-IRisgflKVQETFARVSGYCEqtdiHSPSI- 913
Cdd:PRK13538 16 LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGlaRPDAGEVLwqGEpIR-----RQRDEYHQDLLYLG----HQPGIk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 914 ---TVEESLIYSAwlRLVPEINPQTkirfVKQVLETIELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDE 990
Cdd:PRK13538 87 telTALENLRFYQ--RLHGPGDDEA----LWEALAQVGLAGFEDVPVRQ-----LSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190
....*....|....*....|....*....|....
gi 15228112 991 PTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQP 1024
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
841-1041 |
6.97e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.98 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 841 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIE-GEIRISGFLKVQET--FARVSGYCEQtdiHSPSITV 915
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllQPTEGKVTvGDIVVSSTSKQKEIkpVRKKVGVVFQ---FPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 916 EESLIYSAwlrlvpEINPQTkIRFVKQVLETIELEEIKdaLVGVA------GVSGLSTEQRKRLTVAVELVANPSIIFMD 989
Cdd:PRK13643 99 EETVLKDV------AFGPQN-FGIPKEKAEKIAAEKLE--MVGLAdefwekSPFELSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15228112 990 EPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRG 1041
Cdd:PRK13643 170 EPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMD-DVADYADYVYLLEKG 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
153-394 |
7.55e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 60.24 E-value: 7.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 153 KILTD-VSGIISPGRLTLLLGPPGCGKTTLLKALSGNLennlKCYGEISYNGHGLNEVVPQ---KTSAYISQhDLHIAEM 228
Cdd:PRK11174 363 KTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL----PYQGSLKINGIELRELDPEswrKHLSWVGQ-NPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 229 TTRETIDFsARCQgvgsrtdimmevskrekdggiIPDPEIDAymkaisvkGLKRSLQTDYILKI-LGLDicaeTLVGNAM 307
Cdd:PRK11174 438 TLRDNVLL-GNPD---------------------ASDEQLQQ--------ALENAWVSEFLPLLpQGLD----TPIGDQA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 308 kRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHiTNATVFVS-----LLQpapesydlFDDI 382
Cdd:PRK11174 484 -AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR-RQTTLMVThqledLAQ--------WDQI 553
|
250
....*....|..
gi 15228112 383 VLMAEGKIVYHG 394
Cdd:PRK11174 554 WVMQDGQIVQQG 565
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
856-1041 |
7.67e-09 |
|
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: 57.26 E-value: 7.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 856 LMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGflkvqetfARVSG-YCEQTDIHS--------PSITVEESLIYSAWLR 926
Cdd:cd03301 31 LLGPSGCGKTTTLRMIAGLEEPT--SGRIYIGG--------RDVTDlPPKDRDIAMvfqnyalyPHMTVYDNIAFGLKLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 927 LVP--EINpqtkiRFVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARaAAIVM 1004
Cdd:cd03301 101 KVPkdEID-----ERVREVAELLQIEHLLDRKP-----KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAK-LRVQM 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15228112 1005 RA--VKNVAETGRTIVCTIHQPSihifEAF---DELVLLKRG 1041
Cdd:cd03301 170 RAelKRLQQRLGTTTIYVTHDQV----EAMtmaDRIAVMNDG 207
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
584-760 |
8.31e-09 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 57.13 E-value: 8.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 584 WAYAIPATVLkiplSFFESLVWTCLTYYVIGYTPEPYRFFRQF--MILFAVHFTSISMFrcIAAIFQTGVAAMTAGSFVM 661
Cdd:COG0842 50 LGKVLAYLLR----GLLQALLVLLVALLFFGVPLRGLSLLLLLlvLLLFALAFSGLGLL--ISTLARSQEQASAISNLVI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 662 LITFVFAGFAIPYTDMPGWLKWGFWVNPISYAeiglsvneflaprwqkmqptnVTLGRTILeSRGLNYDDymYWVSLSAL 741
Cdd:COG0842 124 LPLTFLSGAFFPIESLPGWLQAIAYLNPLTYF---------------------VEALRALF-LGGAGLAD--VWPSLLVL 179
|
170
....*....|....*....
gi 15228112 742 LGLTIIFntiFTLALSFLK 760
Cdd:COG0842 180 LAFAVVL---LALALRLFR 195
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
850-1002 |
9.36e-09 |
|
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: 58.96 E-value: 9.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 850 PGVlTALMGISGAGKTTLLDVLAG--RKTSGYIE--GEI------RIsgFLKVQetfARVSGYCEQTDIHSPSITVEESL 919
Cdd:COG4148 25 RGV-TALFGPSGSGKTTLLRAIAGleRPDSGRIRlgGEVlqdsarGI--FLPPH---RRRIGYVFQEARLFPHLSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 920 IYSAWlrlvpeinpqtkirFVKQVLETIELEEIKDaLVGVA-----GVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTG 994
Cdd:COG4148 99 LYGRK--------------RAPRAERRISFDEVVE-LLGIGhlldrRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
....*....
gi 15228112 995 LD-ARAAAI 1002
Cdd:COG4148 164 LDlARKAEI 172
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
834-1026 |
1.18e-08 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 57.06 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 834 NEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSgyieGEIRISGflkvqetfarvsgyceqTDIHSP 911
Cdd:COG4181 21 GAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGldRPTS----GTVRLAG-----------------QDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 912 SitvEESLiysAWLRlvpeinpQTKIRFVKQ---------VLETI----ELEEIKDAL---------VGV--------AG 961
Cdd:COG4181 80 D---EDAR---ARLR-------ARHVGFVFQsfqllptltALENVmlplELAGRRDARararallerVGLghrldhypAQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15228112 962 VSGlsTEQRkRLTVAVELVANPSIIFMDEPTTGLDARAAAIV---MRAVKnvAETGRTIVCTIHQPSI 1026
Cdd:COG4181 147 LSG--GEQQ-RVALARAFATEPAILFADEPTGNLDAATGEQIidlLFELN--RERGTTLVLVTHDPAL 209
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
840-1065 |
1.30e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.49 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 840 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLaGRKTSGYiEGEIRISGFLKVQ---ETFARVSGYCEQTDIHSPSITVE 916
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPS-EGEILLDAQPLESwssKAFARKVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 917 E--SLIYSAWLRLVPeinpqtkiRFVKQVLETIElEEIkdALVGVAG-----VSGLSTEQRKRLTVAVELVANPSIIFMD 989
Cdd:PRK10575 104 ElvAIGRYPWHGALG--------RFGAADREKVE-EAI--SLVGLKPlahrlVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228112 990 EPTTGLDARAAAIVMRAVKNVA-ETGRTIVCTIHqpSIHIFEAF-DELVLLkRGGRMIYSG-PLGQHSSCVIEYFQNIP 1065
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSqERGLTVIAVLH--DINMAARYcDYLVAL-RGGEMIAQGtPAELMRGETLEQIYGIP 248
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
841-1045 |
1.53e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 57.40 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 841 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTsgYIEGEIRISGfLKVQETFARvSGYCEQTDIHSPSITVEESLI 920
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVP--YQHGSITLDG-KPVEGPGAE-RGVVFQNEGLLPWRNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 921 YSAWLRLVPEINPQTKIRfvkQVLetieleeikdALVGVAG-----VSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGL 995
Cdd:PRK11248 93 FGLQLAGVEKMQRLEIAH---QML----------KKVGLEGaekryIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15228112 996 DARAAAIVMRAVKNV-AETGRTIVCTIHQPSIHIFEAfDELVLLKRG-GRMI 1045
Cdd:PRK11248 160 DAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMA-TELVLLSPGpGRVV 210
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
855-1025 |
1.66e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.16 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 855 ALMGISGAGKTTLL---DVLAGRKTSGYIEGEIRISGFLKVQETF-----ARVSGYCEQTDIHSPSITVEESLiySAWLR 926
Cdd:PRK14267 34 ALMGPSGCGKSTLLrtfNRLLELNEEARVEGEVRLFGRNIYSPDVdpievRREVGMVFQYPNPFPHLTIYDNV--AIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 927 LVPEINPQTKI-RFVKQVLETIEL-EEIKDALVGVAgvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVM 1004
Cdd:PRK14267 112 LNGLVKSKKELdERVEWALKKAALwDEVKDRLNDYP--SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIE 189
|
170 180
....*....|....*....|.
gi 15228112 1005 RAVKNVaETGRTIVCTIHQPS 1025
Cdd:PRK14267 190 ELLFEL-KKEYTIVLVTHSPA 209
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
848-1050 |
1.84e-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: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 848 FRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIegeirISGFLKVQETFARVS---GYCEQTDIHSPSITVEESLIYS 922
Cdd:TIGR01257 953 FYENQITAFLGHNGAGKTTTLSILTGllPPTSGTV-----LVGGKDIETNLDAVRqslGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 923 AWLRLVPEINPQTKIrfvKQVLETIEL-----EEIKDalvgvagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDA 997
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEM---EAMLEDTGLhhkrnEEAQD----------LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 998 RAaaivMRAVKNVA---ETGRTIVCTIHqpsiHIFEA---FDELVLLKRgGRMIYSG-PL 1050
Cdd:TIGR01257 1095 YS----RRSIWDLLlkyRSGRTIIMSTH----HMDEAdllGDRIAIISQ-GRLYCSGtPL 1145
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
854-1049 |
2.05e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 57.05 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 854 TALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGFLKVQETF----ARVSGYCEQTDIHSPSITVEESLIYSAW-LRLV 928
Cdd:PRK13647 34 TALLGPNGAGKSTLLLHLNGIYLPQ--RGRVKVMGREVNAENEkwvrSKVGLVFQDPDDQVFSSTVWDDVAFGPVnMGLD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 929 P-EINpqtkiRFVKQVLETIELEEIKDAlvgvaGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAV 1007
Cdd:PRK13647 112 KdEVE-----RRVEEALKAVRMWDFRDK-----PPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEIL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15228112 1008 KNVAETGRTIVCTIHQPSIhIFEAFDELVLLKRGGRMIYSGP 1049
Cdd:PRK13647 182 DRLHNQGKTVIVATHDVDL-AAEWADQVIVLKEGRVLAEGDK 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
836-1022 |
2.18e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.44 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 836 KKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG---RKTSGYIEGEIRISgFLKVQETFARVSGYCEQTDIHSPS 912
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGivpRDAGNIIIDDEDIS-LLPLHARARRGIGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 913 ITVEESLIysAWLRLVPEINPQTKIRFVKQVLETIELEEIKDALvgvaGVSgLSTEQRKRLTVAVELVANPSIIFMDEPT 992
Cdd:PRK10895 93 LSVYDNLM--AVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM----GQS-LSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190
....*....|....*....|....*....|
gi 15228112 993 TGLDARAAAIVMRAVKNVAETGRTIVCTIH 1022
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDSGLGVLITDH 195
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
830-996 |
2.31e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 56.33 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 830 GQGynEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISG--FLKVQET-----FARVSGY 902
Cdd:PRK10584 17 GQG--EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGS--SGEVSLVGqpLHQMDEEaraklRAKHVGF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 903 CEQTDIHSPSITVEESLIYSAWLRlvPEINPQTKIRfVKQVLETIELEEIKDALvgvagVSGLSTEQRKRLTVAVELVAN 982
Cdd:PRK10584 93 VFQSFMLIPTLNALENVELPALLR--GESSRQSRNG-AKALLEQLGLGKRLDHL-----PAQLSGGEQQRVALARAFNGR 164
|
170
....*....|....
gi 15228112 983 PSIIFMDEPTTGLD 996
Cdd:PRK10584 165 PDVLFADEPTGNLD 178
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
809-1048 |
2.41e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 58.30 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 809 KPLTITFQDLNYyvdvpvemkgqGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLagrkTSGY--IEGEIRI 886
Cdd:PRK11160 335 DQVSLTLNNVSF-----------TYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL----TRAWdpQQGEILL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 887 SGflkvqetfARVSGYCEQTDIHSPSITVEESLIYSAWLR--LV---PEINPQTKIRFVKQV-LETIeLEEIK--DALVG 958
Cdd:PRK11160 400 NG--------QPIADYSEAALRQAISVVSQRVHLFSATLRdnLLlaaPNASDEALIEVLQQVgLEKL-LEDDKglNAWLG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 959 VAG--VSGlsTEQRkRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHQpsIHIFEAFDELV 1036
Cdd:PRK11160 471 EGGrqLSG--GEQR-RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHR--LTGLEQFDRIC 544
|
250
....*....|..
gi 15228112 1037 LLKrGGRMIYSG 1048
Cdd:PRK11160 545 VMD-NGQIIEQG 555
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
151-356 |
2.84e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.89 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 151 NIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKAL---------------SGNLEN-NLKCY----GEISYNGHGLNEVV 210
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIerlydptegdiiindSHNLKDiNLKWWrskiGVVSQDPLLFSNSI 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 211 PQ--KTSAYiSQHDLHIAEMTTRE---------TIDFSARCQGVGSRTDIMMEVSKRE-----KDGGIIPDPEIDAYMKA 274
Cdd:PTZ00265 477 KNniKYSLY-SLKDLEALSNYYNEdgndsqenkNKRNSCRAKCAGDLNDMSNTTDSNEliemrKNYQTIKDSEVVDVSKK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 275 ISVKGLKRSLQTDYilkilgldicaETLVG-NAMKrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSL 353
Cdd:PTZ00265 556 VLIHDFVSALPDKY-----------ETLVGsNASK--LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
...
gi 15228112 354 QQV 356
Cdd:PTZ00265 623 NNL 625
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
839-998 |
4.26e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 57.02 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 839 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYiegeIRISGfLKVQETFA--RVSGYCEQTDIHSPSIT 914
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGleHQTSGH----IRFHG-TDVSRLHArdRKVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 915 VEESLIYSawLRLVPEIN-PQTKI--RFVKQVLETIELEEIKDALvgvagVSGLSTEQRKRLTVAVELVANPSIIFMDEP 991
Cdd:PRK10851 91 VFDNIAFG--LTVLPRRErPNAAAikAKVTQLLEMVQLAHLADRY-----PAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
....*..
