|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
103-1480 |
0e+00 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 2239.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 103 DGFDAHAIFESFVRDADEQGIHIR--KAGVTIEDVSAKGVDASALEGATFGNILCLPLT-IFKGIKAKRHQKMRQIISNV 179
Cdd:TIGR00956 1 EEFNAKAWVKNFRKLIDSDPIYYKpyKLGVAYKNLSAYGVAADSDYQPTFPNALLKILTrGFRKLKKFRDTKTFDILKPM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 180 NALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQFAGGVSGEVAYDGIPQEEMMKRYKADVIYNGELDVHFPYLTVKQTLD 259
Cdd:TIGR00956 81 DGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 260 FAIACKTPALRVNNVSKKEYIASRRDLYATIFGLRHTYNTKVGNDFVRGVSGGERKRVSIAEALAAKGSIYCWDNATRGL 339
Cdd:TIGR00956 161 FAARCKTPQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 340 DASTALEYAKAIRIMTNLLKSTAFVTIYQASENIYETFDKVTVLYSGKQIYFGLIHEAKPYFAKMGYLCPPRQATAEFLT 419
Cdd:TIGR00956 241 DSATALEFIRALKTSANILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPDRQTTADFLT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 420 ALTDPNgFHLIKPGYENKVPRTAEEFETYWLNSPEFAQMKKDIAAYKEKVNTEKTKEVYDESMAQEKSKYTRKKSYYTVS 499
Cdd:TIGR00956 321 SLTSPA-ERQIKPGYEKKVPRTPQEFETYWRNSPEYAQLMKEIDEYLDRCSESDTKEAYRESHVAKQSKRTRPSSPYTVS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 500 YWEQVKLCTQRGFQRIYGNKSYTVINVCSAIIQSFITGSLFYNTPSSTSGAFSRGGVLYFALLYYSLMGLANIS--FEHR 577
Cdd:TIGR00956 400 FSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGALFFAILFNAFSSLLEIAsmYEAR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 578 PILQKHKGYSLYHPSAEAIGSTLASFPFRMIGLTCFFIILFFLSGLHRTAGSFFTIYLFLTMCSEAINGLFEMVSSVCDT 657
Cdd:TIGR00956 480 PIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFICTLAMSHLFRSIGAVTKT 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 658 LSQANSISGILMMSISMYSTYMIQLPSMHPWFKWISYVLPIRYAFESMLNAEFHGRHMDCAnTLVPSGGDYDNLSDDYKV 737
Cdd:TIGR00956 560 LSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHGRRFECS-QYVPSGGGYDNLGVTNKV 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 738 CAFVGSKPGQSYVLGDDYLKNQFQYVYKHTWRNFGILWCFLLGYVVLKVIFTEYKRPVKGGGDALIFKKGSKRFIAHADE 817
Cdd:TIGR00956 639 CTVVGAEPGQDYVDGDDYLKLSFQYYNSHKWRNFGIIIGFTVFFFFVYILLTEFNKGAKQKGEILVFRRGSLKRAKKAGE 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 818 ESPDNVNDIDAKEQFSS-----ESSGANDEVFDDLEAKG-VFIWKDVCFTIPYEGGKRMLLDNVSGYCIPGTMTALMGES 891
Cdd:TIGR00956 719 TSASNKNDIEAGEVLGStdltdESDDVNDEKDMEKESGEdIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGAS 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 892 GAGKTTLLNTLAQR-NVGIIT-GDMLVNGRPIDASFERRTGYVQQQDIHIAELTVRESLQFSARMRRPQHLPDSEKMDYV 969
Cdd:TIGR00956 799 GAGKTTLLNVLAERvTTGVITgGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYV 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 970 EKIIRVLGMEEYAEALVGEVGCGLNVEQRKKLSIGVELVAKPDLLLFLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCT 1049
Cdd:TIGR00956 879 EEVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCT 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1050 IHQPSATLFEEFDRLLLLRKGGQTVYFGDIGKNSATILNYFERNGARKCDSSENPAEYILEAIGAGATASVKEDWHEKWL 1129
Cdd:TIGR00956 959 IHQPSAILFEEFDRLLLLQKGGQTVYFGDLGENSHTIINYFEKHGAPKCPEDANPAEWMLEVIGAAPGAHANQDYHEVWR 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1130 NSVEFEQTKEKVQDLINDLSKQETKSEVgDKPSKYATSYAYQFRYVLIRTSTSFWRSLNYIMSKMMLMLVGGLYIGFTFF 1209
Cdd:TIGR00956 1039 NSSEYQAVKNELDRLEAELSKAEDDNDP-DALSKYAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFF 1117
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1210 NVGKSYVGLQNAMFAAFISIILSAPAMNQIQGRAIASRELFEVRESQSNMFHWSLVLITQYLSELPYHLFFSTIFFVSSY 1289
Cdd:TIGR00956 1118 KVGTSLQGLQNQMFAVFMATVLFNPLIQQYLPPFVAQRDLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWY 1197
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1290 FPLRIFFEASRS------AVYFLNYCIMFQLYYVGLGLMILYMSPNLPSANVILGLCLSFMLSFCGVTQPVSLMPGFWTF 1363
Cdd:TIGR00956 1198 YPVGFYWNASKTgqvherGVLFWLLSTMFFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIF 1277
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1364 MWKASPYTYFVQNLVGIMLHKKPVVCKKKELNYFNPPNGSTCGEYMKPFLEKATGYIENPDATSDCAYCIYEVGDNYLTH 1443
Cdd:TIGR00956 1278 MYRCSPFTYLVQALLSTGLADVPVTCKVKELLTFNPPSGQTCGEYMKPYLENAGGYLLNPNATDSCSFCQYSYTNDFLEP 1357
|
1370 1380 1390
....*....|....*....|....*....|....*..
gi 1351079 1444 ISSKYSYLWRNFGIFWIYIFFNIIAMVCVYYLFHVRQ 1480
Cdd:TIGR00956 1358 ISSKYSGRWRNFGIFIAFIFFNIIATVFFYWLARVPK 1394
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
163-1378 |
1.89e-128 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 435.43 E-value: 1.89e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 163 GIKAKRHQKMrQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQfAGGVSGEVAYDGIPQEEMMKRYKAdvIYN 242
Cdd:PLN03140 169 GINLAKKTKL-TILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDP-SLKVSGEITYNGYRLNEFVPRKTS--AYI 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 243 GELDVHFPYLTVKQTLDFAIACKTPALR---VNNVSKKEYIA-----SRRDLY--AT----------------IFGLRHT 296
Cdd:PLN03140 245 SQNDVHVGVMTVKETLDFSARCQGVGTRydlLSELARREKDAgifpeAEVDLFmkATamegvksslitdytlkILGLDIC 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 297 YNTKVGNDFVRGVSGGERKRVSIAEALAAKGSIYCWDNATRGLDASTALEYAKAIRIMTNLLKSTAFVTIYQASENIYET 376
Cdd:PLN03140 325 KDTIVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFDL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 377 FDKVTVLYSGKQIYFGLIHEAKPYFAKMGYLCPPRQATAEFLTALT----------DPNgfhliKPGYENKVPRTAEEFE 446
Cdd:PLN03140 405 FDDIILLSEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTskkdqeqywaDRN-----KPYRYISVSEFAERFK 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 447 TYWLNspefAQMKKDIAAYKEKVNTEKTKEVYDEsmaqekskytrkksyYTVSYWEQVKLCTQRGFQRIYGNKSYTVINV 526
Cdd:PLN03140 480 SFHVG----MQLENELSVPFDKSQSHKAALVFSK---------------YSVPKMELLKACWDKEWLLMKRNAFVYVFKT 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 527 CSAIIQSFITGSLFYNTPSST----SGAFSRGGVLyFALLYYSLMGLANISF--EHRPILQKHKGYsLYHPS-AEAIGST 599
Cdd:PLN03140 541 VQIIIVAAIASTVFLRTEMHTrneeDGALYIGALL-FSMIINMFNGFAELALmiQRLPVFYKQRDL-LFHPPwTFTLPTF 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 600 LASFPFRMIGLTCFFIILFFLSGLHRTAGSFFTIYLFLTMCSEAINGLFEMVSSVCDTLSQANSISGILMMSISMYSTYM 679
Cdd:PLN03140 619 LLGIPISIIESVVWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFI 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 680 IQLPSMHPWFKWISYVLPIRYAFESM-LNAEFHGRHMDcantlvpsggdydNLSDDykvcafvgskpgQSYVLGDDYLKN 758
Cdd:PLN03140 699 LPKGEIPNWWEWAYWVSPLSYGFNALaVNEMFAPRWMN-------------KMASD------------NSTRLGTAVLNI 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 759 qFQYVYKHTWRNFGIlwCFLLGYVVL-KVIFT---EYKRPvKGGGDALIFKKGSKRFIAHADEE-----SPDNVNDIDAK 829
Cdd:PLN03140 754 -FDVFTDKNWYWIGV--GALLGFTILfNVLFTlalTYLNP-LGKKQAIISEETAEEMEGEEDSIprslsSADGNNTREVA 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 830 EQFSSESSGANDEVFDDLE-AKGVFIWKDVC--FT--------------IPYE------GGKRM-LLDNVSGYCIPGTMT 885
Cdd:PLN03140 830 IQRMSNPEGLSKNRDSSLEaANGVAPKRGMVlpFTplamsfddvnyfvdMPAEmkeqgvTEDRLqLLREVTGAFRPGVLT 909
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 886 ALMGESGAGKTTLLNTLAQRNVG-IITGDMLVNGRP-IDASFERRTGYVQQQDIHIAELTVRESLQFSARMRRPQHLPDS 963
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAGRKTGgYIEGDIRISGFPkKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKE 989
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 964 EKMDYVEKIIRVLGMEEYAEALVGEVG-CGLNVEQRKKLSIGVELVAKPDLLlFLDEPTSGLDSQSSWAIIQLLRKLSKA 1042
Cdd:PLN03140 990 EKMMFVDEVMELVELDNLKDAIVGLPGvTGLSTEQRKRLTIAVELVANPSII-FMDEPTSGLDARAAAIVMRTVRNTVDT 1068
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1043 GQSILCTIHQPSATLFEEFDRLLLLRKGGQTVYFGDIGKNSATILNYFER-NGARKCDSSENPAEYILEAIGAGATASVK 1121
Cdd:PLN03140 1069 GRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYSGPLGRNSHKIIEYFEAiPGVPKIKEKYNPATWMLEVSSLAAEVKLG 1148
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1122 EDWHEKWLNSVEFEQTKekvqDLINDLSKQETksevGDKPSKYATSYAY----QFRYVLIRTSTSFWRSLNYIMSKMMLM 1197
Cdd:PLN03140 1149 IDFAEHYKSSSLYQRNK----ALVKELSTPPP----GASDLYFATQYSQstwgQFKSCLWKQWWTYWRSPDYNLVRFFFT 1220
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1198 LVGGLYIGFTFFNVG--KSYVGLQNAMFAAFISIILSAPAMN--QIQGRAIASRELFeVRESQSNMFHWSLVLITQYLSE 1273
Cdd:PLN03140 1221 LAAALMVGTIFWKVGtkRSNANDLTMVIGAMYAAVLFVGINNcsTVQPMVAVERTVF-YRERAAGMYSALPYAIAQVVCE 1299
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1274 LPYhlffstIFFVSSYFPLRIF----FEASrSAVYFLNYCIMFQ--LYYVGLGLMILYMSPNLPSANVILGLCLSFMLSF 1347
Cdd:PLN03140 1300 IPY------VLIQTTYYTLIVYamvaFEWT-AAKFFWFYFISFFsfLYFTYYGMMTVSLTPNQQVAAIFAAAFYGLFNLF 1372
|
1290 1300 1310
....*....|....*....|....*....|.
gi 1351079 1348 CGVTQPVSLMPGFWTFMWKASPYTYFVQNLV 1378
Cdd:PLN03140 1373 SGFFIPRPKIPKWWVWYYWICPVAWTVYGLI 1403
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
850-1077 |
2.51e-105 |
|
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: 332.67 E-value: 2.51e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 850 KGVFIWKDVCFTIPYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQR-NVGIITGDMLVNGRPIDASFERR 928
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRkTAGVITGEILINGRPLDKNFQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 929 TGYVQQQDIHIAELTVRESLQFSARMRrpqhlpdsekmdyvekiirvlgmeeyaealvgevgcGLNVEQRKKLSIGVELV 1008
Cdd:cd03232 81 TGYVEQQDVHSPNLTVREALRFSALLR------------------------------------GLSVEQRKRLTIGVELA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1351079 1009 AKPDlLLFLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSATLFEEFDRLLLLRKGGQTVYFG 1077
Cdd:cd03232 125 AKPS-ILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRGGKTVYFG 192
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
173-392 |
5.07e-81 |
|
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: 264.89 E-value: 5.07e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQFaGGVSGEVAYDGIPQEEMMKRYKADVIYNGELDVHFPYL 252
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGN-VSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 253 TVKQTLDFAIACKtpalrvnnvskkeyiasrrdlyatifglrhtyntkvGNDFVRGVSGGERKRVSIAEALAAKGSIYCW 332
Cdd:cd03233 99 TVRETLDFALRCK------------------------------------GNEFVRGISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 333 DNATRGLDASTALEYAKAIRIMTNLLKSTAFVTIYQASENIYETFDKVTVLYSGKQIYFG 392
Cdd:cd03233 143 DNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
871-1289 |
2.97e-79 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 275.00 E-value: 2.97e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 871 LLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQRNVG--IITGDMLVNGRPIDAS-FERRTGYVQQQDIHIAELTVRES 947
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvKGSGSVLLNGMPIDAKeMRAISAYVQQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 948 LQFSARMRRPQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGC--GLNVEQRKKLSIGVELVAKPdLLLFLDEPTSGLD 1025
Cdd:TIGR00955 120 LMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDP-PLLFCDEPTSGLD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1026 SQSSWAIIQLLRKLSKAGQSILCTIHQPSATLFEEFDRLLLLrKGGQTVYFGDIGKnsatILNYFERNGARkCDSSENPA 1105
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILM-AEGRVAYLGSPDQ----AVPFFSDLGHP-CPENYNPA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1106 EYILE--AIGAGATASVKEDWHEKW---LNSVEFEQTKEKVQDLINDLSKQETKSEVGDKpSKYATSYAYQFRYVLIRTS 1180
Cdd:TIGR00955 273 DFYVQvlAVIPGSENESRERIEKICdsfAVSDIGRDMLVNTNLWSGKAGGLVKDSENMEG-IGYNASWWTQFYALLKRSW 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1181 TSFWRSLNYIMSKMMLMLVGGLYIGFTFFNVGKSYVGLQNA-----MFAAFISIILSAPAMNQIQgraiASRELFeVRES 1255
Cdd:TIGR00955 352 LSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNIngalfLFLTNMTFQNVFPVINVFT----AELPVF-LRET 426
|
410 420 430
....*....|....*....|....*....|....
gi 1351079 1256 QSNMFHWSLVLITQYLSELPYHLFFSTIFFVSSY 1289
Cdd:TIGR00955 427 RSGLYRVSAYFLAKTIAELPLFIILPALFTSITY 460
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
855-1077 |
2.40e-68 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 228.20 E-value: 2.40e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 855 WKDVCFTIP--YEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLA-QRNVGIITGDMLVNGRPIDA-SFERRTG 930
Cdd:cd03213 6 FRNLTVTVKssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLGVSGEVLINGRPLDKrSFRKIIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 931 YVQQQDIHIAELTVRESLQFSARMRrpqhlpdsekmdyvekiirvlgmeeyaealvgevgcGLNVEQRKKLSIGVELVAK 1010
Cdd:cd03213 86 YVPQDDILHPTLTVRETLMFAAKLR------------------------------------GLSGGERKRVSIALELVSN 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1351079 1011 PdLLLFLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSATLFEEFDRLLLLRKgGQTVYFG 1077
Cdd:cd03213 130 P-SLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQ-GRVIYFG 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
855-1077 |
4.26e-57 |
|
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: 197.49 E-value: 4.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 855 WKDVCFTIPYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQR--NVGIITGDMLVNGRPID-ASFERRTGY 931
Cdd:cd03234 6 WWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRveGGGTTSGQILFNGQPRKpDQFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 932 VQQQDIHIAELTVRESLQFSARMRRPQHLPDSEKmdyvEKIIRVLGMEEYAEALVG-EVGCGLNVEQRKKLSIGVELVAK 1010
Cdd:cd03234 86 VRQDDILLPGLTVRETLTYTAILRLPRKSSDAIR----KKRVEDVLLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1351079 1011 PDLLlFLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSATLFEEFDRLLLLRKGGqTVYFG 1077
Cdd:cd03234 162 PKVL-ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGE-IVYSG 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
168-710 |
5.25e-52 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 194.50 E-value: 5.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 168 RHQKMRQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIdqfAGGV--SGEVAYDGIPQE-EMMKRYKAdviYNGE 244
Cdd:TIGR00955 33 RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRS---PKGVkgSGSVLLNGMPIDaKEMRAISA---YVQQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 245 LDVHFPYLTVKQTLDFAIACKTPalrvNNVSKKEYIAsRRDLYATIFGLRHTYNTKVGN-DFVRGVSGGERKRVSIAEAL 323
Cdd:TIGR00955 107 DDLFIPTLTVREHLMFQAHLRMP----RRVTKKEKRE-RVDEVLQALGLRKCANTRIGVpGRVKGLSGGERKRLAFASEL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 324 AAKGSIYCWDNATRGLDASTALEYAKAIRIMTNLLKsTAFVTIYQASENIYETFDKVTVLYSGKQIYFGLIHEAKPYFAK 403
Cdd:TIGR00955 182 LTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGK-TIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 404 MGYLCPPRQATAEFLTALTDpngfhlIKPGYENKVPRTAEEFETYWLNSPEFAQMKkdiaaykEKVNTEKTKEVYDESMA 483
Cdd:TIGR00955 261 LGHPCPENYNPADFYVQVLA------VIPGSENESRERIEKICDSFAVSDIGRDML-------VNTNLWSGKAGGLVKDS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 484 QEKSKYTrkksyYTVSYWEQVKLCTQRGFQRIYGNKSYTVINVCSAIIQSFITGSLFYNTPSSTSGAFSRGGVLYFALL- 562
Cdd:TIGR00955 328 ENMEGIG-----YNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFLTn 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 563 --YYSLMGLANISFEHRPILQKHKGYSLYHPSAEAIGSTLASFPFRMIGLTCFFIILFFLSGLHRTAGSFFTIYLFLTMC 640
Cdd:TIGR00955 403 mtFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLV 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 641 SEAINGLFEMVSSVCDTLSQANSISGILMMSISMYSTYMIQLPSMHPWFKWISYVLPIRYAFESMLNAEF 710
Cdd:TIGR00955 483 ANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQW 552
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
164-392 |
2.24e-45 |
|
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: 162.34 E-value: 2.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 164 IKAKRHQKMRQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDqfAGGVSGEVAYDGIPQEemMKRYKADVIYNG 243
Cdd:cd03213 13 VKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRT--GLGVSGEVLINGRPLD--KRSFRKIIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 244 ELDVHFPYLTVKQTLDFAIACktpalrvnnvskkeyiasrrdlyatifglrhtyntkvgndfvRGVSGGERKRVSIAEAL 323
Cdd:cd03213 89 QDDILHPTLTVRETLMFAAKL------------------------------------------RGLSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1351079 324 AAKGSIYCWDNATRGLDASTALEYAKAIRIMTNLLKsTAFVTIYQASENIYETFDKVTVLYSGKQIYFG 392
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGR-TIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
173-710 |
1.28e-43 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 170.06 E-value: 1.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDqfAGGVSGEV-AYDGIPQEEMMKRykadVIYNGELDVHFPY 251
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQ--GNNFTGTIlANNRKPTKQILKR----TGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 252 LTVKQTLDFAIACKTPalrvNNVSKKEYIASRRDLYATIfGLRHTYNTKVGNDFVRGVSGGERKRVSIAEALAAKGSIYC 331
Cdd:PLN03211 155 LTVRETLVFCSLLRLP----KSLTKQEKILVAESVISEL-GLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 332 WDNATRGLDASTALEYAKAIRIMTNLLKsTAFVTIYQASENIYETFDKVTVLYSGKQIYFGLIHEAKPYFAKMGYLCPPR 411
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTLGSLAQKGK-TIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFP 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 412 QATAEFLTALTdpNGFHLIKPGYENKVPRTAEEFETYW--LNSPEFaqmkkdiaayKEKVNTEKTKEVYDESMAQEKSKY 489
Cdd:PLN03211 309 MNPADFLLDLA--NGVCQTDGVSEREKPNVKQSLVASYntLLAPKV----------KAAIEMSHFPQANARFVGSASTKE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 490 TRKKSYYTVSYW-EQVKLCTQRGFQRiYGNKSYTVINVCSAIIQSFITGSLFYNtpSSTSGAFSRGGVLYFALLYYSLMG 568
Cdd:PLN03211 377 HRSSDRISISTWfNQFSILLQRSLKE-RKHESFNTLRVFQVIAAALLAGLMWWH--SDFRDVQDRLGLLFFISIFWGVFP 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 569 LANISF---EHRPILQKHKGYSLYHPSAEAIGSTLASFPFRMIGLTCFFIILFFLSGLHRTAGSFFTIYLFLTMCSEAIN 645
Cdd:PLN03211 454 SFNSVFvfpQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQ 533
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351079 646 GLFEMVSSVCDTLSQANSISGILMMSISMYSTYMI-QLPSMHPWFKWISYVLpirYAFESMLNAEF 710
Cdd:PLN03211 534 GLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYVhKLPSCMAWIKYISTTF---YSYRLLINVQY 596
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
507-708 |
5.16e-43 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 155.89 E-value: 5.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 507 CTQRGFQRIYGNKSYTVINVCSAIIQSFITGSLFYNTPSSTSGaFSRGGVLYFALL---YYSLMGLANISFEHRPILQKH 583
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQGG-LNRPGLLFFSILfnaFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 584 KGYSLYHPSAEAIGSTLASFPFRMIGLTCFFIILFFLSGLHRTAGSFFTIYLFLTMCSEAINGLFEMVSSVCDTLSQANS 663
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1351079 664 ISGILMMSISMYSTYMIQLPSMHPWFKWISYVLPIRYAFESMLNA 708
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
868-1290 |
9.55e-42 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 164.67 E-value: 9.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 868 KRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQRNVG-IITGDMLVNGRPIDASFERRTGYVQQQDIHIAELTVRE 946
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 947 SLQFSARMRRPQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGC-GLNVEQRKKLSIGVELVAKPDLLLfLDEPTSGLD 1025
Cdd:PLN03211 160 TLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIrGISGGERKRVSIAHEMLINPSLLI-LDEPTSGLD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1026 SQSSWAIIQLLRKLSKAGQSILCTIHQPSATLFEEFDRLLLLRKgGQTVYFgdiGKNSATIlNYFERNGARKcDSSENPA 1105
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSE-GRCLFF---GKGSDAM-AYFESVGFSP-SFPMNPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1106 EYILE-AIGAGATASVKEDwhekwlnsvEFEQTKEKVQDLINDL--SKQETKSEVG---DKPSKYATSYAYQFRYVLIRT 1179
Cdd:PLN03211 313 DFLLDlANGVCQTDGVSER---------EKPNVKQSLVASYNTLlaPKVKAAIEMShfpQANARFVGSASTKEHRSSDRI 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1180 STSFW---------RSLN----------YIMSKMMLMLVGGLYIGFTFFNVGKSYVGLqnaMFaaFISIILSA-PAMNQI 1239
Cdd:PLN03211 384 SISTWfnqfsillqRSLKerkhesfntlRVFQVIAAALLAGLMWWHSDFRDVQDRLGL---LF--FISIFWGVfPSFNSV 458
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1351079 1240 ----QGRAIAsrelfeVRESQSNMFHWSLVLITQYLSELPYHLFFSTIFFVSSYF 1290
Cdd:PLN03211 459 fvfpQERAIF------VKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYW 507
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
852-1077 |
5.66e-41 |
|
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: 150.11 E-value: 5.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 852 VFIWKDVCFTIPYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQRNVGI--ITGDMLVNGRPIDASFERRT 929
Cdd:cd03233 3 TLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsVEGDIHYNGIPYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 930 G---YVQQQDIHIAELTVRESLQFSARMRRPQhlpdsekmdyvekIIRvlgmeeyaealvgevgcGLNVEQRKKLSIGVE 1006
Cdd:cd03233 83 GeiiYVSEEDVHFPTLTVRETLDFALRCKGNE-------------FVR-----------------GISGGERKRVSIAEA 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1351079 1007 LVAKPDLLLFlDEPTSGLDSQSSWAIIQLLRKLSKA-GQSILCTIHQPSATLFEEFDRLLLLRKGGQtVYFG 1077
Cdd:cd03233 133 LVSRASVLCW-DNSTRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQ-IYYG 202
|
|
| PDR_CDR |
pfam06422 |
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters ... |
722-810 |
3.18e-40 |
|
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters comprising extracellular loop 3, transmembrane segment 6 and linker region.
Pssm-ID: 461906 [Multi-domain] Cd Length: 92 Bit Score: 143.76 E-value: 3.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 722 VPSGGDYDNLSDDYKVCAFVGSKPGQSYVLGDDYLKNQFQYVYKHTWRNFGILWCFLLGYVVLKVIFTEYKRPVKGGGDA 801
Cdd:pfam06422 1 VPSGPGYENVSGANQVCAVVGAVPGQTFVSGDDYLAASYGYSYSHLWRNFGILIAFWIFFLALYLIATEYNSAAKSKGEV 80
|
....*....
gi 1351079 802 LIFKKGSKR 810
Cdd:pfam06422 81 LVFKRGKAP 89
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
867-1070 |
3.06e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 140.58 E-value: 3.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPIDASFE---RRTGYVQQQDIHIA 940
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLL----GLLRptsGEVRVLGEDVARDPAevrRRIGYVPQEPALYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 941 ELTVRESLQFSARMRRpqhLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLlFLDEP 1020
Cdd:COG1131 87 DLTVRENLRFFARLYG---LPRKEARERIDELLELFGLTDAADRKVGTLSGG----MKQRLGLALALLHDPELL-ILDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1351079 1021 TSGLDSQSSWAIIQLLRKLSKAGQSILCTIHqpsatLFEE----FDRLLLLRKG 1070
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTH-----YLEEaerlCDRVAIIDKG 207
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
163-392 |
1.09e-35 |
|
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: 135.86 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 163 GIKAKRHQKMRQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQfAGGVSGEVAYDGIPqeemMKRY--KADVI 240
Cdd:cd03234 10 GLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEG-GGTTSGQILFNGQP----RKPDqfQKCVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 241 YNGELDVHFPYLTVKQTLDFAIACKTPALRVNNVSKKEyiasrrdlyATIFGLRHTYNTKVGNDFVRGVSGGERKRVSIA 320
Cdd:cd03234 85 YVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKR---------VEDVLLRDLALTRIGGNLVKGISGGERRRVSIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351079 321 EALAAKGSIYCWDNATRGLDASTALeyaKAIRIMTNLLK--STAFVTIYQASENIYETFDKVTVLYSGKQIYFG 392
Cdd:cd03234 156 VQLLWDPKVLILDEPTSGLDSFTAL---NLVSTLSQLARrnRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
856-1070 |
1.16e-34 |
|
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: 132.21 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQRNvGIITGDMLVNGRPIDAS----FERRTGY 931
Cdd:cd03225 3 KNLSFS--YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL-GPTSGEVLVDGKDLTKLslkeLRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 932 V-QQQDIHIAELTVRESLQFSARMRrpqHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAK 1010
Cdd:cd03225 80 VfQNPDDQFFGPTVEEEVAFGLENL---GLPEEEIEERVEEALELVGLEGLRDRSPFTLSGG----QKQRVAIAGVLAMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1011 PDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSaTLFEEFDRLLLLRKG 1070
Cdd:cd03225 153 PDILL-LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDG 210
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
867-1088 |
1.11e-31 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 124.97 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSgYCIP-GTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPI---DASFERRTGYVQQQDIHI 939
Cdd:COG4555 12 GKVPALKDVS-FTAKdGEITGLLGPNGAGKTTLLRMLA----GLLKpdsGSILIDGEDVrkePREARRQIGVLPDERGLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 940 AELTVRESLQFSARMRRpqhLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDE 1019
Cdd:COG4555 87 DRLTVRENIRYFAELYG---LFDEELKKRIEELIELLGLEEFLDRRVGELSTG----MKKKVALARALVHDPKVLL-LDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1351079 1020 PTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSaTLFEEFDRLLLLRKgGQTVYFGDIGKNSATILN 1088
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQ-EVEALCDRVVILHK-GKVVAQGSLDELREEIGE 225
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
1175-1380 |
2.68e-31 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 122.38 E-value: 2.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1175 VLIRTSTSFWRSLNYIMSKMMLMLVGGLYIGFTFFNVGKSYVGLQNAMFAAFISIILSAPAMNQIQGRAIASRELFEvRE 1254
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLY-RE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1255 SQSNMFHWSLVLITQYLSELPYHLFFSTIFFVSSYFPLRIFFEASRSAVYFLnYCIMFQLYYVGLGLMILYMSPNLPSAN 1334
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLL-VLLLTALAASSLGLFISALAPSFEDAS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1351079 1335 VILGLCLSFMLSFCGVTQPVSLMPGFWTFMWKASPYTYFVQNLVGI 1380
Cdd:pfam01061 159 QLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
856-1070 |
1.07e-30 |
|
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: 121.06 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGKRML--LDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPID-------A 923
Cdd:cd03255 4 KNLSKT--YGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILG----GLDRptsGEVRVDGTDISklsekelA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 924 SFERRT-GYVQQQDIHIAELTVRESLQFSARMRRpqhLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLS 1002
Cdd:cd03255 78 AFRRRHiGFVFQSFNLLPDLTALENVELPLLLAG---VPKKERRERAEELLERVGLGDRLNHYPSELSGG----QQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1351079 1003 IGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSK-AGQSILCTIHQPSatLFEEFDRLLLLRKG 1070
Cdd:cd03255 151 IARALANDPKIIL-ADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPE--LAEYADRIIELRDG 216
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
856-1070 |
6.47e-30 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 119.36 E-value: 6.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGKRmLLDNVSgYCI-PGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPIDASFE----R 927
Cdd:COG1122 4 ENLSFS--YPGGTP-ALDDVS-LSIeKGEFVAIIGPNGSGKSTLLRLLN----GLLkptSGEVLVDGKDITKKNLrelrR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 928 RTGYV-QQQDIHIAELTVRESLQFSARMRRpqhLPDSEKMDYVEKIIRVLGMEEYAE----ALVGevgcGlnveQRKKLS 1002
Cdd:COG1122 76 KVGLVfQNPDDQLFAPTVEEDVAFGPENLG---LPREEIRERVEEALELVGLEHLADrpphELSG----G----QKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1351079 1003 I-GVeLVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSAtLFEEFDRLLLLRKG 1070
Cdd:COG1122 145 IaGV-LAMEPEVLV-LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDG 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
856-1078 |
1.38e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 118.65 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGgkRMLLDNVSGyCI-PGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPIDASfERRTGY 931
Cdd:COG1121 10 ENLTVS--YGG--RPVLEDVSL-TIpPGEFVAIVGPNGAGKSTLLKAIL----GLLpptSGTVRLFGKPPRRA-RRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 932 VQQQdIHIAE---LTVRE--SLQFSARMRRPQHLPDSEKmDYVEKIIRVLGMEEYAEALVGEV--GcglnveQRKKLSIG 1004
Cdd:COG1121 80 VPQR-AEVDWdfpITVRDvvLMGRYGRRGLFRRPSRADR-EAVDEALERVGLEDLADRPIGELsgG------QQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351079 1005 VELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSaTLFEEFDRLLLLRKGgqTVYFGD 1078
Cdd:COG1121 152 RALAQDPDLLL-LDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLG-AVREYFDRVLLLNRG--LVAHGP 221
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
864-1064 |
1.77e-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: 117.61 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 864 YEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLaqrnVGII---TGDMLVNGRPIDASFE---RRTGYVQQQDI 937
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKML----TGELrptSGTAYINGYSIRTDRKaarQSLGYCPQFDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 938 HIAELTVRESLQFSARMRrpqHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLlFL 1017
Cdd:cd03263 86 LFDELTVREHLRFYARLK---GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGG----MKRKLSLAIALIGGPSVL-LL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1351079 1018 DEPTSGLDSQSS---WAIIQLLRKlskaGQSILCTIHQPsatlfEEFDRL 1064
Cdd:cd03263 158 DEPTSGLDPASRraiWDLILEVRK----GRSIILTTHSM-----DEAEAL 198
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
867-1067 |
4.49e-29 |
|
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: 116.04 E-value: 4.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSgYCI-PGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPID---ASFERRTGYVQQQDIHI 939
Cdd:COG4133 13 GERLLFSGLS-FTLaAGEALALTGPNGSGKTTLLRILA----GLLPpsaGEVLWNGEPIRdarEDYRRRLAYLGHADGLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 940 AELTVRESLQFSARMRRPQHLPDSekmdyVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDE 1019
Cdd:COG4133 88 PELTVRENLRFWAALYGLRADREA-----IDEALEAVGLAGLADLPVRQLSAG----QKRRVALARLLLSPAPLWL-LDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1351079 1020 PTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPsatLFEEFDRLLLL 1067
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAVLLTTHQP---LELAAARVLDL 202
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
867-1070 |
1.94e-28 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 112.88 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPIDASFE---RRTGYVQQQDIHIA 940
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIL----GLLKpdsGEIKVLGKDIKKEPEevkRRIGYLPEEPSLYE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 941 ELTVRESLQFSarmrrpqhlpdsekmdyvekiirvLGMeeyaealvgevgcglnveqRKKLSIGVELVAKPDlLLFLDEP 1020
Cdd:cd03230 87 NLTVRENLKLS------------------------GGM-------------------KQRLALAQALLHDPE-LLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1351079 1021 TSGLDSQSSWAIIQLLRKLSKAGQSILCTIHqpsatLFEE----FDRLLLLRKG 1070
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSH-----ILEEaerlCDRVAILNNG 171
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
856-1070 |
1.79e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 112.06 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTIPYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPID-------ASF 925
Cdd:COG1136 8 RNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILG----GLDRptsGEVLIDGQDISslserelARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 926 ERRT-GYVQQQdiH--IAELTVRESLQFSARMRRpqhLPDSEKMDYVEKIIRVLGMEEYAEALVGE--VGcglnveQRKK 1000
Cdd:COG1136 84 RRRHiGFVFQF--FnlLPELTALENVALPLLLAG---VSRKERRERARELLERVGLGDRLDHRPSQlsGG------QQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351079 1001 LSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKA-GQSILCTIHQPSatLFEEFDRLLLLRKG 1070
Cdd:COG1136 153 VAIARALVNRPKLIL-ADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPE--LAARADRVIRLRDG 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
872-1022 |
2.51e-27 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 108.89 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPID----ASFERRTGYVQQQDIHIAELTV 944
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIA----GLLSpteGTILLDGQDLTdderKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351079 945 RESLQFSARMRRPQHLPDSEKMdyvEKIIRVLGMEEYAEALVGEVGCGLNVEQRKKLSIGVELVAKPDLLLfLDEPTS 1022
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARA---EEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLL-LDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
856-1070 |
2.23e-26 |
|
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: 116.01 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGKRmLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqRNVGIITGDMLVNGRPID----ASFERRTGY 931
Cdd:COG4988 340 EDVSFS--YPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL-GFLPPYSGSILINGVDLSdldpASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 932 VQQQDiHIAELTVRESLqfsaRMRRPQhLPDSEkmdyVEKIIRVLGMEEYAEAL-------VGEVGCGLNVEQRKKLSIG 1004
Cdd:COG4988 416 VPQNP-YLFAGTIRENL----RLGRPD-ASDEE----LEAALEAAGLDEFVAALpdgldtpLGEGGRGLSGGQAQRLALA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1351079 1005 VELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKaGQS-ILCTiHQPSATlfEEFDRLLLLRKG 1070
Cdd:COG4988 486 RALLRDAPLLL-LDEPTAHLDAETEAEILQALRRLAK-GRTvILIT-HRLALL--AQADRILVLDDG 547
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
872-1077 |
3.05e-26 |
|
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: 108.22 E-value: 3.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLLNTLA---QRNVGIITGDML-VNGRPIDAsfERRTGYVQQQDIHIAELTVRES 947
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAgllEPDAGFATVDGFdVVKEPAEA--RRRLGFVSDSTGLYDRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 948 LQFSARMrrpQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQ 1027
Cdd:cd03266 99 LEYFAGL---YGLKGDELTARLEELADRLGMEELLDRRVGGFSTG----MRQKVAIARALVHDPPVLL-LDEPTTGLDVM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1351079 1028 SSWAIIQLLRKLSKAGQSILCTIH--QPSATLfeeFDRLLLLRKgGQTVYFG 1077
Cdd:cd03266 171 ATRALREFIRQLRALGKCILFSTHimQEVERL---CDRVVVLHR-GRVVYEG 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
847-1078 |
4.12e-26 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 108.98 E-value: 4.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 847 LEAKGVfiwkdvcfTIPYegGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPIDA 923
Cdd:COG1120 2 LEAENL--------SVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALA----GLLKpssGEVLLDGRDLAS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 924 ----SFERRTGYVQQQDIHIAELTVRESLqfsARMRRPqHL-----PDSEKMDYVEKIIRVLGMEEYAEALVGEV--Gcg 992
Cdd:COG1120 68 lsrrELARRIAYVPQEPPAPFGLTVRELV---ALGRYP-HLglfgrPSAEDREAVEEALERTGLEHLADRPVDELsgG-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 993 lnveQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSK-AGQSILCTIHQPS-ATLFeeFDRLLLLrKG 1070
Cdd:COG1120 142 ----ERQRVLIARALAQEPPLLL-LDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNlAARY--ADRLVLL-KD 213
|
....*...
gi 1351079 1071 GQTVYFGD 1078
Cdd:COG1120 214 GRIVAQGP 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
867-1070 |
1.34e-25 |
|
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: 106.45 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPID--ASFERRTGYVQQQDIHIAE 941
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIA----GLERpdsGEILIDGRDVTgvPPERRNIGMVFQDYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 942 LTVRESLQFSARMRRpqhLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEPT 1021
Cdd:cd03259 87 LTVAENIAFGLKLRG---VPKAEIRARVRELLELVGLEGLLNRYPHELSGG----QQQRVALARALAREPSLLL-LDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1351079 1022 SGLDSQSSWAIIQLLRKLSKAGQ--SILCTIHQPSAtlFEEFDRLLLLRKG 1070
Cdd:cd03259 159 SALDAKLREELREELKELQRELGitTIYVTHDQEEA--LALADRIAVMNEG 207
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
823-1070 |
1.19e-24 |
|
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: 110.63 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 823 VNDI-DAKEQFSSESSGANDEVFDDLEAKgvfiwkDVCFTipYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNT 901
Cdd:COG4987 309 LNELlDAPPAVTEPAEPAPAPGGPSLELE------DVSFR--YPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 902 LAqRNVGIITGDMLVNGRPIDASFE----RRTGYVQQqDIHIAELTVRESLQFsARmrrpqhlPD-SEkmdyvEKIIRVL 976
Cdd:COG4987 381 LL-RFLDPQSGSITLGGVDLRDLDEddlrRRIAVVPQ-RPHLFDTTLRENLRL-AR-------PDaTD-----EELWAAL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 977 ---GMEEYAEAL-------VGEVGCGLNVEQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKaGQSI 1046
Cdd:COG4987 446 ervGLGDWLAALpdgldtwLGEGGRRLSGGERRRLALARALLRDAPILL-LDEPTEGLDAATEQALLADLLEALA-GRTV 523
|
250 260
....*....|....*....|....
gi 1351079 1047 LCTIHQPSAtlFEEFDRLLLLRKG 1070
Cdd:COG4987 524 LLITHRLAG--LERMDRILVLEDG 545
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
856-1070 |
2.48e-24 |
|
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: 110.31 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGKRMLLDNVSgycI---PGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPID----ASF 925
Cdd:COG2274 477 ENVSFR--YPGDSPPVLDNIS---LtikPGERVAIVGRSGSGKSTLLKLLL----GLYEptsGRILIDGIDLRqidpASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 926 ERRTGYVqQQDIHIAELTVRESLQFSArmrrpQHLPDSEkmdyVEKIIRVLGMEEYAEAL-------VGEVGCGLNVEQR 998
Cdd:COG2274 548 RRQIGVV-LQDVFLFSGTIRENITLGD-----PDATDEE----IIEAARLAGLHDFIEALpmgydtvVGEGGSNLSGGQR 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1351079 999 KKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKaGQSILCTIHQPSaTLfEEFDRLLLLRKG 1070
Cdd:COG2274 618 QRLAIARALLRNPRILI-LDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLS-TI-RLADRIIVLDKG 685
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
856-1077 |
4.69e-24 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 101.84 E-value: 4.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTIpyegGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPIDASfERRTGYV 932
Cdd:cd03235 3 EDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL----GLLKptsGSIRVFGKPLEKE-RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 933 QQQdiHIAE----LTVRESLQfSARMRRPQHLPDSEKMDYvEKIIRVL---GMEEYAEALVGEVGCGlnveQRKKLSIGV 1005
Cdd:cd03235 74 PQR--RSIDrdfpISVRDVVL-MGLYGHKGLFRRLSKADK-AKVDEALervGLSELADRQIGELSGG----QQQRVLLAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1351079 1006 ELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSaTLFEEFDRLLLLRKGGqtVYFG 1077
Cdd:cd03235 146 ALVQDPDLLL-LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLG-LVLEYFDRVLLLNRTV--VASG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
856-1073 |
4.73e-24 |
|
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: 101.56 E-value: 4.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGKRmLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPIDASFERRT-GY 931
Cdd:cd03226 3 ENISFS--YKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILA----GLIkesSGSILLNGKPIKAKERRKSiGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 932 VQQQ-DIHIAELTVRESLQFSARmrrpqhlPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAK 1010
Cdd:cd03226 76 VMQDvDYQLFTDSVREELLLGLK-------ELDAGNEQAETVLKDLDLYALKERHPLSLSGG----QKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351079 1011 PDLLLFlDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPsatlfeEF-----DRLLLLRKGGQT 1073
Cdd:cd03226 145 KDLLIF-DEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDY------EFlakvcDRVLLLANGAIV 205
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
872-1047 |
1.54e-23 |
|
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: 100.97 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPIDA--SFER------RTgyvqQQDIHI- 939
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIS----GFLRptsGSVLFDGEDITGlpPHEIarlgigRT----FQIPRLf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 940 AELTVRESLQFSARMRRPQHL-------PDSEKMDYVEKIIRVLGMEEYAEALVGEvgcgLNVEQRKKLSIGVELVAKPD 1012
Cdd:cd03219 88 PELTVLENVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAGE----LSYGQQRRLEIARALATDPK 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1351079 1013 LLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSIL 1047
Cdd:cd03219 164 LLL-LDEPAAGLNPEETEELAELIRELRERGITVL 197
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
867-1079 |
1.65e-23 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 101.04 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLaqrnVGIIT---GDMLVNGRPIDA-------SFERRTGYVQQQD 936
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLI----VGLLRpdsGEVLIDGEDISGlseaelyRLRRRMGMLFQSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 937 IHIAELTVRESLQFSARMRRpqHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLlF 1016
Cdd:cd03261 87 ALFDSLTVFENVAFPLREHT--RLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGG----MKKRVALARALALDPELL-L 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1351079 1017 LDEPTSGLDSQSSWAIIQLLRKLSKAGQ--SILCTiHQPSaTLFEEFDRLLLLrKGGQTVYFGDI 1079
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGltSIMVT-HDLD-TAFAIADRIAVL-YDGKIVAEGTP 221
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
173-392 |
1.74e-23 |
|
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: 99.63 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDqfAGGVSGEVAYDGIPQEEMMKRYKAdviYNGELDVHFPYL 252
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKT--AGVITGEILINGRPLDKNFQRSTG---YVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 253 TVKQTLDFAIACktpalrvnnvskkeyiasrrdlyatifglrhtyntkvgndfvRGVSGGERKRVSIAEALAAKGSIYCW 332
Cdd:cd03232 95 TVREALRFSALL------------------------------------------RGLSVEQRKRLTIGVELAAKPSILFL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1351079 333 DNATRGLDASTALeyaKAIRIMTNLLKS--TAFVTIYQASENIYETFDKVTVLYS-GKQIYFG 392
Cdd:cd03232 133 DEPTSGLDSQAAY---NIVRFLKKLADSgqAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
867-1077 |
1.81e-23 |
|
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: 99.96 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSgYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPIDAS---FERRTGYVQQQDIHIA 940
Cdd:cd03264 11 GKKRALDGVS-LTLGPGMYGLLGPNGAGKTTLMRILA----TLTPpssGTIRIDGQDVLKQpqkLRRRIGYLPQEFGVYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 941 ELTVRESLQFSARMRRpqhLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEP 1020
Cdd:cd03264 86 NFTVREFLDYIAWLKG---IPSKEVKARVDEVLELVNLGDRAKKKIGSLSGG----MRRRVGIAQALVGDPSILI-VDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1351079 1021 TSGLDSQSSWAIIQLLRKLSKAGQSILCTiHQPSATLFeEFDRLLLLrKGGQTVYFG 1077
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELGEDRIVILST-HIVEDVES-LCNQVAVL-NKGKLVFEG 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
880-1070 |
4.10e-23 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 99.29 E-value: 4.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 880 IPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPIDAS--------FERRTGYVQQQDIHIAELTVRESL 948
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIA----GLEKpdgGTIVLNGTVLFDSrkkinlppQQRKIGLVFQQYALFPHLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 949 QFSARMRRPqhlpdSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQS 1028
Cdd:cd03297 97 AFGLKRKRN-----REDRISVDELLDLLGLDHLLNRYPAQLSGG----EKQRVALARALAAQPELLL-LDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1351079 1029 SWAIIQLLRKLSKAGQ--SILCTiHQPSaTLFEEFDRLLLLRKG 1070
Cdd:cd03297 167 RLQLLPELKQIKKNLNipVIFVT-HDLS-EAEYLADRIVVMEDG 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
867-1077 |
1.07e-22 |
|
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: 96.74 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPIdasferrtgyvqqQDIHIAELt 943
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA----GLLkpsSGEILLDGKDL-------------ASLSPKEL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 944 vreslqfsARmrrpqhlpdseKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEPTSG 1023
Cdd:cd03214 72 --------AR-----------KIAYVPQALELLGLAHLADRPFNELSGG----ERQRVLLARALAQEPPILL-LDEPTSH 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1351079 1024 LDSQSSWAIIQLLRKLSKA-GQSILCTIHQPS-ATLFeeFDRLLLLrKGGQTVYFG 1077
Cdd:cd03214 128 LDIAHQIELLELLRRLARErGKTVVMVLHDLNlAARY--ADRVILL-KDGRIVAQG 180
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
174-735 |
2.88e-22 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 104.93 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 174 QIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEidQFAGGVSGEVAYDGIPQ-EEMMKRYKAdviYNGELDVHFPYL 252
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR--KTGGYIEGDIRISGFPKkQETFARISG---YCEQNDIHSPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 253 TVKQTLDFAIACKTPAlrvnNVSKKEYIaSRRDLYATIFGLRHTYNTKVGNDFVRGVSGGERKRVSIAEALAAKGSIYCW 332
Cdd:PLN03140 969 TVRESLIYSAFLRLPK----EVSKEEKM-MFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 333 DNATRGLDASTAleyAKAIRIMTNLLKS--TAFVTIYQASENIYETFDKVTVLYSGKQ-IYFGLI----HEAKPYFAKMg 405
Cdd:PLN03140 1044 DEPTSGLDARAA---AIVMRTVRNTVDTgrTVVCTIHQPSIDIFEAFDELLLMKRGGQvIYSGPLgrnsHKIIEYFEAI- 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 406 ylcpprqataefltaltdpngfhlikPGyenkVPRTAEEFE--TYWLNSPEFA---QMKKDIAA-YKEKVNTEKTKEVYD 479
Cdd:PLN03140 1120 --------------------------PG----VPKIKEKYNpaTWMLEVSSLAaevKLGIDFAEhYKSSSLYQRNKALVK 1169
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 480 E-SMAQEKSKYTRKKSYYTVSYWEQVKLCTQRGFQRIYGNKSYTVINVCSAIIQSFITGSLFYN--TPSSTSGAFSRG-G 555
Cdd:PLN03140 1170 ElSTPPPGASDLYFATQYSQSTWGQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFWKvgTKRSNANDLTMViG 1249
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 556 VLYFALLYyslMGLANISFEH------RPILQKHKGYSLYHPSAEAIGSTLASFPFRMIGLTCFFIILFFLSGLHRTAGS 629
Cdd:PLN03140 1250 AMYAAVLF---VGINNCSTVQpmvaveRTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAK 1326
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 630 FFTIYL--FLTMCSEAINGLfeMVSSVCDTLSQANSISGILMMSISMYSTYMIQLPSMHPWFKWISYVLPIRYAFESMLN 707
Cdd:PLN03140 1327 FFWFYFisFFSFLYFTYYGM--MTVSLTPNQQVAAIFAAAFYGLFNLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIV 1404
|
570 580
....*....|....*....|....*...
gi 1351079 708 AEFHgrhmDCANTLVPSGGDYDNLSDDY 735
Cdd:PLN03140 1405 SQYG----DVEDTIKVPGGAPDPTIKWY 1428
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
826-1067 |
3.54e-22 |
|
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: 102.36 E-value: 3.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 826 IDAKEQFSSESSGANDEVFDDLEAKGVfiwkdvcfTIPYEGgKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqR 905
Cdd:TIGR02857 301 LDAAPRPLAGKAPVTAAPASSLEFSGV--------SVAYPG-RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLL-G 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 906 NVGIITGDMLVNGRPID----ASFERRTGYVQQQDiHIAELTVRESLQFSArmrrpqhlPDSEKMDYVEKIIRVlGMEEY 981
Cdd:TIGR02857 371 FVDPTEGSIAVNGVPLAdadaDSWRDQIAWVPQHP-FLFAGTIAENIRLAR--------PDASDAEIREALERA-GLDEF 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 982 AEAL-------VGEVGCGLNVEQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKaGQSILCTIHQPS 1054
Cdd:TIGR02857 441 VAALpqgldtpIGEGGAGLSGGQAQRLALARAFLRDAPLLL-LDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLA 518
|
250
....*....|...
gi 1351079 1055 atLFEEFDRLLLL 1067
Cdd:TIGR02857 519 --LAALADRIVVL 529
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
856-1070 |
1.09e-21 |
|
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: 93.60 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqRNVGIITGDMLVNGRPID----ASFERRTGY 931
Cdd:cd03228 4 KNVSFS--YPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLL-RLYDPTSGEILIDGVDLRdldlESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 932 VqQQDIHIAELTVRESLqFSArmrrpqhlpdsekmdyvekiirvlGmeeyaealvgevgcglnveQRKKLSIGVELVAKP 1011
Cdd:cd03228 81 V-PQDPFLFSGTIRENI-LSG------------------------G-------------------QRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1351079 1012 DLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTiHQPSatLFEEFDRLLLLRKG 1070
Cdd:cd03228 116 PILI-LDEATSALDPETEALILEALRALAKGKTVIVIA-HRLS--TIRDADRIIVLDDG 170
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
856-1070 |
1.99e-21 |
|
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: 92.31 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTIpyegGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqRNVGIITGDMLVNGRPIDASF----ERRTGY 931
Cdd:cd00267 3 ENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIA-GLLKPTSGEILIDGKDIAKLPleelRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 932 VqqqdihiaeltvresLQFSArmrrpqhlpdsekmdyvekiirvlgmeeyaealvgevgcGlnveQRKKLSIGVELVAKP 1011
Cdd:cd00267 78 V---------------PQLSG---------------------------------------G----QRQRVALARALLLNP 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1351079 1012 DLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSaTLFEEFDRLLLLRKG 1070
Cdd:cd00267 100 DLLL-LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPE-LAELAADRVIVLKDG 156
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
860-1070 |
2.49e-21 |
|
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: 99.59 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 860 FTIPYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQ--RNVGIITGDMLVNGRPIDASFE----RRTGYV- 932
Cdd:COG1123 10 LSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllPHGGRISGEVLLDGRDLLELSEalrgRRIGMVf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 933 QQQDIHIAELTVRESLQFSARMRRpqhLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPD 1012
Cdd:COG1123 90 QDPMTQLNPVTVGDQIAEALENLG---LSRAEARARVLELLEAVGLERRLDRYPHQLSGG----QRQRVAIAMALALDPD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1351079 1013 LLLfLDEPTSGLDSQSSWAIIQLLRKLSKA-GQSILCTIHQPsATLFEEFDRLLLLRKG 1070
Cdd:COG1123 163 LLI-ADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDL-GVVAEIADRVVVMDDG 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
184-336 |
2.60e-21 |
|
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: 91.94 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 184 EAGEMILVLGRPGAGCSSFLKVTAGEIDqfagGVSGEVAYDGIP-QEEMMKRYKADVIYNGELDVHFPYLTVKQTLDFAI 262
Cdd:pfam00005 9 NPGEILALVGPNGAGKSTLLKLIAGLLS----PTEGTILLDGQDlTDDERKSLRKEIGYVFQDPQLFPRLTVRENLRLGL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351079 263 ACKTPalrvnnvsKKEYIASRRDLYATIFGLRHTYNTKVGNdFVRGVSGGERKRVSIAEALAAKGSIYCWDNAT 336
Cdd:pfam00005 85 LLKGL--------SKREKDARAEEALEKLGLGDLADRPVGE-RPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
851-1070 |
3.13e-21 |
|
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: 93.81 E-value: 3.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 851 GVFIWKDVCFTipYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNG---RPIDAS 924
Cdd:cd03245 1 GRIEFRNVSFS--YPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLA----GLYKptsGSVLLDGtdiRQLDPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 925 FERR-TGYVQQqDIHIAELTVRESLQFSArmrrpQHLPDSEkmdyVEKIIRVLGMEEYA-------EALVGEVGCGLNVE 996
Cdd:cd03245 75 DLRRnIGYVPQ-DVTLFYGTLRDNITLGA-----PLADDER----ILRAAELAGVTDFVnkhpnglDLQIGERGRGLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351079 997 QRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLsKAGQSILCTIHQPSatLFEEFDRLLLLRKG 1070
Cdd:cd03245 145 QRQAVALARALLNDPPILL-LDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPS--LLDLVDRIIVMDSG 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
872-1075 |
5.48e-21 |
|
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: 92.73 E-value: 5.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLLNTLaqrnVGII---TGDMLVNGRPIDASFERRTGYVQQQDIHIAELTVRESL 948
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMI----LGIIlpdSGEVLFDGKPLDIAARNRIGYLPEERGLYPKMKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 949 QFSARMRrpqHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQS 1028
Cdd:cd03269 92 VYLAQLK---GLKKEEARRRIDEWLERLELSEYANKRVEELSKG----NQQKVQFIAAVIHDPELLI-LDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1351079 1029 SWAIIQLLRKLSKAGQSILCTIHQpsATLFEEF-DRLLLLRKGGQTVY 1075
Cdd:cd03269 164 VELLKDVIRELARAGKTVILSTHQ--MELVEELcDRVLLLNKGRAVLY 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
856-1047 |
5.59e-21 |
|
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: 93.31 E-value: 5.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTIPYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPIDASfERRTGYV 932
Cdd:cd03293 4 RNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIA----GLERptsGEVLVDGEPVTGP-GPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 933 QQQDIHIAELTVRESLQFSARMRRpqhLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPD 1012
Cdd:cd03293 79 FQQDALLPWLTVLDNVALGLELQG---VPKAEARERAEELLELVGLSGFENAYPHQLSGG----MRQRVALARALAVDPD 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 1351079 1013 LLLfLDEPTSGLDSQSSWAIIQLLRKL-SKAGQSIL 1047
Cdd:cd03293 152 VLL-LDEPFSALDALTREQLQEELLDIwRETGKTVL 186
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
867-1070 |
6.55e-21 |
|
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: 92.67 E-value: 6.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPIDASFE--RRTGYVQQQDIHIAE 941
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIL----GLIkpdSGEITFDGKSYQKNIEalRRIGALIEAPGFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 942 LTVRESLQFSARMRRpqhLPDSEkmdyVEKIIRVLGMEEYAEALVGEVGCGLnveqRKKLSIGVELVAKPDLLLfLDEPT 1021
Cdd:cd03268 87 LTARENLRLLARLLG---IRKKR----IDEVLDVVGLKDSAKKKVKGFSLGM----KQRLGIALALLGNPDLLI-LDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1351079 1022 SGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSaTLFEEFDRLLLLRKG 1070
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQGITVLISSHLLS-EIQKVADRIGIINKG 202
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
864-1070 |
8.68e-21 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 93.02 E-value: 8.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 864 YEGGKRMLlDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqRNVGIITGDMLVNGRPIDA-------SFERRTGYVQQQD 936
Cdd:cd03256 10 YPNGKKAL-KDVSLSINPGEFVALIGPSGAGKSTLLRCLN-GLVEPTSGSVLIDGTDINKlkgkalrQLRRQIGMIFQQF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 937 IHIAELTVRESLQFSARMRRP------QHLPDSEKMDYVEKIIRVlGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAK 1010
Cdd:cd03256 88 NLIERLSVLENVLSGRLGRRStwrslfGLFPKEEKQRALAALERV-GLLDKAYQRADQLSGG----QQQRVAIARALMQQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351079 1011 PDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKA-GQSILCTIHQPSATLfEEFDRLLLLRKG 1070
Cdd:cd03256 163 PKLIL-ADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAR-EYADRIVGLKDG 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
881-1047 |
2.19e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 92.41 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 881 PGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPID--ASFER------RTGyvqqQDIHI-AELTVRESL 948
Cdd:COG0411 29 RGEIVGLIGPNGAGKTTLFNLIT----GFYRptsGRILFDGRDITglPPHRIarlgiaRTF----QNPRLfPELTVLENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 949 QFSARMRRPQHLPDS------------EKMDYVEKIIRVLGMEEYAEALVGEvgcgLNVEQRKKLSIGVELVAKPDLLLf 1016
Cdd:COG0411 101 LVAAHARLGRGLLAAllrlprarreerEARERAEELLERVGLADRADEPAGN----LSYGQQRRLEIARALATEPKLLL- 175
|
170 180 190
....*....|....*....|....*....|..
gi 1351079 1017 LDEPTSGLDSQSSWAIIQLLRKLSKA-GQSIL 1047
Cdd:COG0411 176 LDEPAAGLNPEETEELAELIRRLRDErGITIL 207
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
856-1071 |
4.70e-20 |
|
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: 90.75 E-value: 4.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqRNVGIITGDMLVNGRPID----ASFERRTGY 931
Cdd:cd03251 4 KNVTFR--YPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIP-RFYDVDSGRILIDGHDVRdytlASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 932 VqQQDIHIAELTVRESLQFSARMRRPQHLPDSEKMDYVEKIIRvlGMEEYAEALVGEVGCGLNVEQRKKLSIGVELVAKP 1011
Cdd:cd03251 81 V-SQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIM--ELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1351079 1012 DLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSI-----LCTIhqpsatlfEEFDRLLLLRKGG 1071
Cdd:cd03251 158 PILI-LDEATSALDTESERLVQAALERLMKNRTTFviahrLSTI--------ENADRIVVLEDGK 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
881-1047 |
6.36e-20 |
|
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: 90.19 E-value: 6.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 881 PGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPID--ASFER-RTG--YVQQ-QDIhIAELTVRESLQFS 951
Cdd:cd03224 25 EGEIVALLGRNGAGKTTLLKTIM----GLLPprsGSIRFDGRDITglPPHERaRAGigYVPEgRRI-FPELTVEENLLLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 952 ARMRRPQHLPDSekmdyvekIIRVLGM----EEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQ 1027
Cdd:cd03224 100 AYARRRAKRKAR--------LERVYELfprlKERRKQLAGTLSGG----EQQMLAIARALMSRPKLLL-LDEPSEGLAPK 166
|
170 180
....*....|....*....|
gi 1351079 1028 SSWAIIQLLRKLSKAGQSIL 1047
Cdd:cd03224 167 IVEEIFEAIRELRDEGVTIL 186
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
867-1079 |
9.63e-20 |
|
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: 90.53 E-value: 9.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSgYCI-PGTMTALMGESGAGKTTLLNtlaqrnvgIITGDM--------LVNGRPIDAS--FE--RRTGYV- 932
Cdd:COG1119 14 GGKTILDDIS-WTVkPGEHWAILGPNGAGKSTLLS--------LITGDLpptygndvRLFGERRGGEdvWElrKRIGLVs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 933 --QQQDIHiAELTVRESLQ--FSARMRRPQHlPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnvEQRKKLsIGVELV 1008
Cdd:COG1119 85 paLQLRFP-RDETVLDVVLsgFFDSIGLYRE-PTDEQRERARELLELLGLAHLADRPFGTLSQG---EQRRVL-IARALV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1351079 1009 AKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAG--QSILCTiHQPSAtLFEEFDRLLLLRKgGQTVYFGDI 1079
Cdd:COG1119 159 KDPELLI-LDEPTAGLDLGARELLLALLDKLAAEGapTLVLVT-HHVEE-IPPGITHVLLLKD-GRVVAAGPK 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
867-1042 |
1.02e-19 |
|
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: 90.04 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLaqrnVGIIT---GDMLVNGRPIDA-------SFERRTGYVQQQ- 935
Cdd:COG1127 16 GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLI----IGLLRpdsGEILVDGQDITGlsekelyELRRRIGMLFQGg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 936 ---DihiaELTVRESLQFSARMRRpqHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPD 1012
Cdd:COG1127 92 alfD----SLTVFENVAFPLREHT--DLSEAEIRELVLEKLELVGLPGAADKMPSELSGG----MRKRVALARALALDPE 161
|
170 180 190
....*....|....*....|....*....|
gi 1351079 1013 LLlFLDEPTSGLDSQSSWAIIQLLRKLSKA 1042
Cdd:COG1127 162 IL-LYDEPTAGLDPITSAVIDELIRELRDE 190
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
864-1070 |
1.75e-19 |
|
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: 89.47 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 864 YEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTlLNTLAQRNVGIITGDMLVNGRPI----DASFERRTGYVQQQDIhI 939
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKST-LTKLIQRFYVPENGRVLVDGHDLaladPAWLRRQVGVVLQENV-L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 940 AELTVRESLQFSarmrRPQhlPDSEKMDYVEKIIR----VLGMEEYAEALVGEVGCGLNVEQRKKLSIGVELVAKPDLLL 1015
Cdd:cd03252 88 FNRSIRDNIALA----DPG--MSMERVIEAAKLAGahdfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1351079 1016 FlDEPTSGLDSQSSWAIIQLLRKLSkAGQSILCTIHQPSATlfEEFDRLLLLRKG 1070
Cdd:cd03252 162 F-DEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTV--KNADRIIVMEKG 212
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
864-1051 |
1.79e-19 |
|
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: 87.86 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 864 YEGGKRMLlDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPIDAS------FERRTGYV-Q 933
Cdd:TIGR01166 1 YPGGPEVL-KGLNFAAERGEVLALLGANGAGKSTLLLHLN----GLLrpqSGAVLIDGEPLDYSrkglleRRQRVGLVfQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 934 QQDIHIAELTVRESLQFSARmrrPQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDL 1013
Cdd:TIGR01166 76 DPDDQLFAADVDQDVAFGPL---NLGLSEAEVERRVREALTAVGASGLRERPTHCLSGG----EKKRVAIAGAVAMRPDV 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 1351079 1014 LLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIH 1051
Cdd:TIGR01166 149 LL-LDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
867-1070 |
1.93e-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: 87.24 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQRNVgIITGDMLVNGRPIDA------SFERRTGYVQQQDIHIA 940
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE-PDSGSILIDGEDLTDledelpPLRRRIGMVFQDFALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 941 ELTVRESLQFsarmrrpqhlpdsekmdyvekiirvlgmeeyaealvgevgcGLNVEQRKKLSIGVELVAKPDLLLfLDEP 1020
Cdd:cd03229 90 HLTVLENIAL-----------------------------------------GLSGGQQQRVALARALAMDPDVLL-LDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1351079 1021 TSGLDSQSSWAIIQLLRKL-SKAGQSILCTIHQpsatLFEEF---DRLLLLRKG 1070
Cdd:cd03229 128 TSALDPITRREVRALLKSLqAQLGITVVLVTHD----LDEAArlaDRVVVLRDG 177
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
867-1064 |
2.00e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 90.63 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLaqrnVGIIT---GDMLVNGRPID--ASFER-RTGYVQQQDIHIA 940
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRML----LGLTHpdaGSISLCGEPVPsrARHARqRVGVVPQFDNLDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 941 ELTVRESLQFSARMRrpqHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGLnveqRKKLSIGVELVAKPDLLLfLDEP 1020
Cdd:PRK13537 94 DFTVRENLLVFGRYF---GLSAAAARALVPPLLEFAKLENKADAKVGELSGGM----KRRLTLARALVNDPDVLV-LDEP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1351079 1021 TSGLDSQSSWAIIQLLRKLSKAGQSILCTIHqpsatLFEEFDRL 1064
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLARGKTILLTTH-----FMEEAERL 204
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
856-1039 |
2.63e-19 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 89.09 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTIPYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPI----DASFERR 928
Cdd:COG1124 5 RNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALA----GLErpwSGEVTFDGRPVtrrrRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 929 TGYVQQQ---DIHiAELTVRESLqfsarmrrpqhlpdSEKMdyveKIIRVLGMEEYAEALVGEVGcgLNVE--------- 996
Cdd:COG1124 81 VQMVFQDpyaSLH-PRHTVDRIL--------------AEPL----RIHGLPDREERIAELLEQVG--LPPSfldryphql 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1351079 997 ---QRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKL 1039
Cdd:COG1124 140 sggQRQRVAIARALILEPELLL-LDEPTSALDVSVQAEILNLLKDL 184
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
847-1039 |
4.54e-19 |
|
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: 92.66 E-value: 4.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 847 LEAKGVfiwkDVCFTIPYEGGKRmLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPID- 922
Cdd:COG1123 261 LEVRNL----SKRYPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLL----GLLRptsGSILFDGKDLTk 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 923 ------ASFERRTGYVQQQDIH--IAELTVRESLQFSARMRRpqHLPDSEKMDYVEKIIRVLGM-EEYAEALVGEVGCGl 993
Cdd:COG1123 332 lsrrslRELRRRVQMVFQDPYSslNPRMTVGDIIAEPLRLHG--LLSRAERRERVAELLERVGLpPDLADRYPHELSGG- 408
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1351079 994 nveQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKL 1039
Cdd:COG1123 409 ---QRQRVAIARALALEPKLLI-LDEPTSALDVSVQAQILNLLRDL 450
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
866-1070 |
6.21e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.42 E-value: 6.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 866 GGKRMLLDNVSgYCI-PGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPID-------ASFERRTGYVqQ 934
Cdd:COG2884 12 PGGREALSDVS-LEIeKGEFVFLTGPSGAGKSTLLKLLY----GEErptSGQVLVNGQDLSrlkrreiPYLRRRIGVV-F 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 935 QDIH-IAELTVRESLQFSARMrrpQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnvEQrKKLSIGVELVAKPDL 1013
Cdd:COG2884 86 QDFRlLPDRTVYENVALPLRV---TGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGG---EQ-QRVAIARALVNRPEL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1351079 1014 LLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSatLFEEFD-RLLLLRKG 1070
Cdd:COG2884 159 LL-ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE--LVDRMPkRVLELEDG 213
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
856-1041 |
1.15e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 91.76 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGkRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNtLAQRNVGIITGDMLVNGRPID----ASFERRTGY 931
Cdd:COG1132 343 ENVSFS--YPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVN-LLLRFYDPTSGRILIDGVDIRdltlESLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 932 VqQQDIHIAELTVRESLqfsaRMRRPQHlPDSEkmdyVEKIIRVLGMEEYAEAL-------VGEVGCGLNVEQRKKLSIG 1004
Cdd:COG1132 419 V-PQDTFLFSGTIRENI----RYGRPDA-TDEE----VEEAAKAAQAHEFIEALpdgydtvVGERGVNLSGGQRQRIAIA 488
|
170 180 190
....*....|....*....|....*....|....*..
gi 1351079 1005 VELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSK 1041
Cdd:COG1132 489 RALLKDPPILI-LDEATSALDTETEALIQEALERLMK 524
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
856-1077 |
1.36e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 87.09 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTIpyegGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPIDA-SFE----R 927
Cdd:COG4559 5 ENLSVRL----GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLT----GELTpssGEVRLNGRPLAAwSPWelarR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 928 RTgyVQQQDIHIA-ELTVRESlqfsARM-RRPQHLPDSEKMDYVEKIIRVLGMEEYAEALV-----GEvgcglnvEQRkk 1000
Cdd:COG4559 77 RA--VLPQHSSLAfPFTVEEV----VALgRAPHGSSAAQDRQIVREALALVGLAHLAGRSYqtlsgGE-------QQR-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1001 lsigVEL----------VAKPDLLLFLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPS-ATLFEefDRLLLLrK 1069
Cdd:COG4559 142 ----VQLarvlaqlwepVDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNlAAQYA--DRILLL-H 214
|
....*...
gi 1351079 1070 GGQTVYFG 1077
Cdd:COG4559 215 QGRLVAQG 222
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
882-1070 |
4.75e-18 |
|
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: 86.68 E-value: 4.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 882 GTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPI---DASFERRTGYVQQQDIHIAELTVRESLQFSARMr 955
Cdd:TIGR01188 19 GEVFGFLGPNGAGKTTTIRMLT----TLLRptsGTARVAGYDVvrePRKVRRSIGIVPQYASVDEDLTGRENLEMMGRL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 956 rpQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLlFLDEPTSGLDSQSSWAIIQL 1035
Cdd:TIGR01188 94 --YGLPKDEAEERAEELLELFELGEAADRPVGTYSGG----MRRRLDIAASLIHQPDVL-FLDEPTTGLDPRTRRAIWDY 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 1351079 1036 LRKLSKAGQSILCTIHQpsatlFEEF----DRLLLLRKG 1070
Cdd:TIGR01188 167 IRALKEEGVTILLTTHY-----MEEAdklcDRIAIIDHG 200
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
872-1051 |
5.22e-18 |
|
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: 84.34 E-value: 5.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTT---LLNTLAQRNVG--IITG-DMLVNGRPIdasfERRTGYVQQQDIHIAELTVR 945
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTtikMLTTLLKPTSGraTVAGhDVVREPREV----RRRIGIVFQDLSVDDELTGW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 946 ESLQFSARMrrpQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGLnveqRKKLSIGVELVAKPDLLlFLDEPTSGLD 1025
Cdd:cd03265 92 ENLYIHARL---YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGM----RRRLEIARSLVHRPEVL-FLDEPTIGLD 163
|
170 180
....*....|....*....|....*..
gi 1351079 1026 SQSSWAIIQLLRKLSKA-GQSILCTIH 1051
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEfGMTILLTTH 190
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
856-1077 |
5.82e-18 |
|
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: 84.48 E-value: 5.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTIPYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqRNVGIITGDMLVNGRPI----DASFERRTGY 931
Cdd:cd03257 5 KNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAIL-GLLKPTSGSIIFDGKDLlklsRRLRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 932 VQQ--QDIHIA---ELTVRESLQFSARMRRPQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVE 1006
Cdd:cd03257 84 IQMvfQDPMSSlnpRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGG----QRQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1351079 1007 LVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKA-GQSILCTIHQPSatLFEEF-DRLLLLrKGGQTVYFG 1077
Cdd:cd03257 160 LALNPKLLI-ADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLG--VVAKIaDRVAVM-YAGKIVEEG 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
856-1047 |
6.73e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 85.14 E-value: 6.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTIPYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPIDASFERRtGYV 932
Cdd:COG1116 11 RGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA----GLEKptsGEVLVDGKPVTGPGPDR-GVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 933 QQQDihiaeLTVRESLQFSARMRrpqHLPDSEKMDYVEKIIRVLGMEEYAEALVGEvgcglnveqrkkLSIG----VE-- 1006
Cdd:COG1116 86 FQEPallpwLTVLDNVALGLELR---GVPKAERRERARELLELVGLAGFEDAYPHQ------------LSGGmrqrVAia 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1351079 1007 --LVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKL-SKAGQSIL 1047
Cdd:COG1116 151 raLANDPEVLL-MDEPFGALDALTRERLQDELLRLwQETGKTVL 193
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
856-1070 |
1.42e-17 |
|
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: 83.43 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGKrMLLDNVSGYCIPGTMTALMGESGAGKTTLLNtLAQRNVGIITGDMLVNGRPID----ASFERRTGY 931
Cdd:cd03254 6 ENVNFS--YDEKK-PVLKDINFSIKPGETVAIVGPTGAGKTTLIN-LLMRFYDPQKGQILIDGIDIRdisrKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 932 VqQQDIHIAELTVRESLqfsaRMRRPqhlpdSEKMDYVEKIIRVLGMEEYAEAL-------VGEVGCGLNVEQRKKLSIG 1004
Cdd:cd03254 82 V-LQDTFLFSGTIMENI----RLGRP-----NATDEEVIEAAKEAGAHDFIMKLpngydtvLGENGGNLSQGERQLLAIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351079 1005 VELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTiHQPSATLFEefDRLLLLRKG 1070
Cdd:cd03254 152 RAMLRDPKILI-LDEATSNIDTETEKLIQEALEKLMKGRTSIIIA-HRLSTIKNA--DKILVLDDG 213
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
853-1071 |
2.43e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.68 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 853 FIWKDVCFTIPyeggKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqRNVGIITGDMLVNGRPIDA----SFERR 928
Cdd:PRK10575 12 FALRNVSFRVP----GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLG-RHQPPSEGEILLDAQPLESwsskAFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 929 TGYVQQQDIHIAELTVREslqFSARMRRPQH-------LPDSEKmdyVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKL 1001
Cdd:PRK10575 87 VAYLPQQLPAAEGMTVRE---LVAIGRYPWHgalgrfgAADREK---VEEAISLVGLKPLAHRLVDSLSGG----ERQRA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351079 1002 SIGVeLVAKPDLLLFLDEPTSGLDSQSSWAIIQLLRKLSKA-GQSILCTIHQPSATLfEEFDRLLLLRKGG 1071
Cdd:PRK10575 157 WIAM-LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAA-RYCDYLVALRGGE 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
872-1025 |
3.30e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 85.15 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPIDA--SFERRTGYVQQQDI---HiaeLT 943
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIA----GFETpdsGRILLDGRDVTGlpPEKRNVGMVFQDYAlfpH---LT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 944 VRESLQFSARMRRpqhLPDSEKMDYVEKIIRVLGMEEYAEALVGEvgcglnveqrkkLSIG----VE----LVAKPDLLL 1015
Cdd:COG3842 94 VAENVAFGLRMRG---VPKAEIRARVAELLELVGLEGLADRYPHQ------------LSGGqqqrVAlaraLAPEPRVLL 158
|
170
....*....|
gi 1351079 1016 fLDEPTSGLD 1025
Cdd:COG3842 159 -LDEPLSALD 167
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
872-1070 |
5.74e-17 |
|
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: 81.30 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQRNVGIiTGDMLVNGRPIDASFERRTGYVQQ------QDIH-IAELTV 944
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPT-SGTIRVNGQDVSDLRGRAIPYLRRkigvvfQDFRlLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 945 RESLQFSarMRRPQHlPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnvEQrKKLSIGVELVAKPDLLLfLDEPTSGL 1024
Cdd:cd03292 96 YENVAFA--LEVTGV-PPREIRKRVPAALELVGLSHKHRALPAELSGG---EQ-QRVAIARAIVNSPTILI-ADEPTGNL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1351079 1025 DSQSSWAIIQLLRKLSKAGQSILCTIHqpSATLFEEFD-RLLLLRKG 1070
Cdd:cd03292 168 DPDTTWEIMNLLKKINKAGTTVVVATH--AKELVDTTRhRVIALERG 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
867-1041 |
1.21e-16 |
|
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: 80.69 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQRNVGI----ITGDMLVNGRPIDA------SFERRTGYVQQQD 936
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapDEGEVLLDGKDIYDldvdvlELRRRVGMVFQKP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 937 IHIAeLTVRESLQFSARMRRpqhLPDSEKMDY-VEKIIRVLGMEEY----AEALvgevgcGLNVEQRKKLSIGVELVAKP 1011
Cdd:cd03260 91 NPFP-GSIYDNVAYGLRLHG---IKLKEELDErVEEALRKAALWDEvkdrLHAL------GLSGGQQQRLCLARALANEP 160
|
170 180 190
....*....|....*....|....*....|
gi 1351079 1012 DLLLfLDEPTSGLDSQSSWAIIQLLRKLSK 1041
Cdd:cd03260 161 EVLL-LDEPTSALDPISTAKIEELIAELKK 189
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
881-1039 |
1.55e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 82.81 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 881 PGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPID--ASFERRTGYVQQQDI---HiaeLTVRESLQFSA 952
Cdd:COG3839 28 DGEFLVLLGPSGCGKSTLLRMIA----GLEDptsGEILIGGRDVTdlPPKDRNIAMVFQSYAlypH---MTVYENIAFPL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 953 RMRRpqhLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLFlDEPTSGLDSQSSWAI 1032
Cdd:COG3839 101 KLRK---VPKAEIDRRVREAAELLGLEDLLDRKPKQLSGG----QRQRVALGRALVREPKVFLL-DEPLSNLDAKLRVEM 172
|
....*..
gi 1351079 1033 IQLLRKL 1039
Cdd:COG3839 173 RAEIKRL 179
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
856-1072 |
1.64e-16 |
|
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: 78.80 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPID----ASFERR 928
Cdd:cd03246 4 ENVSFR--YPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLIL----GLLrptSGRVRLDGADISqwdpNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 929 TGYVqQQDIHIAELTVRESLqFSARMRRpqhlpdsekmdyvekiiRVLgmeeYAEALVGevgcglnveQRKklsigvelv 1008
Cdd:cd03246 78 VGYL-PQDDELFSGSIAENI-LSGGQRQ-----------------RLG----LARALYG---------NPR--------- 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351079 1009 akpdlLLFLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSatLFEEFDRLLLLRKGGQ 1072
Cdd:cd03246 117 -----ILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDGRV 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
864-1053 |
3.12e-16 |
|
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: 83.95 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 864 YEGGKRMLlDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPI---DASFERRTGYVQQQDI 937
Cdd:TIGR02868 344 YPGAPPVL-DGVSLDLPPGERVAILGPSGSGKSTLLATLA----GLLdplQGEVTLDGVPVsslDQDEVRRRVSVCAQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 938 HIAELTVRESLqfsaRMRRPQhLPDSEKMDYVEKIirvlGMEEYAEAL-------VGEVGCGLNVEQRKKLSIGVELVAK 1010
Cdd:TIGR02868 419 HLFDTTVRENL----RLARPD-ATDEELWAALERV----GLADWLRALpdgldtvLGEGGARLSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1351079 1011 PDLLLfLDEPTSGLDSQSSWAIIQLLRKLSkAGQSILCTIHQP 1053
Cdd:TIGR02868 490 APILL-LDEPTEHLDAETADELLEDLLAAL-SGRTVVLITHHL 530
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
173-387 |
7.39e-16 |
|
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: 76.51 E-value: 7.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQfaggVSGEVAYDGIPqeemmkrykadviyngeldvhfpyl 252
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKP----TSGEILIDGKD------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 253 tvkqtldfaiacktpalrvnnVSKKEYIASRRDLyATIFGLrhtyntkvgndfvrgvSGGERKRVSIAEALAAKGSIYCW 332
Cdd:cd00267 63 ---------------------IAKLPLEELRRRI-GYVPQL----------------SGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1351079 333 DNATRGLDASTALEYAKAIRIMTNLLKSTAFVTiyQASENIYETFDKVTVLYSGK 387
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVT--HDPELAELAADRVIVLKDGK 157
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
864-1053 |
1.03e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 77.40 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 864 YEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLA--QRNVGiitGDMLVNGRPID---ASFERRTGYVQQQDIH 938
Cdd:TIGR01189 8 CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAglLRPDS---GEVRWNGTPLAeqrDEPHENILYLGHLPGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 939 IAELTVRESLQFSARMRRPQHLPDSEKMDYVekiirvlGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLD 1018
Cdd:TIGR01189 85 KPELSALENLHFWAAIHGGAQRTIEDALAAV-------GLTGFEDLPAAQLSAG----QQRRLALARLWLSRRPLWI-LD 152
|
170 180 190
....*....|....*....|....*....|....*
gi 1351079 1019 EPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQP 1053
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
867-1070 |
1.60e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 81.81 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRmLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLaqrnVGII--TGDMLVNG---RPIDASFERRT-GYVqQQDIHIA 940
Cdd:PRK11174 362 GKT-LAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL----LGFLpyQGSLKINGielRELDPESWRKHlSWV-GQNPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 941 ELTVRESLqfsaRMRRPQhLPDSEKMDYVEKIirvlGMEEYAEAL-------VGEVGCGLNVEQRKKLSIGVELVAKPDL 1013
Cdd:PRK11174 436 HGTLRDNV----LLGNPD-ASDEQLQQALENA----WVSEFLPLLpqgldtpIGDQAAGLSVGQAQRLALARALLQPCQL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1351079 1014 LLfLDEPTSGLDSQSSWAIIQLLRKLSkAGQSILCTIHQPSATlfEEFDRLLLLRKG 1070
Cdd:PRK11174 507 LL-LDEPTASLDAHSEQLVMQALNAAS-RRQTTLMVTHQLEDL--AQWDQIWVMQDG 559
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
872-1070 |
2.15e-15 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 77.38 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGI---ITGDMLVNGRpiDASF----ERRTGYVQQqdiHIA---E 941
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIA----GLerpDSGTILFGGE--DATDvpvqERNVGFVFQ---HYAlfrH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 942 LTVRESLQFSARMR-RPQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEP 1020
Cdd:cd03296 89 MTVFDNVAFGLRVKpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGG----QRQRVALARALAVEPKVLL-LDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1351079 1021 TSGLDSQSSWAIIQLLRKL-SKAG-QSILCTIHQPSAtlFEEFDRLLLLRKG 1070
Cdd:cd03296 164 FGALDAKVRKELRRWLRRLhDELHvTTVFVTHDQEEA--LEVADRVVVMNKG 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
856-1070 |
2.21e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.41 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqRNVGIITGDMLVNGRPIDASFE---RRTGYV 932
Cdd:PRK11160 342 NNVSFT--YPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT-RAWDPQQGEILLNGQPIADYSEaalRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 933 QQQDIHIAELTVRESLQFSArmrrpqhlPDSEKmdyvEKIIRVL---GMEEYAE------ALVGEVGCGLNVEQRKKLSI 1003
Cdd:PRK11160 419 VSQRVHLFSATLRDNLLLAA--------PNASD----EALIEVLqqvGLEKLLEddkglnAWLGEGGRQLSGGEQRRLGI 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1351079 1004 GVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKaGQSILCTIHQpsATLFEEFDRLLLLRKG 1070
Cdd:PRK11160 487 ARALLHDAPLLL-LDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHR--LTGLEQFDRICVMDNG 549
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
867-1079 |
3.02e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 78.23 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSgYCIP-GTMTALMGESGAGKTTLLntlaqRNV-GIIT---GDMLVNGRPIDASFERRTGYVqqqdihiAE 941
Cdd:COG4152 12 GDKTAVDDVS-FTVPkGEIFGLLGPNGAGKTTTI-----RIIlGILApdsGEVLWDGEPLDPEDRRRIGYL-------PE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 942 -------LTVRESLQFSARMRrpqHLPDSE---KMDY-VEKiirvLGMEEYAEALVgevgcglnveqrKKLSIG----VE 1006
Cdd:COG4152 79 erglypkMKVGEQLVYLARLK---GLSKAEakrRADEwLER----LGLGDRANKKV------------EELSKGnqqkVQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1351079 1007 LVA----KPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQ-PSAtlfEEF-DRLLLLRKgGQTVYFGDI 1079
Cdd:COG4152 140 LIAallhDPELLI-LDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQmELV---EELcDRIVIINK-GRKVLSGSV 213
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
854-1047 |
6.08e-15 |
|
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: 76.11 E-value: 6.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 854 IWKDVCFTipYEGGkRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqRNVGIITGDMLVNGRPID----ASFERRT 929
Cdd:cd03253 2 EFENVTFA--YDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF-RFYDVSSGSILIDGQDIRevtlDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 930 GYVQQqDIHIAELTVRESLQFsARmrrpqhlPDSEKMDYVE--KII----RVLGMEEYAEALVGEVGCGLNVEQRKKLSI 1003
Cdd:cd03253 78 GVVPQ-DTVLFNDTIGYNIRY-GR-------PDATDEEVIEaaKAAqihdKIMRFPDGYDTIVGERGLKLSGGEKQRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1351079 1004 GVELVAKPDLLLFlDEPTSGLDSQSSWAIIQLLRKLSKAGQSIL 1047
Cdd:cd03253 149 ARAILKNPPILLL-DEATSALDTHTEREIQAALRDVSKGRTTIV 191
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
856-1052 |
6.78e-15 |
|
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: 75.70 E-value: 6.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTIPYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLL---NTLAQRNvgiiTGDMLVNGRPIDA-------SF 925
Cdd:cd03258 5 KNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIrciNGLERPT----SGSVLVDGTDLTLlsgkelrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 926 ERRTGYVQQQDIHIAELTVRESLQFSARMrrpQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGV 1005
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEI---AGVPKAEIEERVLELLELVGLEDKADAYPAQLSGG----QKQRVGIAR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1351079 1006 ELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKL-SKAGQSILCTIHQ 1052
Cdd:cd03258 154 ALANNPKVLL-CDEATSALDPETTQSILALLRDInRELGLTIVLITHE 200
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
881-1047 |
7.00e-15 |
|
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: 75.79 E-value: 7.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 881 PGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPID--ASFER-RTG--YVqQQDIHI-AELTVRESLQFS 951
Cdd:COG0410 28 EGEIVALLGRNGAGKTTLLKAIS----GLLpprSGSIRFDGEDITglPPHRIaRLGigYV-PEGRRIfPSLTVEENLLLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 952 ARMRRPQHlPDSEKMDyvekiiRVLGM----EEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEPTSGLdsq 1027
Cdd:COG0410 103 AYARRDRA-EVRADLE------RVYELfprlKERRRQRAGTLSGG----EQQMLAIGRALMSRPKLLL-LDEPSLGL--- 167
|
170 180
....*....|....*....|....*.
gi 1351079 1028 sswA------IIQLLRKLSKAGQSIL 1047
Cdd:COG0410 168 ---ApliveeIFEIIRRLNREGVTIL 190
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
872-1047 |
9.77e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.91 E-value: 9.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGR------PIDAsfeRRTG-YVQQQDIHIA- 940
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILS----GVYQpdsGEILLDGEpvrfrsPRDA---QAAGiAIIHQELNLVp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 941 ELTVRESLqFSARMRRPQHLPDSEKmdyvekiirvlgMEEYAEALVGEVGCGLNVEQR-KKLSIG----VE----LVAKP 1011
Cdd:COG1129 93 NLSVAENI-FLGREPRRGGLIDWRA------------MRRRARELLARLGLDIDPDTPvGDLSVAqqqlVEiaraLSRDA 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1351079 1012 DLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSIL 1047
Cdd:COG1129 160 RVLI-LDEPTASLTEREVERLFRIIRRLKAQGVAII 194
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
872-1070 |
1.10e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 75.65 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT--GDMLVNGRPID----ASFERRTGYVQQQDIHIAELTVR 945
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMA----GLLPgqGEILLNGRPLSdwsaAELARHRAYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 946 ESLQFsarmrrpqHLPDSEKMDYVEKIIRVLgmeeyAEALvgEVGCGL--NVEQrkkLSIG----VELVAK-----PDL- 1013
Cdd:COG4138 88 QYLAL--------HQPAGASSEAVEQLLAQL-----AEAL--GLEDKLsrPLTQ---LSGGewqrVRLAAVllqvwPTIn 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351079 1014 ----LLFLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSATLFEEfDRLLLLRKG 1070
Cdd:COG4138 150 pegqLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHA-DRVWLLKQG 209
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
864-1070 |
1.66e-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: 79.29 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 864 YEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQrNVGIITGDMLVNGRPIDASF---ERRTGYVQQQDIHIA 940
Cdd:TIGR01257 1947 YSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG-DTTVTSGDATVAGKSILTNIsdvHQNMGYCPQFDAIDD 2025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 941 ELTVRESLQFSARMRrpqHLPDSEkmdyVEKI----IRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLf 1016
Cdd:TIGR01257 2026 LLTGREHLYLYARLR---GVPAEE----IEKVanwsIQSLGLSLYADRLAGTYSGG----NKRKLSTAIALIGCPPLVL- 2093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1351079 1017 LDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQpsatlFEEFD----RLLLLRKG 1070
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHS-----MEECEalctRLAIMVKG 2146
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
865-1053 |
2.25e-14 |
|
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: 73.30 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 865 EGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPID---ASFERRTGYVQQQDIH 938
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILA----GLSpplAGRVLLNGGPLDfqrDSIARGLLYLGHAPGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 939 IAELTVRESLQFSARMrrpqhlpdsEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLD 1018
Cdd:cd03231 85 KTTLSVLENLRFWHAD---------HSDEQVEEALARVGLNGFEDRPVAQLSAG----QQRRVALARLLLSGRPLWI-LD 150
|
170 180 190
....*....|....*....|....*....|....*
gi 1351079 1019 EPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQP 1053
Cdd:cd03231 151 EPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
882-1051 |
2.61e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.11 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 882 GTMTALMGESGAGKTTL---LNtlaqrnvGII---TGDMLVNGRPIDAS------FERRTGYV-QQQDIHIAELTVRESL 948
Cdd:PRK13639 28 GEMVALLGPNGAGKSTLflhFN-------GILkptSGEVLIKGEPIKYDkkslleVRKTVGIVfQNPDDQLFAPTVEEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 949 QFSarmrrPQH--LPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEPTSGLDS 1026
Cdd:PRK13639 101 AFG-----PLNlgLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGG----QKKRVAIAGILAMKPEIIV-LDEPTSGLDP 170
|
170 180
....*....|....*....|....*
gi 1351079 1027 QSSWAIIQLLRKLSKAGQSILCTIH 1051
Cdd:PRK13639 171 MGASQIMKLLYDLNKEGITIIISTH 195
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
856-1050 |
2.64e-14 |
|
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: 74.11 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTIPyeggKR---MLLDNVSGYCIPGTMTALMGESGAGKTTLLNtLAQRNVGIITGDMLVNGRPID----ASFERR 928
Cdd:cd03249 4 KNVSFRYP----SRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVS-LLERFYDPTSGEILLDGVDIRdlnlRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 929 TGYVqQQDIHIAELTVRESLQFSarmRRPQHLPDSE---KMDYVEKIIRVLgMEEYaEALVGEVGCGLNVEQRKKLSIGV 1005
Cdd:cd03249 79 IGLV-SQEPVLFDGTIAENIRYG---KPDATDEEVEeaaKKANIHDFIMSL-PDGY-DTLVGERGSQLSGGQKQRIAIAR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1351079 1006 ELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSI-----LCTI 1050
Cdd:cd03249 153 ALLRNPKILL-LDEATSALDAESEKLVQEALDRAMKGRTTIviahrLSTI 201
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
872-1070 |
3.07e-14 |
|
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: 73.81 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPIDA--SFERRTGYVQQQDIHIAELTVRE 946
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIA----GFETptsGEILLDGKDITNlpPHKRPVNTVFQNYALFPHLTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 947 SLQFSARMRRpqhLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEPTSGLDs 1026
Cdd:cd03300 92 NIAFGLRLKK---LPKAEIKERVAEALDLVQLEGYANRKPSQLSGG----QQQRVAIARALVNEPKVLL-LDEPLGALD- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1351079 1027 qsswaiiqllRKLSKAGQSILCTIHQPSATLF-------EEF----DRLLLLRKG 1070
Cdd:cd03300 163 ----------LKLRKDMQLELKRLQKELGITFvfvthdqEEAltmsDRIAVMNKG 207
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
872-1051 |
3.34e-14 |
|
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: 73.91 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSgYCIP-GTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNG-RPidasFERRTGYVQQQDIHIAE----- 941
Cdd:cd03267 37 LKGIS-FTIEkGEIVGFIGPNGAGKTTTLKILS----GLLQptsGEVRVAGlVP----WKRRKKFLRRIGVVFGQktqlw 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 942 --LTVRESLQFSARMRRpqhLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLlFLDE 1019
Cdd:cd03267 108 wdLPVIDSFYLLAAIYD---LPPARFKKRLDELSELLDLEELLDTPVRQLSLG----QRMRAEIAAALLHEPEIL-FLDE 179
|
170 180 190
....*....|....*....|....*....|...
gi 1351079 1020 PTSGLDSQSSWAIIQLLRKLSKA-GQSILCTIH 1051
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRErGTTVLLTSH 212
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
885-1070 |
5.04e-14 |
|
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: 75.52 E-value: 5.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 885 TALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPI-DASFE-------RRTGYVQQQDIHIAELTVRESLQFSar 953
Cdd:COG4148 28 TALFGPSGSGKTTLLRAIA----GLERpdsGRIRLGGEVLqDSARGiflpphrRRIGYVFQEARLFPHLSVRGNLLYG-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 954 MRRPQHLPDSEKMDYVekiIRVLGMEE----YAEALVGevGcglnveQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSS 1029
Cdd:COG4148 102 RKRAPRAERRISFDEV---VELLGIGHlldrRPATLSG--G------ERQRVAIGRALLSSPRLLL-MDEPLAALDLARK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1351079 1030 WAIIQLLRKLSKAGQ-SILCTIHQPsatlfEEF----DRLLLLRKG 1070
Cdd:COG4148 170 AEILPYLERLRDELDiPILYVSHSL-----DEVarlaDHVVLLEQG 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
867-1052 |
5.08e-14 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 72.56 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqRNVGIITGDMLVNGRPIDASFE------RRTGYVQQQDIHIA 940
Cdd:cd03262 11 GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCIN-LLEEPDSGTIIIDGLKLTDDKKninelrQKVGMVFQQFNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 941 ELTVRESLQFSARMRRpqHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLFlDEP 1020
Cdd:cd03262 90 HLTVLENITLAPIKVK--GMSKAEAEERALELLEKVGLADKADAYPAQLSGG----QQQRVAIARALAMNPKVMLF-DEP 162
|
170 180 190
....*....|....*....|....*....|..
gi 1351079 1021 TSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQ 1052
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
849-1070 |
1.33e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.44 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 849 AKGVFIWKDVCFTipYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNtLAQRNVGIITGDMLVNGRPID----AS 924
Cdd:PRK11176 338 AKGDIEFRNVTFT--YPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIAN-LLTRFYDIDEGEILLDGHDLRdytlAS 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 925 FERRTGYVQQQdIHIAELTV-------------RESLQFSARMrrpqhlpdSEKMDYVEKiirvlgMEEYAEALVGEVGC 991
Cdd:PRK11176 415 LRNQVALVSQN-VHLFNDTIanniayarteqysREQIEEAARM--------AYAMDFINK------MDNGLDTVIGENGV 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1351079 992 GLNVEQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKaGQSILCTIHQPSAtlFEEFDRLLLLRKG 1070
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILI-LDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLST--IEKADEILVVEDG 554
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
867-1064 |
2.57e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.94 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTT---LLNTLAQRNVGIITgdmlVNGRPIDA---SFERRTGYVQQQDIHIA 940
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTiarMILGMTSPDAGKIT----VLGVPVPArarLARARIGVVPQFDNLDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 941 ELTVRESLQFSARMRRpQHLPDSEKMdyVEKIIRVLGMEEYAEALVGEVGCGLnveqRKKLSIGVELVAKPDLLLfLDEP 1020
Cdd:PRK13536 128 EFTVRENLLVFGRYFG-MSTREIEAV--IPSLLEFARLESKADARVSDLSGGM----KRRLTLARALINDPQLLI-LDEP 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1351079 1021 TSGLDSQSSWAIIQLLRKLSKAGQSILCTIHqpsatLFEEFDRL 1064
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLLARGKTILLTTH-----FMEEAERL 238
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
867-1041 |
2.70e-13 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 70.75 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPID--ASFERRTGYVQQQDIHIAE 941
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIA----GLEEptsGRIYIGGRDVTdlPPKDRDIAMVFQNYALYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 942 LTVRESLQFSARMRrpqHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEPT 1021
Cdd:cd03301 87 MTVYDNIAFGLKLR---KVPKDEIDERVREVAELLQIEHLLDRKPKQLSGG----QRQRVALGRAIVREPKVFL-MDEPL 158
|
170 180
....*....|....*....|
gi 1351079 1022 SGLDSQSSWAIIQLLRKLSK 1041
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQ 178
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
845-1070 |
3.08e-13 |
|
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: 70.58 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 845 DDLEakGVFIWKDVCFTIPYEGgKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLaQRNVGIITGDMLVNGRPIDA- 923
Cdd:cd03248 6 DHLK--GIVKFQNVTFAYPTRP-DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALL-ENFYQPQGGQVLLDGKPISQy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 924 ---SFERRTGYVQQQDIHIAElTVRESLQFSarmrrpqhLPDSEKMDYVEKIIR------VLGMEEYAEALVGEVGCGLN 994
Cdd:cd03248 82 ehkYLHSKVSLVGQEPVLFAR-SLQDNIAYG--------LQSCSFECVKEAAQKahahsfISELASGYDTEVGEKGSQLS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351079 995 VEQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKlSKAGQSILCTIHQPSatLFEEFDRLLLLRKG 1070
Cdd:cd03248 153 GGQKQRVAIARALIRNPQVLI-LDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLS--TVERADQILVLDGG 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
875-1070 |
3.31e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.12 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 875 VSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT--GDMLVNGRPID----ASFERRTGYVQQQDIHIAELTVRESL 948
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMA----GLLPgsGSIQFAGQPLEawsaAELARHRAYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 949 QFSarmrRPQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnvE-QRKKLSiGVELVAKPDL-----LLFLDEPTS 1022
Cdd:PRK03695 91 TLH----QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGG---EwQRVRLA-AVVLQVWPDInpagqLLLLDEPMN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1351079 1023 GLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSATLfEEFDRLLLLRKG 1070
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTL-RHADRVWLLKQG 209
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
856-1051 |
4.15e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.04 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTIPyeggkrmlldnvsgyciPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGR-PidasFERRTGY 931
Cdd:COG4586 39 DDISFTIE-----------------PGEIVGFIGPNGAGKSTTIKMLT----GILVptsGEVRVLGYvP----FKRRKEF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 932 VQQqdihIA-----------ELTVRESLQFSARMRRpqhLPDSEKMDYVEKIIRVLGMEEYaealvgevgcgLNVEQRKk 1000
Cdd:COG4586 94 ARR----IGvvfgqrsqlwwDLPAIDSFRLLKAIYR---IPDAEYKKRLDELVELLDLGEL-----------LDTPVRQ- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1001 LSIG----VELVA----KPDLLlFLDEPTSGLDSQSSWAIIQLLRKLSKA-GQSILCTIH 1051
Cdd:COG4586 155 LSLGqrmrCELAAallhRPKIL-FLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSH 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
881-1047 |
9.92e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 9.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 881 PGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPID-----ASFERRTGYVQQqdiH---IAELTVRESLQ 949
Cdd:COG3845 30 PGEIHALLGENGAGKSTLMKILY----GLYQpdsGEILIDGKPVRirsprDAIALGIGMVHQ---HfmlVPNLTVAENIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 950 FSARmRRPQHLPDSEKmdyVEKIIRVLgMEEYaealvgevgcGLNVEQRKK---LSIG----VE----LVAKPDLLLfLD 1018
Cdd:COG3845 103 LGLE-PTKGGRLDRKA---ARARIREL-SERY----------GLDVDPDAKvedLSVGeqqrVEilkaLYRGARILI-LD 166
|
170 180
....*....|....*....|....*....
gi 1351079 1019 EPTSGLDSQSSWAIIQLLRKLSKAGQSIL 1047
Cdd:COG3845 167 EPTAVLTPQEADELFEILRRLAAEGKSII 195
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
882-1070 |
1.10e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.04 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 882 GTMTALMGESGAGKTTLLNTLAqrnvGIITGDMLVN------GRPI--------DASFER-RTGYVQQQDIHIAELTVRE 946
Cdd:PRK09984 30 GEMVALLGPSGSGKSTLLRHLS----GLITGDKSAGshiellGRTVqregrlarDIRKSRaNTGYIFQQFNLVNRLSVLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 947 SLQFSARMRRP------QHLPDSEKMDYVEKIIRVlGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEP 1020
Cdd:PRK09984 106 NVLIGALGSTPfwrtcfSWFTREQKQRALQALTRV-GMVHFAHQRVSTLSGG----QQQRVAIARALMQQAKVIL-ADEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1351079 1021 TSGLDSQSSWAIIQLLRKLSKA-GQSILCTIHQPSATLfEEFDRLLLLRKG 1070
Cdd:PRK09984 180 IASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYAL-RYCERIVALRQG 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
856-1051 |
1.10e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 70.26 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGKRMLLD-NVSgycIP-GTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPIDAS------ 924
Cdd:PRK13636 9 EELNYN--YSDGTHALKGiNIN---IKkGEVTAILGGNGAGKSTLFQNLN----GILkpsSGRILFDGKPIDYSrkglmk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 925 FERRTGYV-QQQDIHIAELTVRESLQFSARMRRpqhLPDSEKMDYVEKIIRVLGMEEyaeaLVGEVGCGLNVEQRKKLSI 1003
Cdd:PRK13636 80 LRESVGMVfQDPDNQLFSASVYQDVSFGAVNLK---LPEDEVRKRVDNALKRTGIEH----LKDKPTHCLSFGQKKRVAI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1351079 1004 GVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKA-GQSILCTIH 1051
Cdd:PRK13636 153 AGVLVMEPKVLV-LDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATH 200
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
878-1079 |
1.42e-12 |
|
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: 68.90 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 878 YCIpgtmtaLMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPID--ASFERRTGYVQQQDIHIAELTVRESLQFSA 952
Cdd:cd03299 27 YFV------ILGPTGSGKSVLLETIA----GFIkpdSGKILLNGKDITnlPPEKRDISYVPQNYALFPHMTVYKNIAYGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 953 RMRRPQHLPDSEKmdyVEKIIRVLGMEE----YAEALVGEvgcglnveQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQS 1028
Cdd:cd03299 97 KKRKVDKKEIERK---VLEIAEMLGIDHllnrKPETLSGG--------EQQRVAIARALVVNPKILL-LDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1351079 1029 SWAIIQLLRKL-SKAGQSILCTIHQpsatlFEEF----DRLLLLRKgGQTVYFGDI 1079
Cdd:cd03299 165 KEKLREELKKIrKEFGVTVLHVTHD-----FEEAwalaDKVAIMLN-GKLIQVGKP 214
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
835-1070 |
1.45e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 72.45 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 835 ESSGANDEVFDDLEAK---------------GVFIWKDVCFTIPYEGgKRMLLDNVSGYCIPGTMTALMGESGAGKTT-- 897
Cdd:TIGR00958 446 QAVGASEKVFEYLDRKpnipltgtlaplnleGLIEFQDVSFSYPNRP-DVPVLKGLTFTLHPGEVVALVGPSGSGKSTva 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 898 -LLNTLAQRNvgiiTGDMLVNGRPIDA----SFERRTGYVQQQDIHIAElTVRESLQFSARMRRPQHLPDSEKMDYVEKI 972
Cdd:TIGR00958 525 aLLQNLYQPT----GGQVLLDGVPLVQydhhYLHRQVALVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAANAHDF 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 973 IrvLGMEEYAEALVGEVGCGLNVEQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLlrkLSKAGQSILCTIHQ 1052
Cdd:TIGR00958 600 I--MEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLI-LDEATSALDAECEQLLQES---RSRASRTVLLIAHR 673
|
250
....*....|....*...
gi 1351079 1053 PSatLFEEFDRLLLLRKG 1070
Cdd:TIGR00958 674 LS--TVERADQILVLKKG 689
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
867-1052 |
2.14e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.58 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLL---NTLAQRNVG-IITGDMLVNGRPIDASFERR-TGYVQQQDIHIAE 941
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKLEEITSGdLIVDGLKVNDPKVDERLIRQeAGMVFQQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 942 LTVRESLQFSARMRRPQHLPDSEKMdyVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLFlDEPT 1021
Cdd:PRK09493 92 LTALENVMFGPLRVRGASKEEAEKQ--ARELLAKVGLAERAHHYPSELSGG----QQQRVAIARALAVKPKLMLF-DEPT 164
|
170 180 190
....*....|....*....|....*....|.
gi 1351079 1022 SGLDSQSSWAIIQLLRKLSKAGQSILCTIHQ 1052
Cdd:PRK09493 165 SALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
167-387 |
4.53e-12 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 67.05 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 167 KRHQKMRQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQfaggVSGEVAYDGIPQEEMMKRykADVIYNGELD 246
Cdd:cd03292 8 KTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELP----TSGTIRVNGQDVSDLRGR--AIPYLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 247 VHF------PYLTVKQTLDFaiacktpALRVNNVSKKEyIASRRDLYATIFGLRHTYNTkvgndFVRGVSGGERKRVSIA 320
Cdd:cd03292 82 VVFqdfrllPDRNVYENVAF-------ALEVTGVPPRE-IRKRVPAALELVGLSHKHRA-----LPAELSGGEQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1351079 321 EALAAKGSIYCWDNATRGLDASTALEyakairIMtNLLKST--AFVTIYQASEN--IYETFDK-VTVLYSGK 387
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWE------IM-NLLKKInkAGTTVVVATHAkeLVDTTRHrVIALERGK 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
856-1078 |
6.20e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.84 E-value: 6.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGKRMLlDNVSGYCIPGTMTALMGESGAGKTTLL---N--TLAQRnvgiitGDMLVNGRPIDASFER--- 927
Cdd:PRK13647 8 EDLHFR--YKDGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLlhlNgiYLPQR------GRVKVMGREVNAENEKwvr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 928 -RTGYV-QQQDIHIAELTVRESLQFSArmrRPQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGV 1005
Cdd:PRK13647 79 sKVGLVfQDPDDQVFSSTVWDDVAFGP---VNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYG----QKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1351079 1006 ELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSATLfEEFDRLLLLrKGGQTVYFGD 1078
Cdd:PRK13647 152 VLAMDPDVIV-LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVL-KEGRVLAEGD 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
867-1070 |
9.78e-12 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 66.41 E-value: 9.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLaqrnVGII---TGDMLVNGRPI-DASFERRT----GYVQQQDIH 938
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMI----VGLVkpdSGKILLDGQDItKLPMHKRArlgiGYLPQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 939 IAELTVRESLQFSARMRrpqHLPDSEKMDYVEKIIRVLGMEEyaeaLVGEVGCGLNVEQRKKLSIGVELVAKPDLLLfLD 1018
Cdd:cd03218 87 FRKLTVEENILAVLEIR---GLSKKEREEKLEELLEEFHITH----LRKSKASSLSGGERRRVEIARALATNPKFLL-LD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1351079 1019 EPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSATLfEEFDRLLLLRKG 1070
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETL-SITDRAYIIYEG 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
167-392 |
1.22e-11 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 65.99 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 167 KRHQKMRQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQfaggVSGEVAYDGIP----QEEMMKRYKADVIY- 241
Cdd:cd03257 12 PTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKP----TSGSIIFDGKDllklSRRLRKIRRKEIQMv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 242 ----NGELDvhfPYLTVKQTLdfaiacKTPALRVNNVSKKEYIASRRDLYATIFGLRhtynTKVGNDFVRGVSGGERKRV 317
Cdd:cd03257 88 fqdpMSSLN---PRMTIGEQI------AEPLRIHGKLSKKEARKEAVLLLLVGVGLP----EEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 318 SIAEALAAKGSIYCWDNATRGLDASTAleyAKAIRIMTNLLKS--TAFVTIyqaSENI---YETFDKVTVLYSGKQIYFG 392
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQ---AQILDLLKKLQEElgLTLLFI---THDLgvvAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
173-398 |
1.89e-11 |
|
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: 65.60 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQfaggVSGEVAYDGI------PQEEMMKRYKADVIY-NGEL 245
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRP----DSGEVLIDGEdisglsEAELYRLRRRMGMLFqSGAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 246 dvhFPYLTVKQTLDFaiacktPaLRVNNVSKKEYIASRRDLYATIFGLRHTYNTKVGNdfvrgVSGGERKRVSIAEALAA 325
Cdd:cd03261 89 ---FDSLTVFENVAF------P-LREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE-----LSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1351079 326 KGSIYCWDNATRGLDASTALEYAKAIRIMTNLLKSTAFVTIYQASEnIYETFDKVTVLYSGKQIYFGLIHEAK 398
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDT-AFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
864-1057 |
2.35e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 65.69 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 864 YEGgkRMLLDNVSGYCIPGTMTALMGESGAGKTT---LLNTLAQRNVG-IITGDMLVNGRPIDASFERRTGYVQQQDIHI 939
Cdd:PRK10895 13 YKG--RRVVEDVSLTVNSGEIVGLLGPNGAGKTTtfyMVVGIVPRDAGnIIIDDEDISLLPLHARARRGIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 940 AELTVRESLQFSARMRrpQHLPDSEKMDYVEKIirvlgMEEY-AEALVGEVGCGLNVEQRKKLSIGVELVAKPDLLLfLD 1018
Cdd:PRK10895 91 RRLSVYDNLMAVLQIR--DDLSAEQREDRANEL-----MEEFhIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL-LD 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 1351079 1019 EPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSATL 1057
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETL 201
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
867-1051 |
2.40e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.16 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqRNVGIITGDMLVNGRPID--ASFE--RRTGYVQQQDIHIAEL 942
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLS-RLMTPAHGHVWLDGEHIQhyASKEvaRRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 943 TVREslqFSARMRRPqHLP-----DSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfL 1017
Cdd:PRK10253 97 TVQE---LVARGRYP-HQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGG----QRQRAWIAMVLAQETAIML-L 167
|
170 180 190
....*....|....*....|....*....|....*
gi 1351079 1018 DEPTSGLDSQSSWAIIQLLRKLSKA-GQSILCTIH 1051
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNREkGYTLAAVLH 202
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
867-1051 |
3.74e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 65.04 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqRNVGIITGDMLVNGRPI----DASFERRTGYVQQQDIHIAEL 942
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RLLTPQSGTVFLGDKPIsmlsSRQLARRLALLPQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 943 TVRESLQFSarmRRPqHLP-----DSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfL 1017
Cdd:PRK11231 92 TVRELVAYG---RSP-WLSlwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGG----QRQRAFLAMVLAQDTPVVL-L 162
|
170 180 190
....*....|....*....|....*....|....
gi 1351079 1018 DEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIH 1051
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELNTQGKTVVTVLH 196
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
872-1070 |
3.81e-11 |
|
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: 62.83 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSgYCI-PGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPIDAsferrtgyvqqqdihiaeLTVRES 947
Cdd:cd03216 16 LDGVS-LSVrRGEVHALLGENGAGKSTLMKILS----GLYKpdsGEILVDGKEVSF------------------ASPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 948 LQfsarmrrpqhlpdsekmdyvekiirvLGMeeyaeALVGEvgcgLNVEQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQ 1027
Cdd:cd03216 73 RR--------------------------AGI-----AMVYQ----LSVGERQMVEIARALARNARLLI-LDEPTAALTPA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1351079 1028 SSWAIIQLLRKLSKAGQSILCTIHQPSaTLFEEFDRLLLLRKG 1070
Cdd:cd03216 117 EVERLFKVIRRLRAQGVAVIFISHRLD-EVFEIADRVTVLRDG 158
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
867-1053 |
3.99e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.12 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPIDASFER-RTGYVQQQDIHIAEL 942
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIA----GLLppaAGTIKLDGGDIDDPDVAeACHYLGHRNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 943 TVRESLQFSARMRRpQHLPDsekmdyVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEPTS 1022
Cdd:PRK13539 89 TVAENLEFWAAFLG-GEELD------IAAALEAVGLAPLAHLPFGYLSAG----QKRRVALARLLVSNRPIWI-LDEPTA 156
|
170 180 190
....*....|....*....|....*....|.
gi 1351079 1023 GLDSQSSWAIIQLLRKLSKAGQSILCTIHQP 1053
Cdd:PRK13539 157 ALDAAAVALFAELIRAHLAQGGIVIAATHIP 187
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
873-1025 |
4.13e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.84 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 873 DNVSgYCIP-GTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPIDA---SFERRTGYVQQqdihiA----- 940
Cdd:NF033858 283 DHVS-FRIRrGEIFGFLGSNGCGKSTTMKMLT----GLLPaseGEAWLFGQPVDAgdiATRRRVGYMSQ-----Afslyg 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 941 ELTVRESLQFSARMRrpqHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGLnveqRKKLSIGVELVAKPDLLLfLDEP 1020
Cdd:NF033858 353 ELTVRQNLELHARLF---HLPAAEIAARVAEMLERFDLADVADALPDSLPLGI----RQRLSLAVAVIHKPELLI-LDEP 424
|
....*
gi 1351079 1021 TSGLD 1025
Cdd:NF033858 425 TSGVD 429
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
884-1070 |
4.56e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 68.12 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 884 MTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPIDASFE---RRTGYVQQQDIHIAELTVRESLQFSARMR-R 956
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILT----GLLpptSGTVLVGGKDIETNLDavrQSLGMCPQHNILFHHLTVAEHILFYAQLKgR 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 957 PQHLPDSEkmdyVEKIIRVLGME----EYAEALVGEVgcglnveqRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAI 1032
Cdd:TIGR01257 1034 SWEEAQLE----MEAMLEDTGLHhkrnEEAQDLSGGM--------QRKLSVAIAFVGDAKVVV-LDEPTSGVDPYSRRSI 1100
|
170 180 190
....*....|....*....|....*....|....*...
gi 1351079 1033 IQLLRKLSKAGQSILCTIHQPSATLFEefDRLLLLRKG 1070
Cdd:TIGR01257 1101 WDLLLKYRSGRTIIMSTHHMDEADLLG--DRIAIISQG 1136
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
109-346 |
4.73e-11 |
|
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: 67.39 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 109 AIFESF--VRDADEQGIHIRKAGVTIEDVSAKGVDASALEGATFGNI-LCLPLTIFKGIKAkRHQKMRQIISNVNALAEA 185
Cdd:TIGR02868 282 AAFEAFaaLPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVgLGKPTLELRDLSA-GYPGAPPVLDGVSLDLPP 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 186 GEMILVLGRPGAGCSSFLKVTAGEIDQfaggVSGEVAYDGIPQEEMMKRYKADVIYNGELDVHFPYLTVKQTLdfAIACK 265
Cdd:TIGR02868 361 GERVAILGPSGSGKSTLLATLAGLLDP----LQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENL--RLARP 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 266 tpalrvnNVSKKEYIA--SRRDLYATIFGLRHTYNTKVGNDFVRgVSGGERKRVSIAEALAAKGSIYCWDNATRGLDAST 343
Cdd:TIGR02868 435 -------DATDEELWAalERVGLADWLRALPDGLDTVLGEGGAR-LSGGERQRLALARALLADAPILLLDEPTEHLDAET 506
|
...
gi 1351079 344 ALE 346
Cdd:TIGR02868 507 ADE 509
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
864-1070 |
5.26e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 64.79 E-value: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 864 YEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQrNVGIITGDMLVNGRPIdASFER----RTGYVQQQDIHI 939
Cdd:PRK13548 10 VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG-ELSPDSGEVRLNGRPL-ADWSPaelaRRRAVLPQHSSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 940 A-ELTVRESLqfsaRM-RRPQHLPDSEKMDYVEKIIRVLGMEEYAEALV-----GEvgcglnvEQRkklsigVEL----- 1007
Cdd:PRK13548 88 SfPFTVEEVV----AMgRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYpqlsgGE-------QQR------VQLarvla 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1351079 1008 -VAKPDL---LLFLDEPTSGLDSQSSWAIIQLLRKL-SKAGQSILCTIHQPS-ATLFEefDRLLLLRKG 1070
Cdd:PRK13548 151 qLWEPDGpprWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNlAARYA--DRIVLLHQG 217
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
856-1052 |
8.91e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.44 E-value: 8.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGKRMLlDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPIDAS----FERR 928
Cdd:PRK13652 7 RDLCYS--YSGSKEAL-NNINFIAPRNSRIAVIGPNGAGKSTLFRHFN----GILKptsGSVLIRGEPITKEnireVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 929 TGYV-QQQDIHIAELTVRESLQFSarmrrPQHLP-DSEKMDY-VEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGV 1005
Cdd:PRK13652 80 VGLVfQNPDDQIFSPTVEQDIAFG-----PINLGlDEETVAHrVSSALHMLGLEELRDRVPHHLSGG----EKKRVAIAG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1351079 1006 ELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKA-GQSILCTIHQ 1052
Cdd:PRK13652 151 VIAMEPQVLV-LDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQ 197
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
867-1051 |
1.10e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.56 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSgYCIP-GTMTALMGESGAGKTTLLNTLAqRNVGIITGDMLVNGRPIDASFER---RTGYVQQQDIHI-AE 941
Cdd:COG4604 12 GGKVVLDDVS-LTIPkGGITALIGPNGAGKSTLLSMIS-RLLPPDSGEVLVDGLDVATTPSRelaKRLAILRQENHInSR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 942 LTVRESLQFSarmRRPQHL--PDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDE 1019
Cdd:COG4604 90 LTVRELVAFG---RFPYSKgrLTAEDREIIDEAIAYLDLEDLADRYLDELSGG----QRQRAFIAMVLAQDTDYVL-LDE 161
|
170 180 190
....*....|....*....|....*....|...
gi 1351079 1020 PTSGLDSQSSWAIIQLLRKLSK-AGQSILCTIH 1051
Cdd:COG4604 162 PLNNLDMKHSVQMMKLLRRLADeLGKTVVIVLH 194
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
882-1070 |
1.44e-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: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 882 GTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGrpIDASF----ERRTGYVQQQDIHIAELTVRES--LQFSA 952
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIA----GFETpqsGRVLING--VDVTAappaDRPVSMLFQENNLFAHLTVEQNvgLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 953 RMR-RPQhlpDSEKMdyvEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELV-AKPDLLlfLDEPTSGLDSQSSW 1030
Cdd:cd03298 98 GLKlTAE---DRQAI---EVALARVGLAGLEKRLPGELSGG----ERQRVALARVLVrDKPVLL--LDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1351079 1031 AIIQLLRKL-SKAGQSILCTIHQPSATLfEEFDRLLLLRKG 1070
Cdd:cd03298 166 EMLDLVLDLhAETKMTVLMVTHQPEDAK-RLAQRVVFLDNG 205
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
161-387 |
1.90e-10 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 62.89 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 161 FKGIKAKRHQKMRQIISNVNALAEAGEMILVLGRPGAGCSSFLKVtageIDQFAGGVSGEVAYDG----IPQEEMMKR-- 234
Cdd:cd03252 3 FEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKL----IQRFYVPENGRVLVDGhdlaLADPAWLRRqv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 235 ---YKADVIYNGeldvhfpylTVKQTldfaIACKTPALRVNNVskkEYIASRRDLYATIFGLRHTYNTKVGNDFVrGVSG 311
Cdd:cd03252 79 gvvLQENVLFNR---------SIRDN----IALADPGMSMERV---IEAAKLAGAHDFISELPEGYDTIVGEQGA-GLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 312 GERKRVSIAEALAAKGSIYCWDNATrgldasTALEYAKAIRIMTNLLK----STAFVTIYQASenIYETFDKVTVLYSGK 387
Cdd:cd03252 142 GQRQRIAIARALIHNPRILIFDEAT------SALDYESEHAIMRNMHDicagRTVIIIAHRLS--TVKNADRIIVMEKGR 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
867-1025 |
1.97e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.09 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVS-----GYCIpgtmtALMGESGAGKTTLLNTLAqrnvGIITGDmlvNGrpiDASFER--RTGYVQQQDIHI 939
Cdd:COG0488 9 GGRPLLDDVSlsinpGDRI-----GLVGRNGAGKSTLLKILA----GELEPD---SG---EVSIPKglRIGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 940 AELTVRESL--------QFSARMRRPQHL---PDSEKMDYVEKIIRVLGMEEY-AEALVGEV--GCGLNVE--------- 996
Cdd:COG0488 74 DDLTVLDTVldgdaelrALEAELEELEAKlaePDEDLERLAELQEEFEALGGWeAEARAEEIlsGLGFPEEdldrpvsel 153
|
170 180 190
....*....|....*....|....*....|..
gi 1351079 997 ---QRKKLSIGVELVAKPDLLLfLDEPTSGLD 1025
Cdd:COG0488 154 sggWRRRVALARALLSEPDLLL-LDEPTNHLD 184
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
161-387 |
2.46e-10 |
|
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: 61.71 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 161 FKGIKAKRHQKMRQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGeidqFAGGVSGEVAYDGIPQEEMMKRYKADVI 240
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNG----LLGPTSGEVLVDGKDLTKLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 241 ynGEL----DVHFPYLTVKQTLDFAiacktpaLRVNNVSKKEyIASRRDLYATIFGL-----RHTYNtkvgndfvrgVSG 311
Cdd:cd03225 78 --GLVfqnpDDQFFGPTVEEEVAFG-------LENLGLPEEE-IEERVEEALELVGLeglrdRSPFT----------LSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 312 GERKRVSIAEALAAKGSIYCWDNATRGLDastaleyAKAIRIMTNLLK--STAFVTIYQAS---ENIYETFDKVTVLYSG 386
Cdd:cd03225 138 GQKQRVAIAGVLAMDPDILLLDEPTAGLD-------PAGRRELLELLKklKAEGKTIIIVThdlDLLLELADRVIVLEDG 210
|
.
gi 1351079 387 K 387
Cdd:cd03225 211 K 211
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
596-705 |
3.07e-10 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 61.37 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 596 IGSTLASFPFRMIGLTCFFIILFFLSGLHRTAGSFFTIYLFLTMCSEAINGLFEMVSSVCDTLSQANSISGILMMSISMY 675
Cdd:COG0842 50 LGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFL 129
|
90 100 110
....*....|....*....|....*....|
gi 1351079 676 STYMIQLPSMHPWFKWISYVLPIRYAFESM 705
Cdd:COG0842 130 SGAFFPIESLPGWLQAIAYLNPLTYFVEAL 159
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
881-1070 |
3.11e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.10 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 881 PGTMTALMGESGAGKTTLLNTLAQRNVGiITGDMLVNGRPIDASFE--------RRTGYVQQQDIHIAELTVRESLQFSA 952
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDG-SSGEVSLVGQPLHQMDEearaklraKHVGFVFQSFMLIPTLNALENVELPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 953 RMRRPQhlpDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnvEQrKKLSIGVELVAKPDlLLFLDEPTSGLDSQSSWAI 1032
Cdd:PRK10584 114 LLRGES---SRQSRNGAKALLEQLGLGKRLDHLPAQLSGG---EQ-QRVALARAFNGRPD-VLFADEPTGNLDRQTGDKI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1351079 1033 IQLLRKLSK--AGQSILCTiHQPsaTLFEEFDRLLLLRKG 1070
Cdd:PRK10584 186 ADLLFSLNRehGTTLILVT-HDL--QLAARCDRRLRLVNG 222
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
861-1051 |
3.79e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.59 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 861 TIPYEGGKRMLLDnvSGYCIP-GTMTALMGESGAGKTTLLNTLAQRnVGIITGDMLVNGRPIDASFERR-TGYV-QQQDI 937
Cdd:PRK15056 13 TVTWRNGHTALRD--ASFTVPgGSIAALVGVNGSGKSTLFKALMGF-VRLASGKISILGQPTRQALQKNlVAYVpQSEEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 938 HIAELTVRESLQFSAR------MRRPQhlpdSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKP 1011
Cdd:PRK15056 90 DWSFPVLVEDVVMMGRyghmgwLRRAK----KRDRQIVTAALARVDMVEFRHRQIGELSGG----QKKRVFLARAIAQQG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1351079 1012 DLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIH 1051
Cdd:PRK15056 162 QVIL-LDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
879-1043 |
3.80e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 61.95 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 879 CIPGTMTALMGESGAGKTTLLNTL-----AQRNVGIITGDMLVNGRPIDA----SFERRTGYVQQQDIHIAELTVRESLq 949
Cdd:PRK11124 25 CPQGETLVLLGPSGAGKSSLLRVLnllemPRSGTLNIAGNHFDFSKTPSDkairELRRNVGMVFQQYNLWPHLTVQQNL- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 950 FSARMrRPQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLFlDEPTSGLDSQSS 1029
Cdd:PRK11124 104 IEAPC-RVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGG----QQQRVAIARALMMEPQVLLF-DEPTAALDPEIT 177
|
170
....*....|....
gi 1351079 1030 WAIIQLLRKLSKAG 1043
Cdd:PRK11124 178 AQIVSIIRELAETG 191
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
851-1070 |
4.53e-10 |
|
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: 61.36 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 851 GVFIWKDVCFTipYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLaQRNVGIITGDMLVNGRPIdASFERRTg 930
Cdd:cd03244 1 GDIEFKNVSLR--YRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLAL-FRLVELSSGSILIDGVDI-SKIGLHD- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 931 yVQQ------QDIHIAELTVRESLQfsarmrrpqhlPDSEKMDyvEKIIRVL---GMEEYAEALVG-------EVGCGLN 994
Cdd:cd03244 76 -LRSrisiipQDPVLFSGTIRSNLD-----------PFGEYSD--EELWQALervGLKEFVESLPGgldtvveEGGENLS 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351079 995 VEQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKlSKAGQSILCTIHQPSATLfeEFDRLLLLRKG 1070
Cdd:cd03244 142 VGQRQLLCLARALLRKSKILV-LDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTII--DSDRILVLDKG 213
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
867-1053 |
7.71e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.20 E-value: 7.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSgYCI-PGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPI---DASFERRTGYVQQQDIHI 939
Cdd:PRK13538 12 DERILFSGLS-FTLnAGELVQIEGPNGAGKTSLLRILA----GLArpdAGEVLWQGEPIrrqRDEYHQDLLYLGHQPGIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 940 AELTVRESLQFSARMRRPQHlpDSEKMDYVEKIirvlGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDE 1019
Cdd:PRK13538 87 TELTALENLRFYQRLHGPGD--DEALWEALAQV----GLAGFEDVPVRQLSAG----QQRRVALARLWLTRAPLWI-LDE 155
|
170 180 190
....*....|....*....|....*....|....*
gi 1351079 1020 PTSGLDSQSSWAIIQLL-RKLSKAGQSILcTIHQP 1053
Cdd:PRK13538 156 PFTAIDKQGVARLEALLaQHAEQGGMVIL-TTHQD 189
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
554-707 |
8.09e-10 |
|
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: 62.41 E-value: 8.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 554 GGVLYFALLYYSLMGLANISFEHRPILQKHKGYSLYHPSAEAIGSTLASFpfrMIGLTCFFIILFFLSGLHRTAGSFFTI 633
Cdd:pfam12698 165 GLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDF---LVGLLQLLIILLLLFGIGIPFGNLGLL 241
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351079 634 YLFLTMCSEAINGLFEMVSSVCDTLSQANSISGILMMSISMYSTYMIQLPSMHPWFKWISYVLPIRYAFESMLN 707
Cdd:pfam12698 242 LLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLR 315
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
867-1070 |
8.59e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 62.41 E-value: 8.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLA---QRNVGIITgdmlVNGRpiDASF----ERRTGYVQQqdiHI 939
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAgleHQTSGHIR----FHGT--DVSRlharDRKVGFVFQ---HY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 940 A---ELTVRESLQFSARM--RRPQhlPDSEKMDYveKIIRVLGMEEYAEaLVGEVGCGLNVEQRKKLSIGVELVAKPDLL 1014
Cdd:PRK10851 84 AlfrHMTVFDNIAFGLTVlpRRER--PNAAAIKA--KVTQLLEMVQLAH-LADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1351079 1015 LfLDEPTSGLDSQSSWAIIQLLRKLSKAGQ--SILCTIHQPSATlfEEFDRLLLLRKG 1070
Cdd:PRK10851 159 L-LDEPFGALDAQVRKELRRWLRQLHEELKftSVFVTHDQEEAM--EVADRVVVMSQG 213
|
|
| ABC_trans_N |
pfam14510 |
ABC-transporter N-terminal; This domain is found at the N-terminus of ABC-transporter proteins ... |
86-153 |
8.85e-10 |
|
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: 56.56 E-value: 8.85e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1351079 86 SRHTTRSGAFNMDSDSDDGFDAHAIFESFVRDADEQG-IHIRKAGVTIEDVSAKGVDASALEGATFGNI 153
Cdd:pfam14510 12 SSSSSSSPESTDPDEEDSEFDLRKWLKNLRRLIDEDGyIKPRKLGVAFKNLTVSGVGAGADYQPTVGNA 80
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
881-1053 |
9.38e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 60.85 E-value: 9.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 881 PGTMTALMGESGAGKTTLLNTLAQRNVGIIT-GDMLVNGR-----PIDasfER-RTG--YVQQQDIHIAELTVRESLQFS 951
Cdd:COG0396 25 PGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTsGSILLDGEdilelSPD---ERaRAGifLAFQYPVEIPGVSVSNFLRTA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 952 ARMRRPQHLPDSEKMDYVEKIIRVLGM-EEYAEAlvgevgcGLNVE----QRKKLSIGVELVAKPDLLLfLDEPTSGLDs 1026
Cdd:COG0396 102 LNARRGEELSAREFLKLLKEKMKELGLdEDFLDR-------YVNEGfsggEKKRNEILQMLLLEPKLAI-LDETDSGLD- 172
|
170 180 190
....*....|....*....|....*....|
gi 1351079 1027 qsSWA---IIQLLRKLSKAGQSILCTIHQP 1053
Cdd:COG0396 173 --IDAlriVAEGVNKLRSPDRGILIITHYQ 200
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
173-343 |
9.71e-10 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 60.24 E-value: 9.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQFaggvSGEVAYDGIPQEEMMKRykadVIY---NGELDVHF 249
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPT----SGSIRVFGKPLEKERKR----IGYvpqRRSIDRDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 250 PyLTVKQTLDFAIACKTPALRvnNVSKKEYIASRRDLYATifGLRHTYNTKVGNdfvrgVSGGERKRVSIAEALAAKGSI 329
Cdd:cd03235 84 P-ISVRDVVLMGLYGHKGLFR--RLSKADKAKVDEALERV--GLSELADRQIGE-----LSGGQQQRVLLARALVQDPDL 153
|
170
....*....|....
gi 1351079 330 YCWDNATRGLDAST 343
Cdd:cd03235 154 LLLDEPFAGVDPKT 167
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
176-352 |
9.81e-10 |
|
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: 63.07 E-value: 9.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 176 ISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGeidqFAGGVSGEVAYDGIPQEEmmkrYKADVIYNGELDVH-FPYLtV 254
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG----FVDPTEGSIAVNGVPLAD----ADADSWRDQIAWVPqHPFL-F 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 255 KQTLDFAIAcktpaLRVNNVSKKEYIASRRDLYATIF--GLRHTYNTKVGNDfVRGVSGGERKRVSIAEALAAKGSIYCW 332
Cdd:TIGR02857 409 AGTIAENIR-----LARPDASDAEIREALERAGLDEFvaALPQGLDTPIGEG-GAGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180
....*....|....*....|
gi 1351079 333 DNATRGLDASTALEYAKAIR 352
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEALR 502
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
866-1074 |
1.06e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.87 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 866 GGKRMLlDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPIDA-SFERrtGYVQQQDIHIAE 941
Cdd:PRK11248 12 GGKPAL-EDINLTLESGELLVVLGPSGCGKTTLLNLIA----GFVPyqhGSITLDGKPVEGpGAER--GVVFQNEGLLPW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 942 LTVRESLQFSARMRrpqHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEPT 1021
Cdd:PRK11248 85 RNVQDNVAFGLQLA---GVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGG----QRQRVGIARALAANPQLLL-LDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1351079 1022 SGLDSQSSWAIIQLLRKL-SKAGQSILCTIHQPSATLFEEFDRLLLLRKGGQTV 1074
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVV 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
856-1070 |
1.11e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 61.35 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGKRMLLDNVSgYCIP-GTMTALMGESGAGKTT---LLNTL----AQRNVGIITGDMLVNGRPIdASFER 927
Cdd:PRK13640 9 KHVSFT--YPDSKKPALNDIS-FSIPrGSWTALIGHNGSGKSTiskLINGLllpdDNPNSKITVDGITLTAKTV-WDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 928 RTGYV-QQQDIHIAELTVRESLQFSARMRRpqhLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVE 1006
Cdd:PRK13640 85 KVGIVfQNPDNQFVGATVGDDVAFGLENRA---VPRPEMIKIVRDVLADVGMLDYIDSEPANLSGG----QKQRVAIAGI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351079 1007 LVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQ----SILCTIHQPSATlfeefDRLLLLRKG 1070
Cdd:PRK13640 158 LAVEPKIII-LDESTSMLDPAGKEQILKLIRKLKKKNNltviSITHDIDEANMA-----DQVLVLDDG 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
867-1051 |
1.20e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 62.17 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPIDA----SFERRTGYVQQQDIHI 939
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAIN----GTLTptaGTVLVAGDDVEAlsarAASRRVASVPQDTSLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 940 AELTVRESLqfsaRMRRPQHLPDSEKMD-----YVEKIIRVLGMEEYAEALVGEVGCGlnvEQRKKLSIGVELVAKPDLL 1014
Cdd:PRK09536 90 FEFDVRQVV----EMGRTPHRSRFDTWTetdraAVERAMERTGVAQFADRPVTSLSGG---ERQRVLLARALAQATPVLL 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 1351079 1015 LflDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIH 1051
Cdd:PRK09536 163 L--DEPTASLDINHQVRTLELVRRLVDDGKTAVAAIH 197
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
882-1070 |
1.48e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.90 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 882 GTMTALMGESGAGKTTLL---NTLAQRNVGII-TGDMLVNGRPIDASFE---RRTGYVQQ-QDIHIAELTVRESLQFSar 953
Cdd:PRK13643 32 GSYTALIGHTGSGKSTLLqhlNGLLQPTEGKVtVGDIVVSSTSKQKEIKpvrKKVGVVFQfPESQLFEETVLKDVAFG-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 954 mrrPQHL----PDSEKMDyVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSS 1029
Cdd:PRK13643 110 ---PQNFgipkEKAEKIA-AEKLEMVGLADEFWEKSPFELSGG----QMRRVAIAGILAMEPEVLV-LDEPTAGLDPKAR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1351079 1030 WAIIQLLRKLSKAGQSILCTIHQPSaTLFEEFDRLLLLRKG 1070
Cdd:PRK13643 181 IEMMQLFESIHQSGQTVVLVTHLMD-DVADYADYVYLLEKG 220
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
867-1077 |
1.71e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.31 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLaQRNVGI-----ITGDMLVNGRPI---DAS-FERRTGYVQQQDI 937
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-NRLIELypearVSGEVYLDGQDIfkmDVIeLRRRVQMVFQIPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 938 HIAELTVRESLQFSARMRRpqhLPDSEKmdyvEKIIRVLGMEEYAEaLVGEVGCGLNVE-------QRKKLSIGVELVAK 1010
Cdd:PRK14247 93 PIPNLSIFENVALGLKLNR---LVKSKK----ELQERVRWALEKAQ-LWDEVKDRLDAPagklsggQQQRLCIARALAFQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1351079 1011 PDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSATLFEEFDRLLLlrkGGQTVYFG 1077
Cdd:PRK14247 165 PEVLL-ADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLY---KGQIVEWG 227
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
844-1070 |
1.74e-09 |
|
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: 59.02 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 844 FDDLEAKGVFIWKDVCFTIPyeggkrmlldnvsgyciPGTMTALMGESGAGKTTLLNTlaqrnvgiITGDM-LVNGRpid 922
Cdd:cd03250 10 WDSGEQETSFTLKDINLEVP-----------------KGELVAIVGPVGSGKSSLLSA--------LLGELeKLSGS--- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 923 ASFERRTGYVQQQD-IHIAelTVRESLQFSARMrrpqhlpDSEKmdYvEKIIRVLGMEEYAEAL-------VGEVGCGLN 994
Cdd:cd03250 62 VSVPGSIAYVSQEPwIQNG--TIRENILFGKPF-------DEER--Y-EKVIKACALEPDLEILpdgdlteIGEKGINLS 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351079 995 VEQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQ--LLRKLSKAGQSILCTiHQPSatLFEEFDRLLLLRKG 1070
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYL-LDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVT-HQLQ--LLPHADQIVVLDNG 203
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
167-421 |
2.46e-09 |
|
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: 59.50 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 167 KRHQKMRQIISNVNALAEAGEMILVLGRPGAGCSSFLKVtageIDQFAGGVSGEVAYDGIPQEEMMKR----YKADViyn 242
Cdd:cd03256 8 KTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRC----LNGLVEPTSGSVLIDGTDINKLKGKalrqLRRQI--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 243 GELDVHF---PYLTVKQTLDFAIACKTPALRV--NNVSKKEYIASRRDLYAtiFGLRHTYNTKVGNdfvrgVSGGERKRV 317
Cdd:cd03256 81 GMIFQQFnliERLSVLENVLSGRLGRRSTWRSlfGLFPKEEKQRALAALER--VGLLDKAYQRADQ-----LSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 318 SIAEALAAKGSIYCWDNATRGLDASTA---LEYAKAIRIMTNLlksTAFVTIYQAsENIYETFDKVTVLYSGKQIYFGli 394
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSrqvMDLLKRINREEGI---TVIVSLHQV-DLAREYADRIVGLKDGRIVFDG-- 227
|
250 260
....*....|....*....|....*..
gi 1351079 395 heakpyfakmgylcPPRQATAEFLTAL 421
Cdd:cd03256 228 --------------PPAELTDEVLDEI 240
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
847-1041 |
2.46e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 59.67 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 847 LEAKGVFIW-------KDVCFTIPyeggkrmlldnvsgyciPGTMTALMGESGAGKTTLLNTL--------AQRnvgiIT 911
Cdd:COG1117 12 IEVRNLNVYygdkqalKDINLDIP-----------------ENKVTALIGPSGCGKSTLLRCLnrmndlipGAR----VE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 912 GDMLVNGRPI-DASFE-----RRTGYVQQQDIHIAeLTVRESLQFSARMrrpQHLPDSEKMDY-VEKIIRvlgmeeyAEA 984
Cdd:COG1117 71 GEILLDGEDIyDPDVDvvelrRRVGMVFQKPNPFP-KSIYDNVAYGLRL---HGIKSKSELDEiVEESLR-------KAA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351079 985 LVGEV-------GCGLNVEQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSK 1041
Cdd:COG1117 140 LWDEVkdrlkksALGLSGGQQQRLCIARALAVEPEVLL-MDEPTSALDPISTAKIEELILELKK 202
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
174-346 |
2.47e-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: 59.02 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 174 QIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQFaggvSGEVAYDGipqeEMMKRYKADVIYNGELDVHFPYLT 253
Cdd:cd03293 18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT----SGEVLVDG----EPVTGPGPDRGYVFQQDALLPWLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 254 VKQTLDFAiacktpaLRVNNVSKKEyIASRRDLYATIFGLRHTyntkvGNDFVRGVSGGERKRVSIAEALAAKGSIYCWD 333
Cdd:cd03293 90 VLDNVALG-------LELQGVPKAE-ARERAEELLELVGLSGF-----ENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170
....*....|...
gi 1351079 334 NATRGLDASTALE 346
Cdd:cd03293 157 EPFSALDALTREQ 169
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
872-1078 |
2.95e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.10 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTL---LNTLAQRNVGII------------------TGDMLVNGRPIDASFE---- 926
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALLLPDTGTIewifkdeknkkktkekekVLEKLVIQKTRFKKIKkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 927 --RRTGYVQQ-QDIHIAELTVRESLQFSARmrrPQHLPDSEKMDYVEKIIRVLGM-EEYAEALVGEVGCGlnveQRKKLS 1002
Cdd:PRK13651 103 irRRVGVVFQfAEYQLFEQTIEKDIIFGPV---SMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGG----QKRRVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351079 1003 IGVELVAKPDLLlFLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSATLfeEFDRLLLLRKGGQTVYFGD 1078
Cdd:PRK13651 176 LAGILAMEPDFL-VFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVL--EWTKRTIFFKDGKIIKDGD 248
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
867-1049 |
3.56e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.40 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQRNVGI----ITGDMLVNGRPIdasFERRTGYVQ-QQDIHIA- 940
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtITGSIVYNGHNI---YSPRTDTVDlRKEIGMVf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 941 ------ELTVRESLQFSARMRrpqHLPDSEKMDY-VEKIIRVLGMEEYAEALVGEVGCGLNVEQRKKLSIGVELVAKPDL 1013
Cdd:PRK14239 93 qqpnpfPMSIYENVVYGLRLK---GIKDKQVLDEaVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKI 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 1351079 1014 LLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCT 1049
Cdd:PRK14239 170 IL-LDEPTSALDPISAGKIEETLLGLKDDYTMLLVT 204
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
858-1049 |
3.84e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 59.34 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 858 VCFTIPYEGgkRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQRNVGI----ITGDMLVNGRPI----DA-SFERR 928
Cdd:PRK14271 25 VNLTLGFAG--KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVsgyrYSGDVLLGGRSIfnyrDVlEFRRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 929 TGYVQQQDiHIAELTVRESLQfsARMRRPQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGLNVEQRKKLSIGVELV 1008
Cdd:PRK14271 103 VGMLFQRP-NPFPMSIMDNVL--AGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1351079 1009 AKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCT 1049
Cdd:PRK14271 180 VNPEVLL-LDEPTSALDPTTTEKIEEFIRSLADRLTVIIVT 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
872-1064 |
4.00e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQRNVGiITGDMLVNGRP---------IDASFErrtgyVQQQDIHIA-E 941
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQP-DAGSILIDGQEmrfasttaaLAAGVA-----IIYQELHLVpE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 942 LTVRESL---QFSARMrrpqhlpdsekmdyveKIIRVLGMEEYAEALVGEVGCGLNVEQR-KKLSIG----VElVAKPDL 1013
Cdd:PRK11288 94 MTVAENLylgQLPHKG----------------GIVNRRLLNYEAREQLEHLGVDIDPDTPlKYLSIGqrqmVE-IAKALA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1351079 1014 L----LFLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQpsatlFEEFDRL 1064
Cdd:PRK11288 157 RnarvIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHR-----MEEIFAL 206
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
856-1070 |
4.09e-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: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqRNVGIITGDMLVNGRPIDASFERRTGY--VQ 933
Cdd:cd03247 4 NNVSFS--YPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLT-GDLKPQQGEITLDGVPVSDLEKALSSLisVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 934 QQDIHIAELTVRESL--QFSArmrrpqhlpdsekmdyvekiirvlgmeeyaealvGEvgcglnveqRKKLSIGVELVAKP 1011
Cdd:cd03247 81 NQRPYLFDTTLRNNLgrRFSG----------------------------------GE---------RQRLALARILLQDA 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1351079 1012 DLLLfLDEPTSGLDSQSSWAIIQLLRKLSKaGQSILCTIHQPSAtlFEEFDRLLLLRKG 1070
Cdd:cd03247 118 PIVL-LDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTG--IEHMDKILFLENG 172
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
872-1079 |
4.45e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.95 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLLNTLA---QRNVGIITgdmlVNGRPIDA-----SFERRTGYVQQQDIHIAELT 943
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSgihEPTKGTIT----INNINYNKldhklAAQLGIGIIYQELSVIDELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 944 VRESLqFSARM--RRPQHLP--DSEKMDYVEKII-RVLGMEEYAEALVGEvgcgLNVEQRKKLSIGVELVAKPDLLLfLD 1018
Cdd:PRK09700 97 VLENL-YIGRHltKKVCGVNiiDWREMRVRAAMMlLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVII-MD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351079 1019 EPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQpSATLFEEFDRLLLLrKGGQTVYFGDI 1079
Cdd:PRK09700 171 EPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK-LAEIRRICDRYTVM-KDGSSVCSGMV 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
867-1070 |
4.54e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.74 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQRNVGiITGDMLVNGRPIDasfERRTGYVQQQDIHIaeltVRE 946
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRA-TSGRIVFDGKDIT---DWQTAKIMREAVAI----VPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 947 SLQFSARMRRPQHLPD----SEKMDYVEKIIRVLGM-EEYAEALVGEVGCGLNVEQrKKLSIGVELVAKPDLLLfLDEPT 1021
Cdd:PRK11614 88 GRRVFSRMTVEENLAMggffAERDQFQERIKWVYELfPRLHERRIQRAGTMSGGEQ-QMLAIGRALMSQPRLLL-LDEPS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1351079 1022 SGLDSQSSWAIIQLLRKLSKAGQSILcTIHQPSATLFEEFDRLLLLRKG 1070
Cdd:PRK11614 166 LGLAPIIIQQIFDTIEQLREQGMTIF-LVEQNANQALKLADRGYVLENG 213
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
881-1057 |
4.56e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.32 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 881 PGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPI-DASFERRTGYVQQQDIHIAELTVRESLQFSARM-- 954
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLA----GLLhveSGQIQIDGKTAtRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLhg 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 955 RRPQHLPDSEkmdyvekiIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGvELVAKPDLLLFLDEPTSGLDSQSSWAIIQ 1034
Cdd:PRK13543 112 RRAKQMPGSA--------LAIVGLAGYEDTLVRQLSAG----QKKRLALA-RLWLSPAPLWLLDEPYANLDLEGITLVNR 178
|
170 180
....*....|....*....|...
gi 1351079 1035 LLRKLSKAGQSILCTIHQPSATL 1057
Cdd:PRK13543 179 MISAHLRGGGAALVTTHGAYAAP 201
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
174-387 |
5.05e-09 |
|
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: 58.27 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 174 QIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGeIDQfagGVSGEVAYDGIPQEEMMKRYKADvIYNGELDVHF---- 249
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG-LDR---PTSGEVRVDGTDISKLSEKELAA-FRRRHIGFVFqsfn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 250 --PYLTVKQTLDFAiacktpaLRVNNVSKKEYIASRRDLyATIFGLRHTYNTKVGNdfvrgVSGGERKRVSIAEALAAKG 327
Cdd:cd03255 93 llPDLTALENVELP-------LLLAGVPKKERRERAEEL-LERVGLGDRLNHYPSE-----LSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351079 328 SIYCWDNATRGLDASTALEyakairIMtNLLKSTA--------FVTiyqASENIYETFDKVTVLYSGK 387
Cdd:cd03255 160 KIILADEPTGNLDSETGKE------VM-ELLRELNkeagttivVVT---HDPELAEYADRIIELRDGK 217
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
861-1027 |
6.23e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.85 E-value: 6.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 861 TIPYEGgkRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLA---QRNVGIITGD------MLVNGRPIDASFerrtgy 931
Cdd:PRK11607 26 TKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAgfeQPTAGQIMLDgvdlshVPPYQRPINMMF------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 932 vqQQDIHIAELTVRESLQFSARMRRpqhLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKP 1011
Cdd:PRK11607 98 --QSYALFPHMTVEQNIAFGLKQDK---LPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGG----QRQRVALARSLAKRP 168
|
170
....*....|....*.
gi 1351079 1012 DLLLfLDEPTSGLDSQ 1027
Cdd:PRK11607 169 KLLL-LDEPMGALDKK 183
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
869-1070 |
6.89e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.68 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 869 RMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLA-------QRNVGIITGDMLVNGRP---IDAS-FERRTGYVQQQdi 937
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltgggAPRGARVTGDVTLNGEPlaaIDAPrLARLRAVLPQA-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 938 hiaeltVRESLQFSAR----MRRPQHLPDSEKMDYVEKIIRVLGMEEY-AEALVGEVGCGLNVEQRKKLSIGVELV---- 1008
Cdd:PRK13547 92 ------AQPAFAFSAReivlLGRYPHARRAGALTHRDGEIAWQALALAgATALVGRDVTTLSGGELARVQFARVLAqlwp 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1351079 1009 ----AKPDLLLFLDEPTSGLDSQSSWAIIQLLRKLSKAGQ-SILCTIHQPSATLfEEFDRLLLLRKG 1070
Cdd:PRK13547 166 phdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlGVLAIVHDPNLAA-RHADRIAMLADG 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
173-343 |
8.30e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 57.19 E-value: 8.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIdqfaGGVSGEVAYDGIPQEEmmKRYKADVIYNGELDVHFPYL 252
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLL----PPAAGTIKLDGGDIDD--PDVAEACHYLGHRNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 253 TVKQTLDFAIACktpalrvnnvskkeYIASRRDLYATI--FGLRHTYNTKVGNdfvrgVSGGERKRVSIAEALAAKGSIY 330
Cdd:PRK13539 89 TVAENLEFWAAF--------------LGGEELDIAAALeaVGLAPLAHLPFGY-----LSAGQKRRVALARLLVSNRPIW 149
|
170
....*....|...
gi 1351079 331 CWDNATRGLDAST 343
Cdd:PRK13539 150 ILDEPTAALDAAA 162
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
864-1070 |
1.09e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.52 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 864 YEGGKRM--LLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQRNVGiITGDMLVNGRPID-----ASFE---RRTGYVQ 933
Cdd:PRK11629 15 YQEGSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTP-TSGDVIFNGQPMSklssaAKAElrnQKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 934 QQDIHIAELTVRESLQFSARMrrpQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDL 1013
Cdd:PRK11629 94 QFHHLLPDFTALENVAMPLLI---GKKKPAEINSRALEMLAAVGLEHRANHRPSELSGG----ERQRVAIARALVNNPRL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1351079 1014 LLfLDEPTSGLDSQSSWAIIQLLRKLSKA-GQSILCTIHQPSatLFEEFDRLLLLRKG 1070
Cdd:PRK11629 167 VL-ADEPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQ--LAKRMSRQLEMRDG 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
173-396 |
1.12e-08 |
|
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: 59.53 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQfAGGVSGEVAYDGIPQEEMMKRYKADVI--YNGELDVHFP 250
Cdd:COG1123 19 VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPH-GGRISGEVLLDGRDLLELSEALRGRRIgmVFQDPMTQLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 251 YLTVKQTLDFAiacktpaLRVNNVSKKEYIASRRDLYATIfGLRHtyntkVGNDFVRGVSGGERKRVSIAEALAAKGSIY 330
Cdd:COG1123 98 PVTVGDQIAEA-------LENLGLSRAEARARVLELLEAV-GLER-----RLDRYPHQLSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351079 331 CWDNATRGLDASTALEYAKAIRIMTNLLKsTAFVTIYQASENIYETFDKVTVLYSGKQIYFGLIHE 396
Cdd:COG1123 165 IADEPTTALDVTTQAEILDLLRELQRERG-TTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
881-1081 |
1.17e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 57.46 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 881 PGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPIDAS--FERRTGYVQQQDIHIAELTVRE--SLQFSAR 953
Cdd:COG3840 24 AGERVAILGPSGAGKSTLLNLIA----GFLPpdsGRILWNGQDLTALppAERPVSMLFQENNLFPHLTVAQniGLGLRPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 954 MRrpqhlPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAII 1033
Cdd:COG3840 100 LK-----LTAEQRAQVEQALERVGLAGLLDRLPGQLSGG----QRQRVALARCLVRKRPILL-LDEPFSALDPALRQEML 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1351079 1034 QLLRKLSKA-GQSILCTIHQPsatlfEEF----DRLLLLrKGGQTVYFGDIGK 1081
Cdd:COG3840 170 DLVDELCRErGLTVLMVTHDP-----EDAariaDRVLLV-ADGRIAADGPTAA 216
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
186-365 |
1.27e-08 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 56.92 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 186 GEMILVLGRPGAGCSSFLKVTAGEIDQFAGGVS--GEVAYDG-----IPQEemmKRYKADVIYNGELdvhFPYLTVKQTL 258
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlnGTVLFDSrkkinLPPQ---QRKIGLVFQQYAL---FPHLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 259 DFAIacktpalrvnnvsKKEYIASRRDLYATIFGLRHTynTKVGNDFVRGVSGGERKRVSIAEALAAKGSIYCWDNATRG 338
Cdd:cd03297 97 AFGL-------------KRKRNREDRISVDELLDLLGL--DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180
....*....|....*....|....*...
gi 1351079 339 LDASTALEYAKAIR-IMTNLLKSTAFVT 365
Cdd:cd03297 162 LDRALRLQLLPELKqIKKNLNIPVIFVT 189
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
160-387 |
1.41e-08 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 56.04 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 160 IFKGIKAKRHQKmrQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAG--EIDqfaggvSGEVAYDGIPQEEMMKRYKA 237
Cdd:cd03229 2 ELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGleEPD------SGSILIDGEDLTDLEDELPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 238 D------VIYNGELdvhFPYLTVKQtldfaiacktpalrvnNVSkkeyiasrrdlyatiFGLrhtyntkvgndfvrgvSG 311
Cdd:cd03229 74 LrrrigmVFQDFAL---FPHLTVLE----------------NIA---------------LGL----------------SG 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351079 312 GERKRVSIAEALAAKGSIYCWDNATRGLDASTALEYAKAIRIMTNLLKSTAFVTIYQASEnIYETFDKVTVLYSGK 387
Cdd:cd03229 104 GQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDE-AARLADRVVVLRDGK 178
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
173-392 |
1.58e-08 |
|
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: 56.43 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGeMILVLGRPGAGCSSFLKVTAGEIDQfaggVSGEVAYDGIPQEEMMKRYKADVIYngeLDVHFPY- 251
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPP----SSGTIRIDGQDVLKQPQKLRRRIGY---LPQEFGVy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 252 --LTVKQTLDFAIACKtpalrvnNVSKKEyiASRRDLYAtifgLRHTYNTKVGNDFVRGVSGGERKRVSIAEALAAKGSI 329
Cdd:cd03264 85 pnFTVREFLDYIAWLK-------GIPSKE--VKARVDEV----LELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1351079 330 YCWDNATRGLDAstaleyAKAIRImTNLLKSTAFVTIYQAS----ENIYETFDKVTVLYSGKQIYFG 392
Cdd:cd03264 152 LIVDEPTAGLDP------EERIRF-RNLLSELGEDRIVILSthivEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
864-1071 |
1.61e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.96 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 864 YEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLnTLAQRNVGIITGDMLVNGRPIDA----SFERRTGYVQQQDIHI 939
Cdd:PRK10789 323 YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLL-SLIQRHFDVSEGDIRFHDIPLTKlqldSWRSRLAVVSQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 940 AElTVRESLQFSarmrRPQHLPdsEKMDYVEKIIRV----LGMEEYAEALVGEVGCGLNVEQRKKLSIGVELVAKPDLLL 1015
Cdd:PRK10789 402 SD-TVANNIALG----RPDATQ--QEIEHVARLASVhddiLRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1351079 1016 fLDEPTSGLDSQSSWAIIQLLRKLSKaGQSILCTIHQPSAtlFEEFDRLLLLRKGG 1071
Cdd:PRK10789 475 -LDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSA--LTEASEILVMQHGH 526
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
869-1052 |
1.71e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.11 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 869 RMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPID---ASFERRTGYVQQQDIHIAEL 942
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIA----GLLnpeKGEILFERQSIKkdlCTYQKQLCFVGHRSGINPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 943 TVRESLQFSARMrrpqhlpDSEKMDyVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEPTS 1022
Cdd:PRK13540 90 TLRENCLYDIHF-------SPGAVG-ITELCRLFSLEHLIDYPCGLLSSG----QKRQVALLRLWMSKAKLWL-LDEPLV 156
|
170 180 190
....*....|....*....|....*....|
gi 1351079 1023 GLDSQSSWAIIQLLRKLSKAGQSILCTIHQ 1052
Cdd:PRK13540 157 ALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
174-387 |
1.97e-08 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 55.40 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 174 QIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDqfagGVSGEVAYDGIPqeemmkrykadviyngeldvhfpylt 253
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLK----PQQGEITLDGVP-------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 254 vkqtldfaiacktpalrvnnVSkkEYIASRRDLYATIFGLRHTYNTKVGNDFVRGVSGGERKRVSIAEALAAKGSIYCWD 333
Cdd:cd03247 66 --------------------VS--DLEKALSSLISVLNQRPYLFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1351079 334 NATRGLDASTALEYakaIRIMTNLLKSTAFVTIYQASENIyETFDKVTVLYSGK 387
Cdd:cd03247 124 EPTVGLDPITERQL---LSLIFEVLKDKTLIWITHHLTGI-EHMDKILFLENGK 173
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
869-1053 |
2.02e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.98 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 869 RMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLaQRNVGIITGDMLVNGR---------PIDA-SFERRTGYVQQQDIH 938
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL-NRLIEIYDSKIKVDGKvlyfgkdifQIDAiKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 939 IAELTVRESLQFSARMRRPQHLPDSEKMdyVEKIIRVLGMEEYAEALVGEVGCGLNVEQRKKLSIGVELVAKPDLLLfLD 1018
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKREIKKI--VEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLL-MD 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1351079 1019 EPTSGLDSQSSWAIIQLLRKLSKAgQSILCTIHQP 1053
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNP 212
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
175-387 |
2.16e-08 |
|
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: 56.47 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 175 IISNVNALAEAGEMILVLGRPGAGCSSFLKVtageIDQFAGGVSGEVAYDGIPQEEM----MKRYKADViyngELDVHFP 250
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNL----IPRFYDVDSGRILIDGHDVRDYtlasLRRQIGLV----SQDVFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 251 YLTVKQTldfaIACKTPalrvnNVSKKEYIASRRDLYAT--IFGLRHTYNTKVGndfVRGV--SGGERKRVSIAEALAAK 326
Cdd:cd03251 89 NDTVAEN----IAYGRP-----GATREEVEEAARAANAHefIMELPEGYDTVIG---ERGVklSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351079 327 GSIYCWDNATRGLDASTALEYAKAI-RIMTNllkSTAFV------TIYQAseniyetfDKVTVLYSGK 387
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALeRLMKN---RTTFViahrlsTIENA--------DRIVVLEDGK 213
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
881-1081 |
2.20e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 57.32 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 881 PGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPIDASfERRTGYVQQQ--------DIHIAELTVRESLQ 949
Cdd:PRK13638 26 LSPVTGLVGANGCGKSTLFMNLS----GLLrpqKGAVLWQGKPLDYS-KRGLLALRQQvatvfqdpEQQIFYTDIDSDIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 950 FSARmrrPQHLPDSEKMDYVEKIIRVLGMEEYAEAlvgEVGCgLNVEQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSS 1029
Cdd:PRK13638 101 FSLR---NLGVPEAEITRRVDEALTLVDAQHFRHQ---PIQC-LSHGQKKRVAIAGALVLQARYLL-LDEPTAGLDPAGR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1351079 1030 WAIIQLLRKLSKAGQSILCTIHQPSaTLFEEFDRLLLLRKgGQTVYFGDIGK 1081
Cdd:PRK13638 173 TQMIAIIRRIVAQGNHVIISSHDID-LIYEISDAVYVLRQ-GQILTHGAPGE 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
167-344 |
2.28e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 56.36 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 167 KRHQK---MRQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGeIDQfagGVSGEVAYDGIPQEEMMKRYKADViYNG 243
Cdd:PRK11629 13 KRYQEgsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGG-LDT---PTSGDVIFNGQPMSKLSSAAKAEL-RNQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 244 ELDvhFPYLTVKQTLDF-AIACKTPALRVNNVSKKEYIASRRDLYATIfGLRHTYNTKVGNdfvrgVSGGERKRVSIAEA 322
Cdd:PRK11629 88 KLG--FIYQFHHLLPDFtALENVAMPLLIGKKKPAEINSRALEMLAAV-GLEHRANHRPSE-----LSGGERQRVAIARA 159
|
170 180
....*....|....*....|..
gi 1351079 323 LAAKGSIYCWDNATRGLDASTA 344
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNA 181
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
867-1052 |
2.32e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.90 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLL---NTLAQRNVGIITgdmlVNGRPIDAsFERRTGYVQQQDIH-IAEL 942
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLrciNFLEKPSEGSIV----VNGQTINL-VRDKDGQLKVADKNqLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 943 TVRESLQFsarmrrpQHLPDSEKMDYVEKI----IRVLGM-----EEYAEALVGEVG----------CGLNVEQRKKLSI 1003
Cdd:PRK10619 91 RTRLTMVF-------QHFNLWSHMTVLENVmeapIQVLGLskqeaRERAVKYLAKVGideraqgkypVHLSGGQQQRVSI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1351079 1004 GVELVAKPDLLLFlDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQ 1052
Cdd:PRK10619 164 ARALAMEPEVLLF-DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
856-1070 |
2.33e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 56.95 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTL---LNTLAQRNVGIITgdmlVNGRPIDAS----FERR 928
Cdd:PRK13635 9 EHISFR--YPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLaklLNGLLLPEAGTIT----VGGMVLSEEtvwdVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 929 TGYV-QQQDIHIAELTVRESLQFSArmrRPQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVEL 1007
Cdd:PRK13635 83 VGMVfQNPDNQFVGATVQDDVAFGL---ENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGG----QKQRVAIAGVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1351079 1008 VAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQ-SILCTIHQpsatlFEEF---DRLLLLRKG 1070
Cdd:PRK13635 156 ALQPDIII-LDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHD-----LDEAaqaDRVIVMNKG 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
850-1026 |
2.59e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.43 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 850 KGVFIWKDVCFTIPyegGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLaQRNVGIITGDMLVNGRPID----ASF 925
Cdd:PRK13657 332 KGAVEFDDVSFSYD---NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL-QRVFDPQSGRILIDGTDIRtvtrASL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 926 ERRTGYVqQQDIHIAELTVRESLQF------SARMRRPqhLPDSEKMDYVEKiiRVLGMeeyaEALVGEVGCGLNVEQRK 999
Cdd:PRK13657 408 RRNIAVV-FQDAGLFNRSIEDNIRVgrpdatDEEMRAA--AERAQAHDFIER--KPDGY----DTVVGERGRQLSGGERQ 478
|
170 180
....*....|....*....|....*..
gi 1351079 1000 KLSIGVELVAKPDLLLfLDEPTSGLDS 1026
Cdd:PRK13657 479 RLAIARALLKDPPILI-LDEATSALDV 504
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
173-387 |
3.07e-08 |
|
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: 54.71 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQFaggvSGEVAYDGIPQEEMMKRYKADVIYNGELDVHFPYL 252
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD----SGEIKVLGKDIKKEPEEVKRRIGYLPEEPSLYENL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 253 TVKQTLDFaiacktpalrvnnvskkeyiasrrdlyatifglrhtyntkvgndfvrgvSGGERKRVSIAEALAAKGSIYCW 332
Cdd:cd03230 89 TVRENLKL-------------------------------------------------SGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351079 333 DNATRGLDastaleyAKAIRIMTNLLKS------TAFVTiyqaS---ENIYETFDKVTVLYSGK 387
Cdd:cd03230 120 DEPTSGLD-------PESRREFWELLRElkkegkTILLS----ShilEEAERLCDRVAILNNGR 172
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
175-389 |
3.34e-08 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 55.72 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 175 IISNVNALAEAGEMILVLGRPGAGCSSFLKVTAG--EIDqfaggvSGEVAYDGI------PQEemmkRYKADVIYNGELd 246
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGleEPT------SGRIYIGGRdvtdlpPKD----RDIAMVFQNYAL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 247 vhFPYLTVKQTLDFAiacktpaLRVNNVSKKEyIASRRDLYATIFGLRHTYNTKVgndfvRGVSGGERKRVSIAEALAAK 326
Cdd:cd03301 84 --YPHMTVYDNIAFG-------LKLRKVPKDE-IDERVREVAELLQIEHLLDRKP-----KQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1351079 327 GSIYCWDNATRGLDASTALEYAKAIRIMTNLLKSTAfvtiyqasenIYETFDKVTVLYSGKQI 389
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTT----------IYVTHDQVEAMTMADRI 201
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
856-1051 |
3.39e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 56.68 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFT----IPYEGgkRMLLDnVSGYCIPGTMTALMGESGAGKTT---LLNTLAQRNVGIITgdmlVNGRPIDA----- 923
Cdd:PRK13649 6 QNVSYTyqagTPFEG--RALFD-VNLTIEDGSYTAFIGHTGSGKSTimqLLNGLHVPTQGSVR----VDDTLITStsknk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 924 ---SFERRTGYVQQ-QDIHIAELTVRESLQFSarmrrPQHLPDSEKMdyVEKIIR-VLGMEEYAEALVGEVGCGLNVEQR 998
Cdd:PRK13649 79 dikQIRKKVGLVFQfPESQLFEETVLKDVAFG-----PQNFGVSQEE--AEALAReKLALVGISESLFEKNPFELSGGQM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1351079 999 KKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIH 1051
Cdd:PRK13649 152 RRVAIAGILAMEPKILV-LDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
886-1041 |
3.55e-08 |
|
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: 57.77 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 886 ALMGESGAGKTTL----LNTLAQRnvgiitGDMLVNGRPIDASFERrtgyvqqqdihiAELTVRESLQ---------FSA 952
Cdd:COG4172 316 GLVGESGSGKSTLglalLRLIPSE------GEIRFDGQDLDGLSRR------------ALRPLRRRMQvvfqdpfgsLSP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 953 RMRrpqhlpdsekmdyVEKII----RVLGM-------EEYAEALVGEVGcgLNVE------------QRKKLSIGVELVA 1009
Cdd:COG4172 378 RMT-------------VGQIIaeglRVHGPglsaaerRARVAEALEEVG--LDPAarhryphefsggQRQRIAIARALIL 442
|
170 180 190
....*....|....*....|....*....|....*.
gi 1351079 1010 KPDLLLfLDEPTSGLD----SQsswaIIQLLRKLSK 1041
Cdd:COG4172 443 EPKLLV-LDEPTSALDvsvqAQ----ILDLLRDLQR 473
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
173-340 |
3.68e-08 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 55.61 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAG--EIDqfaggvSGEVAYDGIP------QEEMMKRYKADVIYNGE 244
Cdd:cd03262 13 FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLleEPD------SGTIIIDGLKltddkkNINELRQKVGMVFQQFN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 245 LdvhFPYLTVKQTLDFAIacktpaLRVNNVSKKEYIASRRDLYAtifglrhtyntKVG-----NDFVRGVSGGERKRVSI 319
Cdd:cd03262 87 L---FPHLTVLENITLAP------IKVKGMSKAEAEERALELLE-----------KVGladkaDAYPAQLSGGQQQRVAI 146
|
170 180
....*....|....*....|.
gi 1351079 320 AEALAAKGSIYCWDNATRGLD 340
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALD 167
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
856-1074 |
3.87e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.81 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGKRMLLD-NVSgycIPG-TMTALMGESGAGKTTLLNtLAQRNVGIITGDMLVNGRPID----ASFERRT 929
Cdd:PRK10790 344 DNVSFA--YRDDNLVLQNiNLS---VPSrGFVALVGHTGSGKSTLAS-LLMGYYPLTEGEIRLDGRPLSslshSVLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 930 GYVQQQDIHIAEltvreslQFSARMRRPQHLpdSEkmdyvEKIIRVL----------GMEEYAEALVGEVGCGLNVEQRK 999
Cdd:PRK10790 418 AMVQQDPVVLAD-------TFLANVTLGRDI--SE-----EQVWQALetvqlaelarSLPDGLYTPLGEQGNNLSVGQKQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1351079 1000 KLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKagQSILCTIHQPSATLFEEfDRLLLLRKgGQTV 1074
Cdd:PRK10790 484 LLALARVLVQTPQILI-LDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVEA-DTILVLHR-GQAV 553
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
872-1043 |
4.12e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.53 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLLNTL-AQRNVGIITGDMLVNGRPIDASFERRT-----GYVQQQDIHIAELTVR 945
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILsGVYPHGTWDGEIYWSGSPLKASNIRDTeragiVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 946 ESLQFSARMRRPQHLPDSEKMDY-VEKIIRVLGMEEYAEAL-VGEVGCGLN--VEQRKKLSigvelvaKPDLLLFLDEPT 1021
Cdd:TIGR02633 97 ENIFLGNEITLPGGRMAYNAMYLrAKNLLRELQLDADNVTRpVGDYGGGQQqlVEIAKALN-------KQARLLILDEPS 169
|
170 180
....*....|....*....|..
gi 1351079 1022 SGLDSQSSWAIIQLLRKLSKAG 1043
Cdd:TIGR02633 170 SSLTEKETEILLDIIRDLKAHG 191
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
881-1025 |
5.12e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 55.36 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 881 PGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNG----------RPIDASFerrtgyvqQQDIHIAELTVRES 947
Cdd:PRK10771 24 RGERVAILGPSGAGKSTLLNLIA----GFLTpasGSLTLNGqdhtttppsrRPVSMLF--------QENNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 948 ----LQFSARMRRPQHlpdsekmDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEPTSG 1023
Cdd:PRK10771 92 iglgLNPGLKLNAAQR-------EKLHAIARQMGIEDLLARLPGQLSGG----QRQRVALARCLVREQPILL-LDEPFSA 159
|
..
gi 1351079 1024 LD 1025
Cdd:PRK10771 160 LD 161
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
168-389 |
6.74e-08 |
|
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: 54.57 E-value: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 168 RHQKMRQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQfaggVSGEVAYDG--IPQEEmmkRYKADVIYNGEL 245
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE----SSGSILLNGkpIKAKE---RRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 246 DVHFPYLTVKQTLDFAIacKTPALRVNnvsKKEYIASRRDLYAtiFGLRHTyntkvgndfvRGVSGGERKRVSIAEALAA 325
Cdd:cd03226 81 DYQLFTDSVREELLLGL--KELDAGNE---QAETVLKDLDLYA--LKERHP----------LSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351079 326 KGSIYCWDNATRGLDASTALEYAKAIRIMTNllKSTAFVTIYQASENIYETFDKVTVLYSGKQI 389
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAA--QGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
867-1026 |
6.93e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 56.27 E-value: 6.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSgYCIP-GTMTALMGESGAGKTTLLNTLAqrnvGI---ITGDMLVNGRPIDASferrtgYVQQQDIHIA-- 940
Cdd:PRK11432 17 GSNTVIDNLN-LTIKqGTMVTLLGPSGCGKTTVLRLVA----GLekpTEGQIFIDGEDVTHR------SIQQRDICMVfq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 941 ------ELTVRESLQFSARMrrpQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLL 1014
Cdd:PRK11432 86 syalfpHMSLGENVGYGLKM---LGVPKEERKQRVKEALELVDLAGFEDRYVDQISGG----QQQRVALARALILKPKVL 158
|
170
....*....|..
gi 1351079 1015 LFlDEPTSGLDS 1026
Cdd:PRK11432 159 LF-DEPLSNLDA 169
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
863-1041 |
9.86e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 55.44 E-value: 9.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 863 PYEggkRMLLDNVSGYCIPGTMTALMGESGAGKTTL---LNTLAQRNVG-IITGDMLVNGRPIDASFER-RTGYV-QQQD 936
Cdd:PRK13637 17 PFE---KKALDNVNIEIEDGEFVGLIGHTGSGKSTLiqhLNGLLKPTSGkIIIDGVDITDKKVKLSDIRkKVGLVfQYPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 937 IHIAELTVRESLQFSARMRrpqHLPDSEKMDYVEKIIRVLGM--EEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLL 1014
Cdd:PRK13637 94 YQLFEETIEKDIAFGPINL---GLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGG----QKRRVAIAGVVAMEPKIL 166
|
170 180
....*....|....*....|....*..
gi 1351079 1015 LfLDEPTSGLDSQSSWAIIQLLRKLSK 1041
Cdd:PRK13637 167 I-LDEPTAGLDPKGRDEILNKIKELHK 192
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
872-1070 |
1.03e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 54.99 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSgYCIP---------------GTMTALMGESGAGKTTL---LNTLAQRNvgiiTGDMLVNGrpIDA-------SFE 926
Cdd:PRK13644 4 LENVS-YSYPdgtpaleninlvikkGEYIGIIGKNGSGKSTLalhLNGLLRPQ----KGKVLVSG--IDTgdfsklqGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 927 RRTGYV-QQQDIHIAELTVRESLQFSarmrrPQHL--PDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSI 1003
Cdd:PRK13644 77 KLVGIVfQNPETQFVGRTVEEDLAFG-----PENLclPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGG----QGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1004 GVELVAKPDLLLFlDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQpsatlFEEF---DRLLLLRKG 1070
Cdd:PRK13644 148 AGILTMEPECLIF-DEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHN-----LEELhdaDRIIVMDRG 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
872-1043 |
1.47e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLLNTL-AQRNVGIITGDMLVNGRPIDASFERRT---GYV--QQQDIHIAELTVR 945
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsGVYPHGTYEGEIIFEGEELQASNIRDTeraGIAiiHQELALVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 946 ESLqFSARMRRPQHLpdsekMDYVEKIIRvlgmeeyAEALVGEVGCGLNVEQR-KKLSIG----VEL---VAKPDLLLFL 1017
Cdd:PRK13549 101 ENI-FLGNEITPGGI-----MDYDAMYLR-------AQKLLAQLKLDINPATPvGNLGLGqqqlVEIakaLNKQARLLIL 167
|
170 180
....*....|....*....|....*.
gi 1351079 1018 DEPTSGLDSQSSWAIIQLLRKLSKAG 1043
Cdd:PRK13549 168 DEPTASLTESETAVLLDIIRDLKAHG 193
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
173-362 |
1.65e-07 |
|
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: 55.93 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQfaggVSGEVAYDGIPqeemMKRYKADVIYNG----ELDVH 248
Cdd:COG4987 348 RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP----QSGSITLGGVD----LRDLDEDDLRRRiavvPQRPH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 249 FPYLTVKQTLdfAIACKTpalrvnnvskkeyiASRRDLYA---------TIFGLRHTYNTKVGNDfVRGVSGGERKRVSI 319
Cdd:COG4987 420 LFDTTLRENL--RLARPD--------------ATDEELWAalervglgdWLAALPDGLDTWLGEG-GRRLSGGERRRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1351079 320 AEALAAKGSIYCWDNATRGLDASTALeyakaiRIMTNLLKSTA 362
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQ------ALLADLLEALA 519
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
175-359 |
1.99e-07 |
|
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: 55.61 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 175 IISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQFaggvSGEVAYDGIPQEEMMKRY---------KADVIYNGel 245
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT----SGRILIDGIDLRQIDPASlrrqigvvlQDVFLFSG-- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 246 dvhfpylTVKQTLdfaiacktpALRVNNVSKKEYI-ASRR-DLYATIFGLRHTYNTKVGnDFVRGVSGGERKRVSIAEAL 323
Cdd:COG2274 564 -------TIRENI---------TLGDPDATDEEIIeAARLaGLHDFIEALPMGYDTVVG-EGGSNLSGGQRQRLAIARAL 626
|
170 180 190
....*....|....*....|....*....|....*.
gi 1351079 324 AAKGSIYCWDNATRGLDASTALeyakaiRIMTNLLK 359
Cdd:COG2274 627 LRNPRILILDEATSALDAETEA------IILENLRR 656
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
872-1113 |
2.12e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.50 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLLNTL-------------AQRNVGIITGDMLvngrpidASFERRT-GYVQQQDI 937
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptsgtyrvAGQDVATLDADAL-------AQLRREHfGFIFQRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 938 HIAELTVRESLQFSARMrrpQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfL 1017
Cdd:PRK10535 97 LLSHLTAAQNVEVPAVY---AGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGG----QQQRVSIARALMNGGQVIL-A 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1018 DEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPsaTLFEEFDRLLLLRKggqtvyfGDIGKNSATILNyfeRNGARK 1097
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP--QVAAQAERVIEIRD-------GEIVRNPPAQEK---VNVAGG 236
|
250
....*....|....*.
gi 1351079 1098 CDSSENPAEYILEAIG 1113
Cdd:PRK10535 237 TEPVVNTASGWRQFVS 252
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
872-1070 |
2.30e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLLNTLaqrnVGII---TGDMLVNGRPID-----ASFERRTGYVQQQDIHIAELT 943
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCL----FGIYqkdSGSILFQGKEIDfksskEALENGISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 944 VRESLqFSARMRRPQHLPDSEKM-DYVEKIIRVLGMEEYAEALVGEvgcgLNVEQRKKLSI--GVELVAKpdlLLFLDEP 1020
Cdd:PRK10982 90 VMDNM-WLGRYPTKGMFVDQDKMyRDTKAIFDELDIDIDPRAKVAT----LSVSQMQMIEIakAFSYNAK---IVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1351079 1021 TSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQpSATLFEEFDRLLLLRKG 1070
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKLKERGCGIVYISHK-MEEIFQLCDEITILRDG 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
160-360 |
2.36e-07 |
|
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: 53.28 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 160 IFKGIKAKRHQKMRQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQfaggVSGEVAYDGIPQEEMMKRYKADV 239
Cdd:cd03263 2 QIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRP----TSGTAYINGYSIRTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 240 IYNGELDVHFPYLTVKQTLDFAiacktpaLRVNNVSKKEYIASRrDLYATIFGLRHTYNTKVGNdfvrgVSGGERKRVSI 319
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFY-------ARLKGLPKSEIKEEV-ELLLRVLGLTDKANKRART-----LSGGMKRKLSL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1351079 320 AEALAAKGSIYCWDNATRGLDAstaleYAKaiRIMTNLLKS 360
Cdd:cd03263 145 AIALIGGPSVLLLDEPTSGLDP-----ASR--RAIWDLILE 178
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
866-1074 |
3.38e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.54 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 866 GGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLaqrnVGIIT---GDMLVNGRPIDA-------SFERRTGYVQQQ 935
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLL----VGLESpsqGNVSWRGEPLAKlnraqrkAFRRDIQMVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 936 DIHI--AELTVRESLqfSARMRRPQHLPDSEKMDYVEKIIRVLGM-EEYAEALVGEVGCGlnveQRKKLSIGVELVAKPD 1012
Cdd:PRK10419 98 SISAvnPRKTVREII--REPLRHLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGG----QLQRVCLARALAVEPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1351079 1013 LLLfLDEPTSGLDSQSSWAIIQLLRKL-SKAGQSILCTIHQPSatLFEEFDRLLLLRKGGQTV 1074
Cdd:PRK10419 172 LLI-LDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLR--LVERFCQRVMVMDNGQIV 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
867-1065 |
3.64e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSgYCIP-GTMTALMGESGAGKTTLLNTLA------QRNVGIITGDMlvngrpIDASFERRTGYvqqqdiHI 939
Cdd:NF033858 12 GKTVALDDVS-LDIPaGCMVGLIGPDGVGKSSLLSLIAgarkiqQGRVEVLGGDM------ADARHRRAVCP------RI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 940 A------------ELTVRESLQFSARM-------RRpqhlpdsekmdyvEKIIRVL---GMEEYAEALVGEVGCGLnveq 997
Cdd:NF033858 79 AympqglgknlypTLSVFENLDFFGRLfgqdaaeRR-------------RRIDELLratGLAPFADRPAGKLSGGM---- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1351079 998 RKKLSIGVELVAKPDLLLfLDEPTSGLDSQSS---WAIIQLLRKlSKAGQSILCtihqpsATLF----EEFDRLL 1065
Cdd:NF033858 142 KQKLGLCCALIHDPDLLI-LDEPTTGVDPLSRrqfWELIDRIRA-ERPGMSVLV------ATAYmeeaERFDWLV 208
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
880-1025 |
3.73e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.11 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 880 IPGT-MTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRP-IDAS-------FERRTGYVQQQdihiAEL----T 943
Cdd:PRK11144 21 LPAQgITAIFGRSGAGKTSLINAIS----GLTRpqkGRIVLNGRVlFDAEkgiclppEKRRIGYVFQD----ARLfphyK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 944 VRESLQFSarMRRpqhlpdseKM-DYVEKIIRVLGME----EYAEALV-GEvgcglnvEQRkkLSIGVELVAKPDLLLfL 1017
Cdd:PRK11144 93 VRGNLRYG--MAK--------SMvAQFDKIVALLGIEplldRYPGSLSgGE-------KQR--VAIGRALLTAPELLL-M 152
|
....*...
gi 1351079 1018 DEPTSGLD 1025
Cdd:PRK11144 153 DEPLASLD 160
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
864-1094 |
4.18e-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: 52.14 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 864 YEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQR-NVGIITGDMLVNGrpidasferrtgyvqqQDihIAEL 942
Cdd:cd03217 8 VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpKYEVTEGEILFKG----------------ED--ITDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 943 TVREslqfSARM------RRPQHLPDSEKMDYvekiIRvlgmeeyaealvgEVGCGLNVEQRKKLSIGVELVAKPDLLLf 1016
Cdd:cd03217 70 PPEE----RARLgiflafQYPPEIPGVKNADF----LR-------------YVNEGFSGGEKKRNEILQLLLLEPDLAI- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351079 1017 LDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSATLFEEFDRLLLLRKgGQTVYFGDigknsATILNYFERNG 1094
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYD-GRIVKSGD-----KELALEIEKKG 199
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
186-364 |
4.20e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 186 GEMILVLGRPGAGCSSFLKVTAGEIDQFAGGVSGE--VAYDgiPQeemmkrY-KADviYNGeldvhfpylTVKQTLDFAi 262
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkISYK--PQ------YiKPD--YDG---------TVEDLLRSI- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 263 ackTPALRvNNVSKKEyIASRrdlyatiFGLRHTYNTKVGNdfvrgVSGGERKRVSIAEALAAKGSIYCWDNATRGLDAS 342
Cdd:PRK13409 425 ---TDDLG-SSYYKSE-IIKP-------LQLERLLDKNVKD-----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180
....*....|....*....|..
gi 1351079 343 TALEYAKAIRIMTNLLKSTAFV 364
Cdd:PRK13409 488 QRLAVAKAIRRIAEEREATALV 509
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
852-1075 |
5.09e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 52.83 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 852 VFIWKDVCFTipYEGGKRMLLDNVSgYCIP-GTMTALMGESGAGKTtllnTLAQRNVGII---TGDMLVNGRPIDAS--- 924
Cdd:PRK13648 7 IIVFKNVSFQ--YQSDASFTLKDVS-FNIPkGQWTSIVGHNGSGKS----TIAKLMIGIEkvkSGEIFYNNQAITDDnfe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 925 -FERRTGYV-QQQDIHIAELTVRESLQFSARmrrpQHLPDSEKM-DYVEKIIRVLGMEEYAE----ALVGevgcglnvEQ 997
Cdd:PRK13648 80 kLRKHIGIVfQNPDNQFVGSIVKYDVAFGLE----NHAVPYDEMhRRVSEALKQVDMLERADyepnALSG--------GQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1351079 998 RKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQ-SILCTIHQPSATLfeEFDRLLLLRKGgqTVY 1075
Cdd:PRK13648 148 KQRVAIAGVLALNPSVII-LDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAM--EADHVIVMNKG--TVY 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
878-1070 |
5.34e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 53.32 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 878 YCIpgtmtalMGESGAGKTTLL---NTLAQRNVGIITGDMLVNGRPIDasFERRTGYVQQQDI-HIAELTVRESLQFsar 953
Cdd:PRK13631 55 YFI-------IGNSGSGKSTLVthfNGLIKSKYGTIQVGDIYIGDKKN--NHELITNPYSKKIkNFKELRRRVSMVF--- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 954 mrrpqHLPDSEKM-DYVEKIIR----VLGMEEY-----AEALVGEVGC----------GLNVEQRKKLSIGVELVAKPDL 1013
Cdd:PRK13631 123 -----QFPEYQLFkDTIEKDIMfgpvALGVKKSeakklAKFYLNKMGLddsylerspfGLSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1351079 1014 LLFlDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSATLfEEFDRLLLLRKG 1070
Cdd:PRK13631 198 LIF-DEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVL-EVADEVIVMDKG 252
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
872-1051 |
6.05e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.91 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLL---NTLAQRNVGIITgdmlVNGRPIDAS--------FERRTGYVQQ-QDIHI 939
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMqhfNALLKPSSGTIT----IAGYHITPEtgnknlkkLRKKVSLVFQfPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 940 AELTVRESLQFSarmrrPQHLPDSEKmDYVEKIIRVLGMEEYAEALVGEVGCGLNVEQRKKLSIGVELVAKPDLLLfLDE 1019
Cdd:PRK13641 99 FENTVLKDVEFG-----PKNFGFSED-EAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILC-LDE 171
|
170 180 190
....*....|....*....|....*....|..
gi 1351079 1020 PTSGLDSQSSWAIIQLLRKLSKAGQSILCTIH 1051
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
889-1050 |
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 1351079 889 GESGAGKTTLLNTLAQrNVGIITGDMLVNGRPIDA-SFERRTGYVQQ--QDIHI---AELTVRESLQFSARMRRPQHLP- 961
Cdd:COG1101 39 GSNGAGKSTLLNAIAG-SLPPDSGSILIDGKDVTKlPEYKRAKYIGRvfQDPMMgtaPSMTIEENLALAYRRGKRRGLRr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 962 --DSEKMDYVEKIIRVLGM--EEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLR 1037
Cdd:COG1101 118 glTKKRRELFRELLATLGLglENRLDTKVGLLSGG----QRQALSLLMATLTKPKLLL-LDEHTAALDPKTAALVLELTE 192
|
170
....*....|...
gi 1351079 1038 KLSKAGQsiLCTI 1050
Cdd:COG1101 193 KIVEENN--LTTL 203
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
872-1070 |
8.43e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.47 E-value: 8.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLLNTLaqrnVGIIT---GDMLVNGRPID-----ASFERRTGYVQQQDIHIAELT 943
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVL----TGIYTrdaGSILYLGKEVTfngpkSSQEAGIGIIHQELNLIPQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 944 VRESL----QFSARMRRPQHlpdsEKMdYVE--KIIRVLGMEEYAEALVGEVGCGLN--VEQRKKLSIGVELVakpdlll 1015
Cdd:PRK10762 96 IAENIflgrEFVNRFGRIDW----KKM-YAEadKLLARLNLRFSSDKLVGELSIGEQqmVEIAKVLSFESKVI------- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1351079 1016 FLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQpSATLFEEFDRLLLLRKG 1070
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHR-LKEIFEICDDVTVFRDG 217
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
867-1039 |
1.07e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.85 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQR---NVGIITGDMlVNGRPID----ASFERRT------GYVQ 933
Cdd:PRK11701 17 GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARlapDAGEVHYRM-RDGQLRDlyalSEAERRRllrtewGFVH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 934 QQDihiaeltvRESLqfsaRMRRpqhlpdSEKMDYVEKIIRVlGMEEY----AEAL--VGEVGCGLN------------V 995
Cdd:PRK11701 96 QHP--------RDGL----RMQV------SAGGNIGERLMAV-GARHYgdirATAGdwLERVEIDAAriddlpttfsggM 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1351079 996 EQRkkLSIGVELVAKPDlLLFLDEPTSGLDSQSSWAIIQLLRKL 1039
Cdd:PRK11701 157 QQR--LQIARNLVTHPR-LVFMDEPTGGLDVSVQARLLDLLRGL 197
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
174-340 |
1.10e-06 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 51.63 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 174 QIISNVNALAEAGEMILVLGRPGAGCSSFLKVTaGEIDQFAGG---VSGEVAYDGIPQEEMMKRYKADVIYNGELdvhFP 250
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEEITSGdliVDGLKVNDPKVDERLIRQEAGMVFQQFYL---FP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 251 YLTVKQTLDFAiacktpALRVNNVSKKEYIASRRDLYAtifglrhtyntKVG-----NDFVRGVSGGERKRVSIAEALAA 325
Cdd:PRK09493 91 HLTALENVMFG------PLRVRGASKEEAEKQARELLA-----------KVGlaeraHHYPSELSGGQQQRVAIARALAV 153
|
170
....*....|....*
gi 1351079 326 KGSIYCWDNATRGLD 340
Cdd:PRK09493 154 KPKLMLFDEPTSALD 168
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
867-1042 |
1.21e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.69 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPIDA-------SFERRTGYVQQQD 936
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIG----GQIapdHGEILFDGENIPAmsrsrlyTVRKRMSMLFQSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 937 IHIAELTVRESLQFSarMRRPQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGLnvEQRKKLSIGVELvaKPDLLLF 1016
Cdd:PRK11831 94 ALFTDMNVFDNVAYP--LREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGM--ARRAALARAIAL--EPDLIMF 167
|
170 180
....*....|....*....|....*.
gi 1351079 1017 lDEPTSGLDSQSSWAIIQLLRKLSKA 1042
Cdd:PRK11831 168 -DEPFVGQDPITMGVLVKLISELNSA 192
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
860-1074 |
1.22e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.11 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 860 FTIPYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQRnvgiitgdmlvngrpidASFERRTGYVQQQDIHI 939
Cdd:COG2401 34 FGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA-----------------LKGTPVAGCVDVPDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 940 A-ELTVRESLqfsarmrrpqhLPDSEKMDYVEkiirVLGMEEYAEA-----LVGEvgcgLNVEQRKKLSIGVELVAKPDL 1013
Cdd:COG2401 97 GrEASLIDAI-----------GRKGDFKDAVE----LLNAVGLSDAvlwlrRFKE----LSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1351079 1014 LLfLDEPTSGLDSQSSWAIIQLLRKLS-KAGQSILCTIHQPSatlFEEF---DRLLLLRKGGQTV 1074
Cdd:COG2401 158 LV-IDEFCSHLDRQTAKRVARNLQKLArRAGITLVVATHHYD---VIDDlqpDLLIFVGYGGVPE 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
886-1054 |
1.27e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.38 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 886 ALMGESGAGKTTLL---NTLAQRN-VGIITGDMLVNGR--------PIDAsfERRTGYVQQQDIHIAELTVRESLQFSAR 953
Cdd:PRK14267 34 ALMGPSGCGKSTLLrtfNRLLELNeEARVEGEVRLFGRniyspdvdPIEV--RREVGMVFQYPNPFPHLTIYDNVAIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 954 MRRPQHlPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGLNVEQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAII 1033
Cdd:PRK14267 112 LNGLVK-SKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL-MDEPTANIDPVGTAKIE 189
|
170 180
....*....|....*....|.
gi 1351079 1034 QLLRKLSKAGQSILCTiHQPS 1054
Cdd:PRK14267 190 ELLFELKKEYTIVLVT-HSPA 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
867-1039 |
1.36e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTT----LLNTLAQRnvgiitGDMLVNGRPIDaSFERRtgyvqqqdihiAEL 942
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ------GEIWFDGQPLH-NLNRR-----------QLL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 943 TVRESLQ---------FSARMRRPQ--------HLPDSEKMDYVEKIIRVlgMEEyaealvgevgCGLNVE--------- 996
Cdd:PRK15134 359 PVRHRIQvvfqdpnssLNPRLNVLQiieeglrvHQPTLSAAQREQQVIAV--MEE----------VGLDPEtrhrypaef 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1351079 997 ---QRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKL 1039
Cdd:PRK15134 427 sggQRQRIAIARALILKPSLII-LDEPTSSLDKTVQAQILALLKSL 471
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
855-1051 |
1.40e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 51.70 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 855 WKDVCFT----IPYEggkRMLLDNVSGYCIPGTMTALMGESGAGKTTL---LNTLAQRNVGIIT-GDMLVNGRPIDA--- 923
Cdd:PRK13646 5 FDNVSYTyqkgTPYE---HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLiqnINALLKPTTGTVTvDDITITHKTKDKyir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 924 SFERRTGYV-QQQDIHIAELTVRESLQFSarmrrpqhlPDSEKMDyVEKIirvlgmEEYAEALVGEVGCGLNV------- 995
Cdd:PRK13646 82 PVRKRIGMVfQFPESQLFEDTVEREIIFG---------PKNFKMN-LDEV------KNYAHRLLMDLGFSRDVmsqspfq 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 996 ---EQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLS-KAGQSILCTIH 1051
Cdd:PRK13646 146 msgGQMRKIAIVSILAMNPDIIV-LDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSH 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
186-364 |
1.45e-06 |
|
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: 52.86 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 186 GEMILVLGRPGAGCSSFLKVTAGEIDQFAGGVSGE--VAYDgiPQeemmkrY-KADviYNGeldvhfpylTVKQTLDFAI 262
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkISYK--PQ------YiSPD--YDG---------TVEEFLRSAN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 263 ackTPALRVNNVskKEYIASRrdlyatiFGLRHTYNTKVGNdfvrgVSGGERKRVSIAEALAAKGSIYCWDNATRGLDAS 342
Cdd:COG1245 427 ---TDDFGSSYY--KTEIIKP-------LGLEKLLDKNVKD-----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
170 180
....*....|....*....|..
gi 1351079 343 TALEYAKAIRIMTNLLKSTAFV 364
Cdd:COG1245 490 QRLAVAKAIRRFAENRGKTAMV 511
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
881-1052 |
1.57e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.75 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 881 PGTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRP---IDASFERRTG-YVQQQDIHI-AELTVRESLQFsa 952
Cdd:PRK15439 36 AGEVHALLGGNGAGKSTLMKIIA----GIVPpdsGTLEIGGNPcarLTPAKAHQLGiYLVPQEPLLfPNLSVKENILF-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 953 rmRRPQHLPDSEKMdyvekiirvlgmeeyaEALVGEVGCGLNVE-QRKKLSIG----VELV------AKpdlLLFLDEPT 1021
Cdd:PRK15439 110 --GLPKRQASMQKM----------------KQLLAALGCQLDLDsSAGSLEVAdrqiVEILrglmrdSR---ILILDEPT 168
|
170 180 190
....*....|....*....|....*....|.
gi 1351079 1022 SGLDSQSSWAIIQLLRKLSKAGQSILCTIHQ 1052
Cdd:PRK15439 169 ASLTPAETERLFSRIRELLAQGVGIVFISHK 199
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
249-400 |
1.97e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.77 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 249 FP-YLTVKQTLDFAIACKTPALRVnnvsKKEYIASRRDLYATIFGLRHTYNTKvgNDFvrGVSGGERKRVSIAEALAAKG 327
Cdd:PRK13631 124 FPeYQLFKDTIEKDIMFGPVALGV----KKSEAKKLAKFYLNKMGLDDSYLER--SPF--GLSGGQKRRVAIAGILAIQP 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1351079 328 SIYCWDNATRGLDastaleyAKAIRIMTNLLKS------TAFVTIYQAsENIYETFDKVTVLYSGKqiyfgLIHEAKPY 400
Cdd:PRK13631 196 EILIFDEPTAGLD-------PKGEHEMMQLILDakannkTVFVITHTM-EHVLEVADEVIVMDKGK-----ILKTGTPY 261
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
176-352 |
2.44e-06 |
|
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: 50.28 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 176 ISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGeidqFAGGVSGEVAYDGIPQEEM-MKRYKADVIYNGElDVHFPYLTV 254
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAG----LYKPTSGSVLLDGTDIRQLdPADLRRNIGYVPQ-DVTLFYGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 255 KQTLdfaiacktpALRVNNVSKKEYIASRRDLYATIFGLRHT--YNTKVGnDFVRGVSGGERKRVSIAEALAAKGSIYCW 332
Cdd:cd03245 95 RDNI---------TLGAPLADDERILRAAELAGVTDFVNKHPngLDLQIG-ERGRGLSGGQRQAVALARALLNDPPILLL 164
|
170 180
....*....|....*....|
gi 1351079 333 DNATRGLDASTALEYAKAIR 352
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLR 184
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
173-343 |
2.55e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.47 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGeidqFAGGVSGEVAYDGIPQEEMMKRyKADVIYNGELdvhFPYL 252
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAG----FVPYQHGSITLDGKPVEGPGAE-RGVVFQNEGL---LPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 253 TVKQTLDFAiacktpaLRVNNVSKKEYIASRRDLYATIfGLrhtynTKVGNDFVRGVSGGERKRVSIAEALAAKGSIYCW 332
Cdd:PRK11248 86 NVQDNVAFG-------LQLAGVEKMQRLEIAHQMLKKV-GL-----EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170
....*....|.
gi 1351079 333 DNATRGLDAST 343
Cdd:PRK11248 153 DEPFGALDAFT 163
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
856-1025 |
2.93e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 51.60 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTIpyegGKRMLLDNVSgYCI-PGTMTALMGESGAGKTTLLNtlaqrnvgIITGDMlvngRPIDASFER----RTG 930
Cdd:COG0488 319 EGLSKSY----GDKTLLDDLS-LRIdRGDRIGLIGPNGAGKSTLLK--------LLAGEL----EPDSGTVKLgetvKIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 931 YV-QQQDIHIAELTVRESLQFSARMRRPQH----LpdsEKM----DYVEKIIRVL-GmeeyaealvGEvgcglnveqRKK 1000
Cdd:COG0488 382 YFdQHQEELDPDKTVLDELRDGAPGGTEQEvrgyL---GRFlfsgDDAFKPVGVLsG---------GE---------KAR 440
|
170 180
....*....|....*....|....*
gi 1351079 1001 LSIGVELVAKPDLLLfLDEPTSGLD 1025
Cdd:COG0488 441 LALAKLLLSPPNVLL-LDEPTNHLD 464
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
887-1070 |
3.16e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 51.10 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 887 LMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPI-DASFERR-TGYVQQQDIHIAELTVRESLQFSARMrrpQHLP 961
Cdd:PRK09452 45 LLGPSGCGKTTVLRLIA----GFETpdsGRIMLDGQDItHVPAENRhVNTVFQSYALFPHMTVFENVAFGLRM---QKTP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 962 DSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEPTSGLD----SQSSWAIIQLLR 1037
Cdd:PRK09452 118 AAEITPRVMEALRMVQLEEFAQRKPHQLSGG----QQQRVAIARAVVNKPKVLL-LDESLSALDyklrKQMQNELKALQR 192
|
170 180 190
....*....|....*....|....*....|....
gi 1351079 1038 KLskaGQS-ILCTIHQPSAtlFEEFDRLLLLRKG 1070
Cdd:PRK09452 193 KL---GITfVFVTHDQEEA--LTMSDRIVVMRDG 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
860-1081 |
3.60e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 50.42 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 860 FTIPYEGGKrmLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQRNVgiITGDMLVNGRpidASFERRTGYVQQQDIHi 939
Cdd:PRK14258 13 LSFYYDTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE--LESEVRVEGR---VEFFNQNIYERRVNLN- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 940 aeltvRESLQFSARMRRPQHLPDS------------------EKMDYVEKIIRVLGMEEYAEALVGEVGCGLNVEQRKKL 1001
Cdd:PRK14258 85 -----RLRRQVSMVHPKPNLFPMSvydnvaygvkivgwrpklEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1002 SIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLS-KAGQSILCTIHQ-PSATLFEEFDRLLLLRKG--GQTVYFG 1077
Cdd:PRK14258 160 CIARALAVKPKVLL-MDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNlHQVSRLSDFTAFFKGNENriGQLVEFG 238
|
....
gi 1351079 1078 DIGK 1081
Cdd:PRK14258 239 LTKK 242
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
864-1052 |
3.61e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.09 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 864 YEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQrNVGIITGDMLVngrpidasfERRTGYVQQQdIHIAELT 943
Cdd:PTZ00243 668 FELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS-QFEISEGRVWA---------ERSIAYVPQQ-AWIMNAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 944 VRESLQFSarmrrpqhlpDSEKMDYVEKIIRVLGMEEYAEAL-------VGEVGCGLNVEQRKKLSIGVELVAKPDLLLf 1016
Cdd:PTZ00243 737 VRGNILFF----------DEEDAARLADAVRVSQLEADLAQLgggleteIGEKGVNLSGGQKARVSLARAVYANRDVYL- 805
|
170 180 190
....*....|....*....|....*....|....*...
gi 1351079 1017 LDEPTSGLDSQSSWAIIQ--LLRKLskAGQSILCTIHQ 1052
Cdd:PTZ00243 806 LDDPLSALDAHVGERVVEecFLGAL--AGKTRVLATHQ 841
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
867-1057 |
4.01e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 49.64 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLaqrnVGIIT---GDMLVNGRPI-DASFERRT----GYVQQQdih 938
Cdd:COG1137 14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMI----VGLVKpdsGRIFLDGEDItHLPMHKRArlgiGYLPQE--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 939 iA----ELTVRESLQFSARMRRpqhLPDSEKMDYVEKIIRVLGMEE----YAEALVGevGcglnveQRKKLSIGVELVAK 1010
Cdd:COG1137 87 -AsifrKLTVEDNILAVLELRK---LSKKEREERLEELLEEFGITHlrksKAYSLSG--G------ERRRVEIARALATN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1351079 1011 PDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSATL 1057
Cdd:COG1137 155 PKFIL-LDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETL 200
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
881-1070 |
4.38e-06 |
|
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: 48.14 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 881 PGTMTALMGESGAGKTTLLNTLAqRNVGIITGDMLVngrpIDASFERRTGYVQQQDIHIAELtvreslqfsarmrrpqhl 960
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALA-RELGPPGGGVIY----IDGEDILEEVLDQLLLIIVGGK------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 961 pdsekmdyvekiirvlgmeeyaealvgevgcGLNVEQRKKLSIGVELVAKPDL-LLFLDEPTSGLDSQSSWAIIQ----- 1034
Cdd:smart00382 58 -------------------------------KASGSGELRLRLALALARKLKPdVLILDEITSLLDAEQEALLLLleelr 106
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1351079 1035 -LLRKLSKAGQSILCTIHQP----SATLFEEFDRLLLLRKG 1070
Cdd:smart00382 107 lLLLLKSEKNLTVILTTNDEkdlgPALLRRRFDRRIVLLLI 147
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
176-392 |
4.54e-06 |
|
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: 49.65 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 176 ISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQFAGGV--SGEVAYDGIPQEemmkRYKADVIYNGELdvhFPYLT 253
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfGGEDATDVPVQE----RNVGFVFQHYAL---FRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 254 VKQTLDFAIACKTPALRVNNVSKKEYIasrRDLyatifgLRHTYNTKVGNDFVRGVSGGERKRVSIAEALAAKGSIYCWD 333
Cdd:cd03296 91 VFDNVAFGLRVKPRSERPPEAEIRAKV---HEL------LKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 334 NATRGLDASTALEYAKAIR-IMTNLLKSTAFVTIYQasENIYETFDKVTVLYSGKQIYFG 392
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRrLHDELHVTTVFVTHDQ--EEALEVADRVVVMNKGRIEQVG 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
166-396 |
5.45e-06 |
|
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: 49.46 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 166 AKRHQKmRQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEI--DQfaggvsGEVAYDG--IPQEEMMKRYKADVIY 241
Cdd:cd03218 7 SKRYGK-RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkpDS------GKILLDGqdITKLPMHKRARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 242 NGELDVHFPYLTVKQTLDFAiacktpaLRVNNVSKKEyIASRRDLYATIFGLRHTYNTKVGndfvrGVSGGERKRVSIAE 321
Cdd:cd03218 80 LPQEASIFRKLTVEENILAV-------LEIRGLSKKE-REEKLEELLEEFHITHLRKSKAS-----SLSGGERRRVEIAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1351079 322 ALAAKGSIYCWDNATRGLDASTALEYAKAIRImtnlLKSTAF-VTIyqASENIYETF---DKVTVLYSGKQIYFGLIHE 396
Cdd:cd03218 147 ALATNPKFLLLDEPFAGVDPIAVQDIQKIIKI----LKDRGIgVLI--TDHNVRETLsitDRAYIIYEGKVLAEGTPEE 219
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
186-364 |
6.21e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 49.33 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 186 GEMILVLGRPGAGCSSFLKVTAGEIDQFAGGVSGE---VAYDgiPQeemmkrykadviyngeldvhfpYLTVKQ--TLDF 260
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEldtVSYK--PQ----------------------YIKADYegTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 261 AIACKTPalrvnnvskkeyiasrrdlyatIFGLRHTYNTKVGNDF---------VRGVSGGERKRVSIAEALAAKGSIYC 331
Cdd:cd03237 81 LLSSITK----------------------DFYTHPYFKTEIAKPLqieqildreVPELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190
....*....|....*....|....*....|....*
gi 1351079 332 WDNATRGLDASTALEYAKAIR--IMTNllKSTAFV 364
Cdd:cd03237 139 LDEPSAYLDVEQRLMASKVIRrfAENN--EKTAFV 171
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
881-1047 |
6.60e-06 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 48.20 E-value: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 881 PGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRPIDASferrtgyvqqqdihiaelTVREslqfsARMRRP 957
Cdd:cd03215 25 AGEIVGIAGLVGNGQTELAEALF----GLRppaSGEITLDGKPVTRR------------------SPRD-----AIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 958 QHLPDSEKMDYVekiirVLGMEEYAEALVGEVGCGLNVeQrkKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLR 1037
Cdd:cd03215 78 AYVPEDRKREGL-----VLDLSVAENIALSSLLSGGNQ-Q--KVVLARWLARDPRVLI-LDEPTRGVDVGAKAEIYRLIR 148
|
170
....*....|
gi 1351079 1038 KLSKAGQSIL 1047
Cdd:cd03215 149 ELADAGKAVL 158
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
173-387 |
9.85e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 47.91 E-value: 9.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAG----EIdqfaggVSGEVAYDG--IPQEEMMKRYKADViyngeld 246
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpkyEV------TEGEILFKGedITDLPPEERARLGI------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 247 vhfpyltvkqTLDFAIACKTPALRVNnvskkeyiasrrdlyatifglrhtyntkvgnDFVRGV----SGGERKRVSIAEA 322
Cdd:cd03217 80 ----------FLAFQYPPEIPGVKNA-------------------------------DFLRYVnegfSGGEKKRNEILQL 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351079 323 LAAKGSIYCWDNATRGLDAsTALE-YAKAIRIMTNLLKSTAFVTIYQaseNI--YETFDKVTVLYSGK 387
Cdd:cd03217 119 LLLEPDLAILDEPDSGLDI-DALRlVAEVINKLREEGKSVLIITHYQ---RLldYIKPDRVHVLYDGR 182
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
168-392 |
1.10e-05 |
|
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: 49.90 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 168 RHQKMRQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAG--EIDqfaggvSGEVAYDGIP----QEEMMKRYKADVIY 241
Cdd:COG1123 273 RGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGllRPT------SGSILFDGKDltklSRRSLRELRRRVQM 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 242 -----NGELDvhfPYLTVKQTLDFAiacktpaLRVNNVSKKEYIASRRDLYATIFGLrhtyNTKVGNDFVRGVSGGERKR 316
Cdd:COG1123 347 vfqdpYSSLN---PRMTVGDIIAEP-------LRLHGLLSRAERRERVAELLERVGL----PPDLADRYPHELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 317 VSIAEALAAKGSIYCWDNATRGLDASTALEyakairIMtNLLK--------STAFVT-----IYQASeniyetfDKVTVL 383
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQ------IL-NLLRdlqrelglTYLFIShdlavVRYIA-------DRVAVM 478
|
....*....
gi 1351079 384 YSGKQIYFG 392
Cdd:COG1123 479 YDGRIVEDG 487
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
865-1077 |
1.12e-05 |
|
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: 48.30 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 865 EGGKRMLLDNVS-----GYCIpgtmtALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRpIDASFERRTGYVqqqd 936
Cdd:cd03220 31 EVGEFWALKDVSfevprGERI-----GLIGRNGAGKSTLLRLLA----GIYppdSGTVTVRGR-VSSLLGLGGGFN---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 937 ihiAELTVRESLQFSARMRRpqhLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLf 1016
Cdd:cd03220 97 ---PELTGRENIYLNGRLLG---LSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSG----MKARLAFAIATALEPDILL- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1351079 1017 LDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSatLFEEF-DRLLLLRKgGQTVYFG 1077
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPS--SIKRLcDRALVLEK-GKIRFDG 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
856-1050 |
1.14e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 48.83 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipYEGGKRMLLDNVSgYCIP-GTMTALMGESGAGKTTLLNTLaqrnVGII---TGDMLVNGRPIDAS--FERRT 929
Cdd:PRK13632 11 ENVSFS--YPNSENNALKNVS-FEINeGEYVAILGHNGSGKSTISKIL----TGLLkpqSGEIKIDGITISKEnlKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 930 --GYV-QQQDIHIAELTVRESLQFSARMRRpqhLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVE 1006
Cdd:PRK13632 84 kiGIIfQNPDNQFIGATVEDDIAFGLENKK---VPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGG----QKQRVAIASV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1351079 1007 LVAKPDLLLFlDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTI 1050
Cdd:PRK13632 157 LALNPEIIIF-DESTSMLDPKGKREIKKIMVDLRKTRKKTLISI 199
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
174-339 |
1.39e-05 |
|
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: 47.81 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 174 QIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQFaggvSGEVAYDG-----IPQEEMMKRYKADVIYNGELdvh 248
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR----SGSIRFDGrditgLPPHERARAGIGYVPEGRRI--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 249 FPYLTVKQTLDFAIACKTPalrvnnvskkeyiASRRDLYATIFG----LRHTYNTKVGNdfvrgVSGGERKRVSIAEALA 324
Cdd:cd03224 87 FPELTVEENLLLGAYARRR-------------AKRKARLERVYElfprLKERRKQLAGT-----LSGGEQQMLAIARALM 148
|
170
....*....|....*
gi 1351079 325 AKGSIYCWDNATRGL 339
Cdd:cd03224 149 SRPKLLLLDEPSEGL 163
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
173-396 |
1.50e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 48.65 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQfaggVSGEVAYDG--IPQEEM--MKRYKADVIYNGELDVH 248
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKP----TSGSVLIRGepITKENIreVRKFVGLVFQNPDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 249 FPylTVKQTLDFAiacktpalRVNNVSKKEYIASRRDLYATIFGLRHtYNTKVGNDfvrgVSGGERKRVSIAEALAAKGS 328
Cdd:PRK13652 93 SP--TVEQDIAFG--------PINLGLDEETVAHRVSSALHMLGLEE-LRDRVPHH----LSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 329 IYCWDNATRGLDastALEYAKAIRIMTNLLKSTAFVTIYQAS--ENIYETFDKVTVLYSGKQIYFGLIHE 396
Cdd:PRK13652 158 VLVLDEPTAGLD---PQGVKELIDFLNDLPETYGMTVIFSTHqlDLVPEMADYIYVMDKGRIVAYGTVEE 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
882-1070 |
1.57e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 49.26 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 882 GTMTALMGESGAGKTTLLNTLaQRNVGIITGDMLVNGRPI----DASF----ERRTGYVQQQDIHIAELTVRESLQFSAR 953
Cdd:PRK10070 54 GEIFVIMGLSGSGKSTMVRLL-NRLIEPTRGQVLIDGVDIakisDAELrevrRKKIAMVFQSFALMPHMTVLDNTAFGME 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 954 MrrpQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGLnveqRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAII 1033
Cdd:PRK10070 133 L---AGINAEERREKALDALRQVGLENYAHSYPDELSGGM----RQRVGLARALAINPDILL-MDEAFSALDPLIRTEMQ 204
|
170 180 190
....*....|....*....|....*....|....*..
gi 1351079 1034 QLLRKLSKAGQSILCTIHQPSATLFEEFDRLLLLRKG 1070
Cdd:PRK10070 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
867-1039 |
1.72e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 48.24 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 867 GKRMLLDNVSgYCIPGT-MTALMGESGAGKTTLLNTLAQRNvgiitgDmLVNGRPIDASFERRTGYVQQQDIHIAELTVR 945
Cdd:PRK14243 21 GSFLAVKNVW-LDIPKNqITAFIGPSGCGKSTILRCFNRLN------D-LIPGFRVEGKVTFHGKNLYAPDVDPVEVRRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 946 ESLQFsarmRRPQHLPDSEKmDYVEKIIRVLG----MEEYAE------ALVGEV-------GCGLNVEQRKKLSIGVELV 1008
Cdd:PRK14243 93 IGMVF----QKPNPFPKSIY-DNIAYGARINGykgdMDELVErslrqaALWDEVkdklkqsGLSLSGGQQQRLCIARAIA 167
|
170 180 190
....*....|....*....|....*....|.
gi 1351079 1009 AKPDLLLfLDEPTSGLDSQSSWAIIQLLRKL 1039
Cdd:PRK14243 168 VQPEVIL-MDEPCSALDPISTLRIEELMHEL 197
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
892-1047 |
1.75e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 49.25 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 892 GAGKTTLLNTLAqrnvGI---ITGDMLVNGRPID-----ASFERRTGYV----QQQDIhIAELTVRE--SLQFSARMRRP 957
Cdd:COG1129 288 GAGRTELARALF----GAdpaDSGEIRLDGKPVRirsprDAIRAGIAYVpedrKGEGL-VLDLSIREniTLASLDRLSRG 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 958 QHLPDSEKMDYVEKIIRVL-----GMEEYAEALVGevgcGlNveQrKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAI 1032
Cdd:COG1129 363 GLLDRRRERALAEEYIKRLriktpSPEQPVGNLSG----G-N--Q-QKVVLAKWLATDPKVLI-LDEPTRGIDVGAKAEI 433
|
170
....*....|....*
gi 1351079 1033 IQLLRKLSKAGQSIL 1047
Cdd:COG1129 434 YRLIRELAAEGKAVI 448
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
186-352 |
2.15e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 186 GEMILVLGRPGAGCSSFLKVTAGEIDQFAGGVSGEVAYDgipqeEMMKRYKADV-------IYNGELDV-HFP-YL---- 252
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWD-----EVLKRFRGTElqnyfkkLYNGEIKVvHKPqYVdlip 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 253 -----TVKQTLDfaiacktpalRVNNVSKKEYIASRrdlyatiFGLRHTYNTKVGNdfvrgVSGGERKRVSIAEALAAKG 327
Cdd:PRK13409 174 kvfkgKVRELLK----------KVDERGKLDEVVER-------LGLENILDRDISE-----LSGGELQRVAIAAALLRDA 231
|
170 180
....*....|....*....|....*
gi 1351079 328 SIYCWDNATRGLDASTALEYAKAIR 352
Cdd:PRK13409 232 DFYFFDEPTSYLDIRQRLNVARLIR 256
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
176-340 |
2.45e-05 |
|
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: 47.33 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 176 ISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQFAGGVS-GEVAYDGIPQEEMMKRYKADVIYNGELdvhfPYL-- 252
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwSNKNESEPSFEATRSRNRYSVAYAAQK----PWLln 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 253 -TVKQTLDFAiackTPAlrvnNVSKKEYIASRRDLYATIFGLRHTYNTKVGNdfvRGV--SGGERKRVSIAEALAAKGSI 329
Cdd:cd03290 93 aTVEENITFG----SPF----NKQRYKAVTDACSLQPDIDLLPFGDQTEIGE---RGInlSGGQRQRICVARALYQNTNI 161
|
170
....*....|.
gi 1351079 330 YCWDNATRGLD 340
Cdd:cd03290 162 VFLDDPFSALD 172
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
176-340 |
2.58e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 48.29 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 176 ISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGeidqFAGGVSGEVAYDGI----------PQEEMMKRYKAdviyngel 245
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG----FEQPTAGQIMLDGVdlshvppyqrPINMMFQSYAL-------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 246 dvhFPYLTVKQTLDFAiacktpaLRVNNVSKKEyIASRrdlYATIFGLRHTyntkvgNDFVR----GVSGGERKRVSIAE 321
Cdd:PRK11607 103 ---FPHMTVEQNIAFG-------LKQDKLPKAE-IASR---VNEMLGLVHM------QEFAKrkphQLSGGQRQRVALAR 162
|
170
....*....|....*....
gi 1351079 322 ALAAKGSIYCWDNATRGLD 340
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALD 181
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
873-1051 |
2.98e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 47.29 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 873 DNVSGYCIPGTMTALMGESGAGKTTLLNTLA--QRNVGiitGDMLVNGRPID--ASFE-RRTGYVQQ-QDIHI-AELTVR 945
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTgfYKPTG---GTILLRGQHIEglPGHQiARMGVVRTfQHVRLfREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 946 ESL------QFSARM----------RRPQhlpdSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVA 1009
Cdd:PRK11300 99 ENLlvaqhqQLKTGLfsgllktpafRRAE----SEALDRAATWLERVGLLEHANRQAGNLAYG----QQRRLEIARCMVT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1351079 1010 KPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKA-GQSILCTIH 1051
Cdd:PRK11300 171 QPEILM-LDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEH 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
167-392 |
3.04e-05 |
|
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: 46.98 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 167 KRHQKMRQIISNVNAL---AEAGEMILVLGRPGAGCSSFLKVTAGEIDQFAGGVsgEVAYDGIPQEEMMKRYKADVIYNG 243
Cdd:cd03266 9 KRFRDVKKTVQAVDGVsftVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA--TVDGFDVVKEPAEARRRLGFVSDS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 244 elDVHFPYLTVKQTLD-FAiacktpalRVNNVSKKEYIAsRRDLYATIFGLRHTYNTKVGndfvrGVSGGERKRVSIAEA 322
Cdd:cd03266 87 --TGLYDRLTARENLEyFA--------GLYGLKGDELTA-RLEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351079 323 LAAKGSIYCWDNATRGLDASTALEYAKAIRIMTNLLKSTAFVT-IYQASEniyETFDKVTVLYSGKQIYFG 392
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSThIMQEVE---RLCDRVVVLHRGRVVYEG 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
173-387 |
3.04e-05 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 48.16 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQFAG-------GVSGEVAYDgipqeemmkRYKADVIYNGEL 245
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGhirfhgtDVSRLHARD---------RKVGFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 246 dvhFPYLTVKQTLDFAIACKTPALRVNnvskKEYIASRRDLYATIFGLRHtyntkVGNDFVRGVSGGERKRVSIAEALAA 325
Cdd:PRK10851 86 ---FRHMTVFDNIAFGLTVLPRRERPN----AAAIKAKVTQLLEMVQLAH-----LADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1351079 326 KGSIYCWDNATRGLDASTALEYAKAIRIMTNLLKSTA-FVTIYQasENIYETFDKVTVLYSGK 387
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSvFVTHDQ--EEAMEVADRVVVMSQGN 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
856-1097 |
3.10e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 47.00 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTIPyeggkrmlldnvsgyciPGTMTALMGESGAGKTTLLNTLAqrnvGII---TGDMLVNGRpIDASFERRTGYV 932
Cdd:COG1134 43 KDVSFEVE-----------------RGESVGIIGRNGAGKSTLLKLIA----GILeptSGRVEVNGR-VSALLELGAGFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 933 qqqdihiAELTVRESLQFSAR---MRRPQHlpdSEKMDYVekiirvlgmEEYAEalVGE-----VgcglnveqrKKLSIG 1004
Cdd:COG1134 101 -------PELTGRENIYLNGRllgLSRKEI---DEKFDEI---------VEFAE--LGDfidqpV---------KTYSSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1005 --VEL---VA---KPDLLLfLDEPTSGLDS---QSSwaiIQLLRKLSKAGQSILCTIHQPSAtlFEEF-DRLLLLRKgGQ 1072
Cdd:COG1134 151 mrARLafaVAtavDPDILL-VDEVLAVGDAafqKKC---LARIRELRESGRTVIFVSHSMGA--VRRLcDRAIWLEK-GR 223
|
250 260
....*....|....*....|....*
gi 1351079 1073 TVYFGDIgknsATILNYFERNGARK 1097
Cdd:COG1134 224 LVMDGDP----EEVIAAYEALLAGR 244
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
175-344 |
3.29e-05 |
|
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: 46.69 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 175 IISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQFAGGV--SGEVAYdgIPQEEMmkrykadvIYNGeldvhfpyl 252
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVsvPGSIAY--VSQEPW--------IQNG--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 253 TVK-----------QTLDFAI-ACktpALrvnnvskkeyiasRRDLYATIFGLrhtyNTKVGndfVRGV--SGGERKRVS 318
Cdd:cd03250 81 TIRenilfgkpfdeERYEKVIkAC---AL-------------EPDLEILPDGD----LTEIG---EKGInlSGGQKQRIS 137
|
170 180
....*....|....*....|....*.
gi 1351079 319 IAEALAAKGSIYCWDNATRGLDASTA 344
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVG 163
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
881-1025 |
3.93e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.09 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 881 PGTMTALMGESGAGKTTLLNTLAQR-NVGIITGDMLVNGRPI-DASFERRTG----YVQQQDIHIAELTVRESLQFS--- 951
Cdd:PRK09580 26 PGEVHAIMGPNGSGKSTLSATLAGReDYEVTGGTVEFKGKDLlELSPEDRAGegifMAFQYPVEIPGVSNQFFLQTAlna 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1351079 952 ARMRRPQHLPDS-EKMDYVEKIIRVLGMEEyaEALVGEVGCGLNVEQRKKLSIGVELVAKPDLLLfLDEPTSGLD 1025
Cdd:PRK09580 106 VRSYRGQEPLDRfDFQDLMEEKIALLKMPE--DLLTRSVNVGFSGGEKKRNDILQMAVLEPELCI-LDESDSGLD 177
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
856-1039 |
4.15e-05 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 47.38 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTIPYEGGKRMLLDNVSgYCIP-GTMTALMGESGAGKTTLLNTLA--QRNVgiiTGDMLVNGRPIDA-------SF 925
Cdd:COG1135 5 ENLSKTFPTKGGPVTALDDVS-LTIEkGEIFGIIGYSGAGKSTLIRCINllERPT---SGSVLVDGVDLTAlserelrAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 926 ERRTGYVQQQDIHIAELTVRESLQFSARMrrpQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEvgcgLNVEQRKKLSIGV 1005
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEI---AGVPKAEIRKRVAELLELVGLSDKADAYPSQ----LSGGQKQRVGIAR 153
|
170 180 190
....*....|....*....|....*....|....
gi 1351079 1006 ELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKL 1039
Cdd:COG1135 154 ALANNPKVLL-CDEATSALDPETTRSILDLLKDI 186
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
173-227 |
4.33e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 46.69 E-value: 4.33e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDqfagGVSGEVAYDGIP 227
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELS----PDSGEVRLNGRP 65
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
174-389 |
4.35e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 46.99 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 174 QIISNVNALAEAGEMILVLGRPGAGCSS-FLkvtageidQFAGGV---SGEVAYDGIP----QEEMMK-RYKADVIYNGE 244
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTlFL--------HFNGILkptSGEVLIKGEPikydKKSLLEvRKTVGIVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 245 LDVHF-PylTVKQtlDFAIACKTPALRVNNVSKKEYIASRRdlyatiFGLRhTYNTKVGNDFvrgvSGGERKRVSIAEAL 323
Cdd:PRK13639 88 DDQLFaP--TVEE--DVAFGPLNLGLSKEEVEKRVKEALKA------VGME-GFENKPPHHL----SGGQKKRVAIAGIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1351079 324 AAKGSIYCWDNATRGLDASTAleyAKAIRIMTNLLKSTAFVTIYQASENIYETF-DKVTVLYSGKQI 389
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGA---SQIMKLLYDLNKEGITIIISTHDVDLVPVYaDKVYVMSDGKII 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
174-396 |
4.52e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.86 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 174 QIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQfaggVSGEVAYDGIPQEEMMKRYKAD----VIYNgELDVhF 249
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP----TKGTITINNINYNKLDHKLAAQlgigIIYQ-ELSV-I 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 250 PYLTVKQTLDFAIACKTPALRVNNVSKKEyIASRRDLYATIFGLRHTYNTKVGNdfvrgVSGGERKRVSIAEALAAKGSI 329
Cdd:PRK09700 93 DELTVLENLYIGRHLTKKVCGVNIIDWRE-MRVRAAMMLLRVGLKVDLDEKVAN-----LSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351079 330 YCWDNATRGLdasTALEYAKAIRIMTNLLKS-TAFVTIYQASENIYETFDKVTVLYSGKQIYFGLIHE 396
Cdd:PRK09700 167 IIMDEPTSSL---TNKEVDYLFLIMNQLRKEgTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSD 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
889-1026 |
4.61e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 47.33 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 889 GESGAGKTTLLNTLAqrnvG---IITGDMLVNGRPID--ASFERRTGYVQQQDIHIAELTVRESLQFSARMRRPQHlpdS 963
Cdd:PRK11000 36 GPSGCGKSTLLRMIA----GledITSGDLFIGEKRMNdvPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKK---E 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1351079 964 EKMDYVEKIIRVLGMEEYAE----ALVGEvgcglnveQRKKLSIGVELVAKPDLLLfLDEPTSGLDS 1026
Cdd:PRK11000 109 EINQRVNQVAEVLQLAHLLDrkpkALSGG--------QRQRVAIGRTLVAEPSVFL-LDEPLSNLDA 166
|
|
| PDR_CDR |
pfam06422 |
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters ... |
1437-1469 |
5.42e-05 |
|
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters comprising extracellular loop 3, transmembrane segment 6 and linker region.
Pssm-ID: 461906 [Multi-domain] Cd Length: 92 Bit Score: 43.22 E-value: 5.42e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1351079 1437 GDNYL-THISSKYSYLWRNFGI---FWI-YIFFNIIAM 1469
Cdd:pfam06422 31 GDDYLaASYGYSYSHLWRNFGIliaFWIfFLALYLIAT 68
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
872-1070 |
5.56e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 46.92 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLLntlaQRNVGII---TGDMLVNGRPIDASFE---------RRTGYVQQ-QDIH 938
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMI----QLTNGLIiseTGQTIVGDYAIPANLKkikevkrlrKEIGLVFQfPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 939 IAELTVRESLQFSarmrrPQHLPDSEKMDYvEKIIRVLGM----EEYAEALVGEVGCGlnveQRKKLSIGvELVAKPDLL 1014
Cdd:PRK13645 103 LFQETIEKDIAFG-----PVNLGENKQEAY-KKVPELLKLvqlpEDYVKRSPFELSGG----QKRRVALA-GIIAMDGNT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1351079 1015 LFLDEPTSGLDSQSSWAIIQLLRKLSKA-GQSILCTIHQPSATLfEEFDRLLLLRKG 1070
Cdd:PRK13645 172 LVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVL-RIADEVIVMHEG 227
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
1051-1081 |
7.61e-05 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 46.82 E-value: 7.61e-05
10 20 30
....*....|....*....|....*....|.
gi 1351079 1051 HQPSATLFEEFDRLLLLRKGGQTVYFGDIGK 1081
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLTVYHGPVKK 31
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
170-357 |
7.78e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.01 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 170 QKMRQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQfaggVSGEVAYDGIPqeemMKRYKADViYNGELDV-- 247
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDV----SEGDIRFHDIP----LTKLQLDS-WRSRLAVvs 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 248 HFPYL---TVKQTldfaIACKTPALRVNNVskkEYIASRRDLYATIFGLRHTYNTKVGNdfvRGV--SGGERKRVSIAEA 322
Cdd:PRK10789 396 QTPFLfsdTVANN----IALGRPDATQQEI---EHVARLASVHDDILRLPQGYDTEVGE---RGVmlSGGQKQRISIARA 465
|
170 180 190
....*....|....*....|....*....|....*
gi 1351079 323 LAAKGSIYCWDNATRGLDASTalEYakaiRIMTNL 357
Cdd:PRK10789 466 LLLNAEILILDDALSAVDGRT--EH----QILHNL 494
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
184-360 |
8.89e-05 |
|
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: 47.09 E-value: 8.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 184 EAGEMILVLGRPGAGCSSFLKVTAGEIDQFAGGVSGEVAYDgipqeEMMKRYKADV-------IYNGELDV-HFP-YL-- 252
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWD-----EVLKRFRGTElqdyfkkLANGEIKVaHKPqYVdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 253 -------TVKQTLDfaiacktpalRVNNVSKKEYIASRrdlyatiFGLRHTYNTKVGNdfvrgVSGGERKRVSIAEALAA 325
Cdd:COG1245 172 ipkvfkgTVRELLE----------KVDERGKLDELAEK-------LGLENILDRDISE-----LSGGELQRVAIAAALLR 229
|
170 180 190
....*....|....*....|....*....|....*
gi 1351079 326 KGSIYCWDNATRGLDASTALEYAKAIRIMTNLLKS 360
Cdd:COG1245 230 DADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKY 264
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
173-392 |
8.91e-05 |
|
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: 45.74 E-value: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAG--EIDqfaggvSGEVAYDG-----IPQEEMMK-RYKADVIY-NG 243
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGllRPD------SGEILVDGqditgLSEKELYElRRRIGMLFqGG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 244 ELdvhFPYLTVKQTLDFAiacktpaLRVN-NVSKKEyIASRRDLYATIFGLRHTYNTkvgndFVRGVSGGERKRVSIAEA 322
Cdd:COG1127 92 AL---FDSLTVFENVAFP-------LREHtDLSEAE-IRELVLEKLELVGLPGAADK-----MPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 323 LAAKGSIYCWDNATRGLDASTALEYAKAIRIMTNLLKSTAFVTIYQASEnIYETFDKVTVLYSGKQIYFG 392
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDS-AFAIADRVAVLADGKIIAEG 224
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
1278-1382 |
1.00e-04 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 45.19 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1278 LFFSTIFFVSSYFPLRIFFeASRSAVYFLNYCIMFQLYYVGLGLMILYMSPNLPSANVILGLCLSFMLSFCGVTQPVSLM 1357
Cdd:COG0842 61 LLQALLVLLVALLFFGVPL-RGLSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESL 139
|
90 100
....*....|....*....|....*
gi 1351079 1358 PGFWTFMWKASPYTYFVQNLVGIML 1382
Cdd:COG0842 140 PGWLQAIAYLNPLTYFVEALRALFL 164
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
173-396 |
1.05e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 45.81 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQFAGG--VSGEVAYDG--IPQEEMMK-RYKADVIYngELDV 247
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKikVDGKVLYFGkdIFQIDAIKlRKEVGMVF--QQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 248 HFPYLTVKQTLDFAiacktpaLRVNNVSKKEYIASRRDLYATIFGLRHTYNTKVgNDFVRGVSGGERKRVSIAEALAAKG 327
Cdd:PRK14246 101 PFPHLSIYDNIAYP-------LKSHGIKEKREIKKIVEECLRKVGLWKEVYDRL-NSPASQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351079 328 SIYCWDNATRGLD--ASTALEyakaiRIMTNLLKSTAFVTIYQASENIYETFDKVTVLYSGKQIYFGLIHE 396
Cdd:PRK14246 173 KVLLMDEPTSMIDivNSQAIE-----KLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNE 238
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
867-1039 |
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 1351079 867 GKRMLLDNVSGYCIPGTMTALMGESGAGKTTLlntlaqrnVGIITGDMLVNGRPIDASFERRTGYVQQQdIHI---AELT 943
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTL--------VRVVLGLVAPDEGVIKRNGKLRIGYVPQK-LYLdttLPLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 944 VRESLqfsaRMRrpqhlPDSEKMDYVEKIIRVlgmeeYAEALVGEVGCGLNVEQRKKLSIGVELVAKPDLLLfLDEPTSG 1023
Cdd:PRK09544 86 VNRFL----RLR-----PGTKKEDILPALKRV-----QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV-LDEPTQG 150
|
170
....*....|....*.
gi 1351079 1024 LDSQSSWAIIQLLRKL 1039
Cdd:PRK09544 151 VDVNGQVALYDLIDQL 166
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
880-1299 |
1.89e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 880 IP-GTMTALMGESGAGKTTLLNTLAQRNVGIITGDMLVNGrpidasferRTGYVQQQDiHIAELTVRESLQFSARMrRPQ 958
Cdd:PLN03232 640 IPvGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRG---------SVAYVPQVS-WIFNATVRENILFGSDF-ESE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 959 HLPDSEKMDYVEKIIRVLGMEEYAEalVGEVGCGLNVEQRKKLSIGVELVAKPDLLLFlDEPTSGLDSQSSWAIIQLLRK 1038
Cdd:PLN03232 709 RYWRAIDVTALQHDLDLLPGRDLTE--IGERGVNISGGQKQRVSMARAVYSNSDIYIF-DDPLSALDAHVAHQVFDSCMK 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1039 LSKAGQSILCTIHQpsATLFEEFDRLLLLRKG--GQTVYFGDIGKNSATILNYFERNGARKCDSSENPAEYILEAIGAGA 1116
Cdd:PLN03232 786 DELKGKTRVLVTNQ--LHFLPLMDRIILVSEGmiKEEGTFAELSKSGSLFKKLMENAGKMDATQEVNTNDENILKLGPTV 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1117 TAsvkeDWHEKWLNSVefEQTKEKVQDLIndlsKQETKsEVGdkpskyATSYAYQFRY---------VLI---------- 1177
Cdd:PLN03232 864 TI----DVSERNLGST--KQGKRGRSVLV----KQEER-ETG------IISWNVLMRYnkavgglwvVMIllvcylttev 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1178 -RTSTSFWRSLNYIMSKMMLMLVGGLYIGFTFFNVGKSYVGLQNAMFA-------------AFISIILSAPAM---NQIQ 1240
Cdd:PLN03232 927 lRVSSSTWLSIWTDQSTPKSYSPGFYIVVYALLGFGQVAVTFTNSFWLissslhaakrlhdAMLNSILRAPMLffhTNPT 1006
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351079 1241 GRAIA--SRELFEVRESQSNMFHWSLVLITQYLSELPYHLFFSTIfFVSSYFPLRIFFEAS 1299
Cdd:PLN03232 1007 GRVINrfSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTI-SLWAIMPLLILFYAA 1066
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
169-343 |
1.96e-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: 44.49 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 169 HQKMRQIISNVNALAEAGEMILVLGRPGAGCSSFLKVtageIDQFAGGVSGEVAYDG-----IPQEEMMK-RYKADVIYN 242
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRC----INGLERPTSGSVLVDGtdltlLSGKELRKaRRRIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 243 geldvHFPYLTVKQTLDfAIACktpALRVNNVSKKEyIASRRDLYATIFGLRHTYNTKVGNdfvrgVSGGERKRVSIAEA 322
Cdd:cd03258 90 -----HFNLLSSRTVFE-NVAL---PLEIAGVPKAE-IEERVLELLELVGLEDKADAYPAQ-----LSGGQKQRVGIARA 154
|
170 180
....*....|....*....|.
gi 1351079 323 LAAKGSIYCWDNATRGLDAST 343
Cdd:cd03258 155 LANNPKVLLCDEATSALDPET 175
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
297-364 |
2.00e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 45.72 E-value: 2.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351079 297 YNTKVGNdfvRG--VSGGERKRVSIAEALAAKGSIYCWDNATRGLDASTALEYAKAI-RIMTNllkSTAFV 364
Cdd:PRK13657 461 YDTVVGE---RGrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALdELMKG---RTTFI 525
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
881-1094 |
2.84e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.25 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 881 PGTMTALMGESGAGKTTLLNTLA-QRNVGIITGDMLVNGRPI-DASFERRT------GYvqQQDIHIAELTVRESLQFSA 952
Cdd:CHL00131 32 KGEIHAIMGPNGSGKSTLSKVIAgHPAYKILEGDILFKGESIlDLEPEERAhlgiflAF--QYPIEIPGVSNADFLRLAY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 953 RMRRP-QHLPDSEKMDYVEKI---IRVLGMEE-YAEALVGEvgcGLNVEQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQ 1027
Cdd:CHL00131 110 NSKRKfQGLPELDPLEFLEIInekLKLVGMDPsFLSRNVNE---GFSGGEKKRNEILQMALLDSELAI-LDETDSGLDID 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351079 1028 SSWAIIQLLRKLSKAGQSILCTIHqpsatlfeeFDRLL---------LLRKgGQTVYFGDigknsATILNYFERNG 1094
Cdd:CHL00131 186 ALKIIAEGINKLMTSENSIILITH---------YQRLLdyikpdyvhVMQN-GKIIKTGD-----AELAKELEKKG 246
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
176-371 |
3.48e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 45.01 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 176 ISNVNALAEAGEMILVLGRPGAGCSSFlkvtAGEIDQFAGGVSGEVAYDGIPQEEM----MKRYKADVIYNgeldVHFPY 251
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTI----ANLLTRFYDIDEGEILLDGHDLRDYtlasLRNQVALVSQN----VHLFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 252 LTVKQTLDFAiacktpalRVNNVSKKEYIASRRDLYATIF--GLRHTYNTKVGNDFVRgVSGGERKRVSIAEALAAKGSI 329
Cdd:PRK11176 431 DTIANNIAYA--------RTEQYSREQIEEAARMAYAMDFinKMDNGLDTVIGENGVL-LSGGQRQRIAIARALLRDSPI 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1351079 330 YCWDNATRGLDAstalEYAKAIRIMTNLLKS--TAFV------TIYQASE 371
Cdd:PRK11176 502 LILDEATSALDT----ESERAIQAALDELQKnrTSLViahrlsTIEKADE 547
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
173-364 |
4.28e-04 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 44.77 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAG--EIDqfaggvSGEVAYDGIPqeemMKRYKADVIYNgeldvHF- 249
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfyDPT------SGRILIDGVD----IRDLTLESLRR-----QIg 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 250 -----PYL---TVKQTLDFAiacktpalrVNNVSKKEYIASRRDLYAT--IFGLRHTYNTKVGNdfvRGV--SGGERKRV 317
Cdd:COG1132 418 vvpqdTFLfsgTIRENIRYG---------RPDATDEEVEEAAKAAQAHefIEALPDGYDTVVGE---RGVnlSGGQRQRI 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1351079 318 SIAEALAAKGSIYCWDNATRGLDASTALEYAKAIRimtNLLKS-TAFV 364
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALE---RLMKGrTTIV 530
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
173-341 |
4.52e-04 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 44.71 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSflkvTAGEIDQFAGGVSGEVAYDGIPQEEMMKRY---------KADVIYNG 243
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKST----VAALLQNLYQPTGGQVLLDGVPLVQYDHHYlhrqvalvgQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 244 ELDVHFPYltvkqTLDFaiackTPALRVNNVSKKeyiASRRDLyatIFGLRHTYNTKVGNDFVRgVSGGERKRVSIAEAL 323
Cdd:TIGR00958 570 SVRENIAY-----GLTD-----TPDEEIMAAAKA---ANAHDF---IMEFPNGYDTEVGEKGSQ-LSGGQKQRIAIARAL 632
|
170
....*....|....*...
gi 1351079 324 AAKGSIYCWDNATRGLDA 341
Cdd:TIGR00958 633 VRKPRVLILDEATSALDA 650
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
309-421 |
4.67e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.56 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 309 VSGGERKRVSIAEALAAKGSIYCWDNATRGLDASTALEYAKAIRIMTNLLKSTAFVTIYQASENIYETfDKVTVLYSGKQ 388
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLS-DRIHVFEGEPG 150
|
90 100 110
....*....|....*....|....*....|....*.
gi 1351079 389 IYfgliheakpyfakmGYLCPP---RQATAEFLTAL 421
Cdd:cd03222 151 VY--------------GIASQPkgtREGINRFLRGY 172
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
861-1070 |
4.73e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 43.69 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 861 TIPYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQrnVGIITGDMLVNG---RPIDASFERRTGYVQQQDI 937
Cdd:cd03289 9 TAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLR--LLNTEGDIQIDGvswNSVPLQKWRKAFGVIPQKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 938 HIAELTVRESLQfsarmrrpqhlPDSEKMDyvEKIIRV---LGMEEYAEALVGEV-------GCGLNVEQRKKLSIGVEL 1007
Cdd:cd03289 87 FIFSGTFRKNLD-----------PYGKWSD--EEIWKVaeeVGLKSVIEQFPGQLdfvlvdgGCVLSHGHKQLMCLARSV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351079 1008 VAKPDLLLfLDEPTSGLDSQSswaiIQLLRKLSK---AGQSILCTIHQPSATLfeEFDRLLLLRKG 1070
Cdd:cd03289 154 LSKAKILL-LDEPSAHLDPIT----YQVIRKTLKqafADCTVILSEHRIEAML--ECQRFLVIEEN 212
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
862-1025 |
5.27e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 43.16 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 862 IPYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQRnVGIITGDMLVNGRPIDA----SFERRTGYVQQQDI 937
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASL-ISPTSGTLLFEGEDISTlkpeIYRQQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 938 HIAElTVRESLQFSARMRRPQhlPDSEKMdyVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfL 1017
Cdd:PRK10247 92 LFGD-TVYDNLIFPWQIRNQQ--PDPAIF--LDDLERFALPDTILTKNIAELSGG----EKQRISLIRNLQFMPKVLL-L 161
|
....*...
gi 1351079 1018 DEPTSGLD 1025
Cdd:PRK10247 162 DEITSALD 169
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
963-1065 |
6.07e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.96 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 963 SEKMDYVEKIIRVLGMEEYAEALVGEVGCGLNVEQ--------RKKLSIG-VELVA----------KPDLLLFLDEPTSG 1023
Cdd:cd03227 32 SGKSTILDAIGLALGGAQSATRRRSGVKAGCIVAAvsaeliftRLQLSGGeKELSAlalilalaslKPRPLYILDEIDRG 111
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1351079 1024 LDSQSSWAIIQLLRKLSKAGQSILCTIHQPsaTLFEEFDRLL 1065
Cdd:cd03227 112 LDPRDGQALAEAILEHLVKGAQVIVITHLP--ELAELADKLI 151
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
872-907 |
6.72e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 43.77 E-value: 6.72e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQRNV 907
Cdd:PRK01889 185 LDVLAAWLSGGKTVALLGSSGVGKSTLVNALLGEEV 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
175-380 |
8.55e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 43.48 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 175 IISNVNALAEAGEMILVLGRPGAGCSSFLKVTAG--EIdqfaggVSGEVAYDGIPQEEM--MKRYKADVIYNGELdvhFP 250
Cdd:PRK11000 18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGleDI------TSGDLFIGEKRMNDVppAERGVGMVFQSYAL---YP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 251 YLTVKQTLDFAiacktpaLRVNNVSKKEyIASRRDLYATIFGLRHTYNTKVgndfvRGVSGGERKRVSIAEALAAKGSIY 330
Cdd:PRK11000 89 HLSVAENMSFG-------LKLAGAKKEE-INQRVNQVAEVLQLAHLLDRKP-----KALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1351079 331 CWDNATRGLDAstALEYAKAIRImTNL---LKSTAfvtiyqasenIYETFDKV 380
Cdd:PRK11000 156 LLDEPLSNLDA--ALRVQMRIEI-SRLhkrLGRTM----------IYVTHDQV 195
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
166-227 |
8.77e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.89 E-value: 8.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351079 166 AKRHqkmRQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQ--FAGG--VSGEVAYDGIP 227
Cdd:PRK13547 10 ARRH---RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggAPRGarVTGDVTLNGEP 72
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
872-1070 |
9.20e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 42.80 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 872 LDNVSGYCIPGTMTALMGESGAGKTT---LLNTLAQRNVG--IITGDMLVngrpIDASFERR--TGYV-QQQDIHIAELT 943
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLEAESGqiIIDGDLLT----EENVWDIRhkIGMVfQNPDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 944 VRESLQFSArmrRPQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGlnveQRKKLSIGVELVAKPDLLLfLDEPTSG 1023
Cdd:PRK13650 99 VEDDVAFGL---ENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGG----QKQRVAIAGAVAMRPKIII-LDEATSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1351079 1024 LDSQSSWAIIQLLRKLSKAGQSILCTI-HQpsatlFEEF---DRLLLLRKG 1070
Cdd:PRK13650 171 LDPEGRLELIKTIKGIRDDYQMTVISItHD-----LDEValsDRVLVMKNG 216
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
886-1046 |
1.01e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 886 ALMGESGAGKTTLLNTLAQRNVgiitgdmLVNG-------RPIDASFErrtgyvQQQDIHIAE----------------- 941
Cdd:PRK10938 33 AFVGANGSGKSALARALAGELP-------LLSGerqsqfsHITRLSFE------QLQKLVSDEwqrnntdmlspgeddtg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 942 LTVRESLQfsarmrrpqhlpdsekmDYVEKIIRVlgmEEYAEALvgevGCGLNVEQR-KKLSIGvE---------LVAKP 1011
Cdd:PRK10938 100 RTTAEIIQ-----------------DEVKDPARC---EQLAQQF----GITALLDRRfKYLSTG-EtrktllcqaLMSEP 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1351079 1012 DLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSI 1046
Cdd:PRK10938 155 DLLI-LDEPFDGLDVASRQQLAELLASLHQSGITL 188
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
845-1079 |
1.03e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.69 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 845 DDLEAKGVFIWKDVCFTIPYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKT----TLLNTLAQRNVGIITGDMLVNGRP 920
Cdd:PRK10261 5 DELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLLRRRS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 921 IDASFERRTGYVQQQDIHIAEL---------------TVRESLQFSARMRrpQHLPDSEKMDYVEKIIRVLGMEEyAEAL 985
Cdd:PRK10261 85 RQVIELSEQSAAQMRHVRGADMamifqepmtslnpvfTVGEQIAESIRLH--QGASREEAMVEAKRMLDQVRIPE-AQTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 986 VGEVGCGLNVEQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSATLFEEFDRLL 1065
Cdd:PRK10261 162 LSRYPHQLSGGMRQRVMIAMALSCRPAVLI-ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVL 240
|
250
....*....|....
gi 1351079 1066 LLRKgGQTVYFGDI 1079
Cdd:PRK10261 241 VMYQ-GEAVETGSV 253
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
839-1047 |
1.11e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.23 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 839 ANDEVFDDLEAKGVFIWKDVcftIPYEGGKrmlLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQRNvGIITGDMLVNG 918
Cdd:PRK09700 252 AMKENVSNLAHETVFEVRNV---TSRDRKK---VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVD-KRAGGEIRLNG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 919 R------PIDA---------SFERRTGYVQQQDIHiAELTVRESLQFSARMRRPQHLPDSEKMDYVEKIIRVLGMEEYA- 982
Cdd:PRK09700 325 KdisprsPLDAvkkgmayitESRRDNGFFPNFSIA-QNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSv 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1351079 983 EALVGEVGCGlnveQRKKLSIGVELVAKPDLLLFlDEPTSGLDSQSSWAIIQLLRKLSKAGQSIL 1047
Cdd:PRK09700 404 NQNITELSGG----NQQKVLISKWLCCCPEVIIF-DEPTRGIDVGAKAEIYKVMRQLADDGKVIL 463
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
882-1079 |
1.37e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.04 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 882 GTMTALMGESGAGKTTLLNTLAqrnvGIIT---GDMLVNGRPIDAsfERRTGYVQQ-----QDIHIaeltvreslqFSAR 953
Cdd:PRK10522 349 GELLFLIGGNGSGKSTLAMLLT----GLYQpqsGEILLDGKPVTA--EQPEDYRKLfsavfTDFHL----------FDQL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 954 MRRPQHLPDSEKmdyVEKIIRVLGMEEYAEALVGEVgcgLNVE----QRKKLSIGVELVAKPDLLLfLDEptsgldsqss 1029
Cdd:PRK10522 413 LGPEGKPANPAL---VEKWLERLKMAHKLELEDGRI---SNLKlskgQKKRLALLLALAEERDILL-LDE---------- 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351079 1030 WAIIQ-----------LLRKLSKAGQSILCTIHQPSatLFEEFDRLLLLRKGGQTVYFGDI 1079
Cdd:PRK10522 476 WAADQdphfrrefyqvLLPLLQEMGKTIFAISHDDH--YFIHADRLLEMRNGQLSELTGEE 534
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
171-365 |
1.88e-03 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 41.66 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 171 KMRQIISNVNALAEAGEMILVLGRPGAGCSSFLKV-------TAGEIDqfaggvSGEVAYDGI----PQEEMMKRYKADV 239
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinlleqpEAGTIR------VGDITIDTArslsQQKGLIRQLRQHV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 240 IY---NGELdvhFPYLTVkqtLDFAIacKTPALrVNNVSKKEYIASRRDLYAtifglrhtyntKVG-----NDFVRGVSG 311
Cdd:PRK11264 88 GFvfqNFNL---FPHRTV---LENII--EGPVI-VKGEPKEEATARARELLA-----------KVGlagkeTSYPRRLSG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1351079 312 GERKRVSIAEALAAKGSIYCWDNATRGLDASTALEYAKAIRIMTNLLKSTAFVT 365
Cdd:PRK11264 148 GQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT 201
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
290-352 |
1.95e-03 |
|
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: 41.69 E-value: 1.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1351079 290 IFGLRHTYNTKVGNdfvRG--VSGGERKRVSIAEALAAKGSIYCWDNATRGLDASTALEYAKAIR 352
Cdd:cd03248 133 ISELASGYDTEVGE---KGsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALY 194
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
866-1047 |
2.05e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.68 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 866 GGKRMLLDNVSGyciPGT--------------MTALMGesgAGKTTLLNTL---AQRNVGIIT--GDMLVNGRPIDA--- 923
Cdd:PRK10762 254 GEVRLKVDNLSG---PGVndvsftlrkgeilgVSGLMG---AGRTELMKVLygaLPRTSGYVTldGHEVVTRSPQDGlan 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 924 -----SfERRTGyvqqqDIHIAELTVRE--SL----QFSARMRRPQHlpDSEKMDyVEKIIRVLGMEE-YAEALVGEVGC 991
Cdd:PRK10762 328 givyiS-EDRKR-----DGLVLGMSVKEnmSLtalrYFSRAGGSLKH--ADEQQA-VSDFIRLFNIKTpSMEQAIGLLSG 398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1351079 992 GlnveQRKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSIL 1047
Cdd:PRK10762 399 G----NQQKVAIARGLMTRPKVLI-LDEPTRGVDVGAKKEIYQLINQFKAEGLSII 449
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
286-397 |
2.08e-03 |
|
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: 41.37 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 286 LYATIFGLRHTYNTKVGNdfvRGV--SGGERKRVSIAEALAAKGSIYCWDNATRGLDASTALEYAKAI-RIMTNllkSTA 362
Cdd:cd03249 118 IHDFIMSLPDGYDTLVGE---RGSqlSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALdRAMKG---RTT 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1351079 363 FV------TIyQASENIYeTFDKVTV--------LYSGKQIYFGLIHEA 397
Cdd:cd03249 192 IViahrlsTI-RNADLIA-VLQNGQVveqgthdeLMAQKGVYAKLVKAQ 238
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1203-1382 |
2.29e-03 |
|
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: 41.99 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1203 YIGFTFFNVGKSYVGLQNAMFAAFISIILSAPAMNQIqgraiasrelfeVRESQSNMFHWSLV----LITQYLSE-LPYH 1277
Cdd:pfam12698 147 VESTPLFNPQSGYAYYLVGLILMIIILIGAAIIAVSI------------VEEKESRIKERLLVsgvsPLQYWLGKiLGDF 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 1278 LFFSTIFFVSSYFPLRIFFEASRSAVYFLNYcIMFQLYYVGLGLMILYMSPNLPSANVILGLCLSFMLSFCGVTQPVSLM 1357
Cdd:pfam12698 215 LVGLLQLLIILLLLFGIGIPFGNLGLLLLLF-LLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDP 293
|
170 180
....*....|....*....|....*
gi 1351079 1358 PGFWTFMWKASPYTYFVQNLVGIML 1382
Cdd:pfam12698 294 PSFLQWIFSIIPFFSPIDGLLRLIY 318
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
856-1041 |
3.09e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 41.23 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 856 KDVCFTipY----EGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTL---LNTLAQRNvgiiTGDMLVNGrpIDASFE-- 926
Cdd:PRK13633 8 KNVSYK--YesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIPS----EGKVYVDG--LDTSDEen 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 927 -----RRTGYV-QQQDIHIAELTVRESLQFSarmrrPQHL--PDSEKMDYVEKIIRVLGMEEY---AEALvgevgcgLNV 995
Cdd:PRK13633 80 lwdirNKAGMVfQNPDNQIVATIVEEDVAFG-----PENLgiPPEEIRERVDESLKKVGMYEYrrhAPHL-------LSG 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1351079 996 EQRKKLSIGVELVAKPDLLLFlDEPTSGLDSQSSWAIIQLLRKLSK 1041
Cdd:PRK13633 148 GQKQRVAIAGILAMRPECIIF-DEPTAMLDPSGRREVVNTIKELNK 192
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
303-392 |
4.79e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 40.60 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 303 NDFVRGVSGGERKRVSIAEALAAKGSIYCWDNATRGLDASTAleyAKAIRIMTNLLKSTAFVTIYQASENIYETFDKVTV 382
Cdd:PRK14267 144 NDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGT---AKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAF 220
|
90
....*....|
gi 1351079 383 LYSGKQIYFG 392
Cdd:PRK14267 221 LYLGKLIEVG 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
173-326 |
4.83e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 41.20 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQFAGGVS----GEVAYdgIPQEemmkrykadviyngelDVH 248
Cdd:COG0488 11 RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSipkgLRIGY--LPQE----------------PPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351079 249 FPYLTVkqtLDFAIACKTPALRVnnvsKKEY----------------IASRRDLYATIFGlrHTYNTKV----------G 302
Cdd:COG0488 73 DDDLTV---LDTVLDGDAELRAL----EAELeeleaklaepdedlerLAELQEEFEALGG--WEAEARAeeilsglgfpE 143
|
170 180
....*....|....*....|....*..
gi 1351079 303 NDF---VRGVSGGERKRVSIAEALAAK 326
Cdd:COG0488 144 EDLdrpVSELSGGWRRRVALARALLSE 170
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
880-913 |
6.33e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.69 E-value: 6.33e-03
10 20 30
....*....|....*....|....*....|....
gi 1351079 880 IPGTMTALMGESGAGKTTLLNTLAQRNVgIITGD 913
Cdd:cd01854 83 LKGKTSVLVGQSGVGKSTLLNALLPELV-LATGE 115
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
998-1070 |
7.45e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 7.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1351079 998 RKKLSIGVELVAKPDLLLfLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILcTIHQPSATLFEEFDRLLLLRKG 1070
Cdd:PRK10982 397 QQKVIIGRWLLTQPEILM-LDEPTRGIDVGAKFEIYQLIAELAKKDKGII-IISSEMPELLGITDRILVMSNG 467
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
886-939 |
7.46e-03 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 38.98 E-value: 7.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1351079 886 ALMGESGAGKTTLLNTLAQRNVGIITGdmlVNGRPIDASFERRTGYVQQQDIHI 939
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEVSD---VPGTTRDPDVYVKELDKGKVKLVL 51
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
173-217 |
8.32e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 8.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1351079 173 RQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQFAGGV 217
Cdd:PRK15064 332 GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
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