|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-1442 |
0e+00 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 1800.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 19 DEAEHALQWAEIQRLPTFKRLRSSLVDKYGEGTEKGK----KVVDVTKLGAMERHLMIEKLIKHIENDNLKLLKKIRRRM 94
Cdd:PLN03140 41 DEDEEALKWAAIEKLPTYSRLRTSIMKSFVENDVYGNqllhKEVDVTKLDGNDRQKFIDMVFKVAEEDNEKFLKKFRNRI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 95 ERVGVEFPSIEVRYEHLGVEAACEVvEGKALPTLWNSLKHVFLDLLKLSGVR-TNEANIKILTDVSGIISPGRLTLLLGP 173
Cdd:PLN03140 121 DRVGIKLPTVEVRFEHLTVEADCYI-GSRALPTLPNAARNIAESALGMLGINlAKKTKLTILKDASGIIKPSRMTLLLGP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 174 PGCGKTTLLKALSGNLENNLKVldifsfgcfllqmcescllffslfyfpqcYGEISYNGHGLNEVVPQKTSAYISQHDLH 253
Cdd:PLN03140 200 PSSGKTTLLLALAGKLDPSLKV-----------------------------SGEITYNGYRLNEFVPRKTSAYISQNDVH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 254 IAEMTTRETIDFSARCQGVGSRTDIMMEVSKREKDGGIIPDPEIDAYMKAISVKGLKRSLQTDYILKILGLDICAETLVG 333
Cdd:PLN03140 251 VGVMTVKETLDFSARCQGVGTRYDLLSELARREKDAGIFPEAEVDLFMKATAMEGVKSSLITDYTLKILGLDICKDTIVG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 334 NAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSLLQPAPESYDLFDDIVL 413
Cdd:PLN03140 331 DEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFDLFDDIIL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 414 MAEGKIVYHGPRDDVLKFFEECGFQCPERKGVADFLQEVISKKDQGQYWLHQNLPHSFVSVDTLSKRFKDLEIGRKIEEA 493
Cdd:PLN03140 411 LSEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKKDQEQYWADRNKPYRYISVSEFAERFKSFHVGMQLENE 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 494 LSKPYDISKTHKDALSFNVYSLPKWELFRACISREFLLMKRNYFVYLFKTFQLVLAAIITMTVFIRTRMDI-DIIHGNSY 572
Cdd:PLN03140 491 LSVPFDKSQSHKAALVFSKYSVPKMELLKACWDKEWLLMKRNAFVYVFKTVQIIIVAAIASTVFLRTEMHTrNEEDGALY 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 573 MSCLFFATVVLLVDGIPELSMTVQRLSVFYKQKQLCFYPAWAYAIPATVLKIPLSFFESLVWTCLTYYVIGYTPEPYRFF 652
Cdd:PLN03140 571 IGALLFSMIINMFNGFAELALMIQRLPVFYKQRDLLFHPPWTFTLPTFLLGIPISIIESVVWVVITYYSIGFAPEASRFF 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 653 RQFMILFAVHFTSISMFRCIAAIFQTGVAAMTAGSFVMLITFVFAGFAIPYTDMPGWLKWGFWVNPISYAEIGLSVNEFL 732
Cdd:PLN03140 651 KQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEWAYWVSPLSYGFNALAVNEMF 730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 733 APRW-QKMQPTNVT-LGRTILESRGLNYDDYMYWVSLSALLGLTIIFNTIFTLALSFLKSPTSSRPMISQDKLSELQGTK 810
Cdd:PLN03140 731 APRWmNKMASDNSTrLGTAVLNIFDVFTDKNWYWIGVGALLGFTILFNVLFTLALTYLNPLGKKQAIISEETAEEMEGEE 810
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 811 DSSVK-----------------------KNKPLDSSIKTNE--DPGK-MILPFKPLTITFQDLNYYVDVPVEMKGQGYNE 864
Cdd:PLN03140 811 DSIPRslssadgnntrevaiqrmsnpegLSKNRDSSLEAANgvAPKRgMVLPFTPLAMSFDDVNYFVDMPAEMKEQGVTE 890
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 865 KKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYIEGEIRISGFLKVQETFARVSGYCEQTDIHSPSITV 944
Cdd:PLN03140 891 DRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTV 970
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 945 EESLIYSAWLRLVPEINPQTKIRFVKQVLETIELEEIKDALVGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGL 1024
Cdd:PLN03140 971 RESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1025 DARAAAIVMRAVKNVAETGRTIVCTIHQPSIHIFEAFDELVLLKRGGRMIYSGPLGQHSSCVIEYFQNIPGVAKIRDKYN 1104
Cdd:PLN03140 1051 DARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYSGPLGRNSHKIIEYFEAIPGVPKIKEKYN 1130
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1105 PATWMLEVTSESVETELDMDFAKIYNESDLYKNNSELVKELSKPDHGSSDLHFKRTFAQNWWEQFKSCLWKMSLSYWRSP 1184
Cdd:PLN03140 1131 PATWMLEVSSLAAEVKLGIDFAEHYKSSSLYQRNKALVKELSTPPPGASDLYFATQYSQSTWGQFKSCLWKQWWTYWRSP 1210
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1185 SYNLMRIGHTFISSFIFGLLFWNQGKKIDTQQNLFTVLGAIYGLVLFVGINNCTSALQYFETERNVMYRERFAGMYSAFA 1264
Cdd:PLN03140 1211 DYNLVRFFFTLAAALMVGTIFWKVGTKRSNANDLTMVIGAMYAAVLFVGINNCSTVQPMVAVERTVFYRERAAGMYSALP 1290
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1265 YALAQVVTEIPYIFIQSAEFVIVIYPMIGFYASFSKVFWSLYAMFCNLLCFNYLAMFLISITPNFMVAAILQSLFFTTFN 1344
Cdd:PLN03140 1291 YAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMMTVSLTPNQQVAAIFAAAFYGLFN 1370
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1345 IFAGFLIPKPQIPKWWVWFYYITPTSWTLNLFFSSQYGDIHQKINAFGETK--TVASFLEDYFGFHHDRLMITAIILIAF 1422
Cdd:PLN03140 1371 LFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIVSQYGDVEDTIKVPGGAPdpTIKWYIQDHYGYDPDFMGPVAAVLVGF 1450
|
1450 1460
....*....|....*....|
gi 1063705989 1423 PIALATMYAFFVAKLNFQKR 1442
Cdd:PLN03140 1451 TVFFAFIFAFCIRTLNFQTR 1470
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
80-1388 |
0e+00 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 1106.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 80 ENDNLKLLKKIRRRMERVGVEFP--SIEVRYEHLGVEAACevVEGKALPTLWNSLKHVFLDLLKLSGVRTNEANIKILTD 157
Cdd:TIGR00956 2 EFNAKAWVKNFRKLIDSDPIYYKpyKLGVAYKNLSAYGVA--ADSDYQPTFPNALLKILTRGFRKLKKFRDTKTFDILKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 158 VSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLKVLDifsfgcfllqmcescllffslfyfpqcyGEISYNGHGLNE 237
Cdd:TIGR00956 80 MDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVE----------------------------GVITYDGITPEE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 238 VVPQKT--SAYISQHDLHIAEMTTRETIDFSARCQGVGSRTDIMMEVSKREKdggiipdpeidaymkaisvkglkrslQT 315
Cdd:TIGR00956 132 IKKHYRgdVVYNAETDVHFPHLTVGETLDFAARCKTPQNRPDGVSREEYAKH--------------------------IA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 316 DYILKILGLDICAETLVGNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFV 395
Cdd:TIGR00956 186 DVYMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLV 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 396 SLLQPAPESYDLFDDIVLMAEGKIVYHGPRDDVLKFFEECGFQCPERKGVADFLQEVISKKdQGQYWLHQNLPhSFVSVD 475
Cdd:TIGR00956 266 AIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPDRQTTADFLTSLTSPA-ERQIKPGYEKK-VPRTPQ 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 476 TLSKRFKDLEIGRKIEEALSKPYD---------------ISKTHKDALSFNVYSLPKWELFRACISREFLLMKRNYFVYL 540
Cdd:TIGR00956 344 EFETYWRNSPEYAQLMKEIDEYLDrcsesdtkeayreshVAKQSKRTRPSSPYTVSFSMQVKYCLARNFLRMKGNPSFTL 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 541 FKTFQLVLAAIITMTVFIRTRMDIDiiHGNSYMSCLFFATVVLLVDGIPELSMTVQRLSVFYKQKQLCFYPAWAYAIPAT 620
Cdd:TIGR00956 424 FMVFGNIIMALILSSVFYNLPKNTS--DFYSRGGALFFAILFNAFSSLLEIASMYEARPIVEKHRKYALYHPSADAIASI 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 621 VLKIPLSFFESLVWTCLTYYVIGYTPEPYRFFRQFMILFAVHFTSISMFRCIAAIFQTGVAAMTAGSFVMLITFVFAGFA 700
Cdd:TIGR00956 502 ISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFA 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 701 IPYTDMPGWLKWGFWVNPISYAEIGLSVNEFLAPRWQKMQP-------TNVTLGRTILESRGL-------NYDDYM---- 762
Cdd:TIGR00956 582 IPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHGRRFECSQYvpsgggyDNLGVTNKVCTVVGAepgqdyvDGDDYLklsf 661
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 763 ------YWVSLSALLGLTIIFNTIFTLALSFLKSPTSSRPMISQDKLSELQGTKDSSVKKNKPLDssIKTNEDpgkmiLP 836
Cdd:TIGR00956 662 qyynshKWRNFGIIIGFTVFFFFVYILLTEFNKGAKQKGEILVFRRGSLKRAKKAGETSASNKND--IEAGEV-----LG 734
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 837 FKPLTITFQDLNYYVDVPVEMKG-----------QGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKT 905
Cdd:TIGR00956 735 STDLTDESDDVNDEKDMEKESGEdifhwrnltyeVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT 814
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 906 SGYIEGEIRISGFLKVQETFARVSGYCEQTDIHSPSITVEESLIYSAWLRLVPEINPQTKIRFVKQVLETIELEEIKDAL 985
Cdd:TIGR00956 815 TGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAV 894
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 986 VGVAGvSGLSTEQRKRLTVAVELVANP-SIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIHIFEAFDEL 1064
Cdd:TIGR00956 895 VGVPG-EGLNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRL 973
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1065 VLLKRGGRMIYSGPLGQHSSCVIEYFQnIPGVAKIRDKYNPATWMLEVTSESVETELDMDFAKIYNESDLYKNNSELVKE 1144
Cdd:TIGR00956 974 LLLQKGGQTVYFGDLGENSHTIINYFE-KHGAPKCPEDANPAEWMLEVIGAAPGAHANQDYHEVWRNSSEYQAVKNELDR 1052
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1145 LSKPDHGSSDLHF---KRTFAQNWWEQFKSCLWKMSLSYWRSPSYNLMRIGHTFISSFIFGLLFWNQGKkidTQQNLFTV 1221
Cdd:TIGR00956 1053 LEAELSKAEDDNDpdaLSKYAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVGT---SLQGLQNQ 1129
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1222 LGAIYGLVLFVGINNcTSALQYFETERNVM-YRERFAGMYSAFAYALAQVVTEIPYIFIQSAEFVIVIYPMIGFYASFSK 1300
Cdd:TIGR00956 1130 MFAVFMATVLFNPLI-QQYLPPFVAQRDLYeVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFYWNASK 1208
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1301 V---------FWSLYAMFcnLLCFNYLAMFLISITPNFMVAAILQSLFFTTFNIFAGFLIPKPQIPKWWVWFYYITPTSW 1371
Cdd:TIGR00956 1209 TgqvhergvlFWLLSTMF--FLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTY 1286
|
1370
....*....|....*..
gi 1063705989 1372 TLNLFFSSQYGDIHQKI 1388
Cdd:TIGR00956 1287 LVQALLSTGLADVPVTC 1303
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
839-1077 |
5.68e-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: 5.68e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 839 PLTITFQDLNYYVDVPvemkgqgynEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYIEGEIRISGF 918
Cdd:cd03232 1 GSVLTWKNLNYTVPVK---------GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 919 lKVQETFARVSGYCEQTDIHSPSITVEESLIYSAWLRlvpeinpqtkirfvkqvletieleeikdalvgvagvsGLSTEQ 998
Cdd:cd03232 72 -PLDKNFQRSTGYVEQQDVHSPNLTVREALRFSALLR-------------------------------------GLSVEQ 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705989 999 RKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIHIFEAFDELVLLKRGGRMIYSG 1077
Cdd:cd03232 114 RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRGGKTVYFG 192
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
858-1371 |
3.40e-92 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 311.98 E-value: 3.40e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 858 KGQGYNEK-KLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGY-IEGEIRISGFLKVQETFARVSGYCEQT 935
Cdd:TIGR00955 28 RGCFCRERpRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkGSGSVLLNGMPIDAKEMRAISAYVQQD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 936 DIHSPSITVEESLIYSAWLRLVPEINPQTKIRFVKQVLETIELEEIKDALVGVAG-VSGLSTEQRKRLTVAVELVANPSI 1014
Cdd:TIGR00955 108 DLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGrVKGLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1015 IFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIHIFEAFDELVLLKrGGRMIYSGPLGQhsscVIEYFQNIP 1094
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMA-EGRVAYLGSPDQ----AVPFFSDLG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1095 gvAKIRDKYNPATWMLEV--TSESVETELDMDFAKIYNE---SDLYKNNSELVKELSKPDHG---SSDLHFKRTFAQNWW 1166
Cdd:TIGR00955 263 --HPCPENYNPADFYVQVlaVIPGSENESRERIEKICDSfavSDIGRDMLVNTNLWSGKAGGlvkDSENMEGIGYNASWW 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1167 EQFKSCLWKMSLSYWRSPSYNLMRIGHTFISSFIFGLLFWNQGKKIDTQQNlftVLGAIYGLVLFVGINNCTSALQYFET 1246
Cdd:TIGR00955 341 TQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQN---INGALFLFLTNMTFQNVFPVINVFTA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1247 ERNVMYRERFAGMYSAFAYALAQVVTEIPYIFIQSAEFVIVIYPMIGFYASFSKVFWSLyamFCNLLCFNY---LAMFLI 1323
Cdd:TIGR00955 418 ELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFL---FLVTLVANVatsFGYLIS 494
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1063705989 1324 SITPNFMVAAILQSLFFTTFNIFAGFLIPKPQIPKWWVWFYYItptSW 1371
Cdd:TIGR00955 495 CAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYL---SW 539
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
839-1077 |
1.59e-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: 240.15 E-value: 1.59e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 839 PLTITFQDLNYYVDVPVemkgqgyNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYIEGEIRISGF 918
Cdd:cd03213 1 GVTLSFRNLTVTVKSSP-------SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 919 LKVQETFARVSGYCEQTDIHSPSITVEESLIYSAWLRlvpeinpqtkirfvkqvletieleeikdalvgvagvsGLSTEQ 998
Cdd:cd03213 74 PLDKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------------GLSGGE 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705989 999 RKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIHIFEAFDELVLLKRgGRMIYSG 1077
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQ-GRVIYFG 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
116-785 |
7.82e-67 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 238.41 E-value: 7.82e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 116 ACEVVEGKALPTLWNSLKHVFLDLLKLSGVRTNEANIK-ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLK 194
Cdd:TIGR00955 1 LTYSWRNSDVFGRVAQDGSWKQLVSRLRGCFCRERPRKhLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 195 VLdifsfgcfllqmcescllffslfyfpqcyGEISYNGHGLNEVVPQKTSAYISQHDLHIAEMTTRETIDFSARCQgvgs 274
Cdd:TIGR00955 81 GS-----------------------------GSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLR---- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 275 rtdimmevskrekdggiipdpeidayMKAISVKGLKRsLQTDYILKILGLDICAETLVGNA-MKRGISGGQKKRLTTAEM 353
Cdd:TIGR00955 128 --------------------------MPRRVTKKEKR-ERVDEVLQALGLRKCANTRIGVPgRVKGLSGGERKRLAFASE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 354 IVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHiTNATVFVSLLQPAPESYDLFDDIVLMAEGKIVYHGPRDDVLKFFE 433
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQ-KGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFS 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 434 ECGFQCPERKGVADFLQEVISkkdqgqywlhqNLPHSFV-SVDTLSK---RFKDLEIGRKIEEALSKPYDISK---THKD 506
Cdd:TIGR00955 260 DLGHPCPENYNPADFYVQVLA-----------VIPGSENeSRERIEKicdSFAVSDIGRDMLVNTNLWSGKAGglvKDSE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 507 ALSFNVYSLPKWELFRACISREFLLMKRNYFVYLFKTFQLVLAAIITMTVFIRTRMD---IDIIHGNSYMSCLF--FATV 581
Cdd:TIGR00955 329 NMEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTqkgVQNINGALFLFLTNmtFQNV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 582 VLLVDGIPelsmtvQRLSVFYKQKQLCFYPAWAYAIPATVLKIPLSFFESLVWTCLTYYVIGYTPEPYRFFRQFMILFAV 661
Cdd:TIGR00955 409 FPVINVFT------AELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLV 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 662 HFTSISMFRCIAAIFQTGVAAMTAGSFVMLITFVFAGFAIPYTDMPGWLKWGFWVNPISYAEIGLSVNEFLAPRWQKMQP 741
Cdd:TIGR00955 483 ANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVDNIECTS 562
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1063705989 742 TNVTL-----GRTILESRGLNYDDymYWVSLSALLGLTIIFNTIFTLAL 785
Cdd:TIGR00955 563 ANTTGpcpssGEVILETLSFRNAD--LYLDLIGLVILIFFFRLLAYFAL 609
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
146-423 |
1.67e-66 |
|
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: 223.29 E-value: 1.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 146 RTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLKVldifsfgcfllqmcescllffslfyfpqcY 225
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSV-----------------------------E 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 226 GEISYNGHGLNEV--VPQKTSAYISQHDLHIAEMTTRETIDFSARCQGvgsrtdimmevskrekdggiipdpeidaymka 303
Cdd:cd03233 65 GDIHYNGIPYKEFaeKYPGEIIYVSEEDVHFPTLTVRETLDFALRCKG-------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 304 isvkglkrslqtdyilkilgldicaetlvgNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQ 383
Cdd:cd03233 113 ------------------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIR 162
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1063705989 384 QVAHITNATVFVSLLQPAPESYDLFDDIVLMAEGKIVYHG 423
Cdd:cd03233 163 TMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
839-1383 |
1.76e-60 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 220.91 E-value: 1.76e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 839 PLTITFQDLNYYVDVPvEMKGQGYNEKKL-----------------QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLA 901
Cdd:PLN03211 37 PITLKFMDVCYRVKFE-NMKNKGSNIKRIlghkpkisdetrqiqerTILNGVTGMASPGEILAVLGPSGSGKSTLLNALA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 902 GRKTSGYIEGEIRISGFLKVQETFARvSGYCEQTDIHSPSITVEESLIYSAWLRLVPEINPQTKIRFVKQVLETIELEEI 981
Cdd:PLN03211 116 GRIQGNNFTGTILANNRKPTKQILKR-TGFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKC 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 982 KDALVGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIHIFEAF 1061
Cdd:PLN03211 195 ENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1062 DELVLLKRgGRMIYSGPLGQhsscVIEYFQNIPGVAKIrdKYNPATWMLEVT---------SESVETELDMDFAKIYNE- 1131
Cdd:PLN03211 275 DSVLVLSE-GRCLFFGKGSD----AMAYFESVGFSPSF--PMNPADFLLDLAngvcqtdgvSEREKPNVKQSLVASYNTl 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1132 -----------SDLYKNNSELVKELSKPDHGSSDlhfkRTFAQNWWEQFkSCLWKMSLSYWRSPSYNLMRIGHTFISSFI 1200
Cdd:PLN03211 348 lapkvkaaiemSHFPQANARFVGSASTKEHRSSD----RISISTWFNQF-SILLQRSLKERKHESFNTLRVFQVIAAALL 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1201 FGLLFWNQGKKiDTQQNlftvLGAIYGLVLFVGINNCTSALQYFETERNVMYRERFAGMYSAFAYALAQVVTEIPYIFIQ 1280
Cdd:PLN03211 423 AGLMWWHSDFR-DVQDR----LGLLFFISIFWGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELIL 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1281 SAEFVIVIYPMIGFYASFSKVFWSLYAMFCNLLCFNYLAMFLISITPNFMVAAILQSLFFTTFNIFAGFLIPKpqIPKWW 1360
Cdd:PLN03211 498 PTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYVHK--LPSCM 575
|
570 580
....*....|....*....|...
gi 1063705989 1361 VWFYYITPTSWTLNLFFSSQYGD 1383
Cdd:PLN03211 576 AWIKYISTTFYSYRLLINVQYGE 598
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
1172-1376 |
8.48e-56 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 192.49 E-value: 8.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1172 CLWKMSLSYWRSPSYNLMRIGHTFISSFIFGLLFWNQGkkidTQQNLFTVLGAIYGLVLFVGINNCTSALQYFETERNVM 1251
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG----NQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1252 YRERFAGMYSAFAYALAQVVTEIPYIFIQSAEFVIVIYPMIGFYASFSKVFWSLYAMFCNLLCFNYLAMFLISITPNFMV 1331
Cdd:pfam01061 77 YRELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFED 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063705989 1332 AAILQSLFFTTFNIFAGFLIPKPQIPKWWVWFYYITPTSWTLNLF 1376
Cdd:pfam01061 157 ASQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEAL 201
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
851-1077 |
1.03e-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: 1.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 851 VDVPVEMKGQGyneKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYI-EGEIRISGFLKVQETFARVS 929
Cdd:cd03234 7 WDVGLKAKNWN---KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTtSGQILFNGQPRKPDQFQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 930 GYCEQTDIHSPSITVEESLIYSAWLRLvPEINPQtKIRfvKQVLETIELEEIKDALVGVAGVSGLSTEQRKRLTVAVELV 1009
Cdd:cd03234 84 AYVRQDDILLPGLTVRETLTYTAILRL-PRKSSD-AIR--KKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705989 1010 ANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIHIFEAFDELVLLKRgGRMIYSG 1077
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSS-GEIVYSG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
135-423 |
6.37e-44 |
|
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: 158.10 E-value: 6.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 135 VFLDLLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENnlkvldifsfgcfllqmcescll 214
Cdd:cd03213 5 SFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTG----------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 215 ffslfyfPQCYGEISYNGHGLNEVVPQKTSAYISQHDLHIAEMTTRETIDFSARCqgvgsrtdimmevskrekdggiipd 294
Cdd:cd03213 62 -------LGVSGEVLINGRPLDKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKL------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 295 peidaymkaisvkglkrslqtdyilkilgldicaetlvgnamkRGISGGQKKRLTTA-EMIVGPTkALFMDEITNGLDSS 373
Cdd:cd03213 110 -------------------------------------------RGLSGGERKRVSIAlELVSNPS-LLFLDEPTSGLDSS 145
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1063705989 374 TAFQIIKSLQQVAHiTNATVFVSLLQPAPESYDLFDDIVLMAEGKIVYHG 423
Cdd:cd03213 146 SALQVMSLLRRLAD-TGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
524-729 |
4.50e-42 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 153.20 E-value: 4.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 524 CISREFLLMKRNYFVYLFKTFQLVLAAIITMTVFIRTRmdiDIIHGNSYMSCLFFATVVLLVDGIPELS-MTVQRLSVFY 602
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG---NQQGGLNRPGLLFFSILFNAFSALSGISpVFEKERGVLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 603 KQKQLCFYPAWAYAIPATVLKIPLSFFESLVWTCLTYYVIGYTPEPYRFFRQFMILFAVHFTSISMFRCIAAIFQTGVAA 682
Cdd:pfam01061 78 RELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063705989 683 MTAGSFVMLITFVFAGFAIPYTDMPGWLKWGFWVNPISYAEIGLSVN 729
Cdd:pfam01061 158 SQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
153-423 |
6.58e-38 |
|
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: 142.02 E-value: 6.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkvldifsfgcfllqmcescllffslfyfPQCYGEISYNG 232
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGG-----------------------------GTTSGQILFNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 233 HGLNEVVPQKTSAYISQHDLHIAEMTTRETIDFSARCQgvgsrtdimmevSKREKDGGIIpdpeidayMKAISVKGLKRs 312
Cdd:cd03234 72 QPRKPDQFQKCVAYVRQDDILLPGLTVRETLTYTAILR------------LPRKSSDAIR--------KKRVEDVLLRD- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 313 lqtdyilkilgldiCAETLVGNAMKRGISGGQKKRLTTA-EMIVGPtKALFMDEITNGLDSSTAFQIIKSLQQVAHiTNA 391
Cdd:cd03234 131 --------------LALTRIGGNLVKGISGGERRRVSIAvQLLWDP-KVLILDEPTSGLDSFTALNLVSTLSQLAR-RNR 194
|
250 260 270
....*....|....*....|....*....|..
gi 1063705989 392 TVFVSLLQPAPESYDLFDDIVLMAEGKIVYHG 423
Cdd:cd03234 195 IVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
861-1077 |
3.14e-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: 3.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 861 GYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRkTSGY--IEGEIRISGF--LKVQETFARVSGYCEQTD 936
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR-TEGNvsVEGDIHYNGIpyKEFAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 937 IHSPSITVEESLIYSAWLRlvpeinpqtkirfvkqvletieleeikdalvGVAGVSGLSTEQRKRLTVAVELVANPSIIF 1016
Cdd:cd03233 93 VHFPTLTVRETLDFALRCK-------------------------------GNEFVRGISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705989 1017 MDEPTTGLDARAAAIVMRAVKNVA-ETGRTIVCTIHQPSIHIFEAFDELVLLkRGGRMIYSG 1077
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTMAdVLKTTTFVSLYQASDEIYDLFDKVLVL-YEGRQIYYG 202
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
865-1079 |
1.94e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 129.41 E-value: 1.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 865 KKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGFlKVQETFARVS---GYCEQTDIHS 939
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGllRPTSG----EVRVLGE-DVARDPAEVRrriGYVPQEPALY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 940 PSITVEESLIYSAWLRLVPEINPQTKIRfvkQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDE 1019
Cdd:COG1131 86 PDLTVRENLRFFARLYGLPRKEARERID---ELLELFGLTDAADRKVG-----TLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063705989 1020 PTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSihifEA---FDELVLLKRgGRMIYSGPL 1079
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLE----EAerlCDRVAIIDK-GRIVADGTP 215
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
154-722 |
1.03e-32 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 136.55 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkvldifsfgCFLlqmcescllffslfyfpqcyGEISYNGH 233
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGN----------NFT--------------------GTILANNR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 234 GLNEVVPQKTsAYISQHDLHIAEMTTRETIDFSARCQgvgsrtdIMMEVSKREKdggiipdpeidaymkaisvkglkrSL 313
Cdd:PLN03211 133 KPTKQILKRT-GFVTQDDILYPHLTVRETLVFCSLLR-------LPKSLTKQEK------------------------IL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 314 QTDYILKILGLDICAETLVGNAMKRGISGGQKKRLTTA-EMIVGPTkALFMDEITNGLDSSTAFQIIKSLQQVAHiTNAT 392
Cdd:PLN03211 181 VAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAhEMLINPS-LLILDEPTSGLDATAAYRLVLTLGSLAQ-KGKT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 393 VFVSLLQPAPESYDLFDDIVLMAEGKIVYHGPRDDVLKFFEECGFQCPERKGVADFLQEV---------ISKKDQGQywL 463
Cdd:PLN03211 259 IVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLangvcqtdgVSEREKPN--V 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 464 HQNLPHSFVSVdtLSKRFKD-LEIGRKIEEalSKPYDISKTHKDALSFNVYSLPKWeLFRACISREFLLMKRNYFVY-LF 541
Cdd:PLN03211 337 KQSLVASYNTL--LAPKVKAaIEMSHFPQA--NARFVGSASTKEHRSSDRISISTW-FNQFSILLQRSLKERKHESFnTL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 542 KTFQLVLAAIITMTVFIRTrmdiDIIHGNSYMSCLFFATVVLLVdgIPELSMTV---QRLSVFYKQKQLCFYPAWAYAIP 618
Cdd:PLN03211 412 RVFQVIAAALLAGLMWWHS----DFRDVQDRLGLLFFISIFWGV--FPSFNSVFvfpQERAIFVKERASGMYTLSSYFMA 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 619 ATVLKIPLSFFESLVWTCLTYYVIGYTPEPYRFFRQFMILFAVHFTSISMFRCIAAIFQTGVAAMTAGSFVMLITFVFAG 698
Cdd:PLN03211 486 RIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGG 565
|
570 580
....*....|....*....|....
gi 1063705989 699 FAIpyTDMPGWLKWGFWVNPISYA 722
Cdd:PLN03211 566 FYV--HKLPSCMAWIKYISTTFYS 587
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
865-1088 |
1.67e-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: 121.50 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 865 KKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGFLKVQETFARVS--GYCEQTDIHSP 940
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGllKPDSG----SILIDGEDVRKEPREARRqiGVLPDERGLYD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 941 SITVEESLIYSAWLRLVPEINPQTKIrfvKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDEP 1020
Cdd:COG4555 88 RLTVRENIRYFAELYGLFDEELKKRI---EELIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705989 1021 TTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRgGRMIYSGPLGQHSSCVIE 1088
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIMQ-EVEALCDRVVILHK-GKVVAQGSLDELREEIGE 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
861-1077 |
2.97e-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: 2.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 861 GYNEKKLqlLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGFlKVQETFARVsGYCEQT--- 935
Cdd:cd03235 8 SYGGHPV--LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGllKPTSG----SIRVFGK-PLEKERKRI-GYVPQRrsi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 936 DIHSPsITVEESLIYSAWLRLVPeINPQTKIRF--VKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPS 1013
Cdd:cd03235 80 DRDFP-ISVRDVVLMGLYGHKGL-FRRLSKADKakVDEALERVGLSELADRQIG-----ELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 1014 IIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRggRMIYSG 1077
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLG-LVLEYFDRVLLLNR--TVVASG 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
862-1077 |
9.84e-29 |
|
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: 9.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 862 YNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGFLKVQETFA--RVSGYCEQTDI 937
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGelRPTSG----TAYINGYSIRTDRKAarQSLGYCPQFDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 938 HSPSITVEESLIYSAWLRLVPEinpQTKIRFVKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFM 1017
Cdd:cd03263 86 LFDELTVREHLRFYARLKGLPK---SEIKEEVELLLRVLGLTDKANKRAR-----TLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705989 1018 DEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHqpSIHIFEAF-DELVLLKRgGRMIYSG 1077
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRK-GRSIILTTH--SMDEAEALcDRIAIMSD-GKLRCIG 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
842-1078 |
1.11e-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: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 842 ITFQDLNYyvdvpvemkgqGYNEKklQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSgyieGEIRISGfL 919
Cdd:COG1121 7 IELENLTV-----------SYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGllPPTS----GTVRLFG-K 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 920 KVQETFARVsGYCEQT---DIHSPsITVEEsLIYSAWLRLVPEINPQTKI--RFVKQVLETIELEEIKDALVGvagvsGL 994
Cdd:COG1121 69 PPRRARRRI-GYVPQRaevDWDFP-ITVRD-VVLMGRYGRRGLFRRPSRAdrEAVDEALERVGLEDLADRPIG-----EL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 995 STEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRggRMI 1074
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLG-AVREYFDRVLLLNR--GLV 217
|
....
gi 1063705989 1075 YSGP 1078
Cdd:COG1121 218 AHGP 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
862-1070 |
1.97e-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: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 862 YNEKKLqlLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGflkvqetfarvsgyceqtdihsps 941
Cdd:cd00267 9 YGGRTA--LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT--SGEILIDG------------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 942 itveesliysawlrlvpeinpqtkirfvkQVLETIELEEIKDalvGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPT 1021
Cdd:cd00267 61 -----------------------------KDIAKLPLEELRR---RIGYVPQLSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063705989 1022 TGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIhIFEAFDELVLLKRG 1070
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPEL-AELAADRVIVLKDG 156
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
865-1077 |
2.16e-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: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 865 KKLQLLSEITGAFRPGVlTALMGISGAGKTTLLDVLAG-RKTSgyiEGEIRISGF--LKVQETFARVSGYCEQTDIHSPS 941
Cdd:cd03264 11 GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATlTPPS---SGTIRIDGQdvLKQPQKLRRRIGYLPQEFGVYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 942 ITVEESLIYSAWLRlvpEINPQTKIRFVKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDEPT 1021
Cdd:cd03264 87 FTVREFLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIG-----SLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1022 TGLDARAAAIVMRAVKNVAETGRTIVCTihqpsiHIFE----AFDELVLLKrGGRMIYSG 1077
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 ... |
862-1070 |
8.14e-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: 8.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 862 YNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKtsGYIEGEIRISGFLKVQET---FARVSGYCEQtdih 938
Cdd:cd03225 9 YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL--GPTSGEVLVDGKDLTKLSlkeLRRKVGLVFQ---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 939 SP-----SITVEESLIYSAWLRLVPEinPQTKIRfVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPS 1013
Cdd:cd03225 83 NPddqffGPTVEEEVAFGLENLGLPE--EEIEER-VEEALELVGLEGLRDRSP-----FTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705989 1014 IIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRG 1070
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDG 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
861-1078 |
1.95e-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: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 861 GYNEKklQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGEiRISGfLKVQEtFARVSGYCEQTD 936
Cdd:COG1120 10 GYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGllKPSSGevLLDGR-DLAS-LSRRE-LARRIAYVPQEP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 937 IHSPSITVEESLIY------SAWLRLVPEinpqtKIRFVKQVLETIELEEIKDALvgvagVSGLSTEQRKRLTVAVELVA 1010
Cdd:COG1120 85 PAPFGLTVRELVALgryphlGLFGRPSAE-----DREAVEEALERTGLEHLADRP-----VDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705989 1011 NPSIIFMDEPTTGLDARAAAIVMRAVKN-VAETGRTIVCTIHQPSiHIFEAFDELVLLKrGGRMIYSGP 1078
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRlARERGRTVVMVLHDLN-LAARYADRLVLLK-DGRIVAQGP 221
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
145-423 |
4.02e-25 |
|
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: 104.25 E-value: 4.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 145 VRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNlennlKVLDIFSfgcfllqmcescllffslfyfpqc 224
Cdd:cd03232 13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGR-----KTAGVIT------------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 225 yGEISYNGHGLNEVVpQKTSAYISQHDLHIAEMTTRETIDFSARCqgvgsrtdimmevskrekdggiipdpeidaymkai 304
Cdd:cd03232 64 -GEILINGRPLDKNF-QRSTGYVEQQDVHSPNLTVREALRFSALL----------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 305 svkglkrslqtdyilkilgldicaetlvgnamkRGISGGQKKRLTTA-EMIVGPTkALFMDEITNGLDSSTAFQIIKSLQ 383
Cdd:cd03232 107 ---------------------------------RGLSVEQRKRLTIGvELAAKPS-ILFLDEPTSGLDSQAAYNIVRFLK 152
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1063705989 384 QVAHiTNATVFVSLLQPAPESYDLFDDIVLMAE-GKIVYHG 423
Cdd:cd03232 153 KLAD-SGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
861-1077 |
9.52e-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: 9.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 861 GYNEKklQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG-RKTSGyieGEIRISGflkvqetfarvsgyceqTDIHS 939
Cdd:cd03214 8 GYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGlLKPSS---GEILLDG-----------------KDLAS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 940 PSItveesliySAWLRlvpeinpqtKIRFVKQVLETIELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDE 1019
Cdd:cd03214 66 LSP--------KELAR---------KIAYVPQALELLGLAHLADRPFNE-----LSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705989 1020 PTTGLDARAAAIVMRAVKNVA-ETGRTIVCTIHQPSiHIFEAFDELVLLKrGGRMIYSG 1077
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLN-LAARYADRVILLK-DGRIVAQG 180
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
869-1053 |
2.63e-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: 2.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 869 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTsgyiEGEIRISGF--LKVQETFARVSGYCEQTDIHSPSITV 944
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGllPPS----AGEVLWNGEpiRDAREDYRRRLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 945 EESLIYSAWLRLVPEINPQtkirfVKQVLETIELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGL 1024
Cdd:COG4133 93 RENLRFWAALYGLRADREA-----IDEALEAVGLAGLADLPVRQ-----LSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180
....*....|....*....|....*....
gi 1063705989 1025 DARAAAIVMRAVKNVAETGRTIVCTIHQP 1053
Cdd:COG4133 163 DAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
842-1078 |
2.21e-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: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 842 ITFQDLNYYvdvpvemkgqgYNEKKlQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGFL 919
Cdd:COG1122 1 IELENLSFS-----------YPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGllKPTSG----EVLVDGKD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 920 KVQETFARVS---GYCEQ---TDIHSPsiTVEESLIYSawlrlvPE---INPQTKIRFVKQVLETIELEEIKDAlvgvaG 990
Cdd:COG1122 65 ITKKNLRELRrkvGLVFQnpdDQLFAP--TVEEDVAFG------PEnlgLPREEIRERVEEALELVGLEHLADR-----P 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 991 VSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRg 1070
Cdd:COG1122 132 PHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLD-LVAELADRVIVLDD- 209
|
....*...
gi 1063705989 1071 GRMIYSGP 1078
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 ... |
861-1070 |
5.66e-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: 5.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 861 GYNEKKLqLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGFLKVQETFARVSGYCEQT-DI 937
Cdd:cd03226 8 SYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGliKESSG----SILLNGKPIKAKERRKSIGYVMQDvDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 938 HSPSITVEESLIYSawLRLVPEINPQtkirfVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSIIFM 1017
Cdd:cd03226 83 QLFTDSVREELLLG--LKELDAGNEQ-----AETVLKDLDLYALKERHP-----LSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063705989 1018 DEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIhIFEAFDELVLLKRG 1070
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEF-LAKVCDRVLLLANG 202
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
151-434 |
6.93e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 96.29 E-value: 6.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 151 NIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfllqmcescLLFFSlfyfpqcYGEISY 230
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLG-------------------------LLRPT-------SGEVRV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 231 NGHglnEVVPQKTSA-----YISQHDLHIAEMTTRETIDFSARCQGVgsrtdimmevskrekdggiiPDPEIDAymkais 305
Cdd:COG1131 60 LGE---DVARDPAEVrrrigYVPQEPALYPDLTVRENLRFFARLYGL--------------------PRKEARE------ 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 306 vkglkrslQTDYILKILGLDICAETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQV 385
Cdd:COG1131 111 --------RIDELLELFGLTDAADRKVGT-----LSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLREL 177
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1063705989 386 AHiTNATVFVS--LLqpaPESYDLFDDIVLMAEGKIVYHGPRDDVL-KFFEE 434
Cdd:COG1131 178 AA-EGKTVLLSthYL---EEAERLCDRVAIIDKGRIVADGTPDELKaRLLED 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
863-1070 |
1.49e-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: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 863 NEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGeIRISGFLKVQETFARVS--GYCEQTd 936
Cdd:cd03255 13 GGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGldRPTSGevRVDG-TDISKLSEKELAAFRRRhiGFVFQS- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 937 iHS--PSITVEESLIYSawLRLVPEINPQTKIRfVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSI 1014
Cdd:cd03255 91 -FNllPDLTALENVELP--LLLAGVPKKERRER-AEELLERVGLGDRLNHYP-----SELSGGQQQRVAIARALANDPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705989 1015 IFMDEPTTGLDARAAAIVMRAVKNVA-ETGRTIVCTIHQPSihIFEAFDELVLLKRG 1070
Cdd:cd03255 162 ILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPE--LAEYADRIIELRDG 216
|
|
| PDR_assoc |
pfam08370 |
Plant PDR ABC transporter associated; This domain is found on the C-terminus of ABC-2 type ... |
736-798 |
5.03e-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: 5.03e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705989 736 WQKMQP--TNVTLGRTILESRGLNYDDYMYWVSLSALLGLTIIFNTIFTLALSFLKSPTSSRPMI 798
Cdd:pfam08370 1 WMKPTAsnGNTTLGVAVLKSRGLFTEAYWYWIGVGALLGFTILFNILFTLALTYLNPLGKSQAII 65
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
865-1077 |
1.59e-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: 91.51 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 865 KKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIEgeIRISGFLKVQETFARVSGYCEQTDIHsPSI 942
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGliKPDSGEIT--FDGKSYQKNIEALRRIGALIEAPGFY-PNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 943 TVEESLIYSAWLRLVPEINpqtkirfVKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDEPTT 1022
Cdd:cd03268 88 TARENLRLLARLLGIRKKR-------IDEVLDVVGLKDSAKKKVK-----GFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063705989 1023 GLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLkRGGRMIYSG 1077
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLISSHLLS-EIQKVADRIGII-NKGKLIEEG 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
870-1022 |
1.90e-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: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 870 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTsgYIEGEIRISG--FLKVQETFARVS-GYCEQTDIHSPSITVEE 946
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS--PTEGTILLDGqdLTDDERKSLRKEiGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705989 947 SLIYSAWLRLVPEINPQTKirfVKQVLETIELEEIKDALVGVAGvSGLSTEQRKRLTVAVELVANPSIIFMDEPTT 1022
Cdd:pfam00005 79 NLRLGLLLKGLSKREKDAR---AEEALEKLGLGDLADRPVGERP-GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
828-1070 |
3.21e-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: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 828 EDPGKMILPFKPLTITFQDLNYyvdvpvemkgqGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKT 905
Cdd:COG4987 320 TEPAEPAPAPGGPSLELEDVSF-----------RYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRflDPQ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 906 SGyiegEIRISGflkV------QETFARVSGYCEQtDIHSPSITVEESLiysawlRLVpeiNPQTKIRFVKQVLETIELE 979
Cdd:COG4987 389 SG----SITLGG---VdlrdldEDDLRRRIAVVPQ-RPHLFDTTLRENL------RLA---RPDATDEELWAALERVGLG 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 980 EIKDAL-------VGVAGvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHQ 1052
Cdd:COG4987 452 DWLAALpdgldtwLGEGG-RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHR 529
|
250
....*....|....*...
gi 1063705989 1053 PSIHifEAFDELVLLKRG 1070
Cdd:COG4987 530 LAGL--ERMDRILVLEDG 545
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
839-1070 |
3.31e-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: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 839 PLTITFQDLNYyvdvpvemkgqGYNEKKlQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISG- 917
Cdd:COG4988 334 PPSIELEDVSF-----------SYPGGR-PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP--YSGSILINGv 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 918 ---FLKVQETFARVSgYCEQTDiHSPSITVEEsliysaWLRLV-PEINPQTkirfVKQVLETIELEEIKDAL-------V 986
Cdd:COG4988 400 dlsDLDPASWRRQIA-WVPQNP-YLFAGTIRE------NLRLGrPDASDEE----LEAALEAAGLDEFVAALpdgldtpL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 987 GVAGvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAEtGRT-IVCTiHQPsiHIFEAFDELV 1065
Cdd:COG4988 468 GEGG-RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTvILIT-HRL--ALLAQADRIL 542
|
....*
gi 1063705989 1066 LLKRG 1070
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 ... |
879-1077 |
9.29e-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: 9.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 879 PGVLTALMGISGAGKTTLLDVLAG--RKTSGYIEgeirISGFLKVQETFA--RVSGYCEQTDIHSPSITVEESLIYSAWL 954
Cdd:cd03266 30 PGEVTGLLGPNGAGKTTTLRMLAGllEPDAGFAT----VDGFDVVKEPAEarRRLGFVSDSTGLYDRLTARENLEYFAGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 955 RlvpEINPQTKIRFVKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMR 1034
Cdd:cd03266 106 Y---GLKGDELTARLEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALRE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063705989 1035 AVKNVAETGRTIVCTIHqpSIHIFEAF-DELVLLKRgGRMIYSG 1077
Cdd:cd03266 178 FIRQLRALGKCILFSTH--IMQEVERLcDRVVVLHR-GRVVYEG 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
155-368 |
1.93e-19 |
|
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: 86.55 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 155 LTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlkvldifsfgcfllqmcescllffslfyfPQCyGEISYNGHG 234
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS-------------------------------PTE-GTILLDGQD 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 235 LNEVVPQKTS---AYISQHDLHIAEMTTRETIDFSARCQGvgsrtdimmeVSKREKDGgiipdpeidaymkaisvkglkr 311
Cdd:pfam00005 49 LTDDERKSLRkeiGYVFQDPQLFPRLTVRENLRLGLLLKG----------LSKREKDA---------------------- 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705989 312 slQTDYILKILGLDICAETLVGNAMKrGISGGQKKRLTTAEMIVGPTKALFMDEITN 368
Cdd:pfam00005 97 --RAEEALEKLGLGDLADRPVGERPG-TLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
868-1070 |
2.07e-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: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 868 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSgyieGEIRISGflkvqETFARVS------GYCEQTDIHS 939
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGleRPDS----GEILIDG-----RDVTGVPperrniGMVFQDYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 940 PSITVEESLIYSAWLRLVPEinPQTKIRfVKQVLETIELEEIKDALvgvagVSGLSTEQRKRLTVAVELVANPSIIFMDE 1019
Cdd:cd03259 85 PHLTVAENIAFGLKLRGVPK--AEIRAR-VRELLELVGLEGLLNRY-----PHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063705989 1020 PTTGLDARAAAIVMRAVKNV-AETGRTIVCTIHQPSihifEAF---DELVLLKRG 1070
Cdd:cd03259 157 PLSALDAKLREELREELKELqRELGITTIYVTHDQE----EALalaDRIAVMNEG 207
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
878-1051 |
2.14e-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: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 878 RPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGFLKVQET--FARVSGYCEQTDIHSPSITVEESLIYSAW 953
Cdd:cd03265 24 RRGEIFGLLGPNGAGKTTTIKMLTTllKPTSG----RATVAGHDVVREPreVRRRIGIVFQDLSVDDELTGWENLYIHAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 954 LRLVPEINPQTKIRfvkQVLETIELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVM 1033
Cdd:cd03265 100 LYGVPGAERRERID---ELLDFVGLLEAADRLVKT-----YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVW 171
|
170
....*....|....*....
gi 1063705989 1034 RAVKN-VAETGRTIVCTIH 1051
Cdd:cd03265 172 EYIEKlKEEFGMTILLTTH 190
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
870-1078 |
7.06e-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: 7.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 870 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGEiRISGfLKVQE--------TFARVSGYceqtdi 937
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGflRPTSGsvLFDGE-DITG-LPPHEiarlgigrTFQIPRLF------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 938 hsPSITVEE------------SLIYSAWLRLVPEINPQtkirfVKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVA 1005
Cdd:cd03219 88 --PELTVLEnvmvaaqartgsGLLLARARREEREARER-----AEELLERVGLADLADRPAG-----ELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063705989 1006 VELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIhIFEAFDELVLLKRgGRMIYSGP 1078
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 ... |
842-1051 |
8.98e-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: 8.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 842 ITFQDLNYYvdvpvemkgqgYNEKklQLLSEITGAFRPGVLTALMGISGAGKTTLL-------DVLAGRKTSG--YIEGE 912
Cdd:cd03260 1 IELRDLNVY-----------YGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLrllnrlnDLIPGAPDEGevLLDGK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 913 IRISGFLKVQETFARVsGYCEQtdihSPSI---TVEESLIYSAWLRLVPEINPQTKIrfVKQVLETIEL-EEIKDALVGv 988
Cdd:cd03260 68 DIYDLDVDVLELRRRV-GMVFQ----KPNPfpgSIYDNVAYGLRLHGIKLKEELDER--VEEALRKAALwDEVKDRLHA- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063705989 989 agvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETgRTIVCTIH 1051
Cdd:cd03260 140 ---LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTH 198
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
865-1070 |
9.07e-19 |
|
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: 9.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 865 KKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGF--LKVQETFARVSGYCEQTDIHSP 940
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGllKPDSG----EIKVLGKdiKKEPEEVKRRIGYLPEEPSLYE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 941 SITVEESLIYSawlrlvpeinpqtkirfvkqvletieleeikdalvgvagvSGlsteQRKRLTVAVELVANPSIIFMDEP 1020
Cdd:cd03230 87 NLTVRENLKLS----------------------------------------GG----MKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063705989 1021 TTGLDARAAAIVMRAVKNVAETGRTIVCTIHqpsiHIFEA---FDELVLLKRG 1070
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSH----ILEEAerlCDRVAILNNG 171
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
862-1070 |
9.31e-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: 9.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 862 YNEKklQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGflkvqETFARVSGYCEQtdihs 939
Cdd:cd03229 10 YGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGleEPDSG----SILIDG-----EDLTDLEDELPP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 940 psitveesliysawlrlvpeinPQTKIRFVKQ---------VLETIELeeikdalvgvagvsGLSTEQRKRLTVAVELVA 1010
Cdd:cd03229 74 ----------------------LRRRIGMVFQdfalfphltVLENIAL--------------GLSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 1011 NPSIIFMDEPTTGLDARAAAIVMRAVKNV-AETGRTIVCTIHQpsihIFEAF---DELVLLKRG 1070
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHD----LDEAArlaDRVVVLRDG 177
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
862-1079 |
1.13e-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: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 862 YNEKKLqlLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGR--KTSGyieGEIRISGflkvqETFARVS--------GY 931
Cdd:COG1119 13 RGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlpPTYG---NDVRLFG-----ERRGGEDvwelrkriGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 932 C--EQTDIHSPSITVEESLI---YSAwLRLVPEINPQTKIRfVKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAV 1006
Cdd:COG1119 83 VspALQLRFPRDETVLDVVLsgfFDS-IGLYREPTDEQRER-ARELLELLGLAHLADRPFG-----TLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 1007 ELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETG-RTIVCTIHQPSIhIFEAFDELVLLKRgGRMIYSGPL 1079
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEE-IPPGITHVLLLKD-GRVVAAGPK 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
870-1078 |
1.21e-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: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 870 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGEIRISGFLKVQETFARVSGYCEQTDIHSPSITVE 945
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGlvEPTSGsvLIDGTDINKLKGKALRQLRRQIGMIFQQFNLIERLSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 946 ESL---------IYSAWLRLVPEinpqtkirfvkqvletielEEIKDAL-----VGVAG-----VSGLSTEQRKRLTVAV 1006
Cdd:cd03256 97 ENVlsgrlgrrsTWRSLFGLFPK-------------------EEKQRALaalerVGLLDkayqrADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063705989 1007 ELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAET-GRTIVCTIHQPSIhIFEAFDELVLLKRgGRMIYSGP 1078
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDL-AREYADRIVGLKD-GRIVFDGP 228
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
140-430 |
2.64e-18 |
|
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: 91.05 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 140 LKLSGV--RTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfllqmcescllffs 217
Cdd:COG2274 474 IELENVsfRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG------------------------------ 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 218 lFYFPQCyGEISYNGHGLNE-----------VVPQktsayisqhDLHIAEMTTRETIDFSArcqgvgsrtdimmevskre 286
Cdd:COG2274 524 -LYEPTS-GRILIDGIDLRQidpaslrrqigVVLQ---------DVFLFSGTIRENITLGD------------------- 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 287 kdggiiPDPEIDAYMKAISVKGLkrslqTDYILKI-LGLDicaeTLVGNaMKRGISGGQKKRLTTAEMIVGPTKALFMDE 365
Cdd:COG2274 574 ------PDATDEEIIEAARLAGL-----HDFIEALpMGYD----TVVGE-GGSNLSGGQRQRLAIARALLRNPRILILDE 637
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 366 ITNGLDSSTAFQIIKSLQQVAHitNATVFV-----SLLQpapesydLFDDIVLMAEGKIVYHGPRDDVLK 430
Cdd:COG2274 638 ATSALDAETEAIILENLRRLLK--GRTVIIiahrlSTIR-------LADRIIVLDKGRIVEDGTHEELLA 698
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
877-1067 |
5.14e-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: 5.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 877 FRPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGflkVQETFARVSGYCEQTdihspsitveesliysAWLRL 956
Cdd:TIGR02857 345 VPPGERVALVGPSGAGKSTLLNLLLGFVDPT--EGSIAVNG---VPLADADADSWRDQI----------------AWVPQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 957 VPEINPQT---KIRF---------VKQVLETIELEEIKDAL-------VGVAGvSGLSTEQRKRLTVAVELVANPSIIFM 1017
Cdd:TIGR02857 404 HPFLFAGTiaeNIRLarpdasdaeIREALERAGLDEFVAALpqgldtpIGEGG-AGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1018 DEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHQPsiHIFEAFDELVLL 1067
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRL--ALAALADRIVVL 529
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
139-430 |
9.43e-18 |
|
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: 84.14 E-value: 9.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 139 LLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkvldifsfgcfllqmcescllffsl 218
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 219 fyfpqcYGEISYNGHGLNE----------VVPQKTSAYisqhdlhiAEMTTRETIDFSARCQGVgsrtdimmevskrekd 288
Cdd:COG4555 55 ------SGSILIDGEDVRKeprearrqigVLPDERGLY--------DRLTVRENIRYFAELYGL---------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 289 ggiipdpeidaymkaisvKGLKRSLQTDYILKILGLDICAETLVGnamkrGISGGQKKRLTTAEMIVGPTKALFMDEITN 368
Cdd:COG4555 105 ------------------FDEELKKRIEELIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 369 GLDSSTAFQIIKSLQQVAHiTNATVFVS--LLQpapESYDLFDDIVLMAEGKIVYHGPRDDVLK 430
Cdd:COG4555 162 GLDVMARRLLREILRALKK-EGKTVLFSshIMQ---EVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
864-1070 |
2.41e-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: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 864 EKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSgyieGEIRISGflkvqetfarvsgyceqTDIHS-- 939
Cdd:COG1136 18 EGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGldRPTS----GEVLIDG-----------------QDISSls 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 940 ----------------------PSITVEESLIYSAWLRLVPEINPQTKIRfvkQVLETIELEEIKDALvgvagVSGLSTE 997
Cdd:COG1136 77 erelarlrrrhigfvfqffnllPELTALENVALPLLLAGVSRKERRERAR---ELLERVGLGDRLDHR-----PSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 998 QRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVA-ETGRTIVCTIHQPsiHIFEAFDELVLLKRG 1070
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDP--ELAARADRVIRLRDG 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
878-1117 |
6.47e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 83.32 E-value: 6.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 878 RPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGF-LKVQETFARVS-GYCEQTDIHSPSITVEESL-IYSAWL 954
Cdd:PRK13537 31 QRGECFGLLGPNGAGKTTTLRMLLGLTHPD--AGSISLCGEpVPSRARHARQRvGVVPQFDNLDPDFTVRENLlVFGRYF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 955 RLvpeiNPQTKIRFVKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMR 1034
Cdd:PRK13537 109 GL----SAAAARALVPPLLEFAKLENKADAKVG-----ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1035 AVKNVAETGRTIVCTIHqpsiHIFEA---FDELVLLKrGGRMIYSGP----LGQHSSC-VIEYFQniPGVAKIRDKYNPA 1106
Cdd:PRK13537 180 RLRSLLARGKTILLTTH----FMEEAerlCDRLCVIE-EGRKIAEGAphalIESEIGCdVIEIYG--PDPVALRDELAPL 252
|
250
....*....|.
gi 1063705989 1107 TWMLEVTSESV 1117
Cdd:PRK13537 253 AERTEISGETL 263
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
868-1081 |
8.55e-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: 8.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 868 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGEIRISGFLKVQETFARVSGYCEQTDIHSPSIT 943
Cdd:cd03261 14 TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGllRPDSGevLIDGEDISGLSEAELYRLRRRMGMLFQSGALFDSLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 944 VEESLIYsaWLRlvpE--INPQTKIR-FVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSIIFMDEP 1020
Cdd:cd03261 94 VFENVAF--PLR---EhtRLSEEEIReIVLEKLEAVGLRGAEDLYP-----AELSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705989 1021 TTGLDARAAAIVMRAVKNVAET-GRTIVCTIHQPSIhIFEAFDELVLLKRgGRMIYSGPLGQ 1081
Cdd:cd03261 164 TAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDT-AFAIADRIAVLYD-GKIVAEGTPEE 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
162-423 |
1.10e-16 |
|
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: 80.63 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 162 ISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfLLQMCEscllffslfyfpqcyGEISYNGHGLNE--VV 239
Cdd:cd03263 25 VYKGEIFGLLGHNGAGKTTTLKMLTG-----------------ELRPTS---------------GTAYINGYSIRTdrKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 240 PQKTSAYISQHDLHIAEMTTRETIDFSARCQGVgSRTDIMMEVSKrekdggiipdpeidaymkaisvkglkrslqtdyIL 319
Cdd:cd03263 73 ARQSLGYCPQFDALFDELTVREHLRFYARLKGL-PKSEIKEEVEL---------------------------------LL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 320 KILGLDICAETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHitNATVFVSLLQ 399
Cdd:cd03263 119 RVLGLTDKANKRART-----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHS 191
|
250 260
....*....|....*....|....
gi 1063705989 400 PApESYDLFDDIVLMAEGKIVYHG 423
Cdd:cd03263 192 MD-EAEALCDRIAIMSDGKLRCIG 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
842-1070 |
1.38e-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: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 842 ITFQDLNYyvdvpvemkgqGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSgyieGEIRISGfl 919
Cdd:cd03228 1 IEFKNVSF-----------SYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRlyDPTS----GEILIDG-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 920 kvqetfarvsgyceqTDIHSPSItveesliysAWLR----LVpeinPQTKIRFVKQVLETIeleeikdalvgvagvsgLS 995
Cdd:cd03228 64 ---------------VDLRDLDL---------ESLRkniaYV----PQDPFLFSGTIRENI-----------------LS 98
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705989 996 TEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHQPSihIFEAFDELVLLKRG 1070
Cdd:cd03228 99 GGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLS--TIRDADRIIVLDDG 170
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
878-1051 |
1.38e-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: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 878 RPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGF--LKVQETFARVSGYCEQTDIHSPSITVEESLIYSAW 953
Cdd:TIGR01188 17 REGEVFGFLGPNGAGKTTTIRMLTTllRPTSG----TARVAGYdvVREPRKVRRSIGIVPQYASVDEDLTGRENLEMMGR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 954 LRLVPEINPQTKIrfvKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVM 1033
Cdd:TIGR01188 93 LYGLPKDEAEERA---EELLELFELGEAADRPVG-----TYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIW 164
|
170
....*....|....*...
gi 1063705989 1034 RAVKNVAETGRTIVCTIH 1051
Cdd:TIGR01188 165 DYIRALKEEGVTILLTTH 182
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
828-1078 |
1.65e-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: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 828 EDPGKMILPFKPLTITFQDLNYyvdvpvemkgqGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKT 905
Cdd:COG2274 460 EGRSKLSLPRLKGDIELENVSF-----------RYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGlyEPT 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 906 SGyiegEIRISGF----LKVQETFARVsGYCEQtDIHSPSITVEESLIYSAwlrlvPEINPQTkirfVKQVLETIEL-EE 980
Cdd:COG2274 529 SG----RILIDGIdlrqIDPASLRRQI-GVVLQ-DVFLFSGTIRENITLGD-----PDATDEE----IIEAARLAGLhDF 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 981 IK------DALVGVAGvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHQPS 1054
Cdd:COG2274 594 IEalpmgyDTVVGEGG-SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLS 671
|
250 260
....*....|....*....|....