gi 15228112 992 TTGLDAR 998
Cdd:PRK10851 164 FGALDAQ 170
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
828-1001 |
4.46e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 57.64 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 828 MKGQG--YNEKKlQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGFLKVqetfarvsGYCEQ 905
Cdd:TIGR03719 7 MNRVSkvVPPKK-EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD--FNGEARPQPGIKV--------GYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 906 TDIHSPSITVEESL------IYSAWLRLvPEIN-----PQTKirFVKQVLETIELEEIKDAL------------------ 956
Cdd:TIGR03719 76 EPQLDPTKTVRENVeegvaeIKDALDRF-NEISakyaePDAD--FDKLAAEQAELQEIIDAAdawdldsqleiamdalrc 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15228112 957 -VGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAA 1001
Cdd:TIGR03719 153 pPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVA 198
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
140-389 |
4.46e-08 |
|
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: 54.50 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlKCYGEISYNGHGLN----EVVPQKTS 215
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE---PDSGSILIDGEDLTdledELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 216 -AYISQHDLHIAEMTTRETIDFsarcqgvgsrtdimmevskrekdggiipdpeidaymkaisvkglkrslqtdyilkilg 294
Cdd:cd03229 78 iGMVFQDFALFPHLTVLENIAL---------------------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 295 ldicaetlvgnamkrGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSLLQPApE 374
Cdd:cd03229 100 ---------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLD-E 163
|
250
....*....|....*
gi 15228112 375 SYDLFDDIVLMAEGK 389
Cdd:cd03229 164 AARLADRVVVLRDGK 178
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
150-400 |
5.45e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 55.79 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 150 ANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLkcyGEISYNGHGLNEVVPQKTSAYIS---QHDLHIA 226
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQS---GTVFLGDKPISMLSSRQLARRLAllpQHHLTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 227 EMTTRETIDFsarcqgvgSRTdimmevskrekdggiipdPEIDAYMKaISVKGLKRSLQTdyiLKILGLDICAETLVGNa 306
Cdd:PRK11231 90 GITVRELVAY--------GRS------------------PWLSLWGR-LSAEDNARVNQA---MEQTRINHLADRRLTD- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 307 mkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAhiTNATVFVSLLQPAPESYDLFDDIVLMA 386
Cdd:PRK11231 139 ----LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELN--TQGKTVVTVLHDLNQASRYCDHLVVLA 212
|
250
....*....|....
gi 15228112 387 EGKIVYHGPRDDVL 400
Cdd:PRK11231 213 NGHVMAQGTPEEVM 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
791-1043 |
5.82e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 57.28 E-value: 5.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 791 LDSSIKTNEDPGKMILPFKPLTITFQDLNYyvdvpvemkgqGYNEKKlQLLSEITGAFRPGVLTALMGISGAGKTTLLDV 870
Cdd:PRK13657 313 EDAVPDVRDPPGAIDLGRVKGAVEFDDVSF-----------SYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 871 L--AGRKTSGYIegeiRISG------------------FlkvQET--FARVSGycEQTDIHSPSITVEEsliysawLRLV 928
Cdd:PRK13657 381 LqrVFDPQSGRI----LIDGtdirtvtraslrrniavvF---QDAglFNRSIE--DNIRVGRPDATDEE-------MRAA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 929 PEInpqtkirfvKQVLETIELEEIK-DALVGVAGvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAV 1007
Cdd:PRK13657 445 AER---------AQAHDFIERKPDGyDTVVGERG-RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAAL 514
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15228112 1008 KNVAEtGRTIVCTIHQPSI-------------HIFEA--FDELVllKRGGR 1043
Cdd:PRK13657 515 DELMK-GRTTFIIAHRLSTvrnadrilvfdngRVVESgsFDELV--ARGGR 562
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
154-365 |
6.11e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 55.64 E-value: 6.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEvvPQKTSAYISQHDLHIAEMTTRET 233
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS---SGEITLDGVPVTG--PGADRGVVFQKDALLPWLNVLDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 234 IDFSARCQGVGsrtdimmevsKREkdggiipdpeidaymkaisvkglkRSLQTDYILKILGLDicaetlvgNAMKRGI-- 311
Cdd:COG4525 97 VAFGLRLRGVP----------KAE------------------------RRARAEELLALVGLA--------DFARRRIwq 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15228112 312 -SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVF 365
Cdd:COG4525 135 lSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVF 189
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
153-422 |
7.09e-08 |
|
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: 55.00 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEVVP---QKTSAYISQHDLHIAEMT 229
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPT---SGEIFIDGEDIREQDPvelRRKIGYVIQQIGLFPHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 230 TRETIdfsarcqgvgsrtdimmevskrekdgGIIPdpeidaymKAISVKGLKRSLQTDYILKILGLDIcaetlvGNAMKR 309
Cdd:cd03295 92 VEENI--------------------------ALVP--------KLLKWPKEKIRERADELLALVGLDP------AEFADR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 310 ---GISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQI---IKSLQQVAHITnaTVFVSllQPAPESYDLFDDIV 383
Cdd:cd03295 132 yphELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLqeeFKRLQQELGKT--IVFVT--HDIDEAFRLADRIA 207
|
250 260 270
....*....|....*....|....*....|....*....
gi 15228112 384 LMAEGKIVYHGPRDDVLKffeecgfqCPERKGVADFLQE 422
Cdd:cd03295 208 IMKNGEIVQVGTPDEILR--------SPANDFVAEFVGA 238
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
149-394 |
1.05e-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: 53.47 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 149 EANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLennlkcygeisynghglnevVPQKTSAYISQHDLHIAEM 228
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDL--------------------KPQQGEITLDGVPVSDLEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 229 TTRETIdfsarcqgvgsrtdimmevskrekdgGIIPdpeidaymkaisvkglkrslQTDYILkilgldicAETLVGNAMK 308
Cdd:cd03247 72 ALSSLI--------------------------SVLN--------------------QRPYLF--------DTTLRNNLGR 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 309 RgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHitNATV-FVSLLQPAPESydlFDDIVLMAE 387
Cdd:cd03247 98 R-FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLiWITHHLTGIEH---MDKILFLEN 171
|
....*..
gi 15228112 388 GKIVYHG 394
Cdd:cd03247 172 GKIIMQG 178
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
848-1022 |
1.07e-07 |
|
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: 54.47 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 848 FRPGVLTALMGISGAGKTTLLDVLagRKTSGYIEGEIRISG----FLKVQETFARVsGYCEQtdihSP---SITVEESLI 920
Cdd:cd03249 26 IPPGKTVALVGSSGCGKSTVVSLL--ERFYDPTSGEILLDGvdirDLNLRWLRSQI-GLVSQ----EPvlfDGTIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 921 YSAWLRLVPEInpqtkIRFVKQVL--ETIE-LEEIKDALVGVAGVSgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDA 997
Cdd:cd03249 99 YGKPDATDEEV-----EEAAKKANihDFIMsLPDGYDTLVGERGSQ-LSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180
....*....|....*....|....*
gi 15228112 998 RAAAIVMRAVKNVAEtGRTIVCTIH 1022
Cdd:cd03249 173 ESEKLVQEALDRAMK-GRTTIVIAH 196
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
109-390 |
1.10e-07 |
|
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: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 109 EHLGVEAACEVVE--------GKALPTLW----NSLKHVFLDLLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGC 176
Cdd:TIGR02633 218 QHVATKDMSTMSEddiitmmvGREITSLYphepHEIGDVILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 177 GKTTLLKALSGNLENnlKCYGEISYNGHGLNEVVPQKTSayisqhdlhiaemttretidfsarcqgvgsRTDIMMEVSKR 256
Cdd:TIGR02633 298 GRTELVQALFGAYPG--KFEGNVFINGKPVDIRNPAQAI------------------------------RAGIAMVPEDR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 257 EKDGgIIPDPEIDaymKAISVKGLKRslqtdyILKILGLDICAET-LVGNAMKR-------------GISGGQKKRLTTA 322
Cdd:TIGR02633 346 KRHG-IVPILGVG---KNITLSVLKS------FCFKMRIDAAAELqIIGSAIQRlkvktaspflpigRLSGGNQQKAVLA 415
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15228112 323 EMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSllQPAPESYDLFDDIVLMAEGKI 390
Cdd:TIGR02633 416 KMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVS--SELAEVLGLSDRVLVIGEGKL 481
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
139-388 |
1.14e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 54.71 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 139 LLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEvvPQKTSAYI 218
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ---HGSITLDGKPVEG--PGAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 219 SQHDLHIAEMTTRETIDFSARCQGVGsrtdimmevsKREKdggiipdpeidaymkaisvkgLKRSLQtdyILKILGLDic 298
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVE----------KMQR---------------------LEIAHQ---MLKKVGLE-- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 299 aetlvgNAMKRGI---SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVsLLQPAPES 375
Cdd:PRK11248 120 ------GAEKRYIwqlSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLL-ITHDIEEA 192
|
250
....*....|...
gi 15228112 376 YDLFDDIVLMAEG 388
Cdd:PRK11248 193 VFMATELVLLSPG 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
163-411 |
1.44e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 54.63 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 163 SPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNE------VVPQKTSAYISQHDLHIAEMTTRETIDF 236
Cdd:PRK13638 25 SLSPVTGLVGANGCGKSTLFMNLSGLLRPQ---KGAVLWQGKPLDYskrgllALRQQVATVFQDPEQQIFYTDIDSDIAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 237 SARCQGVGSRtdimmEVSKRekdggiipdpeIDAYMKAISVKGLKRS-LQtdyilkilgldiCaetlvgnamkrgISGGQ 315
Cdd:PRK13638 102 SLRNLGVPEA-----EITRR-----------VDEALTLVDAQHFRHQpIQ------------C------------LSHGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 316 KKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSllQPAPESYDLFDDIVLMAEGKIVYHGP 395
Cdd:PRK13638 142 KKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISS--HDIDLIYEISDAVYVLRQGQILTHGA 219
|
250
....*....|....*....
gi 15228112 396 RDDVL---KFFEECGFQCP 411
Cdd:PRK13638 220 PGEVFactEAMEQAGLTQP 238
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
842-1048 |
1.60e-07 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 54.07 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 842 SEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKT--SGYIEGEIRISGFLKV-------QETFARVS-GYCEQTDIH-- 909
Cdd:TIGR02323 20 RDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLApdHGTATYIMRSGAELELyqlseaeRRRLMRTEwGFVHQNPRDgl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 910 ----SPSITVEESLIySAWLRLVPEINpQTKIRFVKQVleTIELEEIKDAlvgvagVSGLSTEQRKRLTVAVELVANPSI 985
Cdd:TIGR02323 100 rmrvSAGANIGERLM-AIGARHYGNIR-ATAQDWLEEV--EIDPTRIDDL------PRAFSGGMQQRLQIARNLVTRPRL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228112 986 IFMDEPTTGLDARAAAIVMRAVKN-VAETGRTIVCTIHQPSIHIFEAfDELVLLKRgGRMIYSG 1048
Cdd:TIGR02323 170 VFMDEPTGGLDVSVQARLLDLLRGlVRDLGLAVIIVTHDLGVARLLA-QRLLVMQQ-GRVVESG 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
811-1102 |
1.73e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.40 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 811 LTITFQDLNYyvdvpVEMKGQGYnekKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIE-GEIRIS 887
Cdd:PRK13646 1 MTIRFDNVSY-----TYQKGTPY---EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAllKPTTGTVTvDDITIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 888 GFLKvqetfarvsgyceqtDIHSPSITVEESLIYSAWLRLVPEINPQTKIRFVKQVLEtIELEEIKD---ALVGVAGVS- 963
Cdd:PRK13646 73 HKTK---------------DKYIRPVRKRIGMVFQFPESQLFEDTVEREIIFGPKNFK-MNLDEVKNyahRLLMDLGFSr 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 964 --------GLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNV-AETGRTIVCTIHQPSiHIFEAFDE 1034
Cdd:PRK13646 137 dvmsqspfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMN-EVARYADE 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228112 1035 LVLLKRGGRMIYSGP--LGQHSSCVIEYFQNIPGVAK----IRDKYNPATWMLEVTSEsveteldmDFAKIYNE 1102
Cdd:PRK13646 216 VIVMKEGSIVSQTSPkeLFKDKKKLADWHIGLPEIVQlqydFEQKYQTKLKDIALTEE--------EFVSLYKE 281
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
855-1048 |
1.78e-07 |
|
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: 53.69 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 855 ALMGISGAGKTTLLDVLAG--RKTSGYIEGEIRISGFLKVQETFarvsgyceqtdihSPSITVEESLIYSAWL--RLVPE 930
Cdd:cd03220 52 GLIGRNGAGKSTLLRLLAGiyPPDSGTVTVRGRVSSLLGLGGGF-------------NPELTGRENIYLNGRLlgLSRKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 931 InpQTKIRFVkqvletIELEEIKDALvgVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNV 1010
Cdd:cd03220 119 I--DEKIDEI------IEFSELGDFI--DLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 15228112 1011 AETGRTIVCTIHQPSIhIFEAFDELVLLKRgGRMIYSG 1048
Cdd:cd03220 189 LKQGKTVILVSHDPSS-IKRLCDRALVLEK-GKIRFDG 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
849-1041 |
1.93e-07 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 54.72 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 849 RPGVLTALMGISGAGKTTLLDVLAG--RKTSgyieGEIRISGflkvqetfarvsgyceqTDIHS---------------- 910
Cdd:COG3842 29 EPGEFVALLGPSGCGKTTLLRMIAGfeTPDS----GRILLDG-----------------RDVTGlppekrnvgmvfqdya 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 911 --PSITVEESLIYSAWLRLVPEinPQTKIRfVKQVLETIELEEIKDALvgvagVSGLSTEQRKRltVAV--ELVANPSII 986
Cdd:COG3842 88 lfPHLTVAENVAFGLRMRGVPK--AEIRAR-VAELLELVGLEGLADRY-----PHQLSGGQQQR--VALarALAPEPRVL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15228112 987 FMDEPTTGLDARAAAIVMRAVKNV-AETGRTIVCTIHQPSihifEAF---DELVLLKRG 1041
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQE----EALalaDRIAVMNDG 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
847-1052 |
1.97e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 53.61 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 847 AFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISG----------------FlkvQET--Farvsgyceqtdi 908
Cdd:COG3840 21 TIAAGERVAILGPSGAGKSTLLNLIAGFLPP--DSGRILWNGqdltalppaerpvsmlF---QENnlF------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 909 hsPSITVEE--SLIYSAWLRLvpeiNPQTKIRfVKQVLETIELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSII 986
Cdd:COG3840 84 --PHLTVAQniGLGLRPGLKL----TAEQRAQ-VEQALERVGLAGLLDRLPGQ-----LSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228112 987 FMDEPTTGLDaraaaIVMRA-----VKNVA-ETGRTIVCTIHQPS--IHIfeaFDELVLLKRgGRMIYSGPLGQ 1052
Cdd:COG3840 152 LLDEPFSALD-----PALRQemldlVDELCrERGLTVLMVTHDPEdaARI---ADRVLLVAD-GRIAADGPTAA 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
811-1022 |
2.05e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 54.37 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 811 LTITFQDLNYYVDVPVEMKGQGynekklqlLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGFL 890
