|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
92-1490 |
0e+00 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 2593.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 92 ENFNAKYWVKNLKKLFESDSDYYKPSKLGVAYRNLRAYGIANDSDYQPTVTNALWKFTTEAINKLKKPDDSKYFDILKSM 171
Cdd:TIGR00956 1 EEFNAKAWVKNFRKLIDSDPIYYKPYKLGVAYKNLSAYGVAADSDYQPTFPNALLKILTRGFRKLKKFRDTKTFDILKPM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 172 DAIMRPGELTVVLGRPGAGCSTLLKTIAVNTYGFHIGKESQITYDGLSPHDIERHYRGDVIYSAETDVHFPHLSVGDTLE 251
Cdd:TIGR00956 81 DGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 252 FAARLRTPQNRGEGIDRETYAKHMASVYMATYGLSHTRNTNVGNDFVRGVSGGERKRVSIAEASLSGANIQCWDNATRGL 331
Cdd:TIGR00956 161 FAARCKTPQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 332 DSATALEFIRALKTSATILDTTPLIAIYQCSQDAYELFDNVVVLYEGYQIFFGKASKAKEYFENMGWKCPQRQTTADFLT 411
Cdd:TIGR00956 241 DSATALEFIRALKTSANILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPDRQTTADFLT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 412 SLTNPAEREPLPGYEDKVPRTAQEFETFWKNSPEYAELTKEIDEYFVECERSNTGETYRESHVAKQSNNTRPSSPYTVSF 491
Cdd:TIGR00956 321 SLTSPAERQIKPGYEKKVPRTPQEFETYWRNSPEYAQLMKEIDEYLDRCSESDTKEAYRESHVAKQSKRTRPSSPYTVSF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 492 FMQVRYVIARNFLRMKGDPSIPLISILSQLVMGLILASVFFNLRKSTDTFYFRGGALFFSVLFNAFSSLLEILSLYEARP 571
Cdd:TIGR00956 401 SMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGALFFAILFNAFSSLLEIASMYEARP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 572 IVEKHRKYALYRPSADALASIISELPVKLLMTMSFNIVYYFMVNLRRTAGNFFFYWLMCASCTLVMSHMFRSIGAVTTTI 651
Cdd:TIGR00956 481 IVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFICTLAMSHLFRSIGAVTKTL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 652 ATAMSLSTVFLLAMIIYAGFVLPIPYILGWSRWIRYINPVTYIFESLMVNEFHGREFECGQYIPSGPGFENLPVENKVCT 731
Cdd:TIGR00956 561 SEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHGRRFECSQYVPSGGGYDNLGVTNKVCT 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 732 TVGSTPGSTVVQGTEYIKLAYQFYSSHKWRNFGITVAFAVFFLGVYVALTEFNKGAMQKGEIVLFLKGSLKKHKRK--TA 809
Cdd:TIGR00956 641 VVGAEPGQDYVDGDDYLKLSFQYYNSHKWRNFGIIIGFTVFFFFVYILLTEFNKGAKQKGEILVFRRGSLKRAKKAgeTS 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 810 ASNKGDIEAGPVAGKLDYQDEAEAVNNEKFTEKGStgsvdfpeNREIFFWRDLTYQVKIKKEDRVILDHVDGWVKPGQIT 889
Cdd:TIGR00956 721 ASNKNDIEAGEVLGSTDLTDESDDVNDEKDMEKES--------GEDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLT 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 890 ALMGASGAGKTTLLNCLSERVTTGIITDGERLVNGHALDSSFQRSIGYVQQQDVHLETTTVREALQFSAYLRQSNKISKK 969
Cdd:TIGR00956 793 ALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKS 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 970 EKDDYVDYVIDLLEMTDYADALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLADHG 1049
Cdd:TIGR00956 873 EKMEYVEEVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLADHG 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1050 QAILCTIHQPSALIMAEFDKLLFLQKGGRTAYFGELGENCQTMINYFEKYGADPCPKEANPAEWMLQVVGAAPGSHAKQD 1129
Cdd:TIGR00956 953 QAILCTIHQPSAILFEEFDRLLLLQKGGQTVYFGDLGENSHTIINYFEKHGAPKCPEDANPAEWMLEVIGAAPGAHANQD 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1130 YFEVWRNSSEYQAVREEINRMEAELSKLPRDNDPEALLKYAAPLWKQYLLVSWRTIVQDWRSPGYIYSKLILVISSSLFI 1209