gi 1063705989 1055 ihIFEAFDELVLLKRgGRMIYSGP 1078
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 ... |
879-1077 |
3.96e-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: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 879 PGVLTALMGISGAGKTTLLDVLAG--RKTSGYIE------GEIRISGFLKVQEtfaRVSGYCEQTDIHSPSITVEESLIY 950
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGleKPDGGTIVlngtvlFDSRKKINLPPQQ---RKIGLVFQQYALFPHLNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 951 SawlrLVPEINPQTKIRfVKQVLETIELEEIKDAlvgvaGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAA 1030
Cdd:cd03297 99 G----LKRKRNREDRIS-VDELLDLLGLDHLLNR-----YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 1031 IVMRAVKNVAEtgrtivcTIHQPSIHIF----EAF---DELVLLkRGGRMIYSG 1077
Cdd:cd03297 169 QLLPELKQIKK-------NLNIPVIFVThdlsEAEylaDRIVVM-EDGRLQYIG 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
870-1073 |
5.06e-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: 5.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 870 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGF----LKVQET--FARVSGYCEQTDIHSPSIT 943
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELP--TSGTIRVNGQdvsdLRGRAIpyLRRKIGVVFQDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 944 VEESLIYSawLRLVpEINPQTKIRFVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTG 1023
Cdd:cd03292 95 VYENVAFA--LEVT-GVPPREIRKRVPAALELVGLSHKHRALP-----AELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1024 LDARAAAIVMRAVKNVAETGRTIVCTIHQPSihIFEAFDELVLLKRGGRM 1073
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTTVVVATHAKE--LVDTTRHRVIALERGKL 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
880-1077 |
8.57e-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: 8.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 880 GVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGFL--KVQETF-ARVSGYCEQTDIHSPSITVEESLiysAWL 954
Cdd:cd03267 47 GEIVGFIGPNGAGKTTTLKILSGllQPTSG----EVRVAGLVpwKRRKKFlRRIGVVFGQKTQLWWDLPVIDSF---YLL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 955 RLVPEINPQTKIRFVKQVLETIELEEIKDAlvgvaGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMR 1034
Cdd:cd03267 120 AAIYDLPPARFKKRLDELSELLDLEELLDT-----PVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063705989 1035 AVKN-VAETGRTIVCTIHqpSIHIFEAFDELVLLKRGGRMIYSG 1077
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 ... |
869-1070 |
1.13e-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: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 869 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGflkvqetfarvsgyceqTDIHSpsitvee 946
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGllRPTSG----RVRLDG-----------------ADISQ------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 947 sliysawlrlvpeINPQTKIRFVKQVLETIELEE--IKDALvgvagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGL 1024
Cdd:cd03246 69 -------------WDPNELGDHVGYLPQDDELFSgsIAENI--------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063705989 1025 DARAAAIVMRAVKNVAETGRTIVCTIHQPSihIFEAFDELVLLKRG 1070
Cdd:cd03246 128 DVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDG 171
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
862-1081 |
1.13e-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: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 862 YNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGR-KTSGYIEGEIRISGF----LKVQETFARVSGYCEQTD 936
Cdd:COG1123 14 YPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlPHGGRISGEVLLDGRdlleLSEALRGRRIGMVFQDPM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 937 IHSPSITVEESLIYSAWLRLVPeinPQTKIRFVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSIIF 1016
Cdd:COG1123 94 TQLNPVTVGDQIAEALENLGLS---RAEARARVLELLEAVGLERRLDRYP-----HQLSGGQRQRVAIAMALALDPDLLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705989 1017 MDEPTTGLDARAAAIVMRAVKNV-AETGRTIVCTIHQPSIhIFEAFDELVLLKRgGRMIYSGPLGQ 1081
Cdd:COG1123 166 ADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGV-VAEIADRVVVMDD-GRIVEDGPPEE 229
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
154-429 |
1.93e-15 |
|
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: 77.78 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlkvldifsfgcfllqmcescllffslfyfPQCyGEISYNGH 233
Cdd:COG1120 16 VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK-------------------------------PSS-GEVLLDGR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 234 GLNEVVPQ---KTSAYISQHDLHIAEMTTRETIdfsarcqGVG--SRTDIMMEVSKREKDggiipdpEIDAYMKAISVKG 308
Cdd:COG1120 64 DLASLSRRelaRRIAYVPQEPPAPFGLTVRELV-------ALGryPHLGLFGRPSAEDRE-------AVEEALERTGLEH 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 309 LK-RSLQTdyilkilgldicaetlvgnamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAH 387
Cdd:COG1120 130 LAdRPVDE------------------------LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAR 185
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1063705989 388 ITNATVFVSLlqpapesYDL------FDDIVLMAEGKIVYHGPRDDVL 429
Cdd:COG1120 186 ERGRTVVMVL-------HDLnlaaryADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
140-423 |
2.04e-15 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 76.79 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfLLQMCEscllffslf 219
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAG-----------------LERPDS--------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 220 yfpqcyGEISYNGHGLNEVVPQKTS-AYISQHDLHIAEMTTRETIDFSARCQGVgsrtdimmevskrekdggiiPDPEID 298
Cdd:cd03259 55 ------GEILIDGRDVTGVPPERRNiGMVFQDYALFPHLTVAENIAFGLKLRGV--------------------PKAEIR 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 299 AYMKAisvkglkrslqtdyILKILGLDicaetLVGNAMKRGISGGQKKRLTTAE-MIVGPtKALFMDEITNGLDSSTAFQ 377
Cdd:cd03259 109 ARVRE--------------LLELVGLE-----GLLNRYPHELSGGQQQRVALARaLAREP-SLLLLDEPLSALDAKLREE 168
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1063705989 378 I---IKSLQQVAHITnaTVFVSLLQpaPESYDLFDDIVLMAEGKIVYHG 423
Cdd:cd03259 169 LreeLKELQRELGIT--TIYVTHDQ--EEALALADRIAVMNEGRIVQVG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
154-371 |
2.65e-15 |
|
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: 76.36 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfLLQMCEscllffslfyfpqcyGEISYNGH 233
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAG-----------------LLPPSA---------------GEVLWNGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 234 GLNEVVPQ--KTSAYISQHDLHIAEMTTRETIDFSARCQGVGsrtdimmevskrekdggiIPDPEIDAymkaisvkglkr 311
Cdd:COG4133 65 PIRDAREDyrRRLAYLGHADGLKPELTVRENLRFWAALYGLR------------------ADREAIDE------------ 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 312 slqtdyILKILGLDICAETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLD 371
Cdd:COG4133 115 ------ALEAVGLAGLADLPVRQ-----LSAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
148-418 |
6.55e-15 |
|
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: 75.20 E-value: 6.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 148 NEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfllqmcescllffslFYFPQcYGE 227
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNG-------------------------------LLGPT-SGE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 228 ISYNGHGLNEVVPQ---KTSAYISQH-DLHIAEMTTRETIDFSARCQGVgsrtdimmevskrekdggiiPDPEIDAYmka 303
Cdd:cd03225 58 VLVDGKDLTKLSLKelrRKVGLVFQNpDDQFFGPTVEEEVAFGLENLGL--------------------PEEEIEER--- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 304 isvkglkrslqTDYILKILGLDICAETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQ 383
Cdd:cd03225 115 -----------VEEALELVGLEGLRDRSPFT-----LSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLK 178
|
250 260 270
....*....|....*....|....*....|....*....
gi 1063705989 384 QVAHITNATVFVS----LLqpapesYDLFDDIVLMAEGK 418
Cdd:cd03225 179 KLKAEGKTIIIVThdldLL------LELADRVIVLEDGK 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
861-1047 |
7.70e-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: 7.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 861 GYneKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYI--EGEiRISGflkvQETFARVS---GYCE 933
Cdd:cd03224 9 GY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGllPPRSGSIrfDGR-DITG----LPPHERARagiGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 934 QTDIHSPSITVEESLIYSAWLRlvpeinpqtKIRFVKQVLETI-----ELEEIKDALVGVagvsgLSTEQRKRLTVAVEL 1008
Cdd:cd03224 82 EGRRIFPELTVEENLLLGAYAR---------RRAKRKARLERVyelfpRLKERRKQLAGT-----LSGGEQQMLAIARAL 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063705989 1009 VANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIV 1047
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTIL 186
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
869-1053 |
1.13e-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: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 869 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISG--FLKVQETFARVSGYCEQTDIHSPSITVEE 946
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP--DSGEVRWNGtpLAEQRDEPHENILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 947 SLIYsaWLRLVpeinpQTKIRFVKQVLETIELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDA 1026
Cdd:TIGR01189 93 NLHF--WAAIH-----GGAQRTIEDALAAVGLTGFEDLPAAQ-----LSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*..
gi 1063705989 1027 RAAAIVMRAVKNVAETGRTIVCTIHQP 1053
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
140-430 |
1.86e-14 |
|
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: 78.26 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 140 LKLSGVR-TNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENnlkvldifsfgcfllqmcescllffsl 218
Cdd:COG4988 337 IELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP--------------------------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 219 fyfpqcY-GEISYNGHGLNEVVP---QKTSAYISQHDlHIAEMTTRETIDFSARCqgvgsrtdimmevskrekdggiIPD 294
Cdd:COG4988 390 ------YsGSILINGVDLSDLDPaswRRQIAWVPQNP-YLFAGTIRENLRLGRPD----------------------ASD 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 295 PEIDAYMKAISVKGLKRSLQtdyilkiLGLDicaeTLVG-NAmkRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSS 373
Cdd:COG4988 441 EELEAALEAAGLDEFVAALP-------DGLD----TPLGeGG--RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAE 507
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705989 374 TAFQIIKSLQQVAHitNATVFV-----SLLQPApesydlfDDIVLMAEGKIVYHGPRDDVLK 430
Cdd:COG4988 508 TEAEILQALRRLAK--GRTVILithrlALLAQA-------DRILVLDDGRIVEQGTHEELLA 560
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
870-1070 |
2.06e-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: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 870 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGflkvqetfarvsgycEQTDIHSPsitvees 947
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGlyKPDSG----EILVDG---------------KEVSFASP------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 948 liysawlrlvpeinpqtkirfvkqvletieleeiKDAL-VGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDA 1026
Cdd:cd03216 70 ----------------------------------RDARrAGIAMVYQLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063705989 1027 RAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRG 1070
Cdd:cd03216 116 AEVERLFKVIRRLRAQGVAVIFISHRLD-EVFEIADRVTVLRDG 158
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
879-1117 |
2.37e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.02 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 879 PGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGF-LKVQETFARVS-GYCEQTDIHSPSITVEESLI-YSAWLR 955
Cdd:PRK13536 66 SGECFGLLGPNGAGKSTIARMILGMTSPD--AGKITVLGVpVPARARLARARiGVVPQFDNLDLEFTVRENLLvFGRYFG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 956 LvpeiNPQTKIRFVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRA 1035
Cdd:PRK13536 144 M----STREIEAVIPSLLEFARLESKADARV-----SDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWER 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1036 VKNVAETGRTIVCTihqpsIHIFEAF----DELVLLKRGGRMIYSGP---LGQHSSC-VIEYFQNIPgvAKIRDKYNPAT 1107
Cdd:PRK13536 215 LRSLLARGKTILLT-----THFMEEAerlcDRLCVLEAGRKIAEGRPhalIDEHIGCqVIEIYGGDP--HELSSLVKPYA 287
|
250
....*....|
gi 1063705989 1108 WMLEVTSESV 1117
Cdd:PRK13536 288 RRIEVSGETL 297
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
878-1051 |
2.63e-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: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 878 RPGVLTALMGISGAGKTTLLDVLAGRK--TSG--YIEGEIRISGFLKVQETFarvsGYCEQTDIHSPSITVEESLIYSAW 953
Cdd:TIGR01257 1963 RPGECFGLLGVNGAGKTTTFKMLTGDTtvTSGdaTVAGKSILTNISDVHQNM----GYCPQFDAIDDLLTGREHLYLYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 954 LRLVP--EINpqtkiRFVKQVLETIELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAI 1031
Cdd:TIGR01257 2039 LRGVPaeEIE-----KVANWSIQSLGLSLYADRLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
170 180
....*....|....*....|
gi 1063705989 1032 VMRAVKNVAETGRTIVCTIH 1051
Cdd:TIGR01257 2109 LWNTIVSIIREGRAVVLTSH 2128
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
870-1053 |
2.67e-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: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 870 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAG-RKTSGyieGEIRISGF----LKVQETFARVSgYCEQtDIHSPSITV 944
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGlLDPLQ---GEVTLDGVpvssLDQDEVRRRVS-VCAQ-DAHLFDTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 945 EESLIYSAwlrlvPEINPQTkirfVKQVLETIELEEIKDALVG------VAGVSGLSTEQRKRLTVAVELVANPSIIFMD 1018
Cdd:TIGR02868 426 RENLRLAR-----PDATDEE----LWAALERVGLADWLRALPDgldtvlGEGGARLSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|....*
gi 1063705989 1019 EPTTGLDARAAAIVMRAVkNVAETGRTIVCTIHQP 1053
Cdd:TIGR02868 497 EPTEHLDAETADELLEDL-LAALSGRTVVLITHHL 530
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
878-1121 |
3.20e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.15 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 878 RPGVLTALMGISGAGKTTL----LDVLAgrKTSGyiegEIRISGFLKVQETFARVsGYceqtdihsPSITVEESLIYSAW 953
Cdd:COG4152 25 PKGEIFGLLGPNGAGKTTTiriiLGILA--PDSG----EVLWDGEPLDPEDRRRI-GYlpeerglyPKMKVGEQLVYLAR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 954 LRLVPEinPQTKIRfVKQVLETIELEEIKDALVgvagvSGLS-TEQRKrLTVAVELVANPSIIFMDEPTTGLDARAAAIV 1032
Cdd:COG4152 98 LKGLSK--AEAKRR-ADEWLERLGLGDRANKKV-----EELSkGNQQK-VQLIAALLHDPELLILDEPFSGLDPVNVELL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1033 MRAVKNVAETGRTIVCTIHQpsIHIFEAF-DELVLLKRgGRMIYSGPLGQ------------HSSCVIEYFQNIPGVAKI 1099
Cdd:COG4152 169 KDVIRELAAKGTTVIFSSHQ--MELVEELcDRIVIINK-GRKVLSGSVDEirrqfgrntlrlEADGDAGWLRALPGVTVV 245
|
250 260
....*....|....*....|..
gi 1063705989 1100 RDkyNPATWMLEVTSESVETEL 1121
Cdd:COG4152 246 EE--DGDGAELKLEDGADAQEL 265
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
878-1077 |
4.23e-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: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 878 RPGVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGEIRISGFLKVQETFARVSGYCEQTDIHS--PSITVEESLIYS 951
Cdd:cd03257 29 KKGETLGLVGESGSGKSTLARAILGllKPTSGsiIFDGKDLLKLSRRLRKIRRKEIQMVFQDPMSSlnPRMTIGEQIAEP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 952 AWLRLvPEINPQTKIRFVKQVLETIEL-EEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAA 1030
Cdd:cd03257 109 LRIHG-KLSKKEARKEAVLLLLVGVGLpEEVLNRYP-----HELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQA 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063705989 1031 IVMRAVKNV-AETGRTIVCTIHQPSIHIFEAfDELVLLKrGGRMIYSG 1077
Cdd:cd03257 183 QILDLLKKLqEELGLTLLFITHDLGVVAKIA-DRVAVMY-AGKIVEEG 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
862-1077 |
6.98e-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: 6.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 862 YNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRktsgYI--EGEIRISGF----LKVQETFARVsGYCEQt 935
Cdd:cd03245 12 YPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL----YKptSGSVLLDGTdirqLDPADLRRNI-GYVPQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 936 DIHSPSITVEESLIYSAwlrlvPEINPQtkirfvkQVLETIELEEIK----------DALVGVAGvSGLSTEQRKRLTVA 1005
Cdd:cd03245 86 DVTLFYGTLRDNITLGA-----PLADDE-------RILRAAELAGVTdfvnkhpnglDLQIGERG-RGLSGGQRQAVALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705989 1006 VELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHQPSihifeaFDELV---LLKRGGRMIYSG 1077
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 ... |
868-1075 |
7.94e-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: 7.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 868 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGrktsgyI----EGEIRISGFLKVQETFARVsGYCEQTDIHSPSIT 943
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILG------IilpdSGEVLFDGKPLDIAARNRI-GYLPEERGLYPKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 944 VEESLIYSAWLRlvpEINPQTKIRFVKQVLETIELEEIKDAlvgvaGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTG 1023
Cdd:cd03269 87 VIDQLVYLAQLK---GLKKEEARRRIDEWLERLELSEYANK-----RVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063705989 1024 LDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRGGRMIY 1075
Cdd:cd03269 159 LDPVNVELLKDVIRELARAGKTVILSTHQME-LVEELCDRVLLLNKGRAVLY 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
153-434 |
1.02e-13 |
|
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: 71.98 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfLLQmcescllffslfyfPQcYGEISYNG 232
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNG-----------------LLK--------------PT-SGEVLVDG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 233 hglnEVVPQKTSAYISQH--------DLHIAEMTTRETIDFSARCQGVgsrtdimmevskrekdggiiPDPEIDAymkai 304
Cdd:COG1122 63 ----KDITKKNLRELRRKvglvfqnpDDQLFAPTVEEDVAFGPENLGL--------------------PREEIRE----- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 305 svkglkrslQTDYILKILGLDICAE----TLvgnamkrgiSGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTA---FQ 377
Cdd:COG1122 114 ---------RVEEALELVGLEHLADrpphEL---------SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRrelLE 175
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705989 378 IIKSLQQvAHITnaTVFVS----LLqpapesYDLFDDIVLMAEGKIVYHGPRDDVLKFFEE 434
Cdd:COG1122 176 LLKRLNK-EGKT--VIIVThdldLV------AELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
876-1047 |
1.33e-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: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 876 AFRPGVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGEiRISGfLKVQE--------TFARVSGYceqtdihsPSIT 943
Cdd:COG0411 26 EVERGEIVGLIGPNGAGKTTLFNLITGfyRPTSGriLFDGR-DITG-LPPHRiarlgiarTFQNPRLF--------PELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 944 VEESL-----------IYSAWLRLVPEINPQTKIR-FVKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVAN 1011
Cdd:COG0411 96 VLENVlvaaharlgrgLLAALLRLPRARREEREAReRAEELLERVGLADRADEPAG-----NLSYGQQRRLEIARALATE 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063705989 1012 PSIIFMDEPTTGLDARAAAIVMRAVKNV-AETGRTIV 1047
Cdd:COG0411 171 PKLLLLDEPAAGLNPEETEELAELIRRLrDERGITIL 207
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
861-1077 |
1.39e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 72.35 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 861 GYNEKKLqlLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIE-GEIRISGFLKVQetFARVSGYCEQTDI 937
Cdd:PRK11231 11 GYGTKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARllTPQSGTVFlGDKPISMLSSRQ--LARRLALLPQHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 938 HSPSITVEESLIY--SAWLRLVPEINPQTKIRfVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSII 1015
Cdd:PRK11231 87 TPEGITVRELVAYgrSPWLSLWGRLSAEDNAR-VNQAMEQTRINHLADRRL-----TDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705989 1016 FMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIH---QPSIHIfeafDELVLLKrGGRMIYSG 1077
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQASRYC----DHLVVLA-NGHVMAQG 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
861-1077 |
1.49e-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: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 861 GYNEKKlQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRktsgYI--EGEIRISGF------LKV---------QE 923
Cdd:cd03254 11 SYDEKK-PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRF----YDpqKGQILIDGIdirdisRKSlrsmigvvlQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 924 TFARVSGYCEQTDIHSPSITVEEsliysaWLRLVPEINPQTKIRFVKQVLETIeleeikdalVGVAGvSGLSTEQRKRLT 1003
Cdd:cd03254 86 TFLFSGTIMENIRLGRPNATDEE------VIEAAKEAGAHDFIMKLPNGYDTV---------LGENG-GNLSQGERQLLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 1004 VAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHQPSIhIFEAfDELVLLKRgGRMIYSG 1077
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLST-IKNA-DKILVLDD-GKIIEEG 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
861-1071 |
3.49e-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: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 861 GYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAgrKTSGYIEGEIRISGfLKVQE----TFARVSGYCEQtD 936
Cdd:cd03251 9 RYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIP--RFYDVDSGRILIDG-HDVRDytlaSLRRQIGLVSQ-D 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 937 IHSPSITVEESLIYSAwlrlvPEINPQTKIRFVKQV--LETI-ELEEIKDALVGVAGVSgLSTEQRKRLTVAVELVANPS 1013
Cdd:cd03251 85 VFLFNDTVAENIAYGR-----PGATREEVEEAARAAnaHEFImELPEGYDTVIGERGVK-LSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705989 1014 IIFMDEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHQPSIhIFEAfDELVLLKRGG 1071
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLST-IENA-DRIVVLEDGK 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
154-423 |
5.34e-13 |
|
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: 69.48 E-value: 5.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLennlkvldifsfgcfllqmcescllffslfyfPQCYGEISYNGH 233
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLL--------------------------------KPTSGSIRVFGK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 234 GLNEV------VPQKTSAyisQHDLHIaemTTRETIdfsarCQGVGSRTDIMMEVSKREKDggiipdpeidaymKAisvk 307
Cdd:cd03235 62 PLEKErkrigyVPQRRSI---DRDFPI---SVRDVV-----LMGLYGHKGLFRRLSKADKA-------------KV---- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 308 glkrslqtDYILKILGLDICAETLVGNAmkrgiSGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVaH 387
Cdd:cd03235 114 --------DEALERVGLSELADRQIGEL-----SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLREL-R 179
|
250 260 270
....*....|....*....|....*....|....*...
gi 1063705989 388 ITNATVFVSL--LQPAPesyDLFDDIVLMAeGKIVYHG 423
Cdd:cd03235 180 REGMTILVVThdLGLVL---EYFDRVLLLN-RTVVASG 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
140-423 |
5.97e-13 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 69.53 E-value: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 140 LKLSGVRTNEANIKILTDVSGIISPGrLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfllqmcescllffslf 219
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILAT-------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 220 YFPQCYGEISYNGHglnEVVPQKTSA-----YISQHDLHIAEMTTRETIDFSARCQGvgsrtdimmevskrekdggiIPD 294
Cdd:cd03264 48 LTPPSSGTIRIDGQ---DVLKQPQKLrrrigYLPQEFGVYPNFTVREFLDYIAWLKG--------------------IPS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 295 PEIDAymkaisvkglkrslQTDYILKILGLDICAETLVGnamkrGISGGQKKRLTTAEMIVGPTKALFMDEITNGLD--S 372
Cdd:cd03264 105 KEVKA--------------RVDEVLELVNLGDRAKKKIG-----SLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDpeE 165
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1063705989 373 STAFQIIksLQQVAhiTNATVFVS--LLQPAPESYdlfDDIVLMAEGKIVYHG 423
Cdd:cd03264 166 RIRFRNL--LSELG--EDRIVILSthIVEDVESLC---NQVAVLNKGKLVFEG 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
868-1053 |
6.42e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 70.33 E-value: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 868 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLaGRKTSGYIEGEIRISGFLKVQETFA--------RVSgYCEQTDIHS 939
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-NRLIELYPEARVSGEVYLDGQDIFKmdvielrrRVQ-MVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 940 PSITVEESLIYSAWLRLVPEINPQTKIRfVKQVLETIEL-EEIKDALVGVAGvsGLSTEQRKRLTVAVELVANPSIIFMD 1018
Cdd:PRK14247 95 PNLSIFENVALGLKLNRLVKSKKELQER-VRWALEKAQLwDEVKDRLDAPAG--KLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063705989 1019 EPTTGLD----ARAAAIVMRAVKNVaetgrTIVCTIHQP 1053
Cdd:PRK14247 172 EPTANLDpentAKIESLFLELKKDM-----TIVLVTHFP 205
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
870-1070 |
9.03e-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: 9.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 870 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGEiRISGfLKVQEtfaRVSGYCEQTDIHSPSITVE 945
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGleRPDSGtiLFGGE-DATD-VPVQE---RNVGFVFQHYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 946 ESLIYSAWLRLVPEINPQTKIRF-VKQVLETIELEEIKDALvgvagVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGL 1024
Cdd:cd03296 93 DNVAFGLRVKPRSERPPEAEIRAkVHELLKLVQLDWLADRY-----PAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063705989 1025 DARAAAIVMRAVKNVA-ETGRTIVCTIHQPSiHIFEAFDELVLLKRG 1070
Cdd:cd03296 168 DAKVRKELRRWLRRLHdELHVTTVFVTHDQE-EALEVADRVVVMNKG 213
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
837-1070 |
9.54e-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: 9.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 837 FKPLTITFQ---DLNYYVDVPVEMKGQGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYIEGEI 913
Cdd:COG2401 10 LMRVTKVYSsvlDLSERVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 914 risgflkvqetfarvsgyceqtDIHSPSITVEESLIYSAWlrlvpeinpqtKIRFVKQVLETIELEEIKDALVGVAGVSG 993
Cdd:COG2401 90 ----------------------DVPDNQFGREASLIDAIG-----------RKGDFKDAVELLNAVGLSDAVLWLRRFKE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 994 LSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVA-ETGRT-IVCTIH-------QPSIHIFEAFDEL 1064
Cdd:COG2401 137 LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLArRAGITlVVATHHydviddlQPDLLIFVGYGGV 216
|
....*.
gi 1063705989 1065 VLLKRG 1070
Cdd:COG2401 217 PEEKRR 222
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
870-1051 |
1.68e-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: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 870 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIE---GEIRIS--GFLKVQETFARVSGYCEQtDIHSPsi 942
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGllRPQSGAVLidgEPLDYSrkGLLERRQRVGLVFQDPDD-QLFAA-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 943 TVEESLIYSAwLRLVpeinpqtkirfvkqvLETIELEE-IKDALVGVaGVSG--------LSTEQRKRLTVAVELVANPS 1013
Cdd:TIGR01166 85 DVDQDVAFGP-LNLG---------------LSEAEVERrVREALTAV-GASGlrerpthcLSGGEKKRVAIAGAVAMRPD 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 1063705989 1014 IIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIH 1051
Cdd:TIGR01166 148 VLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
879-1053 |
2.22e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.59 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 879 PGVLTALMGISGAGKTTLLDVLAG--RKTSGYIEGEIRISGFLKVQEtfarVSGYCEQTDIHSPSITVEESLiysawlrl 956
Cdd:PRK13539 27 AGEALVLTGPNGSGKTTLLRLIAGllPPAAGTIKLDGGDIDDPDVAE----ACHYLGHRNAMKPALTVAENL-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 957 vpeinpqtkiRFVKQVLETIELEeIKDAL--VGVAGVSG-----LSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAA 1029
Cdd:PRK13539 95 ----------EFWAAFLGGEELD-IAAALeaVGLAPLAHlpfgyLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170 180
....*....|....*....|....
gi 1063705989 1030 AIVMRAVKNVAETGRTIVCTIHQP 1053
Cdd:PRK13539 164 ALFAELIRAHLAQGGIVIAATHIP 187
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
878-1047 |
2.78e-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: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 878 RPGVLTALMGISGAGKTTLLDVLAG--RKTSGYI--EGEiRISGflkvQETFARVS---GYCEQT-DIHsPSITVEESLI 949
Cdd:COG0410 27 EEGEIVALLGRNGAGKTTLLKAISGllPPRSGSIrfDGE-DITG----LPPHRIARlgiGYVPEGrRIF-PSLTVEENLL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 950 YSAWLRlvpeinpqTKIRFVKQVLETI-----ELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGL 1024
Cdd:COG0410 101 LGAYAR--------RDRAEVRADLERVyelfpRLKERRRQRAGT-----LSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
170 180
....*....|....*....|...
gi 1063705989 1025 DARAAAIVMRAVKNVAETGRTIV 1047
Cdd:COG0410 168 APLIVEEIFEIIRRLNREGVTIL 190
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
140-418 |
3.32e-12 |
|
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: 66.25 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 140 LKLSGV--RTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfllqmcescllffs 217
Cdd:cd03228 1 IEFKNVsfSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLR------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 218 lFYFPQCyGEISYNGHGLNEVVPQ---KTSAYISQHDlHIAEMTTRETIdfsarcqgvgsrtdimmevskrekdggiipd 294
Cdd:cd03228 51 -LYDPTS-GEILIDGVDLRDLDLEslrKNIAYVPQDP-FLFSGTIRENI------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 295 peidaymkaisvkglkrslqtdyilkilgldicaetlvgnamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSST 374
Cdd:cd03228 97 ---------------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1063705989 375 AFQIIKSLQQVAHitNATVFV-----SLLQpapesydLFDDIVLMAEGK 418
Cdd:cd03228 132 EALILEALRALAK--GKTVIViahrlSTIR-------DADRIIVLDDGR 171
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
870-1070 |
3.55e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.71 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 870 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISG----FLKVQETFArvSG----YCEqtdIH-SP 940
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD--AGSILIDGqemrFASTTAALA--AGvaiiYQE---LHlVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 941 SITVEESLiysaWLRLVPE----INPQTKIRFVKQvletiELEEIKDALVGVAGVSGLSTEQRKRLTVAVELVANPSIIF 1016
Cdd:PRK11288 93 EMTVAENL----YLGQLPHkggiVNRRLLNYEARE-----QLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 1017 MDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRG 1070
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRME-EIFALCDAITVFKDG 216
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
852-1078 |
4.36e-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: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 852 DVPVEMKG--QGYNEKklQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGflkvqETFAR 927
Cdd:COG1127 3 EPMIEVRNltKSFGDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGllRPDSG----EILVDG-----QDITG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 928 VSGYcEQTDIHSP------------SITVEESLIYsaWLRLVPEINPQTKIRFVKQVLEtieleeikdaLVGVAGV---- 991
Cdd:COG1127 72 LSEK-ELYELRRRigmlfqggalfdSLTVFENVAF--PLREHTDLSEAEIRELVLEKLE----------LVGLPGAadkm 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 992 -SGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAET-GRTIVCTIHQ-PSihIFEAFDELVLLK 1068
Cdd:COG1127 139 pSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDlDS--AFAIADRVAVLA 216
|
250
....*....|
gi 1063705989 1069 RgGRMIYSGP 1078
Cdd:COG1127 217 D-GKIIAEGT 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
152-429 |
4.55e-12 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 70.32 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 152 IKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfLLQmcescllffslfyfPQCyGEISYN 231
Cdd:COG1123 278 VRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG-----------------LLR--------------PTS-GSILFD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 232 GHGLNEVVPQKTSA------YISQHDLH--IAEMTTRETIDFSARCQGVGSRTDImmevskREKdggiipdpeIDAYMKA 303
Cdd:COG1123 326 GKDLTKLSRRSLRElrrrvqMVFQDPYSslNPRMTVGDIIAEPLRLHGLLSRAER------RER---------VAELLER 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 304 IsvkGLKRSLQTDYIlkilgldicaetlvgnamkRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQ 383
Cdd:COG1123 391 V---GLPPDLADRYP-------------------HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLR 448
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1063705989 384 QVAHITNAT-VFVSllqpapesYDL------FDDIVLMAEGKIVYHGPRDDVL 429
Cdd:COG1123 449 DLQRELGLTyLFIS--------HDLavvryiADRVAVMYDGRIVEDGPTEEVF 493
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
153-423 |
4.85e-12 |
|
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: 65.92 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfllqmcescllffslfYFPQCYGEISYNG 232
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAG--------------------------------LLKPSSGEILLDG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 233 HGLNEVVPQKTS---AYISQhdlhiaemttretidfsarcqgvgsrtdimmevskrekdggiipdpeidaYMKAISVKGL 309
Cdd:cd03214 61 KDLASLSPKELArkiAYVPQ--------------------------------------------------ALELLGLAHL 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 310 K-RSLQTdyilkilgldicaetlvgnamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHI 388
Cdd:cd03214 91 AdRPFNE------------------------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARE 146
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1063705989 389 TNATVFVSLlqpapesYDL------FDDIVLMAEGKIVYHG 423
Cdd:cd03214 147 RGKTVVMVL-------HDLnlaaryADRVILLKDGRIVAQG 180
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
151-420 |
7.04e-12 |
|
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: 66.13 E-value: 7.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 151 NIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfLLQmcescllffslfyfpQCYGEISY 230
Cdd:cd03226 12 GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG-----------------LIK---------------ESSGSILL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 231 NGHGLNEVVPQKTSAYISQH-DLHIAEMTTRETIDFSArcqgvgsrtdimmevskrekdggiipdPEIDAYMKaisvkgl 309
Cdd:cd03226 60 NGKPIKAKERRKSIGYVMQDvDYQLFTDSVREELLLGL---------------------------KELDAGNE------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 310 krslQTDYILKILGLDICAEtlvgnAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHIT 389
Cdd:cd03226 106 ----QAETVLKDLDLYALKE-----RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQG 176
|
250 260 270
....*....|....*....|....*....|....*
gi 1063705989 390 NATVFVS----LLqpapesYDLFDDIVLMAEGKIV 420
Cdd:cd03226 177 KAVIVIThdyeFL------AKVCDRVLLLANGAIV 205
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
164-423 |
2.90e-11 |
|
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: 64.62 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 164 PGRLTLLLGPPGCGKTTLLKALSGnlennLKVLDIfsfgcfllqmcescllffslfyfpqcyGEISYNGHGLNEvvpQKT 243
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAG-----LEKPDG---------------------------GTIVLNGTVLFD---SRK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 244 SAYISQHDLHIA----------EMTTRETIDFSARCQGVGSRTDimmevskrekdggiipdpeidaymkaisvkglkrsl 313
Cdd:cd03297 67 KINLPPQQRKIGlvfqqyalfpHLNVRENLAFGLKRKRNREDRI------------------------------------ 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 314 QTDYILKILGLDicaetLVGNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATV 393
Cdd:cd03297 111 SVDELLDLLGLD-----HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPV 185
|
250 260 270
....*....|....*....|....*....|.
gi 1063705989 394 -FVSllQPAPESYDLFDDIVLMAEGKIVYHG 423
Cdd:cd03297 186 iFVT--HDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
140-428 |
3.06e-11 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 65.05 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKvldifsfgcfllqmcescllffslf 219
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG-LERPDS------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 220 yfpqcyGEISYNGHGLNEVVPQKTS-AYISQHDLHIAEMTTRETIDFSARCQGVGSRTdimmevskrekdggiiPDPEID 298
Cdd:cd03296 57 ------GTILFGGEDATDVPVQERNvGFVFQHYALFRHMTVFDNVAFGLRVKPRSERP----------------PEAEIR 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 299 AYMKAisvkglkrslqtdyILKILGLDicaetLVGNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQI 378
Cdd:cd03296 115 AKVHE--------------LLKLVQLD-----WLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKEL 175
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1063705989 379 IKSLQQV---AHITnaTVFVSLLQpaPESYDLFDDIVLMAEGKIVYHGPRDDV 428
Cdd:cd03296 176 RRWLRRLhdeLHVT--TVFVTHDQ--EEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
880-1077 |
3.19e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.42 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 880 GVLTALMGISGAGKTTLLdvlagRKTSGYIEG----EIRISGFLKVQETFARVSGYCEQTDIHSPSI----------TVE 945
Cdd:PRK09984 30 GEMVALLGPSGSGKSTLL-----RHLSGLITGdksaGSHIELLGRTVQREGRLARDIRKSRANTGYIfqqfnlvnrlSVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 946 ESLIYSA------WLRLVPEINPQTKIRFVKQvletieLEEIKDALVGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDE 1019
Cdd:PRK09984 105 ENVLIGAlgstpfWRTCFSWFTREQKQRALQA------LTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705989 1020 PTTGLDARAAAIVMRAVKNVAET-GRTIVCTIHQPSIHIfeAFDELVLLKRGGRMIYSG 1077
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYAL--RYCERIVALRQGHVFYDG 235
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
868-1078 |
3.38e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.41 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 868 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYI--EGE---IRISGFLKVQETFARVSGYCEQ----TD 936
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGllRPQKGAVlwQGKpldYSKRGLLALRQQVATVFQDPEQqifyTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 937 IHSpsitveeSLIYSAWLRLVPEinpQTKIRFVKQVLETIELEEIKDAlvgvaGVSGLSTEQRKRLTVAVELVANPSIIF 1016
Cdd:PRK13638 95 IDS-------DIAFSLRNLGVPE---AEITRRVDEALTLVDAQHFRHQ-----PIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705989 1017 MDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIhIFEAFDELVLLKRGGRMIYSGP 1078
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 ... |
869-1053 |
3.59e-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: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 869 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIEGEIRISGFlkVQETFARVSGYCEQTDIHSPSITVEE 946
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGlsPPLAGRVLLNGGPLDF--QRDSIARGLLYLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 947 SLiysawlRLVPEINPQTKIrfvKQVLETIELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDA 1026
Cdd:cd03231 93 NL------RFWHADHSDEQV---EEALARVGLNGFEDRPVAQ-----LSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180
....*....|....*....|....*..
gi 1063705989 1027 RAAAIVMRAVKNVAETGRTIVCTIHQP 1053
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
869-1070 |
3.61e-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: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 869 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAgrktsgyieGEI-RISGFLKVQETFArvsgYCEQTdihsPSI---TV 944
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALL---------GELeKLSGSVSVPGSIA----YVSQE----PWIqngTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 945 EESLIYSAwlrlvpEINPQtkirFVKQVLETIELEEIKDAL-------VGVAGVSgLSTEQRKRLTVAVELVANPSIIFM 1017
Cdd:cd03250 83 RENILFGK------PFDEE----RYEKVIKACALEPDLEILpdgdlteIGEKGIN-LSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 1018 DEPTTGLDAR-AAAIVMRAVKNVAETGRTIVCTIHQpsIHIFEAFDELVLLKRG 1070
Cdd:cd03250 152 DDPLSAVDAHvGRHIFENCILGLLLNNKTRILVTHQ--LQLLPHADQIVVLDNG 203
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
877-1047 |
3.69e-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: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 877 FRPGVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGEiRISGFLKVQ-ETFARVSGYCEQTDIHS--PSITVEESLi 949
Cdd:COG1123 288 LRRGETLGLVGESGSGKSTLARLLLGllRPTSGsiLFDGK-DLTKLSRRSlRELRRRVQMVFQDPYSSlnPRMTVGDII- 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 950 ySAWLRLVPEINPQTKIRFVKQVLETIEL-EEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARA 1028
Cdd:COG1123 366 -AEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPH-----ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSV 439
|
170 180
....*....|....*....|
gi 1063705989 1029 AAIVMRAVKNV-AETGRTIV 1047
Cdd:COG1123 440 QAQILNLLRDLqRELGLTYL 459
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
878-1074 |
4.49e-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: 4.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 878 RPGVLTALMGISGAGKTTLLDVLAG--RKTSgyieGEIRISGfLKVQETFARVsGYCEQTDIHSPSITVEESLIysawlr 955
Cdd:cd03293 28 EEGEFVALVGPSGCGKSTLLRIIAGleRPTS----GEVLVDG-EPVTGPGPDR-GYVFQQDALLPWLTVLDNVA------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 956 LVPEINPQTKIRFVKQVLETIEleeikdaLVGVAGVSG-----LSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAA 1030
Cdd:cd03293 96 LGLELQGVPKAEARERAEELLE-------LVGLSGFENayphqLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTRE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063705989 1031 IVMRAVKNV-AETGRTIVCTIHQpsihIFEAF---DELVLL-KRGGRMI 1074
Cdd:cd03293 169 QLQEELLDIwRETGKTVLLVTHD----IDEAVflaDRVVVLsARPGRIV 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
137-429 |
4.79e-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: 67.24 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 137 LDLLKLSgVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLKVldifsfgcfllqmcescllff 216
Cdd:COG1123 5 LEVRDLS-VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRI--------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 217 slfyfpqcYGEISYNGH---GLNEVVPQKTSAYISQH-DLHIAEMTTRETIDFSARCQGVgSRTDIMMEVSKrekdggii 292
Cdd:COG1123 63 --------SGEVLLDGRdllELSEALRGRRIGMVFQDpMTQLNPVTVGDQIAEALENLGL-SRAEARARVLE-------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 293 pdpeidaymkaisvkglkrslqtdyILKILGLDicaetlvgNAMKRGI---SGGQKKRLTTAEMIVGPTKALFMDEITNG 369
Cdd:COG1123 126 -------------------------LLEAVGLE--------RRLDRYPhqlSGGQRQRVAIAMALALDPDLLIADEPTTA 172
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705989 370 LDSSTAFQIIKSLQQVAHITNATV-FVSllQPAPESYDLFDDIVLMAEGKIVYHGPRDDVL 429
Cdd:COG1123 173 LDVTTQAEILDLLRELQRERGTTVlLIT--HDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
155-395 |
5.53e-11 |
|
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: 66.93 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 155 LTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfLLQMCEscllffslfyfpqcyGEISYNGHG 234
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG-----------------FVDPTE---------------GSIAVNGVP 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 235 LNEVVP---QKTSAYISQHDlHIAEMTTRETIDFSarcQGVGSRTDImmevskrekdggiipdpeIDAYMKAisvkGLKR 311
Cdd:TIGR02857 386 LADADAdswRDQIAWVPQHP-FLFAGTIAENIRLA---RPDASDAEI------------------REALERA----GLDE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 312 SLQTdyilkiLGLDIcaETLVGNAmKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAhiTNA 391
Cdd:TIGR02857 440 FVAA------LPQGL--DTPIGEG-GAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGR 508
|
....
gi 1063705989 392 TVFV 395
Cdd:TIGR02857 509 TVLL 512
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
1219-1383 |
5.71e-11 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 63.30 E-value: 5.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1219 FTVLGAIYGLVLFVGINNCTSALqYFETERNVMYRERFAGMySAFAYALAQVVTEIPYIFIQSAEFVIVIYPMIGFYASF 1298
Cdd:COG0842 4 FLVPGLLAMSLLFTALMLTALSI-AREREQGTLERLLVTPV-SRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1299 SKVFWSLYAMFCNLLCFNYLAMFLISITPNFMVAAILQSLFFTTFNIFAGFLIPKPQIPKWWVWFYYITPTSWTLNLFFS 1378
Cdd:COG0842 82 LSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRA 161
|
....*
gi 1063705989 1379 SQYGD 1383
Cdd:COG0842 162 LFLGG 166
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
141-418 |
5.99e-11 |
|
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: 62.26 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 141 KLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLennlkvldifsfgcfllqmcescllffslfy 220
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 221 fPQCYGEISYNGHGLNEVVPQKTSAYIsqhdlhiaemttretidfsarcqgvgsrtdimmevskrekdgGIIPdpeiday 300
Cdd:cd00267 50 -KPTSGEILIDGKDIAKLPLEELRRRI------------------------------------------GYVP------- 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 301 mkaisvkglkrslqtdyilkilgldicaetlvgnamkrGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIK 380
Cdd:cd00267 80 --------------------------------------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLE 121
|
250 260 270
....*....|....*....|....*....|....*...
gi 1063705989 381 SLQQVAhITNATVFVSLLQPaPESYDLFDDIVLMAEGK 418
Cdd:cd00267 122 LLRELA-EEGRTVIIVTHDP-ELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
842-1077 |
9.88e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 64.48 E-value: 9.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 842 ITFQDLNY-YVDVPVEMKGQGYNEKKlqllseitgafrpGVLTALMGISGAGKTTLLDVLAG--RKTSGYI-----EGEI 913
Cdd:PRK13636 6 LKVEELNYnYSDGTHALKGININIKK-------------GEVTAILGGNGAGKSTLFQNLNGilKPSSGRIlfdgkPIDY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 914 RISGFLKVQETFARVSgycEQTDIHSPSITVEESLIYSAWLRLVPEINPQTKIRfvkQVLETIELEEIKDAlvgvaGVSG 993
Cdd:PRK13636 73 SRKGLMKLRESVGMVF---QDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVD---NALKRTGIEHLKDK-----PTHC 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 994 LSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVA-ETGRTIVCTIHqpSIHIFEAFDELVLLKRGGR 1072
Cdd:PRK13636 142 LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQkELGLTIIIATH--DIDIVPLYCDNVFVMKEGR 219
|
....*
gi 1063705989 1073 MIYSG 1077
Cdd:PRK13636 220 VILQG 224
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
877-1077 |
1.11e-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: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 877 FRPGVLTALMGISGAGKTTLLDVLAGRKtsGY--IEGEIRISG----FLKVQETFARVSGYCEQTDIHSPSITVEESLIY 950
Cdd:COG0396 23 IKPGEVHAIMGPNGSGKSTLAKVLMGHP--KYevTSGSILLDGedilELSPDERARAGIFLAFQYPVEIPGVSVSNFLRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 951 SAWLRLVPEINPQTKIRFVKQVLETIELEEikDAL---VGVagvsGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDAR 1027
Cdd:COG0396 101 ALNARRGEELSAREFLKLLKEKMKELGLDE--DFLdryVNE----GFSGGEKKRNEILQMLLLEPKLAILDETDSGLDID 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063705989 1028 AAAIVMRAVKNVAETGRTIVCTIHQPSI--HIfEAfDELVLLKrGGRMIYSG 1077
Cdd:COG0396 175 ALRIVAEGVNKLRSPDRGILIITHYQRIldYI-KP-DFVHVLV-DGRIVKSG 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
877-1047 |
1.30e-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: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 877 FRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGflkvqetfarvsgycEQTDIHSPS------ItveeSL 948
Cdd:COG1129 27 LRPGEVHALLGENGAGKSTLMKILSGvyQPDSG----EILLDG---------------EPVRFRSPRdaqaagI----AI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 949 IYSAwLRLVPEI---------NPQTKIRFV---------KQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVA 1010
Cdd:COG1129 84 IHQE-LNLVPNLsvaeniflgREPRRGGLIdwramrrraRELLARLGLDIDPDTPVG-----DLSVAQQQLVEIARALSR 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063705989 1011 NPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIV 1047
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLFRIIRRLKAQGVAII 194
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
876-1077 |
1.32e-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: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 876 AFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYieGEIRISGflkVQETFAR-----VSGYCEQTDIHsPSITVEESLIY 950
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQS--GRVLING---VDVTAAPpadrpVSMLFQENNLF-AHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 951 SawlrlvpeINPQTKIRFVKQvletielEEIKDAL--VGVAGV-----SGLSTEQRKRLTVAVELVANPSIIFMDEPTTG 1023
Cdd:cd03298 94 G--------LSPGLKLTAEDR-------QAIEVALarVGLAGLekrlpGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063705989 1024 LD-ARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRgGRMIYSG 1077
Cdd:cd03298 159 LDpALRAEMLDLVLDLHAETKMTVLMVTHQPE-DAKRLAQRVVFLDN-GRIAAQG 211
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
151-430 |
2.04e-10 |
|
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: 62.56 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 151 NIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKalsgnlennlkvldifsfgcfLLQMcescllffslFYFPqCYGEISY 230
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVS---------------------LLER----------FYDP-TSGEILL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 231 NGHGLNEVVPQKTS---AYISQhDLHIAEMTTRETIDFsarcqGVGSRTDIMMEVSKREKdggiipdpEIDAYmkaisvk 307
Cdd:cd03249 63 DGVDIRDLNLRWLRsqiGLVSQ-EPVLFDGTIAENIRY-----GKPDATDEEVEEAAKKA--------NIHDF------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 308 glkrslqtdyilkILGLDICAETLVGNamkRG--ISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQV 385
Cdd:cd03249 122 -------------IMSLPDGYDTLVGE---RGsqLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA 185
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1063705989 386 ahITNATVFV-----SLLQPApesydlfDDIVLMAEGKIVYHGPRDDVLK 430
Cdd:cd03249 186 --MKGRTTIViahrlSTIRNA-------DLIAVLQNGQVVEQGTHDELMA 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
154-429 |
2.11e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 62.87 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlkvldifsfgcfllqmcescllffslfyfPQCyGEISYNGH 233
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELS-------------------------------PDS-GEVRLNGR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 234 GLNEVVPQ---KTSAYISQHdlhiaemtTRETIDFSARcqgvgsrtdimmEV----------SKREKdggiipDPEIDAY 300
Cdd:PRK13548 65 PLADWSPAelaRRRAVLPQH--------SSLSFPFTVE------------EVvamgraphglSRAED------DALVAAA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 301 MKAISVKGLK-RSLQTdyilkilgldicaetlvgnamkrgISGGQKKRLTTAEMIV------GPTKALFMDEITNGLDSS 373
Cdd:PRK13548 119 LAQVDLAHLAgRDYPQ------------------------LSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLA 174
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705989 374 TAFQIIKSLQQVAHITNATVFVSLlqpapesYDL------FDDIVLMAEGKIVYHGPRDDVL 429
Cdd:PRK13548 175 HQHHVLRLARQLAHERGLAVIVVL-------HDLnlaaryADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
140-419 |
2.14e-10 |
|
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: 62.12 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 140 LKLSGVR----TNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkVLDIFSfgcfllqmcescllf 215
Cdd:cd03255 1 IELKNLSktygGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG-------LDRPTS--------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 216 fslfyfpqcyGEISYNGHGLNEVVPQKTSAY----IS----QHDLhIAEMTTRETIDFSARCQGVGSRtdimmevskrek 287
Cdd:cd03255 59 ----------GEVRVDGTDISKLSEKELAAFrrrhIGfvfqSFNL-LPDLTALENVELPLLLAGVPKK------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 288 dggiipdpeiDAYMKAISVkglkrslqtdyiLKILGLDICAETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEIT 367
Cdd:cd03255 116 ----------ERRERAEEL------------LERVGLGDRLNHYPSE-----LSGGQQQRVAIARALANDPKIILADEPT 168
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1063705989 368 NGLDSSTAFQIIKSLQQVAHITNAT-VFVSllqPAPESYDLFDDIVLMAEGKI 419
Cdd:cd03255 169 GNLDSETGKEVMELLRELNKEAGTTiVVVT---HDPELAEYADRIIELRDGKI 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
880-1051 |
2.27e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.17 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 880 GVLTALMGISGAGKTTLLDVLAG--RKTSG--YIEGE-IRIS--GFLKVQETFARVSgycEQTD--IHSPsiTVEESLIY 950
Cdd:PRK13639 28 GEMVALLGPNGAGKSTLFLHFNGilKPTSGevLIKGEpIKYDkkSLLEVRKTVGIVF---QNPDdqLFAP--TVEEDVAF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 951 SAWLRLVPEinpqtkirfvkqvlETIElEEIKDALVGVaGVSG--------LSTEQRKRLTVAVELVANPSIIFMDEPTT 1022
Cdd:PRK13639 103 GPLNLGLSK--------------EEVE-KRVKEALKAV-GMEGfenkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180
....*....|....*....|....*....
gi 1063705989 1023 GLDARAAAIVMRAVKNVAETGRTIVCTIH 1051
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
869-1054 |
2.30e-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: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 869 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRktsgYI--EGEIRISGF---LKVQETFARVSGYCEQtdihspsit 943
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF----YVpeNGRVLVDGHdlaLADPAWLRRQVGVVLQ--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 944 veESLIYSAWLR----LVPEINPQTKIRFVKQVLET----IELEEIKDALVGVAGVsGLSTEQRKRLTVAVELVANPSII 1015
Cdd:cd03252 84 --ENVLFNRSIRdniaLADPGMSMERVIEAAKLAGAhdfiSELPEGYDTIVGEQGA-GLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063705989 1016 FMDEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHQPS 1054
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLS 198
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
870-1078 |
2.57e-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: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 870 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAGrKTSGyiEGEIRISGF----LKVQEtFARVSGYCEQTDIHSPSITVE 945
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPG--QGEILLNGRplsdWSAAE-LARHRAYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 946 EsliYSAwLRLVPEINPQTKIRFVKQVLETIELEeikDALvgVAGVSGLS-TE-QRKRLtVAVEL----VANPS--IIFM 1017
Cdd:COG4138 88 Q---YLA-LHQPAGASSEAVEQLLAQLAEALGLE---DKL--SRPLTQLSgGEwQRVRL-AAVLLqvwpTINPEgqLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705989 1018 DEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIHIFEAfDELVLLKRgGRMIYSGP 1078
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHA-DRVWLLKQ-GKLVASGE 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
869-1078 |
2.77e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.09 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 869 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGflkvqetfarvsgyceqTDIHSPSITVEESL 948
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT--AGTVLVAG-----------------DDVEALSARAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 949 IYSawlrlVPEinpQTKIRF---VKQVLE-----------------TIELEEIKDAlVGVAG-----VSGLSTEQRKRLT 1003
Cdd:PRK09536 79 VAS-----VPQ---DTSLSFefdVRQVVEmgrtphrsrfdtwtetdRAAVERAMER-TGVAQfadrpVTSLSGGERQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705989 1004 VAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHqpSIHIFEAF-DELVLLKrGGRMIYSGP 1078
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIH--DLDLAARYcDELVLLA-DGRVRAAGP 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
153-419 |
3.88e-10 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 60.49 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkvldifsfgcfllqmcescllffslfyfpqcYGEISYNG 232
Cdd:cd03230 14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD--------------------------------SGEIKVLG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 233 HGLNEVVPQ--KTSAYISQHDLHIAEMTTRETIDFSarcqgvgsrtdimmevskrekdggiipdpeidaymkaisvkglk 310
Cdd:cd03230 62 KDIKKEPEEvkRRIGYLPEEPSLYENLTVRENLKLS-------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 311 rslqtdyilkilgldicaetlvgnamkrgisGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTA---FQIIKSLQQvah 387
Cdd:cd03230 98 -------------------------------GGMKQRLALAQALLHDPELLILDEPTSGLDPESRrefWELLRELKK--- 143
|
250 260 270
....*....|....*....|....*....|....
gi 1063705989 388 iTNATVFVS--LLQPAPEsydLFDDIVLMAEGKI 419
Cdd:cd03230 144 -EGKTILLSshILEEAER---LCDRVAILNNGRI 173
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
820-1047 |
5.02e-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: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 820 LDSSIKTNEDPGKMILPFKPLTITFQDLNYyvdvpvemkgqGYNEKKlQLLSEITGAFRPGVLTALMGISGAGKTTLLDV 899
Cdd:COG1132 318 LDEPPEIPDPPGAVPLPPVRGEIEFENVSF-----------SYPGDR-PVLKDISLTIPPGETVALVGPSGSGKSTLVNL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 900 LAGRktsgY--IEGEIRISGflkvqetfarvsgyceqTDIHSpsITVEEsliysawLR----LVPE--------I--Npq 963
Cdd:COG1132 386 LLRF----YdpTSGRILIDG-----------------VDIRD--LTLES-------LRrqigVVPQdtflfsgtIreN-- 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 964 tkIRF---------VKQVLETIELEE-IK------DALVGVAGVSgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDAR 1027
Cdd:COG1132 434 --IRYgrpdatdeeVEEAAKAAQAHEfIEalpdgyDTVVGERGVN-LSGGQRQRIAIARALLKDPPILILDEATSALDTE 510
|
250 260
....*....|....*....|
gi 1063705989 1028 AAAIVMRAVKNVAEtGRTIV 1047
Cdd:COG1132 511 TEALIQEALERLMK-GRTTI 529
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
862-1032 |
5.35e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 61.72 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 862 YNEKKLqlLSEITGAFRPGVLTALMGISGAGKTTLLDVLagrKTSGYIEGEIRISGFLKvqetFARVSGYCEQTD----- 936
Cdd:PRK14239 15 YNKKKA--LNSVSLDFYPNEITALIGPSGSGKSTLLRSI---NRMNDLNPEVTITGSIV----YNGHNIYSPRTDtvdlr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 937 ------IHSPS---ITVEESLIYSawLRLVPEINPQTKIRFVKQVLETIEL-EEIKDALVGVAgvSGLSTEQRKRLTVAV 1006
Cdd:PRK14239 86 keigmvFQQPNpfpMSIYENVVYG--LRLKGIKDKQVLDEAVEKSLKGASIwDEVKDRLHDSA--LGLSGGQQQRVCIAR 161
|
170 180
....*....|....*....|....*.
gi 1063705989 1007 ELVANPSIIFMDEPTTGLDARAAAIV 1032
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKI 187
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
140-420 |
5.98e-10 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 60.73 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLEnnlkvlDIFSfgcfllqmcescllffslf 219
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAG-LE------EPTS------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 220 yfpqcyGEISYNGHGLNEVVPQKTS-AYISQHDLHIAEMTTRETIDFSARCQGVgsrtdimmevskrekdggiiPDPEID 298
Cdd:cd03301 55 ------GRIYIGGRDVTDLPPKDRDiAMVFQNYALYPHMTVYDNIAFGLKLRKV--------------------PKDEID 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 299 aymkaisvkglKRSLQTDYILKIlgldicaETLVGNAMKRgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQI 378
Cdd:cd03301 109 -----------ERVREVAELLQI-------EHLLDRKPKQ-LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQM 169
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1063705989 379 ---IKSLQQVAHITnaTVFVSLLQpaPESYDLFDDIVLMAEGKIV 420
Cdd:cd03301 170 raeLKRLQQRLGTT--TIYVTHDQ--VEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
153-428 |
6.52e-10 |
|
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: 61.04 E-value: 6.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkvldifsfgcfllqmcescllffslfyfpqcYGEISYNG 232
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT--------------------------------SGSVLIDG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 233 HGLNEVVPQKT------SAYISQHDLHIAEMTTRETIdFSARcqgVGSRT---DIMMEVSKREKDGGIipdpeidaymka 303
Cdd:cd03256 63 TDINKLKGKALrqlrrqIGMIFQQFNLIERLSVLENV-LSGR---LGRRStwrSLFGLFPKEEKQRAL------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 304 isvkglkrslqtdYILKILGLDICAETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQ 383
Cdd:cd03256 127 -------------AALERVGLLDKAYQRADQ-----LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLK 188
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1063705989 384 QVAHITNATVFVSLLQPapesyDL----FDDIVLMAEGKIVYHGPRDDV 428
Cdd:cd03256 189 RINREEGITVIVSLHQV-----DLareyADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
140-428 |
7.16e-10 |
|
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: 60.66 E-value: 7.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLKVLDifsfgcfllqmcescllffslf 219
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPD---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 220 yfpqcYGEISYNGHGLNEV-------------VPQKTSAYisqhdlhiaEMTTRETIDFSARCQGVGSRTDimmevskre 286
Cdd:cd03260 59 -----EGEVLLDGKDIYDLdvdvlelrrrvgmVFQKPNPF---------PGSIYDNVAYGLRLHGIKLKEE--------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 287 kdggiipdpeidayMKAISVKGLKRSLQTDYILKilgldicaetlvgNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEI 366
Cdd:cd03260 116 --------------LDERVEEALRKAALWDEVKD-------------RLHALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705989 367 TNGLDSSTAFQI---IKSLQQVAHItnatVFVS--LLQPAPESydlfDDIVLMAEGKIVYHGPRDDV 428
Cdd:cd03260 169 TSALDPISTAKIeelIAELKKEYTI----VIVThnMQQAARVA----DRTAFLLNGRLVEFGPTEQI 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
862-1077 |
1.08e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.79 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 862 YNEK---KLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYieGEIRISGF-LKVQETFARVSGYCEQTDI 937
Cdd:PRK13631 31 FDEKqenELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKY--GTIQVGDIyIGDKKNNHELITNPYSKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 938 HS--------------PSI-----TVEESLIYSawlrlvPEINPQTKIRFVKQVLETIELEEIKDALVGVAGVsGLSTEQ 998
Cdd:PRK13631 109 KNfkelrrrvsmvfqfPEYqlfkdTIEKDIMFG------PVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPF-GLSGGQ 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705989 999 RKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRgGRMIYSG 1077
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 ... |
867-1052 |
1.27e-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: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 867 LQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGFLKVQETFARV---SGYCEQTDIHSP--- 940
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQT--LEGKVHWSNKNESEPSFEATrsrNRYSVAYAAQKPwll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 941 SITVEESLIYSAwlrlvpeinPQTKIRFvKQVLETIELEEIKDAL-------VGVAGVSgLSTEQRKRLTVAVELVANPS 1013
Cdd:cd03290 92 NATVEENITFGS---------PFNKQRY-KAVTDACSLQPDIDLLpfgdqteIGERGIN-LSGGQRQRICVARALYQNTN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063705989 1014 IIFMDEPTTGLDARAAAIVMRA--VKNVAETGRTIVCTIHQ 1052
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHK 201
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
865-1051 |
1.31e-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: 60.25 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 865 KKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIE-GEIRISGfLKVQETfARVS-GYCEQtdihSP 940
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGlvKPDSGKILlDGQDITK-LPMHKR-ARLGiGYLPQ----EA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 941 SI----TVEESLiysawlRLVPEINPQTK---IRFVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPS 1013
Cdd:cd03218 85 SIfrklTVEENI------LAVLEIRGLSKkerEEKLEELLEEFHITHLRKSKA-----SSLSGGERRRVEIARALATNPK 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1063705989 1014 IIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIH 1051
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDH 191
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
140-430 |
1.45e-09 |
|
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: 60.14 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfllqmcescllffslF 219
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISG-------------------------------F 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 220 YFPQcYGEISYNGHGLNEVVPQKTSAY-IS---QHDLHIAEMTTRETIDFSARCQgvgSRTDIMMEVSKREKdggiipdP 295
Cdd:cd03219 50 LRPT-SGSVLFDGEDITGLPPHEIARLgIGrtfQIPRLFPELTVLENVMVAAQAR---TGSGLLLARARREE-------R 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 296 EIDAymkaisvkglkrslQTDYILKILGLDICAETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTA 375
Cdd:cd03219 119 EARE--------------RAEELLERVGLADLADRPAGE-----LSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEET 179
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705989 376 FQIIKSLQQVAHITNATVFV----SLLqpapesYDLFDDIVLMAEGKIVYHGPRDDVLK 430
Cdd:cd03219 180 EELAELIRELRERGITVLLVehdmDVV------MSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
880-1078 |
1.48e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.67 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 880 GVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGFLKVQETFARVSGYC---EQTDIHSPsITVEESLI----- 949
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGfvRLASG----KISILGQPTRQALQKNLVAYVpqsEEVDWSFP-VLVEDVVMmgryg 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 950 YSAWLRLVPEINPQTkirfVKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAA 1029
Cdd:PRK15056 108 HMGWLRRAKKRDRQI----VTAALARVDMVEFRHRQIG-----ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063705989 1030 AIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKrgGRMIYSGP 1078
Cdd:PRK15056 179 ARIISLLRELRDEGKTMLVSTHNLG-SVTEFCDYTVMVK--GTVLASGP 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
142-430 |
1.83e-09 |
|
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: 59.82 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 142 LSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfLLQmcescllffslfyf 221
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVG-----------------LLR-------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 222 pqcygeisynghglnevvPQKTSAYISQHDlhIAEMTTRETIDFSARC----QGVGSRTDimMEVSK------REKdgGI 291
Cdd:cd03261 52 ------------------PDSGEVLIDGED--ISGLSEAELYRLRRRMgmlfQSGALFDS--LTVFEnvafplREH--TR 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 292 IPDPEIDaymkaisvkglkrslqtdyilkilglDICAETL--VG-----NAMKRGISGGQKKRLTTAEMIVGPTKALFMD 364
Cdd:cd03261 108 LSEEEIR--------------------------EIVLEKLeaVGlrgaeDLYPAELSGGMKKRVALARALALDPELLLYD 161
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705989 365 EITNGLD--SSTAF-QIIKSLQQVAHITnaTVFVSllQPAPESYDLFDDIVLMAEGKIVYHGPRDDVLK 430
Cdd:cd03261 162 EPTAGLDpiASGVIdDLIRSLKKELGLT--SIMVT--HDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
140-449 |
1.85e-09 |
|
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: 59.56 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfllqmcescllffslF 219
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAG-------------------------------F 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 220 YFPQCyGEISYNGHGLNEVVPQK-TSAYISQHDLHIAEMTTRETIDFSARCQGVgSRTDIMMEVSKrekdggiipdpeid 298
Cdd:cd03300 50 ETPTS-GEILLDGKDITNLPPHKrPVNTVFQNYALFPHLTVFENIAFGLRLKKL-PKAEIKERVAE-------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 299 aYMKAISVKGLkrslqtdyilkilgldicaetlvGNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSS--TAF 376
Cdd:cd03300 114 -ALDLVQLEGY-----------------------ANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKlrKDM 169
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705989 377 QI-IKSLQQVAHITnaTVFVSLLQpaPESYDLFDDIVLMAEGKIVYHG-PRDdvlkFFEEcgfqcPERKGVADFL 449
Cdd:cd03300 170 QLeLKRLQKELGIT--FVFVTHDQ--EEALTMSDRIAVMNKGKIQQIGtPEE----IYEE-----PANRFVADFI 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
868-1054 |
2.29e-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: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 868 QLLSEITGAFRPGVLTALMGISGAGKTTLLDV--LAGRKTSGYIE-GEIRISGF--LKVQETFARV----SGYCEQTDIH 938
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinLLEQPEAGTIRvGDITIDTArsLSQQKGLIRQlrqhVGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 939 SPSITVEESLIYSAwlRLVPEINPQTKIRFVKQVLetieleeikdALVGVAGVSG-----LSTEQRKRLTVAVELVANPS 1013
Cdd:PRK11264 97 FPHRTVLENIIEGP--VIVKGEPKEEATARARELL----------AKVGLAGKETsyprrLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063705989 1014 IIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPS 1054
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
148-423 |
2.70e-09 |
|
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: 58.76 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 148 NEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfllqmcescllffslFYFPQCyGE 227
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAG-------------------------------LYKPTS-GS 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 228 ISYNGHGLNEVVPQKTSA---YISQhDLHIAEMTTRETIDFSArcqgvgsrtdimmevskrekdgGIIPDPEIdayMKAI 304
Cdd:cd03245 61 VLLDGTDIRQLDPADLRRnigYVPQ-DVTLFYGTLRDNITLGA----------------------PLADDERI---LRAA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 305 SVKGLkrslqTDYILKI-LGLDicaeTLVGNAmKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQ 383
Cdd:cd03245 115 ELAGV-----TDFVNKHpNGLD----LQIGER-GRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLR 184
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1063705989 384 QV-AHITN--ATVFVSLLqpapesyDLFDDIVLMAEGKIVYHG 423
Cdd:cd03245 185 QLlGDKTLiiITHRPSLL-------DLVDRIIVMDSGRIVADG 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
820-1070 |
3.43e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.40 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 820 LDSSIKTNEDPGKMILPFKPLTITFQDLnyyvdVPVEMKGQgynekklQLLSEITGAFRPGVLTALMGISGAGKTTLLDV 899
Cdd:PRK11174 328 LETPLAHPQQGEKELASNDPVTIEAEDL-----EILSPDGK-------TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 900 LagrktSGYI--EGEIRISGflkvqetfarvsgyCEQTDI----------------HSPSITVEESLIYSAwlrlvPEIN 961
Cdd:PRK11174 396 L-----LGFLpyQGSLKING--------------IELRELdpeswrkhlswvgqnpQLPHGTLRDNVLLGN-----PDAS 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 962 PQTkirfVKQVLETIELEEIKDALV-GVA-----GVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRA 1035
Cdd:PRK11174 452 DEQ----LQQALENAWVSEFLPLLPqGLDtpigdQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
250 260 270
....*....|....*....|....*....|....*
gi 1063705989 1036 VKNVAETGRTIVCTiHQpsIHIFEAFDELVLLKRG 1070
Cdd:PRK11174 528 LNAASRRQTTLMVT-HQ--LEDLAQWDQIWVMQDG 559
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
862-1029 |
3.44e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 59.06 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 862 YNEKKLQ--LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISG-FLKVQETFARVS------GYC 932
Cdd:PRK11629 15 YQEGSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTP--TSGDVIFNGqPMSKLSSAAKAElrnqklGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 933 EQTDIHSPSITVEESLiysAWLRLVPEINPQTKIRFVKQVLETIELEEikdalVGVAGVSGLSTEQRKRLTVAVELVANP 1012
Cdd:PRK11629 93 YQFHHLLPDFTALENV---AMPLLIGKKKPAEINSRALEMLAAVGLEH-----RANHRPSELSGGERQRVAIARALVNNP 164
|
170
....*....|....*..
gi 1063705989 1013 SIIFMDEPTTGLDARAA 1029
Cdd:PRK11629 165 RLVLADEPTGNLDARNA 181
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
842-1077 |
3.60e-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: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 842 ITFQDLNYyvdvpvemkgqGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGF--L 919
Cdd:cd03247 1 LSINNVSF-----------SYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ--QGEITLDGVpvS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 920 KVQETFARVSGYCEQTdIHSPSITVEESLiysawlrlvpeinpqtKIRFvkqvletieleeikdalvgvagvsglSTEQR 999
Cdd:cd03247 68 DLEKALSSLISVLNQR-PYLFDTTLRNNL----------------GRRF--------------------------SGGER 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1000 KRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHqpsiHI--FEAFDELVLLKRgGRMIYSG 1077
Cdd:cd03247 105 QRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITH----HLtgIEHMDKILFLEN-GKIIMQG 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
877-1070 |
3.86e-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: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 877 FRPGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGflkvqetfARVsgyceqTDIHS--------------- 939
Cdd:COG3839 26 IEDGEFLVLLGPSGCGKSTLLRMIAGleDPTSG----EILIGG--------RDV------TDLPPkdrniamvfqsyaly 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 940 PSITVEESLIYSAWLRLVP--EINPQtkirfVKQVLETIELEEIKDALVgvagvSGLSTEQRKRltVAV--ELVANPSII 1015
Cdd:COG3839 88 PHMTVYENIAFPLKLRKVPkaEIDRR-----VREAAELLGLEDLLDRKP-----KQLSGGQRQR--VALgrALVREPKVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705989 1016 FMDEPTTGLDA--RAAaivMRA--VKNVAETGRTIVCTIHQPSihifEAF---DELVLLKRG 1070
Cdd:COG3839 156 LLDEPLSNLDAklRVE---MRAeiKRLHRRLGTTTIYVTHDQV----EAMtlaDRIAVMNDG 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
869-1028 |
4.68e-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: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 869 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTsgYIEGEIRISGFLKVqetfarvsGYCEQTDIHSPSITVEESL 948
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELE--PDSGEVSIPKGLRI--------GYLPQEPPLDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 949 I--YSAWLRLVPEIN-PQTKIRFVKQVLETI-ELEE-------------IKDALVGV--------AGVSGLSTEQRKRLT 1003
Cdd:COG0488 83 LdgDAELRALEAELEeLEAKLAEPDEDLERLaELQEefealggweaearAEEILSGLgfpeedldRPVSELSGGWRRRVA 162
|
170 180
....*....|....*....|....*
gi 1063705989 1004 VAVELVANPSIIFMDEPTTGLDARA 1028
Cdd:COG0488 163 LARALLSEPDLLLLDEPTNHLDLES 187
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
144-430 |
5.33e-09 |
|
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: 58.40 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 144 GVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKalsgnlennlkvldifsfgcfllqmcescllFFSLFYFPQ 223
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVN-------------------------------LIPRFYDVD 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 224 CyGEISYNGHGLNEVVPQ---KTSAYISQhDLHIAEMTTRETIDFSARcqgvgsrtdimmevskrekdggiipdpeiDAY 300
Cdd:cd03251 56 S-GRILIDGHDVRDYTLAslrRQIGLVSQ-DVFLFNDTVAENIAYGRP-----------------------------GAT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 301 MKAIsVKGLKRSLQTDYILKI-LGLDicaeTLVGnamKRGI--SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQ 377
Cdd:cd03251 105 REEV-EEAARAANAHEFIMELpEGYD----TVIG---ERGVklSGGQRQRIAIARALLKDPPILILDEATSALDTESERL 176
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705989 378 IIKSLQQVAhiTNATVFV-----SLLQPApesydlfDDIVLMAEGKIVYHGPRDDVLK 430
Cdd:cd03251 177 VQAALERLM--KNRTTFViahrlSTIENA-------DRIVVLEDGKIVERGTHEELLA 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
157-423 |
5.49e-09 |
|
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: 58.15 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 157 DVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlkvldifsfgcfllqmcescllffslfyfpqcygeisynghgln 236
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLK---------------------------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 237 evvPQKTSAYISQHDLhiaemtTRETIDFSARCQGVGSRTDIMMEVSKREkdggiipdpeiDAYMKA--ISVKGLKRSLQ 314
Cdd:cd03265 52 ---PTSGRATVAGHDV------VREPREVRRRIGIVFQDLSVDDELTGWE-----------NLYIHArlYGVPGAERRER 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 315 TDYILKILGLDICAETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVF 394
Cdd:cd03265 112 IDELLDFVGLLEAADRLVKT-----YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTIL 186
|
250 260
....*....|....*....|....*....
gi 1063705989 395 VSlLQPAPESYDLFDDIVLMAEGKIVYHG 423
Cdd:cd03265 187 LT-THYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
140-394 |
6.20e-09 |
|
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: 57.87 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 140 LKLSGV----RTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfllqmcescllf 215
Cdd:cd03293 1 LEVRNVsktyGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAG---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 216 fslFYFPQCyGEISYNGHGLNEVVPQKtsAYISQHDLHIAEMTTRETIDFSARCQGvgsrtdimmeVSKREKdggiipDP 295
Cdd:cd03293 53 ---LERPTS-GEVLVDGEPVTGPGPDR--GYVFQQDALLPWLTVLDNVALGLELQG----------VPKAEA------RE 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 296 EIDAYMKAIsvkGLKRSLqtdyilkilgldicaetlvgNAMKRGISGGQKKRLTTAE-MIVGPtKALFMDEITNGLDSST 374
Cdd:cd03293 111 RAEELLELV---GLSGFE--------------------NAYPHQLSGGMRQRVALARaLAVDP-DVLLLDEPFSALDALT 166
|
250 260
....*....|....*....|
gi 1063705989 375 AFQIIKSLQQVAHITNATVF 394
Cdd:cd03293 167 REQLQEELLDIWRETGKTVL 186
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
842-1032 |
6.26e-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: 6.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 842 ITFQDLNYYvdvpvemkgqgYNEKklQLLSEITGAFRPGVLTALMGISGAGKTTLL-------DVLAGRKtsgyIEGEIR 914
Cdd:COG1117 12 IEVRNLNVY-----------YGDK--QALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPGAR----VEGEIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 915 ISGflkvqetfarvsgyceqTDIHSPSITVEEsliysawLR----LV---PeiNPqtkirFVKQVLETI----------- 976
Cdd:COG1117 75 LDG-----------------EDIYDPDVDVVE-------LRrrvgMVfqkP--NP-----FPKSIYDNVayglrlhgiks 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 977 --ELEEI-KDALVGVA-----------GVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIV 1032
Cdd:COG1117 124 ksELDEIvEESLRKAAlwdevkdrlkkSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKI 193
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
869-1053 |
6.64e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.51 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 869 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIE--GE-IRisgflKVQETFARVSGYCEqtdiHSPSI- 942
Cdd:PRK13538 16 LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGlaRPDAGEVLwqGEpIR-----RQRDEYHQDLLYLG----HQPGIk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 943 ---TVEESLIYSAwlRLVPEINPQTkirfVKQVLETIELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDE 1019
Cdd:PRK13538 87 telTALENLRFYQ--RLHGPGDDEA----LWEALAQVGLAGFEDVPVRQ-----LSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190
....*....|....*....|....*....|....
gi 1063705989 1020 PTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQP 1053
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
870-1070 |
7.14e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.98 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 870 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIE-GEIRISGFLKVQET--FARVSGYCEQtdiHSPSITV 944
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllQPTEGKVTvGDIVVSSTSKQKEIkpVRKKVGVVFQ---FPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 945 EESLIYSAwlrlvpEINPQTkIRFVKQVLETIELEEIKdaLVGVA------GVSGLSTEQRKRLTVAVELVANPSIIFMD 1018
Cdd:PRK13643 99 EETVLKDV------AFGPQN-FGIPKEKAEKIAAEKLE--MVGLAdefwekSPFELSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063705989 1019 EPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRG 1070
Cdd:PRK13643 170 EPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMD-DVADYADYVYLLEKG 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
885-1070 |
7.85e-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: 7.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 885 LMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGflkvqetfARVSG-YCEQTDIHS--------PSITVEESLIYSAWLR 955
Cdd:cd03301 31 LLGPSGCGKTTTLRMIAGLEEPT--SGRIYIGG--------RDVTDlPPKDRDIAMvfqnyalyPHMTVYDNIAFGLKLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 956 LVP--EINpqtkiRFVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARaAAIVM 1033
Cdd:cd03301 101 KVPkdEID-----ERVREVAELLQIEHLLDRKP-----KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAK-LRVQM 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1063705989 1034 RA--VKNVAETGRTIVCTIHQPSihifEAF---DELVLLKRG 1070
Cdd:cd03301 170 RAelKRLQQRLGTTTIYVTHDQV----EAMtmaDRIAVMNDG 207
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
139-426 |
8.72e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 59.19 E-value: 8.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 139 LLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcflLQMCEScllffsl 218
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAG------------------FETPDS------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 219 fyfpqcyGEISYNGHGLNEVVPQK----TsayISQHDLHIAEMTTRETIDFSARCQGVgsrtdimmevskrekdggiiPD 294
Cdd:PRK09452 69 -------GRIMLDGQDITHVPAENrhvnT---VFQSYALFPHMTVFENVAFGLRMQKT--------------------PA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 295 PEIDaymkaisvkglKRSLQTdyiLKILGLDICAETLVgnamkRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSST 374
Cdd:PRK09452 119 AEIT-----------PRVMEA---LRMVQLEEFAQRKP-----HQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKL 179
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705989 375 AFQI---IKSLQQVAHITnaTVFVSLLQpaPESYDLFDDIVLMAEGKIVYHG-PRD 426
Cdd:PRK09452 180 RKQMqneLKALQRKLGIT--FVFVTHDQ--EEALTMSDRIVVMRDGRIEQDGtPRE 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
879-1031 |
9.59e-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: 9.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 879 PGVlTALMGISGAGKTTLLDVLAG--RKTSGYIE--GEI------RIsgFLKVQetfARVSGYCEQTDIHSPSITVEESL 948
Cdd:COG4148 25 RGV-TALFGPSGSGKTTLLRAIAGleRPDSGRIRlgGEVlqdsarGI--FLPPH---RRRIGYVFQEARLFPHLSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 949 IYSAWlrlvpeinpqtkirFVKQVLETIELEEIKDaLVGVA-----GVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTG 1023
Cdd:COG4148 99 LYGRK--------------RAPRAERRISFDEVVE-LLGIGhlldrRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
....*....
gi 1063705989 1024 LD-ARAAAI 1031
Cdd:COG4148 164 LDlARKAEI 172
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
863-1055 |
1.21e-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: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 863 NEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSgyieGEIRISGflkvqetfarvsgyceqTDIHSP 940
Cdd:COG4181 21 GAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGldRPTS----GTVRLAG-----------------QDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 941 SitvEESLiysAWLRlvpeinpQTKIRFVKQ---------VLETI----ELEEIKDAL---------VGV--------AG 990
Cdd:COG4181 80 D---EDAR---ARLR-------ARHVGFVFQsfqllptltALENVmlplELAGRRDARararallerVGLghrldhypAQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705989 991 VSGlsTEQRkRLTVAVELVANPSIIFMDEPTTGLDARAAAIV---MRAVKnvAETGRTIVCTIHQPSI 1055
Cdd:COG4181 147 LSG--GEQQ-RVALARAFATEPAILFADEPTGNLDAATGEQIidlLFELN--RERGTTLVLVTHDPAL 209
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
869-1094 |
1.33e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.49 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 869 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLaGRKTSGYiEGEIRISGFLKVQ---ETFARVSGYCEQTDIHSPSITVE 945
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPS-EGEILLDAQPLESwssKAFARKVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 946 E--SLIYSAWLRLVPeinpqtkiRFVKQVLETIElEEIkdALVGVAG-----VSGLSTEQRKRLTVAVELVANPSIIFMD 1018
Cdd:PRK10575 104 ElvAIGRYPWHGALG--------RFGAADREKVE-EAI--SLVGLKPlahrlVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705989 1019 EPTTGLDARAAAIVMRAVKNVA-ETGRTIVCTIHqpSIHIFEAF-DELVLLkRGGRMIYSG-PLGQHSSCVIEYFQNIP 1094
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSqERGLTVIAVLH--DINMAARYcDYLVAL-RGGEMIAQGtPAELMRGETLEQIYGIP 248
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
613-789 |
1.45e-08 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 56.36 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 613 WAYAIPATVLkiplSFFESLVWTCLTYYVIGYTPEPYRFFRQF--MILFAVHFTSISMFrcIAAIFQTGVAAMTAGSFVM 690
Cdd:COG0842 50 LGKVLAYLLR----GLLQALLVLLVALLFFGVPLRGLSLLLLLlvLLLFALAFSGLGLL--ISTLARSQEQASAISNLVI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 691 LITFVFAGFAIPYTDMPGWLKWGFWVNPISYAeiglsvneflaprwqkmqptnVTLGRTILeSRGLNYDDymYWVSLSAL 770
Cdd:COG0842 124 LPLTFLSGAFFPIESLPGWLQAIAYLNPLTYF---------------------VEALRALF-LGGAGLAD--VWPSLLVL 179
|
170
....*....|....*....
gi 1063705989 771 LGLTIIFntiFTLALSFLK 789
Cdd:COG0842 180 LAFAVVL---LALALRLFR 195
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
884-1054 |
1.53e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.16 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 884 ALMGISGAGKTTLL---DVLAGRKTSGYIEGEIRISGFLKVQETF-----ARVSGYCEQTDIHSPSITVEESLiySAWLR 955
Cdd:PRK14267 34 ALMGPSGCGKSTLLrtfNRLLELNEEARVEGEVRLFGRNIYSPDVdpievRREVGMVFQYPNPFPHLTIYDNV--AIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 956 LVPEINPQTKI-RFVKQVLETIEL-EEIKDALVGVAgvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVM 1033
Cdd:PRK14267 112 LNGLVKSKKELdERVEWALKKAALwDEVKDRLNDYP--SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIE 189
|
170 180
....*....|....*....|.
gi 1063705989 1034 RAVKNVaETGRTIVCTIHQPS 1054
Cdd:PRK14267 190 ELLFEL-KKEYTIVLVTHSPA 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
870-1074 |
1.56e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 57.40 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 870 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTsgYIEGEIRISGfLKVQETFARvSGYCEQTDIHSPSITVEESLI 949
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVP--YQHGSITLDG-KPVEGPGAE-RGVVFQNEGLLPWRNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 950 YSAWLRLVPEINPQTKIRfvkQVLetieleeikdALVGVAG-----VSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGL 1024
Cdd:PRK11248 93 FGLQLAGVEKMQRLEIAH---QML----------KKVGLEGaekryIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063705989 1025 DARAAAIVMRAVKNV-AETGRTIVCTIHQPSIHIFEAfDELVLLKRG-GRMI 1074
Cdd:PRK11248 160 DAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMA-TELVLLSPGpGRVV 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
139-429 |
1.79e-08 |
|
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: 57.02 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 139 LLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfllqmcescllffsl 218
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG------------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 219 fYFPQCYG-EISYNGHGL-NEVVPQ-KTS-AYISQ--HDLHIAEMTTRETIdFSARCQGVGsrtdIMMEVSKREKDggii 292
Cdd:COG1119 52 -DLPPTYGnDVRLFGERRgGEDVWElRKRiGLVSPalQLRFPRDETVLDVV-LSGFFDSIG----LYREPTDEQRE---- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 293 pdpeidaymkaisvkglkrslQTDYILKILGLDICAETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDS 372
Cdd:COG1119 122 ---------------------RARELLELLGLAHLADRPFGT-----LSQGEQRRVLIARALVKDPELLILDEPTAGLDL 175
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705989 373 STAFQIIKSLQQVAHITN-ATVFVS-LLQPAPESydlFDDIVLMAEGKIVYHGPRDDVL 429
Cdd:COG1119 176 GARELLLALLDKLAAEGApTLVLVThHVEEIPPG---ITHVLLLKDGRVVAAGPKEEVL 231
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
153-430 |
1.84e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 59.02 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfllqmcescllffslFYFPQCyGEISYNG 232
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLR-------------------------------FYDPTS-GRILIDG 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 233 HGLNEVVPQ---KTSAYISQhDLHIAEMTTRETIDFSarcqgvgsRTDImmevskrekdggiiPDPEIDAYMKAISVkgl 309
Cdd:COG1132 402 VDIRDLTLEslrRQIGVVPQ-DTFLFSGTIRENIRYG--------RPDA--------------TDEEVEEAAKAAQA--- 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 310 krslqTDYILKiL--GLDicaeTLVGnamKRGI--SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQV 385
Cdd:COG1132 456 -----HEFIEA-LpdGYD----TVVG---ERGVnlSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL 522
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1063705989 386 AHitNATVFV-----SLLQPApesydlfDDIVLMAEGKIVYHGPRDDVLK 430
Cdd:COG1132 523 MK--GRTTIViahrlSTIRNA-------DRILVLDDGRIVEQGTHEELLA 563
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
877-1079 |
1.88e-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: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 877 FRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIegeirISGFLKVQETFARVS---GYCEQTDIHSPSITVEESLIYS 951
Cdd:TIGR01257 953 FYENQITAFLGHNGAGKTTTLSILTGllPPTSGTV-----LVGGKDIETNLDAVRqslGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 952 AWLRLVPEINPQTKIrfvKQVLETIEL-----EEIKDalvgvagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDA 1026
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEM---EAMLEDTGLhhkrnEEAQD----------LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1027 RAaaivMRAVKNVA---ETGRTIVCTIHqpsiHIFEA---FDELVLLKRgGRMIYSG-PL 1079
Cdd:TIGR01257 1095 YS----RRSIWDLLlkyRSGRTIIMSTH----HMDEAdllGDRIAIISQ-GRLYCSGtPL 1145
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
883-1078 |
2.10e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 57.05 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 883 TALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGFLKVQETF----ARVSGYCEQTDIHSPSITVEESLIYSAW-LRLV 957
Cdd:PRK13647 34 TALLGPNGAGKSTLLLHLNGIYLPQ--RGRVKVMGREVNAENEkwvrSKVGLVFQDPDDQVFSSTVWDDVAFGPVnMGLD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 958 P-EINpqtkiRFVKQVLETIELEEIKDAlvgvaGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAV 1036
Cdd:PRK13647 112 KdEVE-----RRVEEALKAVRMWDFRDK-----PPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEIL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1063705989 1037 KNVAETGRTIVCTIHQPSIhIFEAFDELVLLKRGGRMIYSGP 1078
Cdd:PRK13647 182 DRLHNQGKTVIVATHDVDL-AAEWADQVIVLKEGRVLAEGDK 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
865-1051 |
2.23e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.44 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 865 KKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG---RKTSGYIEGEIRISgFLKVQETFARVSGYCEQTDIHSPS 941
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGivpRDAGNIIIDDEDIS-LLPLHARARRGIGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 942 ITVEESLIysAWLRLVPEINPQTKIRFVKQVLETIELEEIKDALvgvaGVSgLSTEQRKRLTVAVELVANPSIIFMDEPT 1021
Cdd:PRK10895 93 LSVYDNLM--AVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM----GQS-LSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190
....*....|....*....|....*....|
gi 1063705989 1022 TGLDARAAAIVMRAVKNVAETGRTIVCTIH 1051
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDSGLGVLITDH 195
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
859-1025 |
2.37e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 56.33 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 859 GQGynEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISG--FLKVQET-----FARVSGY 931
Cdd:PRK10584 17 GQG--EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGS--SGEVSLVGqpLHQMDEEaraklRAKHVGF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 932 CEQTDIHSPSITVEESLIYSAWLRlvPEINPQTKIRfVKQVLETIELEEIKDALvgvagVSGLSTEQRKRLTVAVELVAN 1011
Cdd:PRK10584 93 VFQSFMLIPTLNALENVELPALLR--GESSRQSRNG-AKALLEQLGLGKRLDHL-----PAQLSGGEQQRVALARAFNGR 164
|
170
....*....|....
gi 1063705989 1012 PSIIFMDEPTTGLD 1025
Cdd:PRK10584 165 PDVLFADEPTGNLD 178
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
838-1077 |
2.79e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 58.30 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 838 KPLTITFQDLNYyvdvpvemkgqGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLagrkTSGY--IEGEIRI 915
Cdd:PRK11160 335 DQVSLTLNNVSF-----------TYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL----TRAWdpQQGEILL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 916 SGflkvqetfARVSGYCEQTDIHSPSITVEESLIYSAWLR--LV---PEINPQTKIRFVKQV-LETIeLEEIK--DALVG 987
Cdd:PRK11160 400 NG--------QPIADYSEAALRQAISVVSQRVHLFSATLRdnLLlaaPNASDEALIEVLQQVgLEKL-LEDDKglNAWLG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 988 VAG--VSGlsTEQRkRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAEtGRTIVCTIHQpsIHIFEAFDELV 1065
Cdd:PRK11160 471 EGGrqLSG--GEQR-RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHR--LTGLEQFDRIC 544
|
250
....*....|..
gi 1063705989 1066 LLKrGGRMIYSG 1077
Cdd:PRK11160 545 VMD-NGQIIEQG 555
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
139-420 |
3.02e-08 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 55.82 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 139 LLKLSGV----RTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvLDIFSfgcfllqmcescll 214
Cdd:COG1136 4 LLELRNLtksyGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG--------LDRPT-------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 215 ffslfyfpqcYGEISYNGH---GLNE------------VVPQktsayisQHDLhIAEMTTRETIDFSARCQGVGSRtdim 279
Cdd:COG1136 62 ----------SGEVLIDGQdisSLSErelarlrrrhigFVFQ-------FFNL-LPELTALENVALPLLLAGVSRK---- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 280 mevskrekdggiipdpeiDAYMKAisvkglkrslqtDYILKILGLDICAETLVGNamkrgISGGQKKRLTTAEMIVGPTK 359
Cdd:COG1136 120 ------------------ERRERA------------RELLERVGLGDRLDHRPSQ-----LSGGQQQRVAIARALVNRPK 164
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 360 ALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVsllqpA---PESYDLFDDIVLMAEGKIV 420
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVM-----VthdPELAARADRVIRLRDGRIV 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
154-418 |
3.35e-08 |
|
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: 55.55 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLennlkvldifsfgcfllqmcescllffslfyfPQCYGEISYNGh 233
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGEL--------------------------------EKLSGSVSVPG- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 234 glnevvpqkTSAYISQHDLhIAEMTTRETIDFSArcqgvgsrtdimmevskrekdggiipdpEIDA--YMKAISVKGLKR 311
Cdd:cd03250 67 ---------SIAYVSQEPW-IQNGTIRENILFGK----------------------------PFDEerYEKVIKACALEP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 312 slqtDyiLKIL-GLDicaETLVGnamKRGI--SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHI 388
Cdd:cd03250 109 ----D--LEILpDGD---LTEIG---EKGInlSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLL 176
|
250 260 270
....*....|....*....|....*....|....*
gi 1063705989 389 TNATVF-----VSLLQPApesydlfDDIVLMAEGK 418
Cdd:cd03250 177 NNKTRIlvthqLQLLPHA-------DQIVVLDNGR 204
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
140-429 |
3.93e-08 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 55.52 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLennlkvldifsfgcfllqmcescllffslf 219
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 220 yfPQCYGEISYNGHGLNEVVPQKTS----AYISQHDLHIAEMTTRETIDFSARCQGVGSRTDIMMEVSkrekdgGIIPDp 295
Cdd:cd03224 51 --PPRSGSIRFDGRDITGLPPHERAragiGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVY------ELFPR- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 296 eidaymkaisvkgLKRSLQTDyilkilgldicAETLvgnamkrgiSGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTA 375
Cdd:cd03224 122 -------------LKERRKQL-----------AGTL---------SGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIV 168
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705989 376 FQIIKSLQQVAHiTNATVfvsLL--QPAPESYDLFDDIVLMAEGKIVYHGPRDDVL 429
Cdd:cd03224 169 EEIFEAIRELRD-EGVTI---LLveQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
868-1027 |
4.36e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 57.02 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 868 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYiegeIRISGfLKVQETFA--RVSGYCEQTDIHSPSIT 943
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGleHQTSGH----IRFHG-TDVSRLHArdRKVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 944 VEESLIYSawLRLVPEIN-PQTKI--RFVKQVLETIELEEIKDALvgvagVSGLSTEQRKRLTVAVELVANPSIIFMDEP 1020
Cdd:PRK10851 91 VFDNIAFG--LTVLPRRErPNAAAikAKVTQLLEMVQLAHLADRY-----PAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
....*..
gi 1063705989 1021 TTGLDAR 1027
Cdd:PRK10851 164 FGALDAQ 170
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
151-385 |
4.52e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 151 NIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSG-----------NLENNLKVLDIFSFGCFLLQMCESCLLFFSlf 219
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERlydptegdiiiNDSHNLKDINLKWWRSKIGVVSQDPLLFSN-- 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 220 yfpQCYGEISYNGHGLNEVvpQKTSAYISQHDLHIAEMTTRETidfSARCQGVGSRTDIMMEVSKRE-----KDGGIIPD 294
Cdd:PTZ00265 475 ---SIKNNIKYSLYSLKDL--EALSNYYNEDGNDSQENKNKRN---SCRAKCAGDLNDMSNTTDSNEliemrKNYQTIKD 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 295 PEIDAYMKAISVKGLKRSLQTDYilkilgldicaETLVG-NAMKrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSS 373
Cdd:PTZ00265 547 SEVVDVSKKVLIHDFVSALPDKY-----------ETLVGsNASK--LSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
250
....*....|..
gi 1063705989 374 TAFQIIKSLQQV 385
Cdd:PTZ00265 614 SEYLVQKTINNL 625
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
140-449 |
4.53e-08 |
|
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: 55.42 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 140 LKLSGVRTNEANIKiLTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfllqmcescllffslF 219
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAG-------------------------------F 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 220 YFPQCyGEISYNGHGLNEVVPQKTS-AYISQHDLHIAEMTTRETIDFSarcqgvgsrtdimMEVSKREKdggiipdPEID 298
Cdd:cd03299 49 IKPDS-GKILLNGKDITNLPPEKRDiSYVPQNYALFPHMTVYKNIAYG-------------LKKRKVDK-------KEIE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 299 AYMKAISvkglkRSLQTDYILkilgldicaetlvgNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQI 378
Cdd:cd03299 108 RKVLEIA-----EMLGIDHLL--------------NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705989 379 IKSLQQVAHITNATVfVSLLQPAPESYDLFDDIVLMAEGKIVYHGPRDDVLKffeecgfqCPERKGVADFL 449
Cdd:cd03299 169 REELKKIRKEFGVTV-LHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK--------KPKNEFVAEFL 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
857-1030 |
4.57e-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: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 857 MKGQG--YNEKKlQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGFLKVqetfarvsGYCEQ 934
Cdd:TIGR03719 7 MNRVSkvVPPKK-EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD--FNGEARPQPGIKV--------GYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 935 TDIHSPSITVEESL------IYSAWLRLvPEIN-----PQTKirFVKQVLETIELEEIKDAL------------------ 985
Cdd:TIGR03719 76 EPQLDPTKTVRENVeegvaeIKDALDRF-NEISakyaePDAD--FDKLAAEQAELQEIIDAAdawdldsqleiamdalrc 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063705989 986 -VGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAA 1030
Cdd:TIGR03719 153 pPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVA 198
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
153-429 |
5.17e-08 |
|
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: 55.31 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKalsgnlennlkvldifsfgcfllqmcescLLFfsLFYFPQCyGEISYNG 232
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILR-----------------------------LLF--RFYDVSS-GSILIDG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 233 HGLNE-----------VVPQKTSAYisqHDlhiaemTTRETIDFsarcqGVGSRTDImmEVSKREKDGGIipDPEI---- 297
Cdd:cd03253 63 QDIREvtldslrraigVVPQDTVLF---ND------TIGYNIRY-----GRPDATDE--EVIEAAKAAQI--HDKImrfp 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 298 DAYmkaisvkglkrslqtdyilkilgldicaETLVGnamKRG--ISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTA 375
Cdd:cd03253 125 DGY----------------------------DTIVG---ERGlkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTE 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705989 376 FQIIKSLQQ---------VAH----ITNAtvfvsllqpapesydlfDDIVLMAEGKIVYHGPRDDVL 429
Cdd:cd03253 174 REIQAALRDvskgrttivIAHrlstIVNA-----------------DKIIVLKDGRIVERGTHEELL 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
151-430 |
5.55e-08 |
|
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: 55.31 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 151 NIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfllqmcescllffslFYFPQcYGEISY 230
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMR-------------------------------FYDPQ-KGQILI 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 231 NG---HGLNEVVPQKTSAYISQhDLHIAEMTTRETIDFSarcqgvgsrtdimmevskrekdGGIIPDPEIDAYMKAISVK 307
Cdd:cd03254 63 DGidiRDISRKSLRSMIGVVLQ-DTFLFSGTIMENIRLG----------------------RPNATDEEVIEAAKEAGAH 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 308 GLKRSLQTDYilkilgldicaETLVGNAMKrGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAH 387
Cdd:cd03254 120 DFIMKLPNGY-----------DTVLGENGG-NLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK 187
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1063705989 388 itNATVFV-----SLLQPApesydlfDDIVLMAEGKIVYHGPRDDVLK 430
Cdd:cd03254 188 --GRTSIIiahrlSTIKNA-------DKILVLDDGKIIEEGTHDELLA 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
820-1072 |
5.57e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 57.28 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 820 LDSSIKTNEDPGKMILPFKPLTITFQDLNYyvdvpvemkgqGYNEKKlQLLSEITGAFRPGVLTALMGISGAGKTTLLDV 899
Cdd:PRK13657 313 EDAVPDVRDPPGAIDLGRVKGAVEFDDVSF-----------SYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 900 L--AGRKTSGYIegeiRISG------------------FlkvQET--FARVSGycEQTDIHSPSITVEEsliysawLRLV 957
Cdd:PRK13657 381 LqrVFDPQSGRI----LIDGtdirtvtraslrrniavvF---QDAglFNRSIE--DNIRVGRPDATDEE-------MRAA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 958 PEInpqtkirfvKQVLETIELEEIK-DALVGVAGvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAV 1036
Cdd:PRK13657 445 AER---------AQAHDFIERKPDGyDTVVGERG-RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAAL 514
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1063705989 1037 KNVAEtGRTIVCTIHQPSI-------------HIFEA--FDELVllKRGGR 1072
Cdd:PRK13657 515 DELMK-GRTTFIIAHRLSTvrnadrilvfdngRVVESgsFDELV--ARGGR 562
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
154-430 |
6.04e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.60 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLennlkvldifsfgcfllqmCESCLlffslfyfP---QCYGEISY 230
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL-------------------TGGGA--------PrgaRVTGDVTL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 231 NGHGLNEVVPQKTS---AYISQHDLHIAEMTTRETIDFS----ARCQGVGSRtdimmevskreKDGGIIpdpeidayMKA 303
Cdd:PRK13547 69 NGEPLAAIDAPRLArlrAVLPQAAQPAFAFSAREIVLLGryphARRAGALTH-----------RDGEIA--------WQA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 304 ISVKGlkrslqtdyilkilgldicAETLVGNAMKRgISGGQKKRLTTAEMI---------VGPTKALFMDEITNGLDSST 374
Cdd:PRK13547 130 LALAG-------------------ATALVGRDVTT-LSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAH 189
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705989 375 AFQIIKSLQQVAHITNATVFVSLLQPAPESYDLfDDIVLMAEGKIVYHGPRDDVLK 430
Cdd:PRK13547 190 QHRLLDTVRRLARDWNLGVLAIVHDPNLAARHA-DRIAMLADGAIVAHGAPADVLT 244
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
139-423 |
6.29e-08 |
|
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: 54.82 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 139 LLKLSGV----RTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALsgnlennLKVLDIFSfgcfllqmcescll 214
Cdd:cd03257 1 LLEVKNLsvsfPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAI-------LGLLKPTS-------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 215 ffslfyfpqcyGEISYNGHGLNEVVPQ------KTSAYISQhDLHIA---EMTTRETIDFSARCQGVGSRTDIMMEVSKR 285
Cdd:cd03257 60 -----------GSIIFDGKDLLKLSRRlrkirrKEIQMVFQ-DPMSSlnpRMTIGEQIAEPLRIHGKLSKKEARKEAVLL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 286 EKDGgiIPDPEIDAYMKAisvkglkrslqtdyilkilgldicaetlvgnamkRGISGGQKKRLTTAE-MIVGPtKALFMD 364
Cdd:cd03257 128 LLVG--VGLPEEVLNRYP----------------------------------HELSGGQRQRVAIARaLALNP-KLLIAD 170
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 365 EITNGLDSSTAFQIIKSLQQVAHITNATV-FVS----LLQpapesyDLFDDIVLMAEGKIVYHG 423
Cdd:cd03257 171 EPTSALDVSVQAQILDLLKKLQEELGLTLlFIThdlgVVA------KIADRVAVMYAGKIVEEG 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
153-430 |
8.61e-08 |
|
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: 54.60 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfLLQmcescllffslfyfPQcYGEISYNG 232
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIG-----------------LLR--------------PD-SGEILVDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 233 HGLNEvvpqktsayISQHDLHIAE---------------MTTRETIDFSarcqgvgsrtdiMMEVSKrekdggiIPDPEI 297
Cdd:COG1127 67 QDITG---------LSEKELYELRrrigmlfqggalfdsLTVFENVAFP------------LREHTD-------LSEAEI 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 298 D--AYMKaisvkglkrslqtdyiLKILGLDicaetLVGNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLD--SS 373
Cdd:COG1127 119 RelVLEK----------------LELVGLP-----GAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDpiTS 177
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 374 TAF-QIIKSLQQVAHITnaTVFVS--LlqpaPESYDLFDDIVLMAEGKIVYHGPRDDVLK 430
Cdd:COG1127 178 AVIdELIRELRDELGLT--SVVVThdL----DSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
877-1051 |
9.54e-08 |
|
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: 9.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 877 FRPGVLTALMGISGAGKTTLLDVLagRKTSGYIEGEIRISG----FLKVQETFARVsGYCEQtdihSP---SITVEESLI 949
Cdd:cd03249 26 IPPGKTVALVGSSGCGKSTVVSLL--ERFYDPTSGEILLDGvdirDLNLRWLRSQI-GLVSQ----EPvlfDGTIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 950 YSAWLRLVPEInpqtkIRFVKQVL--ETIE-LEEIKDALVGVAGVSgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDA 1026
Cdd:cd03249 99 YGKPDATDEEV-----EEAAKKANihDFIMsLPDGYDTLVGERGSQ-LSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180
....*....|....*....|....*
gi 1063705989 1027 RAAAIVMRAVKNVAEtGRTIVCTIH 1051
Cdd:cd03249 173 ESEKLVQEALDRAMK-GRTTIVIAH 196
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
151-452 |
1.40e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.48 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 151 NIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLENnlkvldifsfgcfllqmcescllffslfyfpQCYGEISY 230
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG-LEH-------------------------------QTSGHIRF 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 231 NGHGLNEV-VPQKTSAYISQHDLHIAEMTTRETIDFSARCqgvgsrtdimmeVSKREKdggiiPDpeidayMKAISVKGL 309
Cdd:PRK10851 62 HGTDVSRLhARDRKVGFVFQHYALFRHMTVFDNIAFGLTV------------LPRRER-----PN------AAAIKAKVT 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 310 KrslqtdyILKILGLDICAetlvgNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHIT 389
Cdd:PRK10851 119 Q-------LLEMVQLAHLA-----DRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEEL 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 390 NAT-VFVSLLQpaPESYDLFDDIVLMAEGKIVYHGPRDDVlkffeecgFQCPERKGVADFLQEV 452
Cdd:PRK10851 187 KFTsVFVTHDQ--EEAMEVADRVVVMSQGNIEQAGTPDQV--------WREPATRFVLEFMGEV 240
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
142-374 |
1.43e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 53.72 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 142 LSGVRTNEAnikILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcflLQMCEScllffslfyf 221
Cdd:PRK13539 8 LACVRGGRV---LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAG------------------LLPPAA---------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 222 pqcyGEISYNGHGLNEVVPQKTSAYISQHDLHIAEMTTRETIDFSARCQGVGsrtdimmevskrekdggiipDPEIDAYM 301
Cdd:PRK13539 57 ----GTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAENLEFWAAFLGGE--------------------ELDIAAAL 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063705989 302 KAISVKGLkrslqtdyilkilgLDICAETLvgnamkrgiSGGQKKRLTTAEMIVGPTKALFMDEITNGLDSST 374
Cdd:PRK13539 113 EAVGLAPL--------------AHLPFGYL---------SAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
840-1131 |
1.56e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.79 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 840 LTITFQDLNYyvdvpVEMKGQGYnekKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIE-GEIRIS 916
Cdd:PRK13646 1 MTIRFDNVSY-----TYQKGTPY---EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAllKPTTGTVTvDDITIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 917 GFLKvqetfarvsgyceqtDIHSPSITVEESLIYSAWLRLVPEINPQTKIRFVKQVLEtIELEEIKD---ALVGVAGVS- 992
Cdd:PRK13646 73 HKTK---------------DKYIRPVRKRIGMVFQFPESQLFEDTVEREIIFGPKNFK-MNLDEVKNyahRLLMDLGFSr 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 993 --------GLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNV-AETGRTIVCTIHQPSiHIFEAFDE 1063
Cdd:PRK13646 137 dvmsqspfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMN-EVARYADE 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 1064 LVLLKRGGRMIYSGP--LGQHSSCVIEYFQNIPGVAK----IRDKYNPATWMLEVTSEsveteldmDFAKIYNE 1131
Cdd:PRK13646 216 VIVMKEGSIVSQTSPkeLFKDKKKLADWHIGLPEIVQlqydFEQKYQTKLKDIALTEE--------EFVSLYKE 281
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
871-1077 |
1.63e-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: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 871 SEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKT--SGYIEGEIRISGFLKV-------QETFARVS-GYCEQTDIH-- 938
Cdd:TIGR02323 20 RDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLApdHGTATYIMRSGAELELyqlseaeRRRLMRTEwGFVHQNPRDgl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 939 ----SPSITVEESLIySAWLRLVPEINpQTKIRFVKQVleTIELEEIKDAlvgvagVSGLSTEQRKRLTVAVELVANPSI 1014
Cdd:TIGR02323 100 rmrvSAGANIGERLM-AIGARHYGNIR-ATAQDWLEEV--EIDPTRIDDL------PRAFSGGMQQRLQIARNLVTRPRL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 1015 IFMDEPTTGLDARAAAIVMRAVKN-VAETGRTIVCTIHQPSIHIFEAfDELVLLKRgGRMIYSG 1077
Cdd:TIGR02323 170 VFMDEPTGGLDVSVQARLLDLLRGlVRDLGLAVIIVTHDLGVARLLA-QRLLVMQQ-GRVVESG 231
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
140-449 |
1.72e-07 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 55.08 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLEnnlkvlDIFSfgcfllqmcescllffslf 219
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG-LE------DPTS------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 220 yfpqcyGEISYNGHGLNEVVPQKTS-AYISQ------HdlhiaeMTTRETIDFSARCQGVgsrtdimmevskrekdggii 292
Cdd:COG3839 58 ------GEILIGGRDVTDLPPKDRNiAMVFQsyalypH------MTVYENIAFPLKLRKV-------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 293 PDPEIDAymkaisvkglkrslQTDYILKILGLDicaETLvgNAMKRGISGGQKKRLTTAEMIVGPTKALFMDE-ITNgLD 371
Cdd:COG3839 106 PKAEIDR--------------RVREAAELLGLE---DLL--DRKPKQLSGGQRQRVALGRALVREPKVFLLDEpLSN-LD 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 372 SSTAFQI---IKSLQQVAHITnaTVFVsllqpapeSYD------LFDDIVLMAEGKIVYHGPRDDVlkffeecgFQCPER 442
Cdd:COG3839 166 AKLRVEMraeIKRLHRRLGTT--TIYV--------THDqveamtLADRIAVMNDGRIQQVGTPEEL--------YDRPAN 227
|
....*..
gi 1063705989 443 KGVADFL 449
Cdd:COG3839 228 LFVAGFI 234
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
884-1077 |
1.83e-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: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 884 ALMGISGAGKTTLLDVLAG--RKTSGYIEGEIRISGFLKVQETFarvsgyceqtdihSPSITVEESLIYSAWL--RLVPE 959
Cdd:cd03220 52 GLIGRNGAGKSTLLRLLAGiyPPDSGTVTVRGRVSSLLGLGGGF-------------NPELTGRENIYLNGRLlgLSRKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 960 InpQTKIRFVkqvletIELEEIKDALvgVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNV 1039
Cdd:cd03220 119 I--DEKIDEI------IEFSELGDFI--DLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 1063705989 1040 AETGRTIVCTIHQPSIhIFEAFDELVLLKRgGRMIYSG 1077
Cdd:cd03220 189 LKQGKTVILVSHDPSS-IKRLCDRALVLEK-GKIRFDG 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
878-1070 |
1.97e-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: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 878 RPGVLTALMGISGAGKTTLLDVLAG--RKTSgyieGEIRISGflkvqetfarvsgyceqTDIHS---------------- 939
Cdd:COG3842 29 EPGEFVALLGPSGCGKTTLLRMIAGfeTPDS----GRILLDG-----------------RDVTGlppekrnvgmvfqdya 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 940 --PSITVEESLIYSAWLRLVPEinPQTKIRfVKQVLETIELEEIKDALvgvagVSGLSTEQRKRltVAV--ELVANPSII 1015
Cdd:COG3842 88 lfPHLTVAENVAFGLRMRGVPK--AEIRAR-VAELLELVGLEGLADRY-----PHQLSGGQQQR--VALarALAPEPRVL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705989 1016 FMDEPTTGLDARAAAIVMRAVKNV-AETGRTIVCTIHQPSihifEAF---DELVLLKRG 1070
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQE----EALalaDRIAVMNDG 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
876-1081 |
2.02e-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: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 876 AFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISG----------------FlkvQET--Farvsgyceqtdi 937
Cdd:COG3840 21 TIAAGERVAILGPSGAGKSTLLNLIAGFLPP--DSGRILWNGqdltalppaerpvsmlF---QENnlF------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 938 hsPSITVEE--SLIYSAWLRLvpeiNPQTKIRfVKQVLETIELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSII 1015
Cdd:COG3840 84 --PHLTVAQniGLGLRPGLKL----TAEQRAQ-VEQALERVGLAGLLDRLPGQ-----LSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 1016 FMDEPTTGLDaraaaIVMRA-----VKNVA-ETGRTIVCTIHQPS--IHIfeaFDELVLLKRgGRMIYSGPLGQ 1081
Cdd:COG3840 152 LLDEPFSALD-----PALRQemldlVDELCrERGLTVLMVTHDPEdaARI---ADRVLLVAD-GRIAADGPTAA 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
840-1051 |
2.19e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.98 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 840 LTITFQDLNYYVDVPVEMKGQGynekklqlLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGFL 919
Cdd:PRK13649 1 MGINLQNVSYTYQAGTPFEGRA--------LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVP--TQGSVRVDDTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 920 kvqetfarVSGYCEQTDIHSPSITV-------EESLIYSAWLRLVPeINPQTkirFVKQVLETIELEEIKDALVGVA--- 989
Cdd:PRK13649 71 --------ITSTSKNKDIKQIRKKVglvfqfpESQLFEETVLKDVA-FGPQN---FGVSQEEAEALAREKLALVGISesl 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705989 990 ---GVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIH 1051
Cdd:PRK13649 139 fekNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
153-371 |
2.34e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 55.07 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkVLDIFSfgcfllqmcescllffslfyfpqcyGEISYNg 232
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG-------ELEPDS-------------------------GEVSIP- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 233 hglnevvPQKTSAYISQHDLHIAEMTTRETIdfsarCQGVGSRTDIMMEVSKREKDGGiIPDPEIDAYMKaisvkglkrs 312
Cdd:COG0488 59 -------KGLRIGYLPQEPPLDDDLTVLDTV-----LDGDAELRALEAELEELEAKLA-EPDEDLERLAE---------- 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 313 LQTDY--------------ILKILGLDIC-AETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLD 371
Cdd:COG0488 116 LQEEFealggweaearaeeILSGLGFPEEdLDRPVSE-----LSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
868-1052 |
2.39e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 53.48 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 868 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLagrktsGYIE----GEIRISG--FLKVQETFAR--------VSGYCE 933
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVL------NLLEmprsGTLNIAGnhFDFSKTPSDKairelrrnVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 934 QTDIHsPSITVEESLIySAWLRLVPEINPQTKIRfVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPS 1013
Cdd:PRK11124 90 QYNLW-PHLTVQQNLI-EAPCRVLGLSKDQALAR-AEKLLERLRLKPYADRFP-----LHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063705989 1014 IIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQ 1052
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
870-1070 |
2.77e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 53.84 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 870 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISG-----FLKVQETFARVSGYCEQTDIHSPSITV 944
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ--KGKVLVSGidtgdFSKLQGIRKLVGIVFQNPETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 945 EESLIYSawlrlvPE--INPQTKIR-FVKQVLETIELEEIKDAlvgvaGVSGLSTEQRKRLTVAVELVANPSIIFMDEPT 1021
Cdd:PRK13644 96 EEDLAFG------PEnlCLPPIEIRkRVDRALAEIGLEKYRHR-----SPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063705989 1022 TGLDARAAAIVMRAVKNVAETGRTIVCTIHqpSIHIFEAFDELVLLKRG 1070
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITH--NLEELHDADRIIVMDRG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
868-1078 |
3.19e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 53.24 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 868 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLagrktSGYIE---GEIRISGFLKVQ---ETFARVSGYCEQtdiHSP- 940
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL-----SGELSpdsGEVRLNGRPLADwspAELARRRAVLPQ---HSSl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 941 --SITVEESLiysaWLRLVP-EINPQTKIRFVKQVLetieleeikdALVGVAGVSG-----LSTEQRKRLTVAVELV--- 1009
Cdd:PRK13548 88 sfPFTVEEVV----AMGRAPhGLSRAEDDALVAAAL----------AQVDLAHLAGrdypqLSGGEQQRVQLARVLAqlw 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705989 1010 ---ANPSIIFMDEPTTGLDARAAAIVMRAVKNVA-ETGRTIVCTIH---QPSihifeAF-DELVLLKrGGRMIYSGP 1078
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHdlnLAA-----RYaDRIVLLH-QGRLVADGT 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
882-1061 |
3.27e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.50 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 882 LTALMGISGAGKTTLLDVLaGRKTSgyIEGEIRISGFLKV--QETFAR---VSGYCEQTDIHSPS-----ITVEESLIYS 951
Cdd:PRK14258 35 VTAIIGPSGCGKSTFLKCL-NRMNE--LESEVRVEGRVEFfnQNIYERrvnLNRLRRQVSMVHPKpnlfpMSVYDNVAYG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 952 awLRLVpEINPQTKIR-FVKQVLETIEL-EEIKDALVGVAgvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAA 1029
Cdd:PRK14258 112 --VKIV-GWRPKLEIDdIVESALKDADLwDEIKHKIHKSA--LDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIAS 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063705989 1030 AIVMRAVKNV---AETGRTIVC-TIHQPS-IHIFEAF 1061
Cdd:PRK14258 187 MKVESLIQSLrlrSELTMVIVShNLHQVSrLSDFTAF 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
154-385 |
3.84e-07 |
|
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: 54.67 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEnnlkvldifsfgcfllqmcescllffslfyfPQcYGEISYNGH 233
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD-------------------------------PL-QGEVTLDGV 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 234 GLNEVVPQKTSAYIS--QHDLHIAEMTTRETIDFSArcqgvgsrtdimmevskrekdggiiPDPEIDAYMKAISVKGLKR 311
Cdd:TIGR02868 398 PVSSLDQDEVRRRVSvcAQDAHLFDTTVRENLRLAR-------------------------PDATDEELWAALERVGLAD 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 312 SLQtdyilkilGLDICAETLVGnAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQV 385
Cdd:TIGR02868 453 WLR--------ALPDGLDTVLG-EGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA 517
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
867-1074 |
6.06e-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: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 867 LQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSgyieGEIRISGflkvqetfARVSGyceqtdiHSPSITV 944
Cdd:COG1116 24 VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGleKPTS----GEVLVDG--------KPVTG-------PGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 945 ---EESLIysAWL------RLVPEINPQTKIRFVKQVLETIEleeikdaLVGVAGVSG-----LSTEQRKRLTVAVELVA 1010
Cdd:COG1116 85 vfqEPALL--PWLtvldnvALGLELRGVPKAERRERARELLE-------LVGLAGFEDayphqLSGGMRQRVAIARALAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705989 1011 NPSIIFMDEPTTGLDA--RAaaiVMRA--VKNVAETGRTIVCTIHQpsihIFEAF---DELVLL-KRGGRMI 1074
Cdd:COG1116 156 DPEVLLMDEPFGALDAltRE---RLQDelLRLWQETGKTVLFVTHD----VDEAVflaDRVVVLsARPGRIV 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
868-1078 |
6.51e-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: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 868 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYIEGEIRISG----FLKVQETFARVSGYCEQTDIHSPSIT 943
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGeditDLPPEERARLGIFLAFQYPPEIPGVK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 944 VEEsliysaWLRLVPEinpqtkirfvkqvletieleeikdalvgvagvsGLSTEQRKRLTVAVELVANPSIIFMDEPTTG 1023
Cdd:cd03217 94 NAD------FLRYVNE---------------------------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705989 1024 LDARAAAIVMRAVKNVAETGRTIVCTIHQPsiHIFEAFD-ELVLLKRGGRMIYSGP 1078
Cdd:cd03217 135 LDIDALRLVAEVINKLREEGKSVLIITHYQ--RLLDYIKpDRVHVLYDGRIVKSGD 188
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
890-1045 |
7.42e-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: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 890 GAGKTTLLDVLAG--RKTSG--YIEG-------EIRISGFLkvqetfARV-----SGYCeqtdihsPSITVEESLIYsAW 953
Cdd:COG1101 42 GAGKSTLLNAIAGslPPDSGsiLIDGkdvtklpEYKRAKYI------GRVfqdpmMGTA-------PSMTIEENLAL-AY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 954 LR-----LVPEINPQtKIRFVKQVLETIE--LEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDA 1026
Cdd:COG1101 108 RRgkrrgLRRGLTKK-RRELFRELLATLGlgLENRLDTKVGL-----LSGGQRQALSLLMATLTKPKLLLLDEHTAALDP 181
|
170 180
....*....|....*....|
gi 1063705989 1027 RAAAIVMRAVKN-VAETGRT 1045
Cdd:COG1101 182 KTAALVLELTEKiVEENNLT 201
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
879-1079 |
7.78e-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: 7.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 879 PGVLTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRISGF--LKVQETFAR----VSGYCEQ--TDIhspsiTVEESL 948
Cdd:COG4586 47 PGEIVGFIGPNGAGKSTTIKMLTGilVPTSG----EVRVLGYvpFKRRKEFARrigvVFGQRSQlwWDL-----PAIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 949 iysAWLRLVPEINPQTKIRFVKQVLETIELEEIKDAlvgvaGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDara 1028
Cdd:COG4586 118 ---RLLKAIYRIPDAEYKKRLDELVELLDLGELLDT-----PVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD--- 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705989 1029 aAIVMRAVKN-----VAETGRTIVCTIHQPS-IhifEAFDELVLLKRGGRMIYSGPL 1079
Cdd:COG4586 187 -VVSKEAIREflkeyNRERGTTILLTSHDMDdI---EALCDRVIVIDHGRIIYDGSL 239
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
869-1081 |
7.87e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.41 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 869 LLSEITGAFRPGVLTALMGISGAGKTTLLDVL--AGRKTSGY-IEGEIRISG-----FLKVQEtFARVSGYCEQTDIHSP 940
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrMNDKVSGYrYSGDVLLGGrsifnYRDVLE-FRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 941 SITVEESLIYSAWLRLVPeinpQTKIRFVKQ--VLETIELEEIKDALVGVAgvSGLSTEQRKRLTVAVELVANPSIIFMD 1018
Cdd:PRK14271 115 MSIMDNVLAGVRAHKLVP----RKEFRGVAQarLTEVGLWDAVKDRLSDSP--FRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063705989 1019 EPTTGLDARAAAIVMRAVKNVAETGRTIVCTihqPSIHIFEAFDELVLLKRGGRMIYSGPLGQ 1081
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVT---HNLAQAARISDRAALFFDGRLVEEGPTEQ 248
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
155-452 |
9.20e-07 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 52.84 E-value: 9.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 155 LTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnLEnnlkvldifsfgcfllqmcescllffslfyFPQcYGEISYNGhg 234
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAG-LE------------------------------TPD-SGRIVLNG-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 235 lnEVVPQKTSA------YISQH-DL--HiaeMTTRETIDFSARCQGVgSRTDImmevskREKdggiipdpeidaymkais 305
Cdd:COG1118 64 --RDLFTNLPPrerrvgFVFQHyALfpH---MTVAENIAFGLRVRPP-SKAEI------RAR------------------ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 306 VKGLkrslqtdyiLKILGLDICAETLVGNamkrgISGGQKKRLTTAEM-IVGPtKALFMDEITNGLDSSTAFQIIKSLQQ 384
Cdd:COG1118 114 VEEL---------LELVQLEGLADRYPSQ-----LSGGQRQRVALARAlAVEP-EVLLLDEPFGALDAKVRKELRRWLRR 178
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063705989 385 V---AHITnaTVFVS--LLqpapESYDLFDDIVLMAEGKIVYHGPRDDVlkffeecgFQCPERKGVADFLQEV 452
Cdd:COG1118 179 LhdeLGGT--TVFVThdQE----EALELADRVVVMNQGRIEQVGTPDEV--------YDRPATPFVARFLGCV 237
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
139-429 |
9.24e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 53.29 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 139 LLKLSGV--RTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNlennlkvldifsfgcfllqmcescllff 216
Cdd:PRK11160 338 SLTLNNVsfTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRA---------------------------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 217 slfYFPQCyGEISYNGHGLNEVvpqktsayisqhdlhiAEMTTRETIDFsarcqgVGSRTDIMmevSKREKDGGIIPDPE 296
Cdd:PRK11160 390 ---WDPQQ-GEILLNGQPIADY----------------SEAALRQAISV------VSQRVHLF---SATLRDNLLLAAPN 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 297 I-DAYMKAISVK-GLKRSLQTDyilkiLGLDicaeTLVGNAmKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSST 374
Cdd:PRK11160 441 AsDEALIEVLQQvGLEKLLEDD-----KGLN----AWLGEG-GRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET 510
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705989 375 AFQIIKSLQQvaHITNATV-FVSLLQPAPESydlFDDIVLMAEGKIVYHGPRDDVL 429
Cdd:PRK11160 511 ERQILELLAE--HAQNKTVlMITHRLTGLEQ---FDRICVMDNGQIIEQGTHQELL 561
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
140-423 |
9.42e-07 |
|
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: 51.06 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvLDIFSfgcfllqmcescllffslf 219
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILG--------LIKPD------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 220 yfpqcYGEISYNGHGL--NEVVPQKTSAYISQHDLHiAEMTTRETIDFSARCQGvgsrtdimmevskrekdggiIPDPEI 297
Cdd:cd03268 54 -----SGEITFDGKSYqkNIEALRRIGALIEAPGFY-PNLTARENLRLLARLLG--------------------IRKKRI 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 298 DAymkaisvkglkrslqtdyILKILGLDICAETLVGnamkrGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDS---ST 374
Cdd:cd03268 108 DE------------------VLDVVGLKDSAKKKVK-----GFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPdgiKE 164
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1063705989 375 AFQIIKSLQQvahiTNATVFVS--LLQpapESYDLFDDIVLMAEGKIVYHG 423
Cdd:cd03268 165 LRELILSLRD----QGITVLISshLLS---EIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
146-423 |
1.09e-06 |
|
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: 51.21 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 146 RTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNlkvldifsfgcfllqmcescllffslfyfpqcY 225
Cdd:cd03266 12 RDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD--------------------------------A 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 226 GEISYNGHGLNE----------VVPQKTSAYisqhdlhiAEMTTRETIDFSARcqgvgsrtdimmevskrekdggiipdp 295
Cdd:cd03266 60 GFATVDGFDVVKepaearrrlgFVSDSTGLY--------DRLTARENLEYFAG--------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 296 eidaymkaisVKGLKRSLQTDYILKILGLDICAETLvgNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLD---S 372
Cdd:cd03266 105 ----------LYGLKGDELTARLEELADRLGMEELL--DRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDvmaT 172
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1063705989 373 STAFQIIKSLQQVAHitnATVFVSLLQPAPESydLFDDIVLMAEGKIVYHG 423
Cdd:cd03266 173 RALREFIRQLRALGK---CILFSTHIMQEVER--LCDRVVVLHRGRVVYEG 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
855-1070 |
1.52e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.48 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 855 VEMKGQGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIegEIRISGFLKVQETFARVSG-- 930
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGihEPTKGTI--TINNINYNKLDHKLAAQLGig 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 931 --YCEQTDIHspSITVEESLIYSAWL-RLVPEIN--PQTKIRFVKQV-LETIELEEIKDALVGvagvsGLSTEQRKRLTV 1004
Cdd:PRK09700 84 iiYQELSVID--ELTVLENLYIGRHLtKKVCGVNiiDWREMRVRAAMmLLRVGLKVDLDEKVA-----NLSISHKQMLEI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705989 1005 AVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLKRG 1070
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLA-EIRRICDRYTVMKDG 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
882-1027 |
1.64e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 52.26 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 882 LTaLMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGflkvqETFARVSGycEQTDIHS--------PSITVEESLIYSAW 953
Cdd:PRK09452 43 LT-LLGPSGCGKTTVLRLIAGFETPD--SGRIMLDG-----QDITHVPA--ENRHVNTvfqsyalfPHMTVFENVAFGLR 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705989 954 LRLVP--EINPQtkirfVKQVLETIELEEIKDalvgvAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDAR 1027
Cdd:PRK09452 113 MQKTPaaEITPR-----VMEALRMVQLEEFAQ-----RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
877-1047 |
1.86e-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: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 877 FRPGVLTALMGISGAGKTTLLDVLAG--RKTsgyiEGEIRISGflkvqetfarvsgycEQTDIHSP-------------- 940
Cdd:COG3845 28 VRPGEIHALLGENGAGKSTLMKILYGlyQPD----SGEILIDG---------------KPVRIRSPrdaialgigmvhqh 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 941 -----SITVEESLIYSAWLRLVPEINPQTKIRFVKQVLETIELeEIK-DALVGvagvsGLSTEQRKRltvaVE----LVA 1010
Cdd:COG3845 89 fmlvpNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGL-DVDpDAKVE-----DLSVGEQQR----VEilkaLYR 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063705989 1011 NPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIV 1047
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSII 195
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
994-1052 |
2.21e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 50.74 E-value: 2.21e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705989 994 LSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQ 1052
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
170-452 |
2.22e-06 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 51.34 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 170 LLGPPGCGKTTLLKALSGnlennlkvLDIFSFGCFLLqmcescllffslfyfpqcygeisyNGHGLNEVVPQKTS-AYIS 248
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAG--------FEQPDSGSIML------------------------DGEDVTNVPPHLRHiNMVF 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 249 QHDLHIAEMTTRETIDFSARCQGVgsrtdimmevskrekdggiiPDPEIDAymkaiSVKGLKRSLQtdyilkilgldica 328
Cdd:TIGR01187 49 QSYALFPHMTVEENVAFGLKMRKV--------------------PRAEIKP-----RVLEALRLVQ-------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 329 etLVGNAMKRGI--SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQI---IKSLQQVAHITnaTVFVSLLQpaPE 403
Cdd:TIGR01187 90 --LEEFADRKPHqlSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMqleLKTIQEQLGIT--FVFVTHDQ--EE 163
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1063705989 404 SYDLFDDIVLMAEGKIVYHG-PRDdvlkFFEEcgfqcPERKGVADFLQEV 452
Cdd:TIGR01187 164 AMTMSDRIAIMRKGKIAQIGtPEE----IYEE-----PANLFVARFIGEI 204
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
139-423 |
2.32e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.80 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 139 LLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNleNNLKVLDifsfgcfllqmcescllffsl 218
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAYKILE--------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 219 fyfpqcyGEISYNGHGLNEVVPQKTS------AYisQHDLHIAemttretidfsarcqGVgSRTDIMMEV--SKREKDGg 290
Cdd:CHL00131 64 -------GDILFKGESILDLEPEERAhlgiflAF--QYPIEIP---------------GV-SNADFLRLAynSKRKFQG- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 291 iipDPEIDA--YMKAISVKglkrslqtdyiLKILGLDicaETLVGNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITN 368
Cdd:CHL00131 118 ---LPELDPleFLEIINEK-----------LKLVGMD---PSFLSRNVNEGFSGGEKKRNEILQMALLDSELAILDETDS 180
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1063705989 369 GLDSSTAFQIIKSLQQVAHITNATVFVSLLQPAPEsYDLFDDIVLMAEGKIVYHG 423
Cdd:CHL00131 181 GLDIDALKIIAEGINKLMTSENSIILITHYQRLLD-YIKPDYVHVMQNGKIIKTG 234
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
162-430 |
2.36e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 51.64 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 162 ISPGRLTLLLGPPGCGKTTLLKALSGnLENNLKVlDIFSFGCFL----LQMCESCLLFFSLFYFPQcygeisynghglne 237
Cdd:PRK11432 29 IKQGTMVTLLGPSGCGKTTVLRLVAG-LEKPTEG-QIFIDGEDVthrsIQQRDICMVFQSYALFPH-------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 238 vvpqktsayisqhdlhiaeMTTRETIDFSARCQGVGSRtdimmEVSKREKDGgiipdpeidaymkaisvkglkrslqtdy 317
Cdd:PRK11432 93 -------------------MSLGENVGYGLKMLGVPKE-----ERKQRVKEA---------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 318 iLKILGLDICAETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSS---TAFQIIKSLQQVAHITnaTVF 394
Cdd:PRK11432 121 -LELVDLAGFEDRYVDQ-----ISGGQQQRVALARALILKPKVLLFDEPLSNLDANlrrSMREKIRELQQQFNIT--SLY 192
|
250 260 270
....*....|....*....|....*....|....*.
gi 1063705989 395 VSLLQpaPESYDLFDDIVLMAEGKIVYHGPRDDVLK 430
Cdd:PRK11432 193 VTHDQ--SEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
869-1070 |
2.53e-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: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 869 LLSEITGAFRPGVLTALMGISGAGKTTLldVLAGRKTSGYIEGEIRISGF----LKVQETFARVSgyceqtdihspsITV 944
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDIFDGKIVIDGIdiskLPLHTLRSRLS------------IIL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 945 EESLIYSAWLRLvpEINPQTKIRfVKQVLETIELEEIK----------DALVGVAGvSGLSTEQRKRLTVAVELVANPSI 1014
Cdd:cd03288 102 QDPILFSGSIRF--NLDPECKCT-DDRLWEALEIAQLKnmvkslpgglDAVVTEGG-ENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705989 1015 IFMDEPTTGLDARAAAIVMRAVKnVAETGRTIVCTIHQPSiHIFEAfDELVLLKRG 1070
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVM-TAFADRTVVTIAHRVS-TILDA-DLVLVLSRG 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
879-1025 |
2.65e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 50.69 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 879 PGVLTALMGISGAGKTTLLDVLAGR--KTSGYIEGEIRISGFLKVQE-------TFARVS-GYCEQ--TDIHSPSIT--- 943
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSARlaPDAGEVHYRMRDGQLRDLYAlseaerrRLLRTEwGFVHQhpRDGLRMQVSagg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 944 -VEESLIYSAWlRLVPEINpQTKIRFVKQVleTIELEEIKDALVGVAGvsGLsteqRKRLTVAVELVANPSIIFMDEPTT 1022
Cdd:PRK11701 111 nIGERLMAVGA-RHYGDIR-ATAGDWLERV--EIDAARIDDLPTTFSG--GM----QQRLQIARNLVTHPRLVFMDEPTG 180
|
...
gi 1063705989 1023 GLD 1025
Cdd:PRK11701 181 GLD 183
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
154-429 |
3.32e-06 |
|
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: 50.18 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfllqmcescllffslFYfpqcygeisyngh 233
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQR-------------------------------FY------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 234 glnevVPQKTSAYISQHDLHIAEMTtretidfSARCQ-GVGSRTDIMMEVSKREKDGGIIPDPEIDAYMKAISVKGLKrs 312
Cdd:cd03252 53 -----VPENGRVLVDGHDLALADPA-------WLRRQvGVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAH-- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 313 lqtDYILKI-LGLDicaeTLVGNaMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAhiTNA 391
Cdd:cd03252 119 ---DFISELpEGYD----TIVGE-QGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC--AGR 188
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1063705989 392 TVFV-----SLLQPApesydlfDDIVLMAEGKIVYHGPRDDVL 429
Cdd:cd03252 189 TVIIiahrlSTVKNA-------DRIIVMEKGRIVEQGSHDELL 224
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
869-1052 |
5.79e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 869 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYI--EGEIRISGFLKVQETFARVSgycEQTDIhSPSITV 944
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGllNPEKGEIlfERQSIKKDLCTYQKQLCFVG---HRSGI-NPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 945 EESLIYsawlrlvpEINPQTKIRFVKQVLETIELEEIKDALVGVagvsgLSTEQRKRLTVAVELVANPSIIFMDEPTTGL 1024
Cdd:PRK13540 92 RENCLY--------DIHFSPGAVGITELCRLFSLEHLIDYPCGL-----LSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180
....*....|....*....|....*...
gi 1063705989 1025 DARAAAIVMRAVKNVAETGRTIVCTIHQ 1052
Cdd:PRK13540 159 DELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
869-1053 |
6.82e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 49.28 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 869 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLaGRKTSGYiEGEIRISG-FLKVQETFARVS--------GYCEQTDIHS 939
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL-NRLIEIY-DSKIKVDGkVLYFGKDIFQIDaiklrkevGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 940 PSITVEESLIYSAWLRLVPEINPQTKIrfVKQVLETIEL-EEIKDALVGVAgvSGLSTEQRKRLTVAVELVANPSIIFMD 1018
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKI--VEECLRKVGLwKEVYDRLNSPA--SQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1063705989 1019 EPTTGLDARAAAIVMRAVKNVAETgRTIVCTIHQP 1053
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNP 212
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
150-186 |
7.62e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 49.24 E-value: 7.62e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1063705989 150 ANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALS 186
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA 49
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
878-1077 |
7.82e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.02 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 878 RPGVLTALMGISGAGKTTLLDVLAGRKTSGYIEGEIRISG----FLKVQETFARVSGYCEQTDIHSPSITVEESLIYSA- 952
Cdd:PRK09580 25 RPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGkdllELSPEDRAGEGIFMAFQYPVEIPGVSNQFFLQTALn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 953 WLRLVPEINPQTKIRFVKQVLETIELEEIKDALVGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIV 1032
Cdd:PRK09580 105 AVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063705989 1033 MRAVKNVAETGRTIVCTIHQPSIHIFEAFDELVLLKRgGRMIYSG 1077
Cdd:PRK09580 185 ADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQ-GRIVKSG 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
884-1070 |
8.13e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 49.42 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 884 ALMGISGAGKTTLLDVLAG--RKTSG--YIEGE-IRISGFLKVQETFARVSgycEQTDIHSPSITVEESLIYSAwlrLVP 958
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGilKPTSGsvLIRGEpITKENIREVRKFVGLVF---QNPDDQIFSPTVEQDIAFGP---INL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 959 EINPQTKIRFVKQVLETIELEEIKDALVgvagvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKN 1038
Cdd:PRK13652 108 GLDEETVAHRVSSALHMLGLEELRDRVP-----HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLND 182
|
170 180 190
....*....|....*....|....*....|...
gi 1063705989 1039 VAET-GRTIVCTIHQPSIhIFEAFDELVLLKRG 1070
Cdd:PRK13652 183 LPETyGMTVIFSTHQLDL-VPEMADYIYVMDKG 214
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1221-1385 |
9.07e-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: 49.70 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1221 VLGAIYGLVLFVGINNCTSALqYFETERNVMYRERFAGMySAFAYALAQVVTEIPYIFIQsaeFVIVIYPMIGFYASFSK 1300
Cdd:pfam12698 163 LVGLILMIIILIGAAIIAVSI-VEEKESRIKERLLVSGV-SPLQYWLGKILGDFLVGLLQ---LLIILLLLFGIGIPFGN 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1301 VFWSLYAMFCNLLCFNYLAMFLISITPNFMVAAILQSLFFTTFNIFAGFLIPKPQIPKWWVWFYYITPTSWTLNLFFSSQ 1380
Cdd:pfam12698 238 LGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLRLI 317
|
....*
gi 1063705989 1381 YGDIH 1385
Cdd:pfam12698 318 YGDSL 322
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
880-1051 |
1.00e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 48.83 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 880 GVLTALMGISGAGKTTLLDVLAGRKTSG----YIEGEiRISGFlkVQETFARVSGYCEQTDIHSPSITVEEsliysawlr 955
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAhghvWLDGE-HIQHY--ASKEVARRIGLLAQNATTPGDITVQE--------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 956 LVpeinpqTKIRFVKQVLETIELEEIKDALVGVAGVSG-----------LSTEQRKRLTVAVELVANPSIIFMDEPTTGL 1024
Cdd:PRK10253 101 LV------ARGRYPHQPLFTRWRKEDEEAVTKAMQATGithladqsvdtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180
....*....|....*....|....*...
gi 1063705989 1025 DARAAAIVMRAVKNV-AETGRTIVCTIH 1051
Cdd:PRK10253 175 DISHQIDLLELLSELnREKGYTLAAVLH 202
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
884-1070 |
1.10e-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: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 884 ALMGISGAGKTTLLDVLAGrktsgYI---EGEIRISGflkvqetfARVSGYCEQTDIHSPSITVEESLIYS----AWLRL 956
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMG-----YYpltEGEIRLDG--------RPLSSLSHSVLRQGVAMVQQDPVVLAdtflANVTL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 957 VPEINPQTkirfVKQVLETIELEEI----KDALVGVAGVSG--LSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAA 1030
Cdd:PRK10790 438 GRDISEEQ----VWQALETVQLAELarslPDGLYTPLGEQGnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ 513
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063705989 1031 IVMRAVKNVAETgRTIVCTIHQPSIhIFEAfDELVLLKRG 1070
Cdd:PRK10790 514 AIQQALAAVREH-TTLVVIAHRLST-IVEA-DTILVLHRG 550
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
869-1078 |
1.19e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.67 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 869 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYIEGEIRISGFLKVQ-ETFARvsgyceqtdIHSPSITVEES 947
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTLNgEPLAA---------IDAPRLARLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 948 LIYSAWLRLVP----EINPQTKIRFVKQVLET-IELEEIKDALVGVAG--------VSGLSTEQRKRLTVAVEL------ 1008
Cdd:PRK13547 87 VLPQAAQPAFAfsarEIVLLGRYPHARRAGALtHRDGEIAWQALALAGatalvgrdVTTLSGGELARVQFARVLaqlwpp 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 1009 ---VANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTI-HQPSIHIFEAfDELVLLKrGGRMIYSGP 1078
Cdd:PRK13547 167 hdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIvHDPNLAARHA-DRIAMLA-DGAIVAHGA 238
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
999-1081 |
1.32e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.96 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 999 RKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIhQPSIHIFEAFDELVLLKRgGRMIYSGP 1078
Cdd:NF000106 150 RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTT-QYMEEAEQLAHELTVIDR-GRVIADGK 227
|
...
gi 1063705989 1079 LGQ 1081
Cdd:NF000106 228 VDE 230
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
878-1079 |
1.42e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 878 RPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIEgeirisgFLKVQETFARVSGYCEQ--TDIHSP-SITVEESLIYSA 952
Cdd:PRK10982 22 RPHSIHALMGENGAGKSTLLKCLFGiyQKDSGSIL-------FQGKEIDFKSSKEALENgiSMVHQElNLVLQRSVMDNM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 953 WLRLVPeinpqTKIRFVKQVLETIELEEIKDAL-VGV---AGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARA 1028
Cdd:PRK10982 95 WLGRYP-----TKGMFVDQDKMYRDTKAIFDELdIDIdprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063705989 1029 AAIVMRAVKNVAETGRTIVCTIHQPSiHIFEAFDELVLLkRGGRMIYSGPL 1079
Cdd:PRK10982 170 VNHLFTIIRKLKERGCGIVYISHKME-EIFQLCDEITIL-RDGQWIATQPL 218
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
153-423 |
1.43e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 49.46 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 153 KILTD-VSGIISPGRLTLLLGPPGCGKTTLLKALSGNL--ENNLKVldifsfgcfllqmcescllffslfyfpqcygeis 229
Cdd:PRK11174 363 KTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLpyQGSLKI---------------------------------- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 230 yNGHGLNEVVPQ---KTSAYISQhDLHIAEMTTRETIDFsARCQgvgsrtdimmevskrekdggiIPDPEIDAymkaisv 306
Cdd:PRK11174 409 -NGIELRELDPEswrKHLSWVGQ-NPQLPHGTLRDNVLL-GNPD---------------------ASDEQLQQ------- 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 307 kGLKRSLQTDYILKI-LGLDicaeTLVGNAMkRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQV 385
Cdd:PRK11174 458 -ALENAWVSEFLPLLpQGLD----TPIGDQA-AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA 531
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1063705989 386 AHiTNATVFVS-----LLQpapesydlFDDIVLMAEGKIVYHG 423
Cdd:PRK11174 532 SR-RQTTLMVThqledLAQ--------WDQIWVMQDGQIVQQG 565
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
852-1025 |
1.56e-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: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 852 DVPVEMKG--QGYNEKKLqlLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGFLKVqetfarvs 929
Cdd:COG0488 313 KKVLELEGlsKSYGDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEP--DSGTVKLGETVKI-------- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 930 GYCEQtdiHSPSITVEESLIysAWLRlvpEINPQTKIRFVKQVLETIeL---EEIkDALVGVagvsgLSTEQRKRLTVAV 1006
Cdd:COG0488 381 GYFDQ---HQEELDPDKTVL--DELR---DGAPGGTEQEVRGYLGRF-LfsgDDA-FKPVGV-----LSGGEKARLALAK 445
|
170
....*....|....*....
gi 1063705989 1007 ELVANPSIIFMDEPTTGLD 1025
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLD 464
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
139-417 |
1.67e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 48.16 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 139 LLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfllqmcescllffsl 218
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAG------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 219 FYFPQcYGEISYNGHGLNEvvPQKTSAYISQHDLHIAEMTTRETIDFSARCQGVGsrtdimmevsKREKdggiipdpeid 298
Cdd:PRK11248 50 FVPYQ-HGSITLDGKPVEG--PGAERGVVFQNEGLLPWRNVQDNVAFGLQLAGVE----------KMQR----------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 299 aymkaisvkgLKRSLQtdyILKILGLDicaetlvgNAMKRGI---SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTA 375
Cdd:PRK11248 106 ----------LEIAHQ---MLKKVGLE--------GAEKRYIwqlSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1063705989 376 FQIIKSLQQVAHITNATVFVsLLQPAPESYDLFDDIVLMAEG 417
Cdd:PRK11248 165 EQMQTLLLKLWQETGKQVLL-ITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
868-1070 |
2.12e-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: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 868 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLagrktsgyiegeiriSGFLKVQETFARVSGYC----EQTDIHSPSIT 943
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALL---------------ENFYQPQGGQVLLDGKPisqyEHKYLHSKVSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 944 V-EESLIYSAWLrlvpeinpQTKIRFVkqvLETIELEEIKDALVGV----------------AGVSG--LSTEQRKRLTV 1004
Cdd:cd03248 93 VgQEPVLFARSL--------QDNIAYG---LQSCSFECVKEAAQKAhahsfiselasgydteVGEKGsqLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705989 1005 AVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETgRTIVCTIHQpsIHIFEAFDELVLLKRG 1070
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHR--LSTVERADQILVLDGG 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
869-1077 |
2.17e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 869 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGrktsgyiEGEIRiSGFLKVQETFARVSgycEQTDIHSPsiTVEESL 948
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS-------QFEIS-EGRVWAERSIAYVP---QQAWIMNA--TVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 949 IYsawlrlvpeINPQTKIRFVKQV----LETiELEEIKDAL---VGVAGVSgLSTEQRKRLTVAVELVANPSIIFMDEPT 1021
Cdd:PTZ00243 742 LF---------FDEEDAARLADAVrvsqLEA-DLAQLGGGLeteIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705989 1022 TGLDARAAAIVMRAVKNVAETGRTIVCTIHQpsIHIFEAFDELVLLKRgGRMIYSG 1077
Cdd:PTZ00243 811 SALDAHVGERVVEECFLGALAGKTRVLATHQ--VHVVPRADYVVALGD-GRVEFSG 863
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
139-187 |
2.36e-05 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 47.78 E-value: 2.36e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1063705989 139 LLKLSGV----RTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSG 187
Cdd:COG1116 7 ALELRGVskrfPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAG 59
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
967-1070 |
2.41e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 47.82 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 967 RFVKQVLETIELEEIKDAlvgvaGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGR-T 1045
Cdd:PRK13648 121 RRVSEALKQVDMLERADY-----EPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiT 195
|
90 100
....*....|....*....|....*..
gi 1063705989 1046 IVCTIHQPSihifEAF--DELVLLKRG 1070
Cdd:PRK13648 196 IISITHDLS----EAMeaDHVIVMNKG 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
870-1048 |
2.53e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.77 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 870 LSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYIEGEIRISG----FLKVQETfarvsgycEQTD---IHS--- 939
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGeelqASNIRDT--------ERAGiaiIHQela 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 940 --PSITVEESLIysawlrLVPEINPQTKIRFVKQVLETIE-LEEIKDALVGVAGVSGLSTEQRKRLTVAVELVANPSIIF 1016
Cdd:PRK13549 93 lvKELSVLENIF------LGNEITPGGIMDYDAMYLRAQKlLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190
....*....|....*....|....*....|..
gi 1063705989 1017 MDEPTTGLDARAAAIVMRAVKNVAETGrtIVC 1048
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDLKAHG--IAC 196
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
840-1070 |
2.92e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 47.52 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 840 LTITFQDLNYYVDVPVEMKGQGynekklqlLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIEgeirisg 917
Cdd:PRK13641 1 MSIKFENVDYIYSPGTPMEKKG--------LDNISFELEEGSFVALVGHTGSGKSTLMQHFNAllKPSSGTIT------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 918 flkvqetfarVSGYceqtdihspSITVEESLIYSAWLR----LVPEInPQTKIrFVKQVLETIEL---------EEIKDA 984
Cdd:PRK13641 66 ----------IAGY---------HITPETGNKNLKKLRkkvsLVFQF-PEAQL-FENTVLKDVEFgpknfgfseDEAKEK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 985 LVGVAGVSGLSTE------------QRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQ 1052
Cdd:PRK13641 125 ALKWLKKVGLSEDliskspfelsggQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHN 204
|
250
....*....|....*...
gi 1063705989 1053 PSiHIFEAFDELVLLKRG 1070
Cdd:PRK13641 205 MD-DVAEYADDVLVLEHG 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
154-394 |
2.95e-05 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 47.55 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfllqmcescllffslFYFPQCyGEISYNGH 233
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAG-------------------------------FLAPSS-GEITLDGV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 234 GLNEvvPQKTSAYISQHDLHIAEMTTRETIDFSARCQGVGsrtdimmevsKREkdggiipdpeidaymkaisvkglkRSL 313
Cdd:COG4525 70 PVTG--PGADRGVVFQKDALLPWLNVLDNVAFGLRLRGVP----------KAE------------------------RRA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 314 QTDYILKILGLDicaetlvgNAMKRGI---SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITN 390
Cdd:COG4525 114 RAEELLALVGLA--------DFARRRIwqlSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTG 185
|
....
gi 1063705989 391 ATVF 394
Cdd:COG4525 186 KGVF 189
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
857-1026 |
3.06e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 857 MKGQG--YNEKKlQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGFLKVqetfarvsGYCEQ 934
Cdd:PRK11819 9 MNRVSkvVPPKK-QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE--FEGEARPAPGIKV--------GYLPQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 935 TDIHSPSITV----EESL--IYSAWLRLvPEIN-----PQTKirFVKQVLETIELEEIKDALVGV--------------- 988
Cdd:PRK11819 78 EPQLDPEKTVrenvEEGVaeVKAALDRF-NEIYaayaePDAD--FDALAAEQGELQEIIDAADAWdldsqleiamdalrc 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1063705989 989 ----AGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDA 1026
Cdd:PRK11819 155 ppwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 196
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
880-1051 |
3.81e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 47.91 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 880 GVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGF-LKVQETFARVSGYCEQTDIHSPSITVEESLIYSAWLRLVP 958
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAGFEQP--TAGQIMLDGVdLSHVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 959 --EINPQtkirfVKQVLETIELEEIKDalvgvAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAV 1036
Cdd:PRK11607 123 kaEIASR-----VNEMLGLVHMQEFAK-----RKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEV 192
|
170
....*....|....*.
gi 1063705989 1037 KNVAE-TGRTIVCTIH 1051
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 |
3.88e-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: 3.88e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1063705989 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLE 190
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELE 51
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
842-1070 |
4.13e-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: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 842 ITFQDLNYyvdvpvemkgqGY-NEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSG----------- 907
Cdd:TIGR00958 479 IEFQDVSF-----------SYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNlyQPTGGqvlldgvplvq 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 908 ----YIEGEIRISGflkvQE--TFARvsgyceqtdihspsiTVEESLIYSAWLRLVPEINPQTKIRFVKQVLEtiELEEI 981
Cdd:TIGR00958 548 ydhhYLHRQVALVG----QEpvLFSG---------------SVRENIAYGLTDTPDEEIMAAAKAANAHDFIM--EFPNG 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 982 KDALVGVAGvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKnvaETGRTIVCTIHQpsIHIFEAF 1061
Cdd:TIGR00958 607 YDTEVGEKG-SQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS---RASRTVLLIAHR--LSTVERA 680
|
....*....
gi 1063705989 1062 DELVLLKRG 1070
Cdd:TIGR00958 681 DQILVLKKG 689
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
862-1077 |
4.15e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.39 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 862 YNEK---KLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGR--KTSGYIEGEIRISGFLKVQETFARVSgyceqtd 936
Cdd:PRK13651 12 FNKKlptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllPDTGTIEWIFKDEKNKKKTKEKEKVL------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 937 ihspsITVEESLIYSAWLRLVPEINPQTKIRFV---KQVLE-TIEleeiKDALVGVA--GVS------------------ 992
Cdd:PRK13651 85 -----EKLVIQKTRFKKIKKIKEIRRRVGVVFQfaeYQLFEqTIE----KDIIFGPVsmGVSkeeakkraakyielvgld 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 993 ---------GLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSiHIFEaFDE 1063
Cdd:PRK13651 156 esylqrspfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD-NVLE-WTK 233
|
250
....*....|....
gi 1063705989 1064 LVLLKRGGRMIYSG 1077
Cdd:PRK13651 234 RTIFFKDGKIIKDG 247
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
864-1055 |
4.37e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 48.18 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 864 EKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLA--GRKTSGyiegEIRISGFLKVQ---ETFARVS----GYCEQ 934
Cdd:PRK10535 18 EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGclDKPTSG----TYRVAGQDVATldaDALAQLRrehfGFIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 935 TDIHSPSIT----VEESLIYSAwlrlvpeinpqtkirfvkqvLETIELEEIKDALVGVAGV--------SGLSTEQRKRL 1002
Cdd:PRK10535 94 RYHLLSHLTaaqnVEVPAVYAG--------------------LERKQRLLRAQELLQRLGLedrveyqpSQLSGGQQQRV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063705989 1003 TVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSI 1055
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQV 206
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
339-423 |
4.49e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 47.15 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 339 GISGGQKKRLTTAEMIVGPTKALFMDEITNGLD---SSTAFQIIKSLQQvahiTNATVFVsLLQPAPESYDLFDDIVLMA 415
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgEHEMMQLILDAKA----NNKTVFV-ITHTMEHVLEVADEVIVMD 250
|
....*...
gi 1063705989 416 EGKIVYHG 423
Cdd:PRK13631 251 KGKILKTG 258
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
139-183 |
5.23e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 46.25 E-value: 5.23e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1063705989 139 LLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLK 183
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLK 51
|
|
| SpoIIIAA |
COG3854 |
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome ... |
72-182 |
5.93e-05 |
|
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443063 Cd Length: 309 Bit Score: 46.68 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 72 IEKLIKHIENDNLKLLKKIRRRMERV-------GVEFPS--IEVRYEHLgvEAACEVVEGKALPTLWNSLKHVFLDLlkl 142
Cdd:COG3854 13 IREALEKLPDPVLDKLEEIRLRLGRPlelrfpgGEYFLSeaYPVTREDL--ERTLNRISNYSLYALEEELRQGYITI--- 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 143 SG---------VRTNEANIKILTDVSG-------------------IISPGRL--TLLLGPPGCGKTTLL 182
Cdd:COG3854 88 PGghrvgiagtVVRESGIVKRIKDISGlniriarevkgtadpilpyIISGGRIynTLIISPPGCGKTTLL 157
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
855-1074 |
6.00e-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: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 855 VEMKGQGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYIEGEIRISGF-LK---VQETFARVSG 930
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSpLKasnIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 931 YCEQTDIHSPSITVEESLIYSAWLRLVPEI-NPQTKIRFVKQVLETIELEEIKDALvgvaGVSGLSTEQRKRLTVAVELV 1009
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLPGGRmAYNAMYLRAKNLLRELQLDADNVTR----PVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705989 1010 ANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGrtIVCTIHQPSIHIFEAFDELVLLKRGGRMI 1074
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHG--VACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
311-429 |
6.67e-05 |
|
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: 47.03 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 311 RSLQTDYILKILGLDICAETLVGNamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQV-AHIT 389
Cdd:TIGR02142 108 RRISFERVIELLGIGHLLGRLPGR-----LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLhAEFG 182
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1063705989 390 NATVFVS-LLQpapESYDLFDDIVLMAEGKIVYHGPRDDVL 429
Cdd:TIGR02142 183 IPILYVShSLQ---EVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
879-1051 |
6.80e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 45.61 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 879 PGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGFLKVQETFARVSGYCEQTDIHSPSITVEESLIYSAWLR-LV 957
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVE--SGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHgRR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 958 PEINPQTKIrfvkqvletieleeikdALVGVAG-----VSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIV 1032
Cdd:PRK13543 114 AKQMPGSAL-----------------AIVGLAGyedtlVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLV 176
|
170
....*....|....*....
gi 1063705989 1033 MRAVKNVAETGRTIVCTIH 1051
Cdd:PRK13543 177 NRMISAHLRGGGAALVTTH 195
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
140-418 |
7.96e-05 |
|
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: 44.87 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennLKVLDifsfgcfllqmcescllffslf 219
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAG-----LEEPD---------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 220 yfpqcYGEISYNGHGLN----EVVPQKTS-AYISQHDLHIAEMTTRETIDFsarcqgvgsrtdimmevskrekdggiipd 294
Cdd:cd03229 54 -----SGSILIDGEDLTdledELPPLRRRiGMVFQDFALFPHLTVLENIAL----------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 295 peidaymkaisvkglkrslqtdyilkilgldicaetlvgnamkrGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSST 374
Cdd:cd03229 100 --------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1063705989 375 AFQIIKSLQQVAHITNATVFVSLLQPApESYDLFDDIVLMAEGK 418
Cdd:cd03229 136 RREVRALLKSLQAQLGITVVLVTHDLD-EAARLADRVVVLRDGK 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
145-189 |
8.27e-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: 8.27e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1063705989 145 VRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNL 189
Cdd:cd03246 8 FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLL 52
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
1051-1105 |
8.64e-05 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 46.82 E-value: 8.64e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1063705989 1051 HQPSIHIFEAFDELVLLKRGGRMIYSGPLGQhsscVIEYFQNIpGVaKIRDKYNP 1105
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLTVYHGPVKK----VEEYFAGL-GI-NVPERVNP 49
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
163-440 |
9.38e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 45.77 E-value: 9.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 163 SPGRLTLLLGPPGCGKTTLLKALSGNLEnnlkvldifsfgcfllqmcescllffslfyfPQcYGEISYNGHGLNE----- 237
Cdd:PRK13638 25 SLSPVTGLVGANGCGKSTLFMNLSGLLR-------------------------------PQ-KGAVLWQGKPLDYskrgl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 238 -VVPQKTSAYISQHDLHIAEMTTRETIDFSARCQGVGSRtdimmEVSKRekdggiipdpeIDAYMKAISVKGLKRS-LQt 315
Cdd:PRK13638 73 lALRQQVATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEA-----EITRR-----------VDEALTLVDAQHFRHQpIQ- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 316 dyilkilgldiCaetlvgnamkrgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFV 395
Cdd:PRK13638 136 -----------C------------LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIS 192
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1063705989 396 SllQPAPESYDLFDDIVLMAEGKIVYHGPRDDVL---KFFEECGFQCP 440
Cdd:PRK13638 193 S--HDIDLIYEISDAVYVLRQGQILTHGAPGEVFactEAMEQAGLTQP 238
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
340-467 |
9.48e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 45.95 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 340 ISGGQKKRLTTAEMI-VGPtKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFvSLLQPAPESyDLFDDIVLMAEGK 418
Cdd:PRK13640 144 LSGGQKQRVAIAGILaVEP-KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVI-SITHDIDEA-NMADQVLVLDDGK 220
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1063705989 419 IVYHGPRDDVLK---FFEECGFQCPerkgvadFLQEVISKKDQGQYWLHQNL 467
Cdd:PRK13640 221 LLAQGSPVEIFSkveMLKEIGLDIP-------FVYKLKNKLKEKGISVPQEI 265
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
340-451 |
1.05e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 45.88 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 340 ISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSLLQpaPESYDLFDDIVLMAEGKI 419
Cdd:PRK13643 145 LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLM--DDVADYADYVYLLEKGHI 222
|
90 100 110
....*....|....*....|....*....|....*
gi 1063705989 420 VYHGPRDDVLK---FFEECGFQCPERKGVADFLQE 451
Cdd:PRK13643 223 ISCGTPSDVFQevdFLKAHELGVPKATHFADQLQK 257
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
340-441 |
1.05e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 45.81 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 340 ISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQI---IKSLQQVAHITnaTVFVSllqpapESYD----LFDDIV 412
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEIlnkIKELHKEYNMT--IILVS------HSMEdvakLADRII 216
|
90 100 110
....*....|....*....|....*....|..
gi 1063705989 413 LMAEGKIVYHGPRDDVLK---FFEECGFQCPE 441
Cdd:PRK13637 217 VMNKGKCELQGTPREVFKeveTLESIGLAVPQ 248
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
868-1025 |
1.07e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 45.49 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 868 QLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYIE--GEIRIsgflkvqetfarvsGYCEQTDIHSPSIt 943
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGlvAPDEGVIKrnGKLRI--------------GYVPQKLYLDTTL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 944 veeSLIYSAWLRLvpeiNPQTKIRFVKQVLETIELEEIKDalvgvAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTG 1023
Cdd:PRK09544 83 ---PLTVNRFLRL----RPGTKKEDILPALKRVQAGHLID-----APMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
..
gi 1063705989 1024 LD 1025
Cdd:PRK09544 151 VD 152
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
164-189 |
1.12e-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: 1.12e-04
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
139-449 |
1.18e-04 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 46.24 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 139 LLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldifsfgcfllqmcescllffsl 218
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG------------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 219 FYFPQCyGEISYNGHGLNEVVPQKTS-AYISQHDL---HiaeMTTRETIDFSARCQGVgsrtdimmevskrekdggiiPD 294
Cdd:COG3842 54 FETPDS-GRILLDGRDVTGLPPEKRNvGMVFQDYAlfpH---LTVAENVAFGLRMRGV--------------------PK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 295 PEIDAymkaisvkglkrslQTDYILKILGLDICAETLVGNamkrgISGGQKKR--LTTAeMIVGPtKALFMDEITNGLDS 372
Cdd:COG3842 110 AEIRA--------------RVAELLELVGLEGLADRYPHQ-----LSGGQQQRvaLARA-LAPEP-RVLLLDEPLSALDA 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 373 ST--AFQI-IKSLQQVAHITnaTVFV--------SLlqpapeSydlfDDIVLMAEGKIVYHGPRDDVlkffeecgFQCPE 441
Cdd:COG3842 169 KLreEMREeLRRLQRELGIT--FIYVthdqeealAL------A----DRIAVMNDGRIEQVGTPEEI--------YERPA 228
|
....*...
gi 1063705989 442 RKGVADFL 449
Cdd:COG3842 229 TRFVADFI 236
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
868-1070 |
1.26e-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: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 868 QLLSEITGAFRPGVLTALMGISGAGKTTLldVLAGRKTSGYIEGEIRISGflkvqetfarvsgyceqTDIhspsitveeS 947
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTL--ILALFRFLEAEEGKIEIDG-----------------IDI---------S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 948 LIYSAWLRLVPEINPQTKIRFVKQVLETIEL------EEIKDALVGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPT 1021
Cdd:cd03369 74 TIPLEDLRSSLTIIPQDPTLFSGTIRSNLDPfdeysdEEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063705989 1022 TGLDARAAAIVMRAVKNVAeTGRTIVCTIHQpsIHIFEAFDELVLLKRG 1070
Cdd:cd03369 154 ASIDYATDALIQKTIREEF-TNSTILTIAHR--LRTIIDYDKILVMDAG 199
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
655-726 |
1.36e-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: 45.84 E-value: 1.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705989 655 FMILFAVHFTSISMFrcIAAIFQTGVAAMTAGSFVMLITFVFAGFAIPYTDMPGWLKWGFWVNPISYAEIGL 726
Cdd:pfam12698 244 LFLLYGLAYIALGYL--LGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGL 313
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
341-429 |
1.73e-04 |
|
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: 45.83 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 341 SGGQKKRLTTAE-MIVGPtKALFMDEITNGLDSSTAFQII---KSLQQVAHItnATVFVSllqpapesYDL------FDD 410
Cdd:COG4172 427 SGGQRQRIAIARaLILEP-KLLVLDEPTSALDVSVQAQILdllRDLQREHGL--AYLFIS--------HDLavvralAHR 495
|
90
....*....|....*....
gi 1063705989 411 IVLMAEGKIVYHGPRDDVL 429
Cdd:COG4172 496 VMVMKDGKVVEQGPTEQVF 514
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
154-187 |
2.03e-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: 2.03e-04
10 20 30
....*....|....*....|....*....|....
gi 1063705989 154 ILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSG 187
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG 411
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
856-1025 |
2.35e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 44.32 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 856 EMKGQGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAG--RKTSGYI--EGEiRISGfLKVQETFARVSgY 931
Cdd:PRK10247 9 QLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASliSPTSGTLlfEGE-DIST-LKPEIYRQQVS-Y 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 932 CEQTdihsPSI---TVEESLIYSAWLRlvpEINPQTKiRFVKQvLETIEL-EEIKDalvgvAGVSGLSTEQRKRLTVAVE 1007
Cdd:PRK10247 86 CAQT----PTLfgdTVYDNLIFPWQIR---NQQPDPA-IFLDD-LERFALpDTILT-----KNIAELSGGEKQRISLIRN 151
|
170
....*....|....*...
gi 1063705989 1008 LVANPSIIFMDEPTTGLD 1025
Cdd:PRK10247 152 LQFMPKVLLLDEITSALD 169
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
338-462 |
2.47e-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: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 338 RGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSLLQPAPESyDLFDDIVLMAEG 417
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIE-DLSDKAIWLENG 245
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1063705989 418 KIVYHGPRDDVLKFFEEcGFQCPERKGVADFLQEVISKKDQGQYW 462
Cdd:TIGR03269 246 EIKEEGTPDEVVAVFME-GVSEVEKECEVEVGEPIIKVRNVSKRY 289
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
109-419 |
2.51e-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: 45.59 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 109 EHLGVEAACEVVE--------GKALPTLW----NSLKHVFLDLLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGC 176
Cdd:TIGR02633 218 QHVATKDMSTMSEddiitmmvGREITSLYphepHEIGDVILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 177 GKTTLLKALsgnlennlkvldifsFGCfllqmcescllffslfYFPQCYGEISYNGHGLNEVVPQKTSayisqhdlhiae 256
Cdd:TIGR02633 298 GRTELVQAL---------------FGA----------------YPGKFEGNVFINGKPVDIRNPAQAI------------ 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 257 mttretidfsarcqgvgsRTDIMMEVSKREKDGgIIPDPEIDaymKAISVKGLKRslqtdyILKILGLDICAET-LVGNA 335
Cdd:TIGR02633 335 ------------------RAGIAMVPEDRKRHG-IVPILGVG---KNITLSVLKS------FCFKMRIDAAAELqIIGSA 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 336 MKR-------------GISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSllQPAP 402
Cdd:TIGR02633 387 IQRlkvktaspflpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVS--SELA 464
|
330
....*....|....*..
gi 1063705989 403 ESYDLFDDIVLMAEGKI 419
Cdd:TIGR02633 465 EVLGLSDRVLVIGEGKL 481
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
153-451 |
2.75e-04 |
|
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: 44.21 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALsgnleNNLkvldifsfgcfllqmcescllffslfyFPQCYGEISYNG 232
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI-----NRL---------------------------IEPTSGEIFIDG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 233 HGLNEVVP---QKTSAYISQHDLHIAEMTTRETIdfsarcqgvgsrtdimmevskrekdgGIIPdpeidaymKAISVKGL 309
Cdd:cd03295 63 EDIREQDPvelRRKIGYVIQQIGLFPHMTVEENI--------------------------ALVP--------KLLKWPKE 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 310 KRSLQTDYILKILGLDIcaetlvGNAMKR---GISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQI---IKSLQ 383
Cdd:cd03295 109 KIRERADELLALVGLDP------AEFADRyphELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLqeeFKRLQ 182
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705989 384 QVAHITnaTVFVSllQPAPESYDLFDDIVLMAEGKIVYHGPRDDVLKffeecgfqCPERKGVADFLQE 451
Cdd:cd03295 183 QELGKT--IVFVT--HDIDEAFRLADRIAIMKNGEIVQVGTPDEILR--------SPANDFVAEFVGA 238
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
983-1039 |
3.00e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 3.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705989 983 DALVGvAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNV 1039
Cdd:PTZ00265 570 ETLVG-SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
866-1047 |
3.27e-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: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 866 KLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGrKTSGYIEGEIRISGflkvqetfarvsgycEQTDIHSPSITVE 945
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKFEGNVFING---------------KPVDIRNPAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 946 ESLIysawlrLVPE------INPQ------------TKIRFVKQVLETIELEEIKDAL----VGVAG----VSGLSTEQR 999
Cdd:TIGR02633 336 AGIA------MVPEdrkrhgIVPIlgvgknitlsvlKSFCFKMRIDAAAELQIIGSAIqrlkVKTASpflpIGRLSGGNQ 409
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063705989 1000 KRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIV 1047
Cdd:TIGR02633 410 QKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAII 457
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
138-190 |
3.64e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 45.06 E-value: 3.64e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1063705989 138 DLLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLE 190
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE 366
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
840-1099 |
4.17e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 43.88 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 840 LTITFQDLNYyvdvpVEMKGQGYNEKKLQLLS-EI-TGAFrpgvlTALMGISGAGKTTLLDVLAG--RKTSGyiegEIRI 915
Cdd:PRK13637 1 MSIKIENLTH-----IYMEGTPFEKKALDNVNiEIeDGEF-----VGLIGHTGSGKSTLIQHLNGllKPTSG----KIII 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 916 SGF------LKVQETFARVsGYCEQTdihsPSITVEESLIYS--AW----LRLVPEinpQTKIRfVKQVLETIEL--EEI 981
Cdd:PRK13637 67 DGVditdkkVKLSDIRKKV-GLVFQY----PEYQLFEETIEKdiAFgpinLGLSEE---EIENR-VKRAMNIVGLdyEDY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 982 KDAlvgvaGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNV-AETGRTIVCTIHqpSIHIFEA 1060
Cdd:PRK13637 138 KDK-----SPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSH--SMEDVAK 210
|
250 260 270
....*....|....*....|....*....|....*....
gi 1063705989 1061 FDELVLLKRGGRMIYSGPlgqhsscVIEYFQNIPGVAKI 1099
Cdd:PRK13637 211 LADRIIVMNKGKCELQGT-------PREVFKEVETLESI 242
|
|
| 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 |
4.53e-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: 4.53e-04
10 20
....*....|....*....|....*..
gi 1063705989 162 ISPGRLTLLLGPPGCGKTTLLKALSGN 188
Cdd:cd19511 24 IRPPKGVLLYGPPGCGKTLLAKALASE 50
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
330-429 |
4.84e-04 |
|
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: 43.34 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 330 TLVGNAMKRG-----ISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFV-----SLLQ 399
Cdd:cd03258 126 ELVGLEDKADaypaqLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLithemEVVK 205
|
90 100 110
....*....|....*....|....*....|
gi 1063705989 400 papesyDLFDDIVLMAEGKIVYHGPRDDVL 429
Cdd:cd03258 206 ------RICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
150-216 |
5.22e-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: 42.14 E-value: 5.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705989 150 ANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGnlennlkvldIFSFGCFLLQMCESCLLFF 216
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG----------LWPWGSGRIGMPEGEDLLF 68
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
137-191 |
5.22e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 43.02 E-value: 5.22e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1063705989 137 LDLLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLEN 191
Cdd:COG2401 28 AIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKG 82
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
861-1047 |
5.49e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.39 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 861 GYNEKKLQllsEITGAFRPGVLTALMGISGAGKTTLLDVLAGrkTSGYIEGEIRISG--------FLKVQETFA------ 926
Cdd:PRK09700 273 SRDRKKVR---DISFSVCRGEILGFAGLVGSGRTELMNCLFG--VDKRAGGEIRLNGkdisprspLDAVKKGMAyitesr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 927 RVSGYCEQTDIhSPSITVEESLIYSAWLRLVPEINPQTKIRFVKQvleTIELEEIKDALVGvAGVSGLSTEQRKRLTVAV 1006
Cdd:PRK09700 348 RDNGFFPNFSI-AQNMAISRSLKDGGYKGAMGLFHEVDEQRTAEN---QRELLALKCHSVN-QNITELSGGNQQKVLISK 422
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063705989 1007 ELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIV 1047
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVIL 463
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
162-198 |
6.00e-04 |
|
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: 44.13 E-value: 6.00e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1063705989 162 ISPGRLTLLLGPPGCGKTTLLKALSGNLENNLKVLDI 198
Cdd:COG0464 188 LPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDL 224
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
71-182 |
6.03e-04 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 43.70 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 71 MIEKLIKHIENDNLKL---LKKIRRRMERVGVEfpsievryEHLGVEAACEVVEGKALPTLWNSLKHVFLDLLKlsgvrt 147
Cdd:COG1419 89 LLEEQLSGLAGESARLppeLAELLERLLEAGVS--------PELARELLEKLPEDLSAEEAWRALLEALARRLP------ 154
|
90 100 110
....*....|....*....|....*....|....*
gi 1063705989 148 neanikilTDVSGIISPGRLTLLLGPPGCGKTTLL 182
Cdd:COG1419 155 --------VAEDPLLDEGGVIALVGPTGVGKTTTI 181
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
160-201 |
6.16e-04 |
|
proteases similar to RecA; RecA-like NTPases. This family 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. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 41.88 E-value: 6.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1063705989 160 GIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLKVLDIFSF 201
Cdd:cd19481 21 YGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSL 62
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
149-423 |
6.30e-04 |
|
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: 42.30 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 149 EANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLennlkvldifsfgcfllqmcescllffslfyfpqcygei 228
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDL--------------------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 229 synghglnevVPQKTSAYISQHDLHIAEMTTRETIdfsarcqgvgsrtdimmevskrekdgGIIPdpeidaymkaisvkg 308
Cdd:cd03247 53 ----------KPQQGEITLDGVPVSDLEKALSSLI--------------------------SVLN--------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 309 lkrslQTDYILkilgldicAETLVGNAMKRgISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHi 388
Cdd:cd03247 82 -----QRPYLF--------DTTLRNNLGRR-FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK- 146
|
250 260 270
....*....|....*....|....*....|....*.
gi 1063705989 389 tNATV-FVSLLQPAPESydlFDDIVLMAEGKIVYHG 423
Cdd:cd03247 147 -DKTLiWITHHLTGIEH---MDKILFLENGKIIMQG 178
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
399-442 |
6.53e-04 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 43.74 E-value: 6.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1063705989 399 QPapeSYDL---FDDIVLMAEG-KIVYHGPRDDVLKFFEECGFQCPER 442
Cdd:pfam19055 2 QP---SYTLfkmFDDLILLAKGgLTVYHGPVKKVEEYFAGLGINVPER 46
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
864-1074 |
6.72e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 43.16 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 864 EKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGFLKVQETF----ARVSGYCEQTDIHS 939
Cdd:PRK13642 17 ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE--FEGKVKIDGELLTAENVwnlrRKIGMVFQNPDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 940 PSITVEESLIYSAWLRLVPEinpQTKIRFVKQVLETIELEEIKdalvgVAGVSGLSTEQRKRLTVAVELVANPSIIFMDE 1019
Cdd:PRK13642 95 VGATVEDDVAFGMENQGIPR---EEMIKRVDEALLAVNMLDFK-----TREPARLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705989 1020 PTTGLDARAAAIVMRAVKNVAETGRTIVCTIhqpsIHIFE--AFDELVLLKRGGRMI 1074
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIHEIKEKYQLTVLSI----THDLDeaASSDRILVMKAGEII 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
979-1075 |
6.87e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 43.23 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 979 EEIKDALvGVAGVSgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETgRTIVCTIH---QPS- 1054
Cdd:PRK14243 139 DEVKDKL-KQSGLS-LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHnmqQAAr 215
|
90 100
....*....|....*....|.
gi 1063705989 1055 IHIFEAFDELVLLKRGGRMIY 1075
Cdd:PRK14243 216 VSDMTAFFNVELTEGGGRYGY 236
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
138-189 |
6.90e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 43.22 E-value: 6.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1063705989 138 DLLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNL 189
Cdd:PRK11831 6 NLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQI 57
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
869-1025 |
7.03e-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: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 869 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGflkvqetfaRVSgYCEQTDIHSPSiTVEESL 948
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPS--EGKIKHSG---------RIS-FSPQTSWIMPG-TIKDNI 507
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705989 949 IYSawlrLVPEINPQTKIRFVKQVLETIELEEIKDALVGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLD 1025
Cdd:TIGR01271 508 IFG----LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
870-1070 |
7.73e-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: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 870 LSEITGAFRPGVLTALMGISGAGKTTLldVLAGRKTSGYIEGEIRISGFLkvqetfarvsgyCEQTDIH----SPSITVE 945
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSL--LLALFRLVELSSGSILIDGVD------------ISKIGLHdlrsRISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 946 ESLIYSAWLR--LVP-------EINpqtkirfvkQVLETIELEEIKDALVG------VAGVSGLSTEQRKRLTVAVELVA 1010
Cdd:cd03244 86 DPVLFSGTIRsnLDPfgeysdeELW---------QALERVGLKEFVESLPGgldtvvEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 1011 NPSIIFMDEPTTGLDARAAAIVMRAVKNvAETGRTIVCTIHQpsIHIFEAFDELVLLKRG 1070
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 |
8.23e-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: 8.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1063705989 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSG 187
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSG 48
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
160-200 |
8.87e-04 |
|
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: 42.85 E-value: 8.87e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1063705989 160 GIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLKVLDIFS 200
Cdd:COG3267 38 ALAQGGGFVVLTGEVGTGKTTLLRRLLERLPDDVKVAYIPN 78
|
|
| RecA-like_BCS1 |
cd19510 |
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ... |
169-198 |
9.31e-04 |
|
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. RecA-like NTPases. This family 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. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410918 [Multi-domain] Cd Length: 153 Bit Score: 41.18 E-value: 9.31e-04
10 20 30
....*....|....*....|....*....|
gi 1063705989 169 LLLGPPGCGKTTLLKALSGNLENNLKVLDI 198
Cdd:cd19510 27 LLYGPPGTGKSSFIAALAGELDYDICDLNL 56
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
962-1070 |
9.93e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.20 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 962 PQTKIRFVKQVLETIELEEIKDALVGVAGVSGLSTEQRKRLTVAVELV--ANPSIIFMDEPTTGLDARAAAIVMRAV--- 1036
Cdd:smart00382 27 GPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALArkLKPDVLILDEITSLLDAEQEALLLLLEelr 106
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1063705989 1037 ---KNVAETGRTIVCTIHQPSI----HIFEAFDELVLLKRG 1070
Cdd:smart00382 107 lllLLKSEKNLTVILTTNDEKDlgpaLLRRRFDRRIVLLLI 147
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
800-1025 |
1.02e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 800 QDKLSELQGTKD---SSVKKNKPLDSSIKTNEDPgKMILPF---KPLTITFQDLNYYVDVPVEMK--GQGYNEKKLqlLS 871
Cdd:PRK10636 253 QERVAHLQSYIDrfrAKATKAKQAQSRIKMLERM-ELIAPAhvdNPFHFSFRAPESLPNPLLKMEkvSAGYGDRII--LD 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 872 EITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGFLKVqetfarvsGYCEQTDIHspsitveesliys 951
Cdd:PRK10636 330 SIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAP--VSGEIGLAKGIKL--------GYFAQHQLE------------- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 952 aWLRlVPEINPQTKIRFVKQVLEtielEEIKDALVG-------VAGVSG-LSTEQRKRLTVAVELVANPSIIFMDEPTTG 1023
Cdd:PRK10636 387 -FLR-ADESPLQHLARLAPQELE----QKLRDYLGGfgfqgdkVTEETRrFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
..
gi 1063705989 1024 LD 1025
Cdd:PRK10636 461 LD 462
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
93-190 |
1.16e-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: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 93 RMERVGVEFPsiEVRYEHLG-----VEAACEVVEgkaLPtlwnsLKHVflDLLKLSGvrtneanikiltdvsgiISPGRL 167
Cdd:COG1222 64 RGTAVPAESP--DVTFDDIGgldeqIEEIREAVE---LP-----LKNP--ELFRKYG-----------------IEPPKG 114
|
90 100
....*....|....*....|...
gi 1063705989 168 TLLLGPPGCGKTTLLKALSGNLE 190
Cdd:COG1222 115 VLLYGPPGTGKTLLAKAVAGELG 137
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
875-1042 |
1.28e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 875 GAFRPG-VLTALmGISGAGKTTLLDVLAGR--KTSGYIEGEIRISgfLKVQETFARVSGyceqtdihspsiTVEEsliys 951
Cdd:PRK13409 360 GEIYEGeVIGIV-GPNGIGKTTFAKLLAGVlkPDEGEVDPELKIS--YKPQYIKPDYDG------------TVED----- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 952 aWLRlvpEINPQTKIRFVK-QVLETIELEEIKDALvgvagVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAA 1030
Cdd:PRK13409 420 -LLR---SITDDLGSSYYKsEIIKPLQLERLLDKN-----VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 490
|
170
....*....|..
gi 1063705989 1031 IVMRAVKNVAET 1042
Cdd:PRK13409 491 AVAKAIRRIAEE 502
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
162-189 |
1.32e-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: 1.32e-03
10 20
....*....|....*....|....*...
gi 1063705989 162 ISPGRLTLLLGPPGCGKTTLLKALSGNL 189
Cdd:cd19518 31 VEPPRGVLLHGPPGCGKTMLANAIAGEL 58
|
|
| ABC_trans_N |
pfam14510 |
ABC-transporter N-terminal; This domain is found at the N-terminus of ABC-transporter proteins ... |
82-130 |
1.45e-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: 1.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1063705989 82 DNLKLLKKIRRRMERVG-VEFPSIEVRYEHLGVEAAceVVEGKALPTLWN 130
Cdd:pfam14510 32 DLRKWLKNLRRLIDEDGyIKPRKLGVAFKNLTVSGV--GAGADYQPTVGN 79
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
332-423 |
1.52e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 42.14 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 332 VGNAMKR-GI-----------SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVsllq 399
Cdd:PRK13636 122 VDNALKRtGIehlkdkpthclSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIII---- 197
|
90 100
....*....|....*....|....*...
gi 1063705989 400 pAPESYDLF----DDIVLMAEGKIVYHG 423
Cdd:PRK13636 198 -ATHDIDIVplycDNVFVMKEGRVILQG 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
140-188 |
1.81e-03 |
|
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: 41.36 E-value: 1.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1063705989 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGN 188
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH 49
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
169-201 |
1.81e-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: 39.88 E-value: 1.81e-03
10 20 30
....*....|....*....|....*....|...
gi 1063705989 169 LLLGPPGCGKTTLLKALSGNLENNLKVLDIFSF 201
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSEL 34
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
161-200 |
1.92e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.49 E-value: 1.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1063705989 161 IISPGRLTLLLGPPGCGKTTLLKALSGNLENNL----------KVLDIFS 200
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLgdyeeepswdEVLKRFR 144
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
161-200 |
1.98e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.46 E-value: 1.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1063705989 161 IISPGRLTLLLGPPGCGKTTLLKALSGNLENNL----------KVLDIFS 200
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLgdydeepswdEVLKRFR 144
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
341-414 |
2.01e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 41.48 E-value: 2.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 341 SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSLLQPAPESyDLFDDIVLM 414
Cdd:COG2401 138 STGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVID-DLQPDLLIF 210
|
|
| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
155-186 |
2.06e-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: 2.06e-03
10 20 30
....*....|....*....|....*....|..
gi 1063705989 155 LTDVSGIISPGRLTLLLGPPGCGKTTLLKALS 186
Cdd:cd19520 25 LFDNSRLLQPPKGVLLYGPPGCGKTMLAKATA 56
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
869-1025 |
2.21e-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: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 869 LLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGyiEGEIRISGflkvqetfaRVSgYCEQTDIHSPSiTVEESL 948
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPS--EGKIKHSG---------RIS-FSSQFSWIMPG-TIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 949 IYSAwlrlvpeinPQTKIRFvKQVLETIELEEI------KDALVGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTT 1022
Cdd:cd03291 119 IFGV---------SYDEYRY-KSVVKACQLEEDitkfpeKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
...
gi 1063705989 1023 GLD 1025
Cdd:cd03291 189 YLD 191
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
138-187 |
2.51e-03 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 41.25 E-value: 2.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1063705989 138 DLLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSG 187
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLG 52
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
153-185 |
2.56e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 41.18 E-value: 2.56e-03
10 20 30
....*....|....*....|....*....|...
gi 1063705989 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKAL 185
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCL 57
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
338-430 |
2.95e-03 |
|
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: 42.24 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 338 RGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQ-------VAH----ITNAtvfvsllqpapesyd 406
Cdd:TIGR03796 614 ANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRRrgctciiVAHrlstIRDC--------------- 678
|
90 100
....*....|....*....|....
gi 1063705989 407 lfDDIVLMAEGKIVYHGPRDDVLK 430
Cdd:TIGR03796 679 --DEIIVLERGKVVQRGTHEELWA 700
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
340-430 |
3.23e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 41.13 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 340 ISGGQKKRLTTAEMIVGPTKALFMDEITNGLD---SSTAFQIIKSLQQVAhitNATVfVSLLQPAPESYdLFDDIVLMAE 416
Cdd:PRK13632 143 LSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgKREIKKIMVDLRKTR---KKTL-ISITHDMDEAI-LADKVIVFSE 217
|
90
....*....|....
gi 1063705989 417 GKIVYHGPRDDVLK 430
Cdd:PRK13632 218 GKLIAQGKPKEILN 231
|
|
| RecA-like_Pch2-like |
cd19508 |
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ... |
157-189 |
3.54e-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: 40.51 E-value: 3.54e-03
10 20 30
....*....|....*....|....*....|...
gi 1063705989 157 DVSGIISPGRLTLLLGPPGCGKTTLLKALSGNL 189
Cdd:cd19508 44 VNTNLITWNRLVLLHGPPGTGKTSLCKALAQKL 76
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
341-428 |
3.62e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.26 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 341 SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHiTNATVFVSlLQPAPESYDLFDDIVLMAEGKIV 420
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLT-TQYMEEAEQLAHELTVIDRGRVI 223
|
....*...
gi 1063705989 421 YHGPRDDV 428
Cdd:NF000106 224 ADGKVDEL 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
140-189 |
3.79e-03 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 41.37 E-value: 3.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1063705989 140 LKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNL 189
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTL 53
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
157-187 |
3.98e-03 |
|
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: 41.24 E-value: 3.98e-03
10 20 30
....*....|....*....|....*....|.
gi 1063705989 157 DVSGIISPGRLTLLLGPPGCGKTTLLKALSG 187
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAG 47
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
340-426 |
4.04e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 40.83 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 340 ISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHiTNATVFVSllqpaPESYDLF----DDIVLMA 415
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIIS-----THDVDLVpvyaDKVYVMS 211
|
90
....*....|..
gi 1063705989 416 EGKIVYHG-PRD 426
Cdd:PRK13639 212 DGKIIKEGtPKE 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
983-1052 |
4.24e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 4.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705989 983 DALVGVAGVSgLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETG-RTIVCTIHQ 1052
Cdd:PTZ00265 1349 DTNVGPYGKS-LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHR 1418
|
|
| RecA-like_PEX1_r2 |
cd19526 |
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ... |
163-219 |
4.28e-03 |
|
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. 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: 410934 [Multi-domain] Cd Length: 158 Bit Score: 39.33 E-value: 4.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705989 163 SPGRLT---LLLGPPGCGKTTLLKALSGNLENNL------------------KVLDIFSFGcfllQMCESCLLFFSLF 219
Cdd:cd19526 22 SPLRLRsgiLLYGPPGCGKTLLASAIASECGLNFisvkgpellnkyigaseqNVRDLFSRA----QSAKPCILFFDEF 95
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
842-1025 |
4.54e-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: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 842 ITFQDLNYYvdvpvemkgqgYNEKKLqlLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSgyIEGEIRISGFLKV 921
Cdd:cd03221 1 IELENLSKT-----------YGGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEP--DEGIVTWGSTVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 922 qetfarvsGYCEQtdihspsitveesliysawlrlvpeinpqtkirfvkqvletieleeikdalvgvagvsgLSTEQRKR 1001
Cdd:cd03221 66 --------GYFEQ-----------------------------------------------------------LSGGEKMR 78
|
170 180
....*....|....*....|....
gi 1063705989 1002 LTVAVELVANPSIIFMDEPTTGLD 1025
Cdd:cd03221 79 LALAKLLLENPNLLLLDEPTNHLD 102
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
326-423 |
4.55e-03 |
|
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: 40.17 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 326 ICAETLVGNAMKR---GISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSLLQPAp 402
Cdd:cd03298 112 ALARVGLAGLEKRlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPE- 190
|
90 100
....*....|....*....|.
gi 1063705989 403 ESYDLFDDIVLMAEGKIVYHG 423
Cdd:cd03298 191 DAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
340-426 |
4.56e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 40.84 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 340 ISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFV--SLLQPAPESydlfDDIVLMAEG 417
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILitHYMEEAVEA----DRIIVMDSG 220
|
90
....*....|
gi 1063705989 418 KIVYHG-PRD 426
Cdd:PRK13633 221 KVVMEGtPKE 230
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
163-189 |
5.85e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 40.25 E-value: 5.85e-03
10 20
....*....|....*....|....*..
gi 1063705989 163 SPGRLTLLLGPPGCGKTTLLKALSGNL 189
Cdd:COG1223 33 WPPRKILFYGPPGTGKTMLAEALAGEL 59
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
321-426 |
5.98e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 40.85 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 321 ILGLDICAETLVGnamKRGI--SGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHitNATVFV--- 395
Cdd:PRK10789 434 ILRLPQGYDTEVG---ERGVmlSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIIsah 508
|
90 100 110
....*....|....*....|....*....|...
gi 1063705989 396 --SLLQPApesydlfDDIVLMAEGKIVYHGPRD 426
Cdd:PRK10789 509 rlSALTEA-------SEILVMQHGHIAQRGNHD 534
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
124-187 |
6.24e-03 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 40.59 E-value: 6.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 124 ALPTLWNSLKHVFLDLLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSG 187
Cdd:PRK11607 4 AIPRPQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG 67
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
1002-1055 |
6.30e-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: 6.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1063705989 1002 LTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSI 1055
Cdd:pfam13304 248 LAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLL 301
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
129-190 |
6.98e-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: 6.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063705989 129 WNSLKHVFLDLLKLSGVRtneanIKILTDVSGIISPGRlTL-LLGPPGCGKTTLLKALSGNLE 190
Cdd:COG1134 21 SRSLKELLLRRRRTRREE-----FWALKDVSFEVERGE-SVgIIGRNGAGKSTLLKLIAGILE 77
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
153-190 |
7.42e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.92 E-value: 7.42e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1063705989 153 KILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLE 190
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFE 711
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
825-1037 |
7.53e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.61 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 825 KTNEDPGKMILPFKPLTITFQDlnyyvdvpvemkgqgyNEKKLQLLSEITGAFRPGVLTALMGISGAGKT-TLLDVLAGR 903
Cdd:PRK10261 3 HSDELDARDVLAVENLNIAFMQ----------------EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 904 KTSGyieGEIRISGFL-------------KVQETFARVSG------YCEQTDIHSPSITVEESLIYSawLRLVPEINPQT 964
Cdd:PRK10261 67 EQAG---GLVQCDKMLlrrrsrqvielseQSAAQMRHVRGadmamiFQEPMTSLNPVFTVGEQIAES--IRLHQGASREE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063705989 965 KIRFVKQVLETIELEEIKDALVGVAgvSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVK 1037
Cdd:PRK10261 142 AMVEAKRMLDQVRIPEAQTILSRYP--HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIK 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
969-1027 |
8.08e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 8.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705989 969 VKQVLETIELEEIKDALVGvagvsGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLD--AR 1027
Cdd:NF033858 378 VAEMLERFDLADVADALPD-----SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDpvAR 433
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
169-198 |
8.11e-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: 38.67 E-value: 8.11e-03
10 20 30
....*....|....*....|....*....|.
gi 1063705989 169 LLLGPPGCGKTTLLKALSGNL-ENNLKVLDI 198
Cdd:cd00009 23 LLYGPPGTGKTTLARAIANELfRPGAPFLYL 53
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
309-427 |
8.59e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 40.33 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705989 309 LKRSLQTDYIL-KILGLDicaeTLVGnamKRG--ISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQV 385
Cdd:PRK13657 445 AERAQAHDFIErKPDGYD----TVVG---ERGrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL 517
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1063705989 386 AHitNATVFV-----SLLQPApesydlfDDIVLMAEGKIVYHGPRDD 427
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 |
9.26e-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: 9.26e-03
10 20
....*....|....*....|....*..
gi 1063705989 159 SGIISPGRLTLLLGPPGCGKTTLLKAL 185
Cdd:cd19509 26 PGLRGPPRGILLYGPPGTGKTLLARAV 52
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
162-201 |
9.27e-03 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 39.13 E-value: 9.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1063705989 162 ISPGRLTLLLGPPGCGKTTL-LKALSGNLENNLKVLdIFSF 201
Cdd:COG0467 17 LPRGSSTLLSGPPGTGKTTLaLQFLAEGLRRGEKGL-YVSF 56
|
|
| |