Cdd:PRK13649 1 MGINLQNVSYTYQAGTPFEGRA--------LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVP--TQGSVRVDDTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 891 kvqetfarVSGYCEQTDIHSPSITV-------EESLIYSAWLRLVPeINPQTkirFVKQVLETIELEEIKDALVGVA--- 960
Cdd:PRK13649 71 --------ITSTSKNKDIKQIRKKVglvfqfpESQLFEETVLKDVA-FGPQN---FGVSQEEAEALAREKLALVGISesl 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228112 961 ---GVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIH 1022
Cdd:PRK13649 139 fekNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
839-1023 |
2.33e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 53.48 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 839 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLagrktsGYIE----GEIRISG--FLKVQETFAR--------VSGYCE 904
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVL------NLLEmprsGTLNIAGnhFDFSKTPSDKairelrrnVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 905 QTDIHsPSITVEESLIySAWLRLVPEINPQTKIRfVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPS 984
Cdd:PRK11124 90 QYNLW-PHLTVQQNLI-EAPCRVLGLSKDQALAR-AEKLLERLRLKPYADRFP-----LHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 15228112 985 IIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQ 1023
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
841-1041 |
2.71e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 53.84 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 841 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISG-----FLKVQETFARVSGYCEQTDIHSPSITV 915
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ--KGKVLVSGidtgdFSKLQGIRKLVGIVFQNPETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 916 EESLIYSawlrlvPE--INPQTKIR-FVKQVLETIELEEIKDAlvgvaGVSGLSTEQRKRLTVAVELVANPSIIFMDEPT 992
Cdd:PRK13644 96 EEDLAFG------PEnlCLPPIEIRkRVDRALAEIGLEKYRHR-----SPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15228112 993 TGLDARAAAIVMRAVKNVAETGRTIVCTIHqpSIHIFEAFDELVLLKRG 1041
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITH--NLEELHDADRIIVMDRG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
839-1049 |
3.12e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 53.24 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 839 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLagrktSGYIE---GEIRISGFLKVQ---ETFARVSGYCEQtdiHSP- 911
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL-----SGELSpdsGEVRLNGRPLADwspAELARRRAVLPQ---HSSl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 912 --SITVEESLiysaWLRLVP-EINPQTKIRFVKQVLetieleeikdALVGVAGVSG-----LSTEQRKRLTVAVELV--- 980
Cdd:PRK13548 88 sfPFTVEEVV----AMGRAPhGLSRAEDDALVAAAL----------AQVDLAHLAGrdypqLSGGEQQRVQLARVLAqlw 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15228112 981 ---ANPSIIFMDEPTTGLDARAAAIVMRAVKNVA-ETGRTIVCTIH---QPSihifeAF-DELVLLKrGGRMIYSGP 1049
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHdlnLAA-----RYaDRIVLLH-QGRLVADGT 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
853-1032 |
3.20e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.50 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 853 LTALMGISGAGKTTLLDVLaGRKTSgyIEGEIRISGFLKV--QETFAR---VSGYCEQTDIHSPS-----ITVEESLIYS 922
Cdd:PRK14258 35 VTAIIGPSGCGKSTFLKCL-NRMNE--LESEVRVEGRVEFfnQNIYERrvnLNRLRRQVSMVHPKpnlfpMSVYDNVAYG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 923 awLRLVpEINPQTKIR-FVKQVLETIEL-EEIKDALVGVAgvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAA 1000
Cdd:PRK14258 112 --VKIV-GWRPKLEIDdIVESALKDADLwDEIKHKIHKSA--LDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIAS 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 15228112 1001 AIVMRAVKNV---AETGRTIVC-TIHQPS-IHIFEAF 1032
Cdd:PRK14258 187 MKVESLIQSLrlrSELTMVIVShNLHQVSrLSDFTAF 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
154-438 |
4.43e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 53.27 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLKCYGEISYNGHGLNEvvpqKTsayisqhdlhIAEMTTRET 233
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTA----KT----------VWDIREKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 234 IDF-SARCQGVGSRT--DIMMEVSKREkdggiIPDPEidayMKAISVKGLKRSLQTDYIlkilgldicaetlvgNAMKRG 310
Cdd:PRK13640 88 IVFqNPDNQFVGATVgdDVAFGLENRA-----VPRPE----MIKIVRDVLADVGMLDYI---------------DSEPAN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 311 ISGGQKKRLTTAEMI-VGPtKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFvSLLQPAPESyDLFDDIVLMAEGK 389
Cdd:PRK13640 144 LSGGQKQRVAIAGILaVEP-KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVI-SITHDIDEA-NMADQVLVLDDGK 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15228112 390 IVYHGPRDDVLK---FFEECGFQCPerkgvadFLQEVISKKDQGQYWLHQNL 438
Cdd:PRK13640 221 LLAQGSPVEIFSkveMLKEIGLDIP-------FVYKLKNKLKEKGISVPQEI 265
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
838-1045 |
5.92e-07 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 52.40 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 838 LQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSgyieGEIRISGflkvqetfARVSGyceqtdiHSPSITV 915
Cdd:COG1116 24 VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGleKPTS----GEVLVDG--------KPVTG-------PGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 916 ---EESLIysAWL------RLVPEINPQTKIRFVKQVLETIEleeikdaLVGVAGVSG-----LSTEQRKRLTVAVELVA 981
Cdd:COG1116 85 vfqEPALL--PWLtvldnvALGLELRGVPKAERRERARELLE-------LVGLAGFEDayphqLSGGMRQRVAIARALAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15228112 982 NPSIIFMDEPTTGLDA--RAaaiVMRA--VKNVAETGRTIVCTIHQpsihIFEAF---DELVLL-KRGGRMI 1045
Cdd:COG1116 156 DPEVLLMDEPFGALDAltRE---RLQDelLRLWQETGKTVLFVTHD----VDEAVflaDRVVVLsARPGRIV 220
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
153-370 |
7.13e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 52.35 E-value: 7.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALS--GNLENNLKCYGEISYNGHGLNEvvpqktsayisqhdlhiaemtT 230
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmNELESEVRVEGRVEFFNQNIYE---------------------R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 231 RETIDFSARcqgvgsrtdimmEVSKREKDGGIIPDPEIDAYMKAISVKGLKRSLQTDYILK--ILGLDICAEtlVGNAMK 308
Cdd:PRK14258 80 RVNLNRLRR------------QVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVEsaLKDADLWDE--IKHKIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15228112 309 RG---ISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQI---IKSLQQVAHITNATVFVSLLQ 370
Cdd:PRK14258 146 KSaldLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVeslIQSLRLRSELTMVIVSHNLHQ 213
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
839-1049 |
7.26e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 51.37 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 839 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYIEGEIRISG----FLKVQETFARVSGYCEQTDIHSPSIT 914
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGeditDLPPEERARLGIFLAFQYPPEIPGVK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 915 VEEsliysaWLRLVPEinpqtkirfvkqvletieleeikdalvgvagvsGLSTEQRKRLTVAVELVANPSIIFMDEPTTG 994
Cdd:cd03217 94 NAD------FLRYVNE---------------------------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15228112 995 LDARAAAIVMRAVKNVAETGRTIVCTIHQPsiHIFEAFD-ELVLLKRGGRMIYSGP 1049
Cdd:cd03217 135 LDIDALRLVAEVINKLREEGKSVLIITHYQ--RLLDYIKpDRVHVLYDGRIVKSGD 188
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
157-400 |
7.42e-07 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 53.19 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 157 DVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNGHGLNEvvpqktsayisqhdlhiaemttretidf 236
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAG-LTRPDE--GEIVLNGRTLFD---------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 237 sarcqgvgSRTDIMMEVSKRE-----KDGGIIPDpeidaymkaISVK-----GLKRS------LQTDYILKILGLDICAE 300
Cdd:TIGR02142 64 --------SRKGIFLPPEKRRigyvfQEARLFPH---------LSVRgnlryGMKRArpserrISFERVIELLGIGHLLG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 301 TLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQV-AHITNATVFVS-LLQpapESYDL 378
Cdd:TIGR02142 127 RLPGR-----LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLhAEFGIPILYVShSLQ---EVLRL 198
|
250 260
....*....|....*....|..
gi 15228112 379 FDDIVLMAEGKIVYHGPRDDVL 400
Cdd:TIGR02142 199 ADRVVVLEDGRVAAAGPIAEVW 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
861-1016 |
7.66e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 52.40 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 861 GAGKTTLLDVLAG--RKTSG--YIEG-------EIRISGFLkvqetfARV-----SGYCeqtdihsPSITVEESLIYsAW 924
Cdd:COG1101 42 GAGKSTLLNAIAGslPPDSGsiLIDGkdvtklpEYKRAKYI------GRVfqdpmMGTA-------PSMTIEENLAL-AY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 925 LR-----LVPEINPQtKIRFVKQVLETIE--LEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDA 997
Cdd:COG1101 108 RRgkrrgLRRGLTKK-RRELFRELLATLGlgLENRLDTKVGL-----LSGGQRQALSLLMATLTKPKLLLLDEHTAALDP 181
|
170 180
....*....|....*....|
gi 15228112 998 RAAAIVMRAVKN-VAETGRT 1016
Cdd:COG1101 182 KTAALVLELTEKiVEENNLT 201
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
840-1052 |
7.69e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.41 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 840 LLSEITGAFRPGVLTALMGISGAGKTTLLDVL--AGRKTSGY-IEGEIRISG-----FLKVQEtFARVSGYCEQTDIHSP 911
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrMNDKVSGYrYSGDVLLGGrsifnYRDVLE-FRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 912 SITVEESLIYSAWLRLVPeinpQTKIRFVKQ--VLETIELEEIKDALVGVAgvSGLSTEQRKRLTVAVELVANPSIIFMD 989
Cdd:PRK14271 115 MSIMDNVLAGVRAHKLVP----RKEFRGVAQarLTEVGLWDAVKDRLSDSP--FRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228112 990 EPTTGLDARAAAIVMRAVKNVAETGRTIVCTihqPSIHIFEAFDELVLLKRGGRMIYSGPLGQ 1052
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVT---HNLAQAARISDRAALFFDGRLVEEGPTEQ 248
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
850-1050 |
8.46e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 52.78 E-value: 8.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 850 PGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGF--LKVQETFAR----VSGYCEQ--TDIhspsiTVEESL 919
Cdd:COG4586 47 PGEIVGFIGPNGAGKSTTIKMLTGilVPTSG----EVRVLGYvpFKRRKEFARrigvVFGQRSQlwWDL-----PAIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 920 iysAWLRLVPEINPQTKIRFVKQVLETIELEEIKDAlvgvaGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDara 999
Cdd:COG4586 118 ---RLLKAIYRIPDAEYKKRLDELVELLDLGELLDT-----PVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD--- 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15228112 1000 aAIVMRAVKN-----VAETGRTIVCTIHQPS-IhifEAFDELVLLKRGGRMIYSGPL 1050
Cdd:COG4586 187 -VVSKEAIREflkeyNRERGTTILLTSHDMDdI---EALCDRVIVIDHGRIIYDGSL 239
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
139-420 |
1.24e-06 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 52.41 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 139 LLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNGHGLNEVVPQKTS-AY 217
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG-FETPDS--GRILLDGRDVTGLPPEKRNvGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 218 ISQHDL---HiaeMTTRETIDFSARCQGVgsrtdimmevskrekdggiiPDPEIDAymkaisvkglkrslQTDYILKILG 294
Cdd:COG3842 82 VFQDYAlfpH---LTVAENVAFGLRMRGV--------------------PKAEIRA--------------RVAELLELVG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 295 LDICAETLVGNamkrgISGGQKKR--LTTAeMIVGPtKALFMDEITNGLDSST--AFQI-IKSLQQVAHITnaTVFV--- 366
Cdd:COG3842 125 LEGLADRYPHQ-----LSGGQQQRvaLARA-LAPEP-RVLLLDEPLSALDAKLreEMREeLRRLQRELGIT--FIYVthd 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15228112 367 -----SLlqpapeSydlfDDIVLMAEGKIVYHGPRDDVlkffeecgFQCPERKGVADFL 420
Cdd:COG3842 196 qeealAL------A----DRIAVMNDGRIEQVGTPEEI--------YERPATRFVADFI 236
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
853-998 |
1.62e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 51.87 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 853 LTaLMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGflkvqETFARVSGycEQTDIHS--------PSITVEESLIYSAW 924
Cdd:PRK09452 43 LT-LLGPSGCGKTTVLRLIAGFETPD--SGRIMLDG-----QDITHVPA--ENRHVNTvfqsyalfPHMTVFENVAFGLR 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228112 925 LRLVP--EINPQtkirfVKQVLETIELEEIKDalvgvAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDAR 998
Cdd:PRK09452 113 MQKTPaaEITPR-----VMEALRMVQLEEFAQ-----RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
826-1041 |
1.70e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.48 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 826 VEMKGQGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIegEIRISGFLKVQETFARVSG-- 901
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGihEPTKGTI--TINNINYNKLDHKLAAQLGig 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 902 --YCEQTDIHspSITVEESLIYSAWL-RLVPEIN--PQTKIRFVKQV-LETIELEEIKDALVGvagvsGLSTEQRKRLTV 975
Cdd:PRK09700 84 iiYQELSVID--ELTVLENLYIGRHLtKKVCGVNiiDWREMRVRAAMmLLRVGLKVDLDEKVA-----NLSISHKQMLEI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228112 976 AVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRG 1041
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLA-EIRRICDRYTVMKDG 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
848-1018 |
1.82e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.34 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 848 FRPGVLTALMGISGAGKTTLLDVLAG--RKTsgyiEGEIRISGflkvqetfarvsgycEQTDIHSP-------------- 911
Cdd:COG3845 28 VRPGEIHALLGENGAGKSTLMKILYGlyQPD----SGEILIDG---------------KPVRIRSPrdaialgigmvhqh 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 912 -----SITVEESLIYSAWLRLVPEINPQTKIRFVKQVLETIELeEIK-DALVGvagvsGLSTEQRKRltvaVE----LVA 981
Cdd:COG3845 89 fmlvpNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGL-DVDpDAKVE-----DLSVGEQQR----VEilkaLYR 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 15228112 982 NPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIV 1018
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSII 195
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
140-400 |
1.89e-06 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 52.15 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLkcyGEISYNGhglnEVVPQKTSAYIS 219
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA---GTVLVAG----DDVEALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 220 QhdlHIAEMTTRETIDFSARCqgvgsRTDIMMEvskrekdggiipdpeidaymkaisvkglkrslQTDYILKILGLDICA 299
Cdd:PRK09536 77 R---RVASVPQDTSLSFEFDV-----RQVVEMG--------------------------------RTPHRSRFDTWTETD 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 300 ETLVGNAMKRG------------ISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHiTNATVFVS 367
Cdd:PRK09536 117 RAAVERAMERTgvaqfadrpvtsLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVD-DGKTAVAA 195
|
250 260 270
....*....|....*....|....*....|....*....