Cdd:TIGR00956 1033 YHEVWRNSSEYQAVKNELDRLEAELSKAEDDNDPDALSKYAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFI 1112
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1210 GFSFFKSKNNLQGLQSQMLAVFMFFVPFTTFIDQMLPYFVKHRAVYEVREAPSRTFSWFAFIAGQITSEIPFQIVVGTIS 1289
Cdd:TIGR00956 1113 GFTFFKVGTSLQGLQNQMFAVFMATVLFNPLIQQYLPPFVAQRDLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIF 1192
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1290 YFCWYYPVGLYANAEPTDSVNSRGVLMWMLLTAFYVYTSTMGQLAISLNELIDNAANLATTLFTLCLMFCGVLAGPNVIP 1369
Cdd:TIGR00956 1193 FFIWYYPVGFYWNASKTGQVHERGVLFWLLSTMFFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMP 1272
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1370 GFWIFMYRCNPFTYLIQAILSTGLANAKVTCAPRELVTLKPPMGETCSSFIGPYTEAAGGYFST-NSDGTCSVCRIDSTN 1448
Cdd:TIGR00956 1273 GFWIFMYRCSPFTYLVQALLSTGLADVPVTCKVKELLTFNPPSGQTCGEYMKPYLENAGGYLLNpNATDSCSFCQYSYTN 1352
|
1370 1380 1390 1400
....*....|....*....|....*....|....*....|..
gi 353526216 1449 QFLESINALFSQRWRNFGIFVAFIGINIILTIFFYWLARVPK 1490
Cdd:TIGR00956 1353 DFLEPISSKYSGRWRNFGIFIAFIFFNIIATVFFYWLARVPK 1394
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
167-1385 |
1.38e-133 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 450.07 E-value: 1.38e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntygfhiGK-------ESQITYDGlspHDIERHY-RGDVIYSAETD 238
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALA--------GKldpslkvSGEITYNG---YRLNEFVpRKTSAYISQND 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 239 VHFPHLSVGDTLEFAAR---------LRTPQNRGE---GIDRE---------TYAKHMASVYMATY-----GLSHTRNTN 292
Cdd:PLN03140 249 VHVGVMTVKETLDFSARcqgvgtrydLLSELARREkdaGIFPEaevdlfmkaTAMEGVKSSLITDYtlkilGLDICKDTI 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 293 VGNDFVRGVSGGERKRVSIAEASLSGANIQCWDNATRGLDSATALEFIRALKTSATILDTTPLIAIYQCSQDAYELFDNV 372
Cdd:PLN03140 329 VGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFDLFDDI 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 373 VVLYEGYQIFFGKASKAKEYFENMGWKCPQRQTTADFLTSLTNPAEREPLPGYEDK------VPRTAQEFETFWKNSPEY 446
Cdd:PLN03140 409 ILLSEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKKDQEQYWADRNKpyryisVSEFAERFKSFHVGMQLE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 447 AELTKEIDEYfvecersntgetyrESHVAKQSnntrpSSPYTVSFFMQVRYVIARNFLRMKGDPSIPLISILSQLVMGLI 526
Cdd:PLN03140 489 NELSVPFDKS--------------QSHKAALV-----FSKYSVPKMELLKACWDKEWLLMKRNAFVYVFKTVQIIIVAAI 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 527 LASVFFNLRKST-----DTFYFrgGALFFSVLFNAFSSLLEILSLYEARPIVEKHRKYALYRPSADALASIISELPVKLL 601
Cdd:PLN03140 550 ASTVFLRTEMHTrneedGALYI--GALLFSMIINMFNGFAELALMIQRLPVFYKQRDLLFHPPWTFTLPTFLLGIPISII 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 602 MTMSFNIVYYFMVNLRRTAGNFFFYWLMCASCTLVMSHMFRSIGAVTTTIATAMSLSTVFLLAMIIYAGFVLPIPYILGW 681
Cdd:PLN03140 628 ESVVWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNW 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 682 SRWIRYINPVTYIFESLMVNEFHGREFEcgqyipsgpgfenlpveNKVCTTVGSTPGSTVVQgteyiklAYQFYSSHKWR 761
Cdd:PLN03140 708 WEWAYWVSPLSYGFNALAVNEMFAPRWM-----------------NKMASDNSTRLGTAVLN-------IFDVFTDKNWY 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 762 NFGIT--VAFAVFFLGVY-VALTEFN----KGAMQKGEIVLFLKGSLKKHKRKTAASNKGDieAGPVAGKLDYQDEAEAV 834