gi 15228112 368 LlqpapesYDL------FDDIVLMAEGKIVYHGPRDDVL 400
Cdd:PRK09536 196 I-------HDLdlaaryCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
965-1023 |
2.16e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 50.74 E-value: 2.16e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15228112 965 LSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQ 1023
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
840-1041 |
2.47e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 50.68 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 840 LLSEITGAFRPGVLTALMGISGAGKTTLldVLAGRKTSGYIEGEIRISGF----LKVQETFARVSgyceqtdihspsITV 915
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDIFDGKIVIDGIdiskLPLHTLRSRLS------------IIL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 916 EESLIYSAWLRLvpEINPQTKIRfVKQVLETIELEEIK----------DALVGVAGvSGLSTEQRKRLTVAVELVANPSI 985
Cdd:cd03288 102 QDPILFSGSIRF--NLDPECKCT-DDRLWEALEIAQLKnmvkslpgglDAVVTEGG-ENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15228112 986 IFMDEPTTGLDARAAAIVMRAVKnVAETGRTIVCTIHQPSiHIFEAfDELVLLKRG 1041
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVM-TAFADRTVVTIAHRVS-TILDA-DLVLVLSRG 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
850-996 |
2.59e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 50.69 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 850 PGVLTALMGISGAGKTTLLDVLAGR--KTSGYIEGEIRISGFLKVQE-------TFARVS-GYCEQ--TDIHSPSIT--- 914
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSARlaPDAGEVHYRMRDGQLRDLYAlseaerrRLLRTEwGFVHQhpRDGLRMQVSagg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 915 -VEESLIYSAWlRLVPEINpQTKIRFVKQVleTIELEEIKDALVGVAGvsGLsteqRKRLTVAVELVANPSIIFMDEPTT 993
Cdd:PRK11701 111 nIGERLMAVGA-RHYGDIR-ATAGDWLERV--EIDAARIDDLPTTFSG--GM----QQRLQIARNLVTHPRLVFMDEPTG 180
|
...
gi 15228112 994 GLD 996
Cdd:PRK11701 181 GLD 183
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
155-394 |
2.78e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 50.62 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 155 LTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlKCYGEISYNGhglnevvpqktsayisqhdlhiaemttrETI 234
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILK---PSSGRILFDG----------------------------KPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 235 DFSARCqgvgsrtdiMMEVskREKDGGIIPDPEIDAYMKA----ISVKGLKRSLQTDYILKilgldicaetLVGNAMKR- 309
Cdd:PRK13636 71 DYSRKG---------LMKL--RESVGMVFQDPDNQLFSASvyqdVSFGAVNLKLPEDEVRK----------RVDNALKRt 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 310 GI-----------SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVsllqpAPESYDL 378
Cdd:PRK13636 130 GIehlkdkpthclSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIII-----ATHDIDI 204
|
250 260
....*....|....*....|
gi 15228112 379 F----DDIVLMAEGKIVYHG 394
Cdd:PRK13636 205 VplycDNVFVMKEGRVILQG 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
153-422 |
4.31e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.12 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLennlkcygeisynghglnevvpQKTSAYISQHDLHIAEMTTRE 232
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLL----------------------QPTEGKVTVGDIVVSSTSKQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 233 TIDfsarcqgvgsrtdimmevSKREKDGGIIPDPEIDAYMKAIsVKGLKRSLQTDYILKILGLDICAETLVGNAMKRG-- 310
Cdd:PRK13643 78 EIK------------------PVRKKVGVVFQFPESQLFEETV-LKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEfw 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 311 ------ISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSLLQpaPESYDLFDDIVL 384
Cdd:PRK13643 139 ekspfeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLM--DDVADYADYVYL 216
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15228112 385 MAEGKIVYHGPRDDVLK---FFEECGFQCPERKGVADFLQE 422
Cdd:PRK13643 217 LEKGHIISCGTPSDVFQevdFLKAHELGVPKATHFADQLQK 257
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
139-213 |
4.66e-06 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 49.70 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 139 LLKLSGV----RTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNGHGLNE------ 208
Cdd:COG1116 7 ALELRGVskrfPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAG-LEKPTS--GEVLVDGKPVTGpgpdrg 83
|
....*
gi 15228112 209 VVPQK 213
Cdd:COG1116 84 VVFQE 88
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
840-1023 |
5.67e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 840 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYI--EGEIRISGFLKVQETFARVSgycEQTDIhSPSITV 915
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGllNPEKGEIlfERQSIKKDLCTYQKQLCFVG---HRSGI-NPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 916 EESLIYsawlrlvpEINPQTKIRFVKQVLETIELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGL 995
Cdd:PRK13540 92 RENCLY--------DIHFSPGAVGITELCRLFSLEHLIDYPCGL-----LSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180
....*....|....*....|....*...
gi 15228112 996 DARAAAIVMRAVKNVAETGRTIVCTIHQ 1023
Cdd:PRK13540 159 DELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1192-1356 |
6.02e-06 |
|
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: 50.08 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1192 VLGAIYGLVLFVGINNCTSALqYFETERNVMYRERFAGMySAFAYALAQVVTEIPYIFIQsaeFVIVIYPMIGFYASFSK 1271
Cdd:pfam12698 163 LVGLILMIIILIGAAIIAVSI-VEEKESRIKERLLVSGV-SPLQYWLGKILGDFLVGLLQ---LLIILLLLFGIGIPFGN 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 1272 VFWSLYAMFCNLLCFNYLAMFLISITPNFMVAAILQSLFFTTFNIFAGFLIPKPQIPKWWVWFYYITPTSWTLNLFFSSQ 1351
Cdd:pfam12698 238 LGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLRLI 317
|
....*
gi 15228112 1352 YGDIH 1356
Cdd:pfam12698 318 YGDSL 322
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
139-212 |
6.24e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 48.94 E-value: 6.24e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228112 139 LLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLkcyGEISYNGHGLNEVVPQ 212
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTS---GTLLFEGEDISTLKPE 77
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
138-398 |
6.50e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 50.45 E-value: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 138 DLLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLkcyGEISYnGHGLNevvpqktSAY 217
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDS---GTVKL-GETVK-------IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 218 ISQHdlhiaemttRETIDFSARcqgvgsrtdiMMEVSKREKDGGiiPDPEIDAYMKAISVKGLKrslqtdyilkilgldi 297
Cdd:COG0488 383 FDQH---------QEELDPDKT----------VLDELRDGAPGG--TEQEVRGYLGRFLFSGDD---------------- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 298 cAETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDsstafqiIKSLQQvahITNA------TV-FVS--- 367
Cdd:COG0488 426 -AFKPVGV-----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLD-------IETLEA---LEEAlddfpgTVlLVShdr 489
|
250 260 270
....*....|....*....|....*....|...
gi 15228112 368 -LLQpapesyDLFDDIVLMAEGKIV-YHGPRDD 398
Cdd:COG0488 490 yFLD------RVATRILEFEDGGVReYPGGYDD 516
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
849-1048 |
7.51e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.02 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 849 RPGVLTALMGISGAGKTTLLDVLAGRKTSGYIEGEIRISG----FLKVQETFARVSGYCEQTDIHSPSITVEESLIYSA- 923
Cdd:PRK09580 25 RPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGkdllELSPEDRAGEGIFMAFQYPVEIPGVSNQFFLQTALn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 924 WLRLVPEINPQTKIRFVKQVLETIELEEIKDALVGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIV 1003
Cdd:PRK09580 105 AVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15228112 1004 MRAVKNVAETGRTIVCTIHQPSIHIFEAFDELVLLKRgGRMIYSG 1048
Cdd:PRK09580 185 ADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQ-GRIVKSG 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
840-1024 |
7.57e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 49.28 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 840 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLaGRKTSGYiEGEIRISG-FLKVQETFARVS--------GYCEQTDIHS 910
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL-NRLIEIY-DSKIKVDGkVLYFGKDIFQIDaiklrkevGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 911 PSITVEESLIYSAWLRLVPEINPQTKIrfVKQVLETIEL-EEIKDALVGVAgvSGLSTEQRKRLTVAVELVANPSIIFMD 989
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKI--VEECLRKVGLwKEVYDRLNSPA--SQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190
....*....|....*....|....*....|....*
gi 15228112 990 EPTTGLDARAAAIVMRAVKNVAETgRTIVCTIHQP 1024
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNP 212
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
855-1041 |
9.77e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 49.03 E-value: 9.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 855 ALMGISGAGKTTLLDVLAG--RKTSG--YIEGE-IRISGFLKVQETFARVSgycEQTDIHSPSITVEESLIYSAwlrLVP 929
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGilKPTSGsvLIRGEpITKENIREVRKFVGLVF---QNPDDQIFSPTVEQDIAFGP---INL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 930 EINPQTKIRFVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKN 1009
Cdd:PRK13652 108 GLDEETVAHRVSSALHMLGLEELRDRVP-----HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLND 182
|
170 180 190
....*....|....*....|....*....|...
gi 15228112 1010 VAET-GRTIVCTIHQPSIhIFEAFDELVLLKRG 1041
Cdd:PRK13652 183 LPETyGMTVIFSTHQLDL-VPEMADYIYVMDKG 214
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
851-1022 |
9.80e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 48.83 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 851 GVLTALMGISGAGKTTLLDVLAGRKTSG----YIEGEiRISGFlkVQETFARVSGYCEQTDIHSPSITVEEsliysawlr 926
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAhghvWLDGE-HIQHY--ASKEVARRIGLLAQNATTPGDITVQE--------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 927 LVpeinpqTKIRFVKQVLETIELEEIKDALVGVAGVSG-----------LSTEQRKRLTVAVELVANPSIIFMDEPTTGL 995
Cdd:PRK10253 101 LV------ARGRYPHQPLFTRWRKEDEEAVTKAMQATGithladqsvdtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180
....*....|....*....|....*...
gi 15228112 996 DARAAAIVMRAVKNV-AETGRTIVCTIH 1022
Cdd:PRK10253 175 DISHQIDLLELLSELnREKGYTLAAVLH 202
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
152-400 |
1.05e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 49.68 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 152 IKILTDVSGIISPGRlTL-LLGPPGCGKTTLLKALSGnLennLKCYGEISYNGHglnevvpqktsayisqhdlHIAEMTT 230
Cdd:COG4172 299 VKAVDGVSLTLRRGE-TLgLVGESGSGKSTLGLALLR-L---IPSEGEIRFDGQ-------------------DLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 231 RETIDFSARCQGV-----GS---RtdimMEVskrekdGGIIPDPeidayMKAISVkGLKRSLQTDYILKIL---GLDica 299
Cdd:COG4172 355 RALRPLRRRMQVVfqdpfGSlspR----MTV------GQIIAEG-----LRVHGP-GLSAAERRARVAEALeevGLD--- 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 300 etlvGNAMKRGI---SGGQKKRLTTAE-MIVGPtKALFMDEITNGLDSSTAFQII---KSLQQVAHItnATVFVSllqpa 372
Cdd:COG4172 416 ----PAARHRYPhefSGGQRQRIAIARaLILEP-KLLVLDEPTSALDVSVQAQILdllRDLQREHGL--AYLFIS----- 483
|
250 260 270
....*....|....*....|....*....|....
gi 15228112 373 pesYDL------FDDIVLMAEGKIVYHGPRDDVL 400
Cdd:COG4172 484 ---HDLavvralAHRVMVMKDGKVVEQGPTEQVF 514
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
855-1041 |
1.07e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 50.10 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 855 ALMGISGAGKTTLLDVLAGrktsgYI---EGEIRISGflkvqetfARVSGYCEQTDIHSPSITVEESLIYS----AWLRL 927
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMG-----YYpltEGEIRLDG--------RPLSSLSHSVLRQGVAMVQQDPVVLAdtflANVTL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 928 VPEINPQTkirfVKQVLETIELEEI----KDALVGVAGVSG--LSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAA 1001
Cdd:PRK10790 438 GRDISEEQ----VWQALETVQLAELarslPDGLYTPLGEQGnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ 513
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15228112 1002 IVMRAVKNVAETgRTIVCTIHQPSIhIFEAfDELVLLKRG 1041
Cdd:PRK10790 514 AIQQALAAVREH-TTLVVIAHRLST-IVEA-DTILVLHRG 550
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
840-1049 |
1.16e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.67 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 840 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYIEGEIRISGFLKVQ-ETFARvsgyceqtdIHSPSITVEES 918
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTLNgEPLAA---------IDAPRLARLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 919 LIYSAWLRLVP----EINPQTKIRFVKQVLET-IELEEIKDALVGVAG--------VSGLSTEQRKRLTVAVEL------ 979
Cdd:PRK13547 87 VLPQAAQPAFAfsarEIVLLGRYPHARRAGALtHRDGEIAWQALALAGatalvgrdVTTLSGGELARVQFARVLaqlwpp 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228112 980 ---VANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTI-HQPSIHIFEAfDELVLLKrGGRMIYSGP 1049
Cdd:PRK13547 167 hdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIvHDPNLAARHA-DRIAMLA-DGAIVAHGA 238
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
970-1052 |
1.29e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.96 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 970 RKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIhQPSIHIFEAFDELVLLKRgGRMIYSGP 1049
Cdd:NF000106 150 RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTT-QYMEEAEQLAHELTVIDR-GRVIADGK 227
|
...
gi 15228112 1050 LGQ 1052
Cdd:NF000106 228 VDE 230
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
137-385 |
1.43e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 47.65 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 137 LDLLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkcygeisynghglnevvpqktsa 216
Cdd:COG2401 28 AIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG----------------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 217 yisqhdlhiaemttretidfSARCQGVGSRTDIMMEVSKREKDG--GIIPDPEIDAYMKAISVKGLkrslqTDYILkilg 294
Cdd:COG2401 79 --------------------ALKGTPVAGCVDVPDNQFGREASLidAIGRKGDFKDAVELLNAVGL-----SDAVL---- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 295 ldicaetlvgnaMKRG---ISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSLLQP 371
Cdd:COG2401 130 ------------WLRRfkeLSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHY 197
|
250
....*....|....
gi 15228112 372 APESyDLFDDIVLM 385
Cdd:COG2401 198 DVID-DLQPDLLIF 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
823-996 |
1.52e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 49.29 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 823 DVPVEMKG--QGYNEKKLqlLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGFLKVqetfarvs 900
Cdd:COG0488 313 KKVLELEGlsKSYGDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEP--DSGTVKLGETVKI-------- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 901 GYCEQtdiHSPSITVEESLIysAWLRlvpEINPQTKIRFVKQVLETIeL---EEIkDALVGVagvsgLSTEQRKRLTVAV 977
Cdd:COG0488 381 GYFDQ---HQEELDPDKTVL--DELR---DGAPGGTEQEVRGYLGRF-LfsgDDA-FKPVGV-----LSGGEKARLALAK 445
|
170
....*....|....*....
gi 15228112 978 ELVANPSIIFMDEPTTGLD 996
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLD 464
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
849-1050 |
1.57e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 849 RPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIEgeirisgFLKVQETFARVSGYCEQ--TDIHSP-SITVEESLIYSA 923
Cdd:PRK10982 22 RPHSIHALMGENGAGKSTLLKCLFGiyQKDSGSIL-------FQGKEIDFKSSKEALENgiSMVHQElNLVLQRSVMDNM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 924 WLRLVPeinpqTKIRFVKQVLETIELEEIKDAL-VGV---AGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARA 999
Cdd:PRK10982 95 WLGRYP-----TKGMFVDQDKMYRDTKAIFDELdIDIdprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15228112 1000 AAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLkRGGRMIYSGPL 1050
Cdd:PRK10982 170 VNHLFTIIRKLKERGCGIVYISHKME-EIFQLCDEITIL-RDGQWIATQPL 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
146-400 |
1.61e-05 |
|
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: 47.96 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 146 RTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNGHGLNEVVP------QKTSAYIS 219
Cdd:cd03258 12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LERPTS--GSVLVDGTDLTLLSGkelrkaRRRIGMIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 220 QHDLHIAEMTTRETIDFSarcqgvgsrtdimMEVSKREKDggiipdpEIDaymkaisvkglKRSLQTdyiLKILGLDICA 299
Cdd:cd03258 89 QHFNLLSSRTVFENVALP-------------LEIAGVPKA-------EIE-----------ERVLEL---LELVGLEDKA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 300 ETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFV-----SLLQpape 374
Cdd:cd03258 135 DAYPAQ-----LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLithemEVVK---- 205
|
250 260
....*....|....*....|....*.
gi 15228112 375 syDLFDDIVLMAEGKIVYHGPRDDVL 400
Cdd:cd03258 206 --RICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
155-428 |
1.90e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.59 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 155 LTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlkcYGEISynghglnEVVPQKTSAYISQHDLhIAEMTTRETI 234
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS-----HAETS-------SVVIRGSVAYVPQVSW-IFNATVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 235 DFSArcqgvgsrtdimmevskrekdggiipDPEIDAYMKAISVKGLKRSLQTdyilkILGLDIcaeTLVGnamKRG--IS 312
Cdd:PLN03232 700 LFGS--------------------------DFESERYWRAIDVTALQHDLDL-----LPGRDL---TEIG---ERGvnIS 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 313 GGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVS-LLQPAPesydLFDDIVLMAEGKIV 391
Cdd:PLN03232 743 GGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTnQLHFLP----LMDRIILVSEGMIK 818
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15228112 392 YHGPRDDVLK---FFEecgfQCPERKGVADFLQEVISKKD 428
Cdd:PLN03232 819 EEGTFAELSKsgsLFK----KLMENAGKMDATQEVNTNDE 854
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
839-1041 |
2.07e-05 |
|
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: 47.47 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 839 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLagrktsgyiegeiriSGFLKVQETFARVSGYC----EQTDIHSPSIT 914
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALL---------------ENFYQPQGGQVLLDGKPisqyEHKYLHSKVSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 915 V-EESLIYSAWLrlvpeinpQTKIRFVkqvLETIELEEIKDALVGV----------------AGVSG--LSTEQRKRLTV 975
Cdd:cd03248 93 VgQEPVLFARSL--------QDNIAYG---LQSCSFECVKEAAQKAhahsfiselasgydteVGEKGsqLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228112 976 AVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETgRTIVCTIHQpsIHIFEAFDELVLLKRG 1041
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHR--LSTVERADQILVLDGG 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
840-1048 |
2.14e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 840 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGrktsgyiEGEIRiSGFLKVQETFARVSgycEQTDIHSPsiTVEESL 919
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS-------QFEIS-EGRVWAERSIAYVP---QQAWIMNA--TVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 920 IYsawlrlvpeINPQTKIRFVKQV----LETiELEEIKDAL---VGVAGVSgLSTEQRKRLTVAVELVANPSIIFMDEPT 992
Cdd:PTZ00243 742 LF---------FDEEDAARLADAVrvsqLEA-DLAQLGGGLeteIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15228112 993 TGLDARAAAIVMRAVKNVAETGRTIVCTIHQpsIHIFEAFDELVLLKRgGRMIYSG 1048
Cdd:PTZ00243 811 SALDAHVGERVVEECFLGALAGKTRVLATHQ--VHVVPRADYVVALGD-GRVEFSG 863
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
165-397 |
2.25e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 47.76 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 165 GRLTLLLGPPGCGKTTLLKALSGNLE---NNLKCYGE-ISYNGHGLNEVvpQKTSAYISQH-DLHIAEMTTRETIDFSAR 239
Cdd:PRK13639 28 GEMVALLGPNGAGKSTLFLHFNGILKptsGEVLIKGEpIKYDKKSLLEV--RKTVGIVFQNpDDQLFAPTVEEDVAFGPL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 240 CQGVGsrtdiMMEVSKREKDGgiipdpeidayMKAISVKGLKrslqtdyilkilgldicaetlvgNAMKRGISGGQKKRL 319
Cdd:PRK13639 106 NLGLS-----KEEVEKRVKEA-----------LKAVGMEGFE-----------------------NKPPHHLSGGQKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 320 TTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHiTNATVFVSllqpaPESYDLF----DDIVLMAEGKIVYHG- 394
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIIS-----THDVDLVpvyaDKVYVMSDGKIIKEGt 220
|
...
gi 15228112 395 PRD 397
Cdd:PRK13639 221 PKE 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
841-1019 |
2.48e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.77 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 841 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYIEGEIRISG----FLKVQETfarvsgycEQTD---IHS--- 910
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGeelqASNIRDT--------ERAGiaiIHQela 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 911 --PSITVEESLIysawlrLVPEINPQTKIRFVKQVLETIE-LEEIKDALVGVAGVSGLSTEQRKRLTVAVELVANPSIIF 987
Cdd:PRK13549 93 lvKELSVLENIF------LGNEITPGGIMDYDAMYLRAQKlLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190
....*....|....*....|....*....|..
gi 15228112 988 MDEPTTGLDARAAAIVMRAVKNVAETGrtIVC 1019
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDLKAHG--IAC 196
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
938-1041 |
2.65e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 47.44 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 938 RFVKQVLETIELEEIKDAlvgvaGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGR-T 1016
Cdd:PRK13648 121 RRVSEALKQVDMLERADY-----EPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiT 195
|
90 100
....*....|....*....|....*..
gi 15228112 1017 IVCTIHQPSihifEAF--DELVLLKRG 1041
Cdd:PRK13648 196 IISITHDLS----EAMeaDHVIVMNKG 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
811-1041 |
2.99e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 47.52 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 811 LTITFQDLNYYVDVPVEMKGQGynekklqlLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIEgeirisg 888
Cdd:PRK13641 1 MSIKFENVDYIYSPGTPMEKKG--------LDNISFELEEGSFVALVGHTGSGKSTLMQHFNAllKPSSGTIT------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 889 flkvqetfarVSGYceqtdihspSITVEESLIYSAWLR----LVPEInPQTKIrFVKQVLETIEL---------EEIKDA 955
Cdd:PRK13641 66 ----------IAGY---------HITPETGNKNLKKLRkkvsLVFQF-PEAQL-FENTVLKDVEFgpknfgfseDEAKEK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 956 LVGVAGVSGLSTE------------QRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQ 1023
Cdd:PRK13641 125 ALKWLKKVGLSEDliskspfelsggQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHN 204
|
250
....*....|....*...
gi 15228112 1024 PSiHIFEAFDELVLLKRG 1041
Cdd:PRK13641 205 MD-DVAEYADDVLVLEHG 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
828-997 |
2.99e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 828 MKGQG--YNEKKlQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGFLKVqetfarvsGYCEQ 905
Cdd:PRK11819 9 MNRVSkvVPPKK-QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE--FEGEARPAPGIKV--------GYLPQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 906 TDIHSPSITV----EESL--IYSAWLRLvPEIN-----PQTKirFVKQVLETIELEEIKDALVGV--------------- 959
Cdd:PRK11819 78 EPQLDPEKTVrenvEEGVaeVKAALDRF-NEIYaayaePDAD--FDALAAEQGELQEIIDAADAWdldsqleiamdalrc 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15228112 960 ----AGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDA 997
Cdd:PRK11819 155 ppwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 196
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
813-1041 |
3.55e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 48.18 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 813 ITFQDLNYyvdvpvemkgqGY-NEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSG----------- 878
Cdd:TIGR00958 479 IEFQDVSF-----------SYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNlyQPTGGqvlldgvplvq 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 879 ----YIEGEIRISGflkvQE--TFARvsgyceqtdihspsiTVEESLIYSAWLRLVPEINPQTKIRFVKQVLEtiELEEI 952
Cdd:TIGR00958 548 ydhhYLHRQVALVG----QEpvLFSG---------------SVRENIAYGLTDTPDEEIMAAAKAANAHDFIM--EFPNG 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 953 KDALVGVAGvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKnvaETGRTIVCTIHQpsIHIFEAF 1032
Cdd:TIGR00958 607 YDTEVGEKG-SQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS---RASRTVLLIAHR--LSTVERA 680
|
....*....
gi 15228112 1033 DELVLLKRG 1041
Cdd:TIGR00958 681 DQILVLKKG 689
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
851-1022 |
3.72e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 47.91 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 851 GVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGF-LKVQETFARVSGYCEQTDIHSPSITVEESLIYSAWLRLVP 929
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAGFEQP--TAGQIMLDGVdLSHVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 930 --EINPQtkirfVKQVLETIELEEIKDalvgvAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAV 1007
Cdd:PRK11607 123 kaEIASR-----VNEMLGLVHMQEFAK-----RKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEV 192
|
170
....*....|....*.
gi 15228112 1008 KNVAE-TGRTIVCTIH 1022
Cdd:PRK11607 193 VDILErVGVTCVMVTH 208
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
153-190 |
3.83e-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: 45.13 E-value: 3.83e-05
10 20 30
....*....|....*....|....*....|....*...
gi 15228112 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLE 190
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELE 51
|
|
| SpoIIIAA |
COG3854 |
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome ... |
72-250 |
4.14e-05 |
|
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443063 Cd Length: 309 Bit Score: 47.07 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 72 IEKLIKHIENDNLKLLKKIRRRMERV-------GVEFPS--IEVRYEHLgvEAACEVVEGKALPTLWNSLKHVFLDLlkl 142
Cdd:COG3854 13 IREALEKLPDPVLDKLEEIRLRLGRPlelrfpgGEYFLSeaYPVTREDL--ERTLNRISNYSLYALEEELRQGYITI--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 143 SG---------VRTNEANIKILTDVSG-------------------IISPGRL--TLLLGPPGCGKTTLLKALSGNLENN 192
Cdd:COG3854 88 PGghrvgiagtVVRESGIVKRIKDISGlniriarevkgtadpilpyIISGGRIynTLIISPPGCGKTTLLRDIARVLSDG 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228112 193 LKCY-----------GEI--SYNGhglnevVPqktsayisQHDlhiaemttretidfsarcqgVGSRTDIM 250
Cdd:COG3854 168 LLGFpgkrvgvvderSEIagCYGG------IP--------QPD--------------------IGIRTDVL 204
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
138-394 |
4.26e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.07 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 138 DLLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGhglnEVVPQktsay 217
Cdd:PRK11831 6 NLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD---HGEILFDG----ENIPA----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 218 ISQHDLHiaemTTRETIDFSARCQGVGSRTDIMMEVSKREKDGGIIPDPEIDA--YMKaisvkglkrslqtdyiLKILGL 295
Cdd:PRK11831 74 MSRSRLY----TVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHStvMMK----------------LEAVGL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 296 DICAetlvgNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNAT-VFVSllQPAPE 374
Cdd:PRK11831 134 RGAA-----KLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTcVVVS--HDVPE 206
|
250 260
....*....|....*....|
gi 15228112 375 SYDLFDDIVLMAEGKIVYHG 394
Cdd:PRK11831 207 VLSIADHAYIVADKKIVAHG 226
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
162-401 |
4.68e-05 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 48.02 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 162 ISPGRLTLLLGPPGCGKTTLLKALSGnlennlkCY----GEISYNGHGLNEVVPQKTSAYIS--QHDLHIAEMTTRETI- 234
Cdd:TIGR03796 502 LQPGQRVALVGGSGSGKSTIAKLVAG-------LYqpwsGEILFDGIPREEIPREVLANSVAmvDQDIFLFEGTVRDNLt 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 235 --DFSarcqgvgsrtdimmevskrekdggiIPDPEIdaymkaisVKGLKRSLQTDYILKILG-LDicAETLVGNamkRGI 311
Cdd:TIGR03796 575 lwDPT-------------------------IPDADL--------VRACKDAAIHDVITSRPGgYD--AELAEGG---ANL 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 312 SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQ-------VAH----ITNAtvfvsllqpapesydlfD 380
Cdd:TIGR03796 617 SGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRRrgctciiVAHrlstIRDC-----------------D 679
|
250 260
....*....|....*....|.
gi 15228112 381 DIVLMAEGKIVYHGPRDDVLK 401
Cdd:TIGR03796 680 EIIVLERGKVVQRGTHEELWA 700
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
835-1026 |
4.69e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.80 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 835 EKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLagrktsGYIE----GEIRISGFLKVQ---ETFARVS----GYC 903
Cdd:PRK10535 18 EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL------GCLDkptsGTYRVAGQDVATldaDALAQLRrehfGFI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 904 EQTDIHSPSIT----VEESLIYSAwlrlvpeinpqtkirfvkqvLETIELEEIKDALVGVAGV--------SGLSTEQRK 971
Cdd:PRK10535 92 FQRYHLLSHLTaaqnVEVPAVYAG--------------------LERKQRLLRAQELLQRLGLedrveyqpSQLSGGQQQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15228112 972 RLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSI 1026
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQV 206
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
310-394 |
4.75e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 47.15 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 310 GISGGQKKRLTTAEMIVGPTKALFMDEITNGLD---SSTAFQIIKSLQQvahiTNATVFVsLLQPAPESYDLFDDIVLMA 386
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgEHEMMQLILDAKA----NNKTVFV-ITHTMEHVLEVADEVIVMD 250
|
....*...
gi 15228112 387 EGKIVYHG 394
Cdd:PRK13631 251 KGKILKTG 258
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
833-1048 |
5.06e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.00 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 833 YNEK---KLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGR--KTSGYIEGEIRISGFLKVQETFARVSgyceqtd 907
Cdd:PRK13651 12 FNKKlptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllPDTGTIEWIFKDEKNKKKTKEKEKVL------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 908 ihspsITVEESLIYSAWLRLVPEINPQTKIRFV---KQVLE-TIEleeiKDALVGVA--GVS------------------ 963
Cdd:PRK13651 85 -----EKLVIQKTRFKKIKKIKEIRRRVGVVFQfaeYQLFEqTIE----KDIIFGPVsmGVSkeeakkraakyielvgld 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 964 ---------GLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEaFDE 1034
Cdd:PRK13651 156 esylqrspfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD-NVLE-WTK 233
|
250
....*....|....
gi 15228112 1035 LVLLKRGGRMIYSG 1048
Cdd:PRK13651 234 RTIFFKDGKIIKDG 247
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
140-408 |
5.07e-05 |
|
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: 45.98 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlkcY----GEISYNGHGLNEvvpqkts 215
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPK-----YevteGEILFKGEDITD------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 216 ayisqhdlhiAEMTTRetidfsARCqGVGsrtdIMMEVSkrekdggiipdPEIDaymkAISVKGLKRSLqtdyilkilgl 295
Cdd:cd03217 69 ----------LPPEER------ARL-GIF----LAFQYP-----------PEIP----GVKNADFLRYV----------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 296 dicaetlvgNAmkrGISGGQKKRLTTAEMIV-GPTKALFmDEITNGLDsSTAFQII-KSLQQVAHITNATVFVSLLQpap 373
Cdd:cd03217 102 ---------NE---GFSGGEKKRNEILQLLLlEPDLAIL-DEPDSGLD-IDALRLVaEVINKLREEGKSVLIITHYQ--- 164
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15228112 374 esyDLFDDIV-----LMAEGKIVYHGPRdDVLKFFEECGF 408
Cdd:cd03217 165 ---RLLDYIKpdrvhVLYDGRIVKSGDK-ELALEIEKKGY 200
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
826-1045 |
5.86e-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: 47.51 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 826 VEMKGQGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYIEGEIRISGF-LK---VQETFARVSG 901
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSpLKasnIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 902 YCEQTDIHSPSITVEESLIYSAWLRLVPEI-NPQTKIRFVKQVLETIELEEIKDALvgvaGVSGLSTEQRKRLTVAVELV 980
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLPGGRmAYNAMYLRAKNLLRELQLDADNVTR----PVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228112 981 ANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGrtIVCTIHQPSIHIFEAFDELVLLKRGGRMI 1045
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHG--VACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
850-1022 |
6.65e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 45.61 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 850 PGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGFLKVQETFARVSGYCEQTDIHSPSITVEESLIYSAWLR-LV 928
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVE--SGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHgRR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 929 PEINPQTKIrfvkqvletieleeikdALVGVAG-----VSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIV 1003
Cdd:PRK13543 114 AKQMPGSAL-----------------AIVGLAGyedtlVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLV 176
|
170
....*....|....*....
gi 15228112 1004 MRAVKNVAETGRTIVCTIH 1022
Cdd:PRK13543 177 NRMISAHLRGGGAALVTTH 195
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
1022-1076 |
7.55e-05 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 46.82 E-value: 7.55e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 15228112 1022 HQPSIHIFEAFDELVLLKRGGRMIYSGPLGQhsscVIEYFQNIpGVaKIRDKYNP 1076
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLTVYHGPVKK----VEEYFAGL-GI-NVPERVNP 49
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
145-189 |
8.09e-05 |
|
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: 44.90 E-value: 8.09e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 15228112 145 VRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNL 189
Cdd:cd03246 8 FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLL 52
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
140-394 |
8.60e-05 |
|
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: 45.35 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEVVPQKTsAYIS 219
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD---SGEVLFDGKPLDIAARNRI-GYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 220 QHDLHIAEMTTRETIDFSARCQGVgSRTDIMmevskrekdggiipdPEIDAYmkaisvkgLKRSLQTDYILKILgldica 299
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGL-KKEEAR---------------RRIDEW--------LERLELSEYANKRV------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 300 ETLvgnamkrgiSGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAfQIIKSLQQVAHITNATVFVSLLQPApESYDLF 379
Cdd:cd03269 127 EEL---------SKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNV-ELLKDVIRELARAGKTVILSTHQME-LVEELC 195
|
250
....*....|....*
gi 15228112 380 DDIVLMAEGKIVYHG 394
Cdd:cd03269 196 DRVLLLNKGRAVLYG 210
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
626-697 |
1.03e-04 |
|
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: 1.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15228112 626 FMILFAVHFTSISMFrcIAAIFQTGVAAMTAGSFVMLITFVFAGFAIPYTDMPGWLKWGFWVNPISYAEIGL 697
Cdd:pfam12698 244 LFLLYGLAYIALGYL--LGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGL 313
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
839-996 |
1.04e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 45.49 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 839 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIE--GEIRIsgflkvqetfarvsGYCEQTDIHSPSIt 914
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGlvAPDEGVIKrnGKLRI--------------GYVPQKLYLDTTL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 915 veeSLIYSAWLRLvpeiNPQTKIRFVKQVLETIELEEIKDalvgvAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTG 994
Cdd:PRK09544 83 ---PLTVNRFLRL----RPGTKKEDILPALKRVQAGHLID-----APMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
..
gi 15228112 995 LD 996
Cdd:PRK09544 151 VD 152
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
164-189 |
1.15e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.90 E-value: 1.15e-04
10 20
....*....|....*....|....*.
gi 15228112 164 PGRLTLLLGPPGCGKTTLLKALSGNL 189
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAREL 26
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
311-412 |
1.19e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 45.81 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 311 ISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQI---IKSLQQVAHITnaTVFVSllqpapESYD----LFDDIV 383
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEIlnkIKELHKEYNMT--IILVS------HSMEdvakLADRII 216
|
90 100 110
....*....|....*....|....*....|..
gi 15228112 384 LMAEGKIVYHGPRDDVLK---FFEECGFQCPE 412
Cdd:PRK13637 217 VMNKGKCELQGTPREVFKeveTLESIGLAVPQ 248
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
839-1041 |
1.23e-04 |
|
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: 44.71 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 839 QLLSEITGAFRPGVLTALMGISGAGKTTLldVLAGRKTSGYIEGEIRISGflkvqetfarvsgyceqTDIhspsitveeS 918
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTL--ILALFRFLEAEEGKIEIDG-----------------IDI---------S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 919 LIYSAWLRLVPEINPQTKIRFVKQVLETIEL------EEIKDALVGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPT 992
Cdd:cd03369 74 TIPLEDLRSSLTIIPQDPTLFSGTIRSNLDPfdeysdEEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15228112 993 TGLDARAAAIVMRAVKNVAeTGRTIVCTIHQpsIHIFEAFDELVLLKRG 1041
Cdd:cd03369 154 ASIDYATDALIQKTIREEF-TNSTILTIAHR--LRTIIDYDKILVMDAG 199
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
124-342 |
1.40e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 45.98 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 124 ALPTLWNSLKHVFLDLLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNG 203
Cdd:PRK11607 4 AIPRPQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG-FEQPTA--GQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 204 HGLNEVVP-QKTSAYISQHDLHIAEMTTRETIDFSArcqgvgsrtdimmevsKREKdggiIPDPEIdaymkaisvkglkr 282
Cdd:PRK11607 81 VDLSHVPPyQRPINMMFQSYALFPHMTVEQNIAFGL----------------KQDK----LPKAEI-------------- 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 283 slqTDYILKILGLDICAEtlVGNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLD 342
Cdd:PRK11607 127 ---ASRVNEMLGLVHMQE--FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
153-204 |
1.43e-04 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 45.03 E-value: 1.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15228112 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALsgN----LENNLKCYGEISYNGH 204
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCL--NrmndLIPGARVEGEILLDGE 78
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
154-342 |
1.71e-04 |
|
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: 44.27 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNGHGLNEV--VPQKTSAYISQHDLHIAEMTTR 231
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAG-LLRPDS--GEVRWNGTPLAEQrdEPHENILYLGHLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 232 ETIDFSARCQGVGSRTdimmevskrekdggiipdpeIDAYMKAISVKGLKrslqtdyilkilglDICAETLvgnamkrgi 311
Cdd:TIGR01189 92 ENLHFWAAIHGGAQRT--------------------IEDALAAVGLTGFE--------------DLPAAQL--------- 128
|
170 180 190
....*....|....*....|....*....|.
gi 15228112 312 SGGQKKRLTTAEMIVGPTKALFMDEITNGLD 342
Cdd:TIGR01189 129 SAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
139-389 |
1.75e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 139 LLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlKCYGEISYNGHGLNEVVP---QKTS 215
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYT---RDAGSILYLGKEVTFNGPkssQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 216 AYISQHDLH-IAEMTTRETIdFSARcqgvgsrtdimmevskrekdggiipdpEIDAYMKAISVKGLKRslQTDYILKILG 294
Cdd:PRK10762 81 IGIIHQELNlIPQLTIAENI-FLGR---------------------------EFVNRFGRIDWKKMYA--EADKLLARLN 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 295 LDICAETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGL-DSSTA--FQIIKSLQQVAHitnATVFVS-LLQ 370
Cdd:PRK10762 131 LRFSSDKLVGE-----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETEslFRVIRELKSQGR---GIVYIShRLK 202
|
250
....*....|....*....
gi 15228112 371 papESYDLFDDIVLMAEGK 389
Cdd:PRK10762 203 ---EIFEICDDVTVFRDGQ 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
139-398 |
1.83e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.81 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 139 LLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEVVPQKTSAY- 217
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD---SGTLEIGGNPCARLTPAKAHQLg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 218 ---ISQHDLHIAEMTTRETIDFS-ARCQGVGSR-TDIMMEVSKrekdggiipdpEIDAYMKAISvkglkrslqtdyilki 292
Cdd:PRK15439 88 iylVPQEPLLFPNLSVKENILFGlPKRQASMQKmKQLLAALGC-----------QLDLDSSAGS---------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 293 lgLDICAETLVgnAMKRGisggqkkrlttaemIVGPTKALFMDEITNGL---DSSTAFQIIKSLQQVAHitnATVFVSll 369
Cdd:PRK15439 141 --LEVADRQIV--EILRG--------------LMRDSRILILDEPTASLtpaETERLFSRIRELLAQGV---GIVFIS-- 197
|
250 260
....*....|....*....|....*....
gi 15228112 370 QPAPESYDLFDDIVLMAEGKIVYHGPRDD 398
Cdd:PRK15439 198 HKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
154-187 |
1.95e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 45.95 E-value: 1.95e-04
10 20 30
....*....|....*....|....*....|....
gi 15228112 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSG 187
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG 411
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
153-433 |
2.05e-04 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 45.56 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKCYGEISYNGHGLNEVVPQKTSAYISQHDLHIAEMTTRE 232
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRG-MDQYEPTSGRIIYHVALCEKCGYVERPSKVGEPCPVCGGTLEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 233 TIDF----SARCQGVGSRTDIMMEVSKREKDGGIIPDPEIDAyMKAISVKGlKRSLQtdyilkiLGLDICAETLVGNAM- 307
Cdd:TIGR03269 93 EVDFwnlsDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEA-LEEIGYEG-KEAVG-------RAVDLIEMVQLSHRIt 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 308 --KRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSLLQPAPESyDLFDDIVLM 385
Cdd:TIGR03269 164 hiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIE-DLSDKAIWL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15228112 386 AEGKIVYHGPRDDVLKFFEEcGFQCPERKGVADFLQEVISKKDQGQYW 433
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVAVFME-GVSEVEKECEVEVGEPIIKVRNVSKRY 289
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
827-996 |
2.29e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 44.32 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 827 EMKGQGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYI--EGEiRISGfLKVQETFARVSgY 902
Cdd:PRK10247 9 QLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASliSPTSGTLlfEGE-DIST-LKPEIYRQQVS-Y 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 903 CEQTdihsPSI---TVEESLIYSAWLRlvpEINPQTKiRFVKQvLETIEL-EEIKDalvgvAGVSGLSTEQRKRLTVAVE 978
Cdd:PRK10247 86 CAQT----PTLfgdTVYDNLIFPWQIR---NQQPDPA-IFLDD-LERFALpDTILT-----KNIAELSGGEKQRISLIRN 151
|
170
....*....|....*...
gi 15228112 979 LVANPSIIFMDEPTTGLD 996
Cdd:PRK10247 152 LQFMPKVLLLDEITSALD 169
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
155-401 |
2.76e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 44.15 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 155 LTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcyGEISYNGHGLNEVVPQKTS---AYISQHdlhiaemttr 231
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS----GSIQFAGQPLEAWSAAELArhrAYLSQQ---------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 232 etidfsarcqgvgSRTDIMMEV----SKREKDGGIIPDPEIDAYMKAISVK---GLKRSLQTdyilkilgldicaetlvg 304
Cdd:PRK03695 78 -------------QTPPFAMPVfqylTLHQPDKTRTEAVASALNEVAEALGlddKLGRSVNQ------------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 305 namkrgISGG--QKKRLTTAEMIVGPT-----KALFMDEITNGLD---SSTAFQIIKSLQQV-------AHITNATvfvs 367
Cdd:PRK03695 127 ------LSGGewQRVRLAAVVLQVWPDinpagQLLLLDEPMNSLDvaqQAALDRLLSELCQQgiavvmsSHDLNHT---- 196
|
250 260 270
....*....|....*....|....*....|....
gi 15228112 368 lLQPApesydlfDDIVLMAEGKIVYHGPRDDVLK 401
Cdd:PRK03695 197 -LRHA-------DRVWLLKQGKLLASGRRDEVLT 222
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
954-1010 |
2.93e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 2.93e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 15228112 954 DALVGvAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNV 1010
Cdd:PTZ00265 570 ETLVG-SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
140-394 |
3.16e-04 |
|
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: 43.64 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 140 LKLSGVRTNEANIKILTDVSgiISPGRLTLLLGPPGCGKTTLLKALSGNLennLKCYGEISYNG--HGLNEVVPQKTSAY 217
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLT--FAQGEITAIVGPSGSGKSTLLNLIAGFE---TPQSGRVLINGvdVTAAPPADRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 218 ISQHDLhIAEMTTRETIDFsarcqgvgsrtdimmevskrekdgGIIPdpeidaymkaisvkGLK-RSLQTDYILKILgld 296
Cdd:cd03298 76 FQENNL-FAHLTVEQNVGL------------------------GLSP--------------GLKlTAEDRQAIEVAL--- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 297 icAETLVGNAMKR---GISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSLLQPAp 373
Cdd:cd03298 114 --ARVGLAGLEKRlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPE- 190
|
250 260
....*....|....*....|.
gi 15228112 374 ESYDLFDDIVLMAEGKIVYHG 394
Cdd:cd03298 191 DAKRLAQRVVFLDNGRIAAQG 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
837-1018 |
3.20e-04 |
|
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: 45.20 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 837 KLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGrKTSGYIEGEIRISGflkvqetfarvsgycEQTDIHSPSITVE 916
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKFEGNVFING---------------KPVDIRNPAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 917 ESLIysawlrLVPE------INPQ------------TKIRFVKQVLETIELEEIKDAL----VGVAG----VSGLSTEQR 970
Cdd:TIGR02633 336 AGIA------MVPEdrkrhgIVPIlgvgknitlsvlKSFCFKMRIDAAAELQIIGSAIqrlkVKTASpflpIGRLSGGNQ 409
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15228112 971 KRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIV 1018
Cdd:TIGR02633 410 QKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAII 457
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
153-398 |
3.76e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.15 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLennlkcygEISyngHGlnEVVPQKTSAYISQHDLhIAEMTTRE 232
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQF--------EIS---EG--RVWAERSIAYVPQQAW-IMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 233 TIDFSarcqgvgsrtdimmevskrekdggiipDPEIDAYM-KAISVKGLKRSLQTdyilkilgLDICAETLVGnamKRGI 311
Cdd:PTZ00243 740 NILFF---------------------------DEEDAARLaDAVRVSQLEADLAQ--------LGGGLETEIG---EKGV 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 312 --SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKS--LQQVAHITN--ATVFVSLLQPApesydlfDDIVLM 385
Cdd:PTZ00243 782 nlSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEEcfLGALAGKTRvlATHQVHVVPRA-------DYVVAL 854
|
250
....*....|...
gi 15228112 386 AEGKIVYHGPRDD 398
Cdd:PTZ00243 855 GDGRVEFSGSSAD 867
|
|
| RecA-like_CDC48_r2-like |
cd19511 |
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ... |
162-188 |
4.44e-04 |
|
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410919 [Multi-domain] Cd Length: 159 Bit Score: 42.27 E-value: 4.44e-04
10 20
....*....|....*....|....*..
gi 15228112 162 ISPGRLTLLLGPPGCGKTTLLKALSGN 188
Cdd:cd19511 24 IRPPKGVLLYGPPGCGKTLLAKALASE 50
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
811-1049 |
5.00e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 43.88 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 811 LTITFQDLNYyvdvpVEMKGQGYNEKKLQLLS-EI-TGAFrpgvlTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRI 886
Cdd:PRK13637 1 MSIKIENLTH-----IYMEGTPFEKKALDNVNiEIeDGEF-----VGLIGHTGSGKSTLIQHLNGllKPTSG----KIII 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 887 SGF------LKVQETFARVsGYCEQTdihsPSITVEESLIYS--AW----LRLVPEinpQTKIRfVKQVLETIEL--EEI 952
Cdd:PRK13637 67 DGVditdkkVKLSDIRKKV-GLVFQY----PEYQLFEETIEKdiAFgpinLGLSEE---EIENR-VKRAMNIVGLdyEDY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 953 KDAlvgvaGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNV-AETGRTIVCTIHqpSIHIFEA 1031
Cdd:PRK13637 138 KDK-----SPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSH--SMEDVAK 210
|
250
....*....|....*...
gi 15228112 1032 FDELVLLKRGGRMIYSGP 1049
Cdd:PRK13637 211 LADRIIVMNKGKCELQGT 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
157-400 |
5.75e-04 |
|
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: 43.94 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 157 DVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNGH-------GLNEVVPQKTSAYISQHDLHIAEMT 229
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAG-LERPDS--GRIRLGGEvlqdsarGIFLPPHRRRIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 230 TRETIDFSARcqgvgsRTdimmevskrekdggiipdpeidaymkaisvKGLKRSLQTDYILKILGLdicaETLvgnaMKR 309
Cdd:COG4148 94 VRGNLLYGRK------RA------------------------------PRAERRISFDEVVELLGI----GHL----LDR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 310 GI---SGGQKKR-------LTtaemivGPtKALFMDEITNGLDSSTAFQIIKSLQQVAH-----ItnatVFVSllqpapE 374
Cdd:COG4148 130 RPatlSGGERQRvaigralLS------SP-RLLLMDEPLAALDLARKAEILPYLERLRDeldipI----LYVS------H 192
|
250 260 270
....*....|....*....|....*....|
gi 15228112 375 SYD----LFDDIVLMAEGKIVYHGPRDDVL 400
Cdd:COG4148 193 SLDevarLADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
370-413 |
5.75e-04 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 44.13 E-value: 5.75e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 15228112 370 QPapeSYDL---FDDIVLMAEG-KIVYHGPRDDVLKFFEECGFQCPER 413
Cdd:pfam19055 2 QP---SYTLfkmFDDLILLAKGgLTVYHGPVKKVEEYFAGLGINVPER 46
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
71-182 |
5.90e-04 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 43.70 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 71 MIEKLIKHIENDNLKL---LKKIRRRMERVGVEfpsievryEHLGVEAACEVVEGKALPTLWNSLKHVFLDLLKlsgvrt 147
Cdd:COG1419 89 LLEEQLSGLAGESARLppeLAELLERLLEAGVS--------PELARELLEKLPEDLSAEEAWRALLEALARRLP------ 154
|
90 100 110
....*....|....*....|....*....|....*
gi 15228112 148 neanikilTDVSGIISPGRLTLLLGPPGCGKTTLL 182
Cdd:COG1419 155 --------VAEDPLLDEGGVIALVGPTGVGKTTTI 181
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
832-1018 |
5.90e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.00 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 832 GYNEKKLQllsEITGAFRPGVLTALMGISGAGKTTLLDVLAGrkTSGYIEGEIRISG--------FLKVQETFA------ 897
Cdd:PRK09700 273 SRDRKKVR---DISFSVCRGEILGFAGLVGSGRTELMNCLFG--VDKRAGGEIRLNGkdisprspLDAVKKGMAyitesr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 898 RVSGYCEQTDIhSPSITVEESLIYSAWLRLVPEINPQTKIRFVKQvleTIELEEIKDALVGvAGVSGLSTEQRKRLTVAV 977
Cdd:PRK09700 348 RDNGFFPNFSI-AQNMAISRSLKDGGYKGAMGLFHEVDEQRTAEN---QRELLALKCHSVN-QNITELSGGNQQKVLISK 422
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15228112 978 ELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIV 1018
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVIL 463
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
835-1045 |
6.58e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 43.16 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 835 EKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGFLKVQETF----ARVSGYCEQTDIHS 910
Cdd:PRK13642 17 ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE--FEGKVKIDGELLTAENVwnlrRKIGMVFQNPDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 911 PSITVEESLIYSAWLRLVPEinpQTKIRFVKQVLETIELEEIKdalvgVAGVSGLSTEQRKRLTVAVELVANPSIIFMDE 990
Cdd:PRK13642 95 VGATVEDDVAFGMENQGIPR---EEMIKRVDEALLAVNMLDFK-----TREPARLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15228112 991 PTTGLDARAAAIVMRAVKNVAETGRTIVCTIhqpsIHIFE--AFDELVLLKRGGRMI 1045
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIHEIKEKYQLTVLSI----THDLDeaASSDRILVMKAGEII 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
950-1046 |
6.72e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 43.23 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 950 EEIKDALvGVAGVSgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETgRTIVCTIH---QPS- 1025
Cdd:PRK14243 139 DEVKDKL-KQSGLS-LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHnmqQAAr 215
|
90 100
....*....|....*....|.
gi 15228112 1026 IHIFEAFDELVLLKRGGRMIY 1046
Cdd:PRK14243 216 VSDMTAFFNVELTEGGGRYGY 236
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
840-996 |
6.99e-04 |
|
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: 44.52 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 840 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGflkvqetfaRVSgYCEQTDIHSPSiTVEESL 919
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPS--EGKIKHSG---------RIS-FSPQTSWIMPG-TIKDNI 507
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15228112 920 IYSawlrLVPEINPQTKIRFVKQVLETIELEEIKDALVGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLD 996
Cdd:TIGR01271 508 IFG----LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
150-187 |
7.73e-04 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 41.76 E-value: 7.73e-04
10 20 30
....*....|....*....|....*....|....*...
gi 15228112 150 ANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSG 187
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG 49
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
119-367 |
7.73e-04 |
|
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: 44.13 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 119 VVEGKALPTLWNSLKHVFLDLLKlsgVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcyGE 198
Cdd:TIGR01271 1202 VIENPHAQKCWPSGGQMDVQGLT---AKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE----GE 1274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 199 ISYNGHGLNEVVPQ---KTSAYISQhDLHIAEMTTRETIDFSARCQgvgsrtdimmevskrekdggiipDPEIDAYMKAI 275
Cdd:TIGR01271 1275 IQIDGVSWNSVTLQtwrKAFGVIPQ-KVFIFSGTFRKNLDPYEQWS-----------------------DEEIWKVAEEV 1330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 276 SVKGLKRSL--QTDYILKILGLDicaetlvgnamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTaFQII-KS 352
Cdd:TIGR01271 1331 GLKSVIEQFpdKLDFVLVDGGYV--------------LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVT-LQIIrKT 1395
|
250
....*....|....*
gi 15228112 353 LQQVahITNATVFVS 367
Cdd:TIGR01271 1396 LKQS--FSNCTVILS 1408
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
841-1041 |
7.92e-04 |
|
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: 42.48 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 841 LSEITGAFRPGVLTALMGISGAGKTTLldVLAGRKTSGYIEGEIRISGFLkvqetfarvsgyCEQTDIH----SPSITVE 916
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSL--LLALFRLVELSSGSILIDGVD------------ISKIGLHdlrsRISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 917 ESLIYSAWLR--LVP-------EINpqtkirfvkQVLETIELEEIKDALVG------VAGVSGLSTEQRKRLTVAVELVA 981
Cdd:cd03244 86 DPVLFSGTIRsnLDPfgeysdeELW---------QALERVGLKEFVESLPGgldtvvEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 982 NPSIIFMDEPTTGLDARAAAIVMRAVKNvAETGRTIVCTIHQpsIHIFEAFDELVLLKRG 1041
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHR--LDTIIDSDRILVLDKG 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
140-187 |
8.05e-04 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 41.65 E-value: 8.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 15228112 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSG 187
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSG 48
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
154-397 |
9.57e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 43.55 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlKCYGEISYNGHGLnevvpqktsayisqHDLHIAEMTTRet 233
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFD---VSEGDIRFHDIPL--------------TKLQLDSWRSR-- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 234 idfsarcQGVGSRTDIMMEVSKrekdGGIIPDPEIDAYMKAISVKGLKRSLQTDyilkILGLDICAETLVGnamKRGI-- 311
Cdd:PRK10789 391 -------LAVVSQTPFLFSDTV----ANNIALGRPDATQQEIEHVARLASVHDD----ILRLPQGYDTEVG---ERGVml 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 312 SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHitNATVFV-----SLLQPApesydlfDDIVLMA 386
Cdd:PRK10789 453 SGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIIsahrlSALTEA-------SEILVMQ 523
|
250
....*....|.
gi 15228112 387 EGKIVYHGPRD 397
Cdd:PRK10789 524 HGHIAQRGNHD 534
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
771-996 |
9.93e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 771 QDKLSELQGTKD---SSVKKNKPLDSSIKTNEDPgKMILPF---KPLTITFQDLNYYVDVPVEMK--GQGYNEKKLqlLS 842
Cdd:PRK10636 253 QERVAHLQSYIDrfrAKATKAKQAQSRIKMLERM-ELIAPAhvdNPFHFSFRAPESLPNPLLKMEkvSAGYGDRII--LD 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 843 EITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGFLKVqetfarvsGYCEQTDIHspsitveesliys 922
Cdd:PRK10636 330 SIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAP--VSGEIGLAKGIKL--------GYFAQHQLE------------- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 923 aWLRlVPEINPQTKIRFVKQVLEtielEEIKDALVG-------VAGVSG-LSTEQRKRLTVAVELVANPSIIFMDEPTTG 994
Cdd:PRK10636 387 -FLR-ADESPLQHLARLAPQELE----QKLRDYLGGfgfqgdkVTEETRrFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
..
gi 15228112 995 LD 996
Cdd:PRK10636 461 LD 462
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
933-1041 |
1.05e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.20 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 933 PQTKIRFVKQVLETIELEEIKDALVGVAGVSGLSTEQRKRLTVAVELV--ANPSIIFMDEPTTGLDARAAAIVMRAV--- 1007
Cdd:smart00382 27 GPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALArkLKPDVLILDEITSLLDAEQEALLLLLEelr 106
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15228112 1008 ---KNVAETGRTIVCTIHQPSI----HIFEAFDELVLLKRG 1041
Cdd:smart00382 107 lllLLKSEKNLTVILTTNDEKDlgpaLLRRRFDRRIVLLLI 147
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
161-198 |
1.05e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 1.05e-03
10 20 30
....*....|....*....|....*....|....*...
gi 15228112 161 IISPGRLTLLLGPPGCGKTTLLKALSGNLENNLKCYGE 198
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEE 132
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
93-190 |
1.13e-03 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 42.69 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 93 RMERVGVEFPsiEVRYEHLG-----VEAACEVVEgkaLPtlwnsLKHVflDLLKLSGvrtneanikiltdvsgiISPGRL 167
Cdd:COG1222 64 RGTAVPAESP--DVTFDDIGgldeqIEEIREAVE---LP-----LKNP--ELFRKYG-----------------IEPPKG 114
|
90 100
....*....|....*....|...
gi 15228112 168 TLLLGPPGCGKTTLLKALSGNLE 190
Cdd:COG1222 115 VLLYGPPGTGKTLLAKAVAGELG 137
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
162-189 |
1.30e-03 |
|
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410926 [Multi-domain] Cd Length: 169 Bit Score: 41.24 E-value: 1.30e-03
10 20
....*....|....*....|....*...
gi 15228112 162 ISPGRLTLLLGPPGCGKTTLLKALSGNL 189
Cdd:cd19518 31 VEPPRGVLLHGPPGCGKTMLANAIAGEL 58
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
846-1013 |
1.38e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.87 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 846 GAFRPG-VLTALmGISGAGKTTLLDVLAGR--KTSGYIEGEIRISgfLKVQETFARVSGyceqtdihspsiTVEEsliys 922
Cdd:PRK13409 360 GEIYEGeVIGIV-GPNGIGKTTFAKLLAGVlkPDEGEVDPELKIS--YKPQYIKPDYDG------------TVED----- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 923 aWLRlvpEINPQTKIRFVK-QVLETIELEEIKDALvgvagVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAA 1001
Cdd:PRK13409 420 -LLR---SITDDLGSSYYKsEIIKPLQLERLLDKN-----VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 490
|
170
....*....|..
gi 15228112 1002 IVMRAVKNVAET 1013
Cdd:PRK13409 491 AVAKAIRRIAEE 502
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
162-193 |
1.39e-03 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 42.59 E-value: 1.39e-03
10 20 30
....*....|....*....|....*....|..
gi 15228112 162 ISPGRLTLLLGPPGCGKTTLLKALSGNLENNL 193
Cdd:COG0464 188 LPPPRGLLLYGPPGTGKTLLARALAGELGLPL 219
|
|
| ABC_trans_N |
pfam14510 |
ABC-transporter N-terminal; This domain is found at the N-terminus of ABC-transporter proteins ... |
82-130 |
1.42e-03 |
|
ABC-transporter N-terminal; This domain is found at the N-terminus of ABC-transporter proteins from fungi, plants to higher eukaryotes. It is predicted to be an intracellular domain.
Pssm-ID: 464194 Cd Length: 80 Bit Score: 38.84 E-value: 1.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15228112 82 DNLKLLKKIRRRMERVG-VEFPSIEVRYEHLGVEAAceVVEGKALPTLWN 130
Cdd:pfam14510 32 DLRKWLKNLRRLIDEDGyIKPRKLGVAFKNLTVSGV--GAGADYQPTVGN 79
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
126-435 |
1.68e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 42.38 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 126 PTLWNSLKHVFldllklsgvRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLennlkcY---GEISYN 202
Cdd:COG4586 18 PGLKGALKGLF---------RREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGIL------VptsGEVRVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 203 GHglnevVPQKtsayisqhdlhiaemttrETIDFSARCqGV--GSRT----DImmevskrekdggiipdPEIDAY--MKA 274
Cdd:COG4586 83 GY-----VPFK------------------RRKEFARRI-GVvfGQRSqlwwDL----------------PAIDSFrlLKA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 275 I---SVKGLKRSLqtDYILKILGLDICAETLVgnamkRGISGGQKKR--LTTAeMIVGPtKALFMDEITNGLDSSTAFQI 349
Cdd:COG4586 123 IyriPDAEYKKRL--DELVELLDLGELLDTPV-----RQLSLGQRMRceLAAA-LLHRP-KILFLDEPTIGLDVVSKEAI 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 350 IKSLQQVAHITNATVFVSllqpapeSYDLfDDI-------VLMAEGKIVYHGPRDDVLKFFEecgfqcPERKGVADFLQE 422
Cdd:COG4586 194 REFLKEYNRERGTTILLT-------SHDM-DDIealcdrvIVIDHGRIIYDGSLEELKERFG------PYKTIVLELAEP 259
|
330 340
....*....|....*....|...
gi 15228112 423 V----------ISKKDQGQYWLH 435
Cdd:COG4586 260 VpplelprggeVIEREGNRVRLE 282
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
140-213 |
2.03e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 42.02 E-value: 2.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228112 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLNEVVPQK 213
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD---SGEVLWDGEPLDPEDRRR 72
|
|
| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
155-186 |
2.04e-03 |
|
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410928 [Multi-domain] Cd Length: 166 Bit Score: 40.49 E-value: 2.04e-03
10 20 30
....*....|....*....|....*....|..
gi 15228112 155 LTDVSGIISPGRLTLLLGPPGCGKTTLLKALS 186
Cdd:cd19520 25 LFDNSRLLQPPKGVLLYGPPGCGKTMLAKATA 56
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
840-996 |
2.16e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 41.77 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 840 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGflkvqetfaRVSgYCEQTDIHSPSiTVEESL 919
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPS--EGKIKHSG---------RIS-FSSQFSWIMPG-TIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 920 IYSAwlrlvpeinPQTKIRFvKQVLETIELEEI------KDALVGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTT 993
Cdd:cd03291 119 IFGV---------SYDEYRY-KSVVKACQLEEDitkfpeKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
...
gi 15228112 994 GLD 996
Cdd:cd03291 189 YLD 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
161-193 |
2.16e-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: 2.16e-03
10 20 30
....*....|....*....|....*....|...
gi 15228112 161 IISPGRLTLLLGPPGCGKTTLLKALSGNLENNL 193
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNL 127
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
138-187 |
2.50e-03 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 41.25 E-value: 2.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15228112 138 DLLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSG 187
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLG 52
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
154-401 |
3.19e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 41.13 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNL---ENNLKCYGeISYNGHGLNEVvpQKTSAYISQH-DLHIAEMT 229
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkpqSGEIKIDG-ITISKENLKEI--RKKIGIIFQNpDNQFIGAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 230 TRETIDFSARCQGVgsrtdimmevsKREKDGGIIPDpeidaYMKAISVKG-LKRSLQTdyilkilgldicaetlvgnamk 308
Cdd:PRK13632 101 VEDDIAFGLENKKV-----------PPKKMKDIIDD-----LAKKVGMEDyLDKEPQN---------------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 309 rgISGGQKKRLTTAEMIVGPTKALFMDEITNGLD---SSTAFQIIKSLQQVAHITnatvFVSLLQPAPESYdLFDDIVLM 385
Cdd:PRK13632 143 --LSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgKREIKKIMVDLRKTRKKT----LISITHDMDEAI-LADKVIVF 215
|
250
....*....|....*.
gi 15228112 386 AEGKIVYHGPRDDVLK 401
Cdd:PRK13632 216 SEGKLIAQGKPKEILN 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
152-234 |
3.27e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.82 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 152 IKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnleNNLKCYGEISYNGhglNEVVPQKTSAYISQ------HDLHI 225
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSG---NYQPDAGSILIDG---QEMRFASTTAALAAgvaiiyQELHL 90
|
90
....*....|
gi 15228112 226 A-EMTTRETI 234
Cdd:PRK11288 91 VpEMTVAENL 100
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
312-399 |
3.54e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.26 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 312 SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHiTNATVFVSlLQPAPESYDLFDDIVLMAEGKIV 391
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLT-TQYMEEAEQLAHELTVIDRGRVI 223
|
....*...
gi 15228112 392 YHGPRDDV 399
Cdd:NF000106 224 ADGKVDEL 231
|
|
| RecA-like_Pch2-like |
cd19508 |
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ... |
157-189 |
3.62e-03 |
|
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as Thyroid hormone receptor interactor 13 (TRIP13) and 16E1BP) is a key regulator of specific chromosomal events, like the control of G2/prophase processes such as DNA break formation and recombination, checkpoint signaling, and chromosome synapsis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
Pssm-ID: 410916 [Multi-domain] Cd Length: 199 Bit Score: 40.12 E-value: 3.62e-03
10 20 30
....*....|....*....|....*....|...
gi 15228112 157 DVSGIISPGRLTLLLGPPGCGKTTLLKALSGNL 189
Cdd:cd19508 44 VNTNLITWNRLVLLHGPPGTGKTSLCKALAQKL 76
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
954-1023 |
4.14e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 4.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228112 954 DALVGVAGVSgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETG-RTIVCTIHQ 1023
Cdd:PTZ00265 1349 DTNVGPYGKS-LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHR 1418
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
311-397 |
4.46e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 40.84 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 311 ISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFV--SLLQPAPESydlfDDIVLMAEG 388
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILitHYMEEAVEA----DRIIVMDSG 220
|
90
....*....|
gi 15228112 389 KIVYHG-PRD 397
Cdd:PRK13633 221 KVVMEGtPKE 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
813-996 |
4.57e-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: 38.97 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 813 ITFQDLNYYvdvpvemkgqgYNEKKLqlLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGFLKV 892
Cdd:cd03221 1 IELENLSKT-----------YGGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEP--DEGIVTWGSTVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 893 qetfarvsGYCEQtdihspsitveesliysawlrlvpeinpqtkirfvkqvletieleeikdalvgvagvsgLSTEQRKR 972
Cdd:cd03221 66 --------GYFEQ-----------------------------------------------------------LSGGEKMR 78
|
170 180
....*....|....*....|....
gi 15228112 973 LTVAVELVANPSIIFMDEPTTGLD 996
Cdd:cd03221 79 LALAKLLLENPNLLLLDEPTNHLD 102
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
140-211 |
5.71e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 40.60 E-value: 5.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228112 140 LKLSGVR-TNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKcyGEISYNGHGLNEVVP 211
Cdd:PRK11650 4 LKLQAVRkSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG-LERITS--GEIWIGGRVVNELEP 73
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
163-189 |
5.82e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 40.25 E-value: 5.82e-03
10 20
....*....|....*....|....*..
gi 15228112 163 SPGRLTLLLGPPGCGKTTLLKALSGNL 189
Cdd:COG1223 33 WPPRKILFYGPPGTGKTMLAEALAGEL 59
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
151-207 |
5.91e-03 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 40.04 E-value: 5.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 15228112 151 NIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkcYGEISYNGHGLN 207
Cdd:COG2884 14 GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPT---SGQVLVNGQDLS 67
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
973-1026 |
6.00e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.45 E-value: 6.00e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 15228112 973 LTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSI 1026
Cdd:pfam13304 248 LAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLL 301
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
169-189 |
6.54e-03 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 38.34 E-value: 6.54e-03
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
129-190 |
6.83e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 40.06 E-value: 6.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228112 129 WNSLKHVFLDLLKLSGVRtneanIKILTDVSGIISPGRlTL-LLGPPGCGKTTLLKALSGNLE 190
Cdd:COG1134 21 SRSLKELLLRRRRTRREE-----FWALKDVSFEVERGE-SVgIIGRNGAGKSTLLKLIAGILE 77
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
796-1008 |
7.36e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.61 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 796 KTNEDPGKMILPFKPLTITFQDlnyyvdvpvemkgqgyNEKKLQLLSEITGAFRPGVLTALMGISGAGKT-TLLDVLAGR 874
Cdd:PRK10261 3 HSDELDARDVLAVENLNIAFMQ----------------EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 875 KTSGyieGEIRISGFL-------------KVQETFARVSG------YCEQTDIHSPSITVEESLIYSawLRLVPEINPQT 935
Cdd:PRK10261 67 EQAG---GLVQCDKMLlrrrsrqvielseQSAAQMRHVRGadmamiFQEPMTSLNPVFTVGEQIAES--IRLHQGASREE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228112 936 KIRFVKQVLETIELEEIKDALVGVAgvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVK 1008
Cdd:PRK10261 142 AMVEAKRMLDQVRIPEAQTILSRYP--HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIK 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
940-998 |
7.90e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 7.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228112 940 VKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLD--AR 998
Cdd:NF033858 378 VAEMLERFDLADVADALPD-----SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDpvAR 433
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
169-192 |
8.57e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 38.28 E-value: 8.57e-03
10 20
....*....|....*....|....
gi 15228112 169 LLLGPPGCGKTTLLKALSGNLENN 192
Cdd:cd00009 23 LLYGPPGTGKTTLARAIANELFRP 46
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
280-398 |
8.62e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 40.33 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228112 280 LKRSLQTDYIL-KILGLDicaeTLVGnamKRG--ISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQV 356
Cdd:PRK13657 445 AERAQAHDFIErKPDGYD----TVVG---ERGrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL 517
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15228112 357 AHitNATVFV-----SLLQPApesydlfDDIVLMAEGKIVYHGPRDD 398
Cdd:PRK13657 518 MK--GRTTFIiahrlSTVRNA-------DRILVFDNGRVVESGSFDE 555
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
159-185 |
9.06e-03 |
|
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410917 [Multi-domain] Cd Length: 163 Bit Score: 38.49 E-value: 9.06e-03
10 20
....*....|....*....|....*..
gi 15228112 159 SGIISPGRLTLLLGPPGCGKTTLLKAL 185
Cdd:cd19509 26 PGLRGPPRGILLYGPPGTGKTLLARAV 52
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
160-194 |
9.21e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 39.77 E-value: 9.21e-03
10 20 30
....*....|....*....|....*....|....*
gi 15228112 160 GIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLK 194
Cdd:COG3267 38 ALAQGGGFVVLTGEVGTGKTTLLRRLLERLPDDVK 72
|
|
| |