Cdd:PLN03140 764 WIGVGalLGFTILFNVLFtLALTYLNplgkKQAIISEETAEEMEGEEDSIPRSLSSADGNN--TREVAIQRMSNPEGLSK 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 835 NNEKFTEKGSTGSVD----FPENREIFFWRDLTYQVKIKKE--------DRV-ILDHVDGWVKPGQITALMGASGAGKTT 901
Cdd:PLN03140 842 NRDSSLEAANGVAPKrgmvLPFTPLAMSFDDVNYFVDMPAEmkeqgvteDRLqLLREVTGAFRPGVLTALMGVSGAGKTT 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 902 LLNCLSERVTTGIItDGERLVNGHA-LDSSFQRSIGYVQQQDVHLETTTVREALQFSAYLRQSNKISKKEKDDYVDYVID 980
Cdd:PLN03140 922 LMDVLAGRKTGGYI-EGDIRISGFPkKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVME 1000
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 981 LLEMTDYADALVGVAG-EGLNVEQRKRLTIGVELVAKPKLLlFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQP 1059
Cdd:PLN03140 1001 LVELDNLKDAIVGLPGvTGLSTEQRKRLTIAVELVANPSII-FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQP 1079
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1060 SALIMAEFDKLLFLQKGGRTAYFGELGENCQTMINYFEKYGADPCPKEA-NPAEWMLQVVGAAPGSHAKQDYFEVWRNSS 1138
Cdd:PLN03140 1080 SIDIFEAFDELLLMKRGGQVIYSGPLGRNSHKIIEYFEAIPGVPKIKEKyNPATWMLEVSSLAAEVKLGIDFAEHYKSSS 1159
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1139 EYQAVREEINrmeaELSKLPRD-NDPEALLKYAAPLWKQYLLVSWRTIVQDWRSPGYIYSKLILVISSSLFIGFSFFK-- 1215
Cdd:PLN03140 1160 LYQRNKALVK----ELSTPPPGaSDLYFATQYSQSTWGQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFWKvg 1235
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1216 -SKNNLQGLQSQMLAVF--MFFVPFTTfIDQMLPYFVKHRAVYeVREAPSRTFSWFAFIAGQITSEIPFQIVVGTisyfc 1292
Cdd:PLN03140 1236 tKRSNANDLTMVIGAMYaaVLFVGINN-CSTVQPMVAVERTVF-YRERAAGMYSALPYAIAQVVCEIPYVLIQTT----- 1308
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1293 wYYPVGLYANA--EPTDSvnsrgVLMWMLLTAF--YVYTSTMGQLAISLNELIDNAANLATTLFTLCLMFCGVLAGPNVI 1368
Cdd:PLN03140 1309 -YYTLIVYAMVafEWTAA-----KFFWFYFISFfsFLYFTYYGMMTVSLTPNQQVAAIFAAAFYGLFNLFSGFFIPRPKI 1382
|
1290
....*....|....*..
gi 353526216 1369 PGFWIFMYRCNPFTYLI 1385
Cdd:PLN03140 1383 PKWWVWYYWICPVAWTV 1399
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
856-1083 |
3.82e-101 |
|
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: 321.11 E-value: 3.82e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 856 IFFWRDLTYQVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTGIITdGERLVNGHALDSSFQRSI 935
Cdd:cd03232 3 VLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVIT-GEILINGRPLDKNFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 936 GYVQQQDVHLETTTVREALQFSAYLRqsnkiskkekddyvdyvidllemtdyadalvgvageGLNVEQRKRLTIGVELVA 1015
Cdd:cd03232 82 GYVEQQDVHSPNLTVREALRFSALLR------------------------------------GLSVEQRKRLTIGVELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 353526216 1016 KPkLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSALIMAEFDKLLFLQKGGRTAYFG 1083
Cdd:cd03232 126 KP-SILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRGGKTVYFG 192
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
875-1303 |
1.64e-88 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 301.58 E-value: 1.64e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 875 ILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTGIITDGERLVNGHALDSSFQRSI-GYVQQQDVHLETTTVREA 953
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPIDAKEMRAIsAYVQQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 954 LQFSAYLRQSNKISKKEKDDYVDYVIDLLEMTDYADALVGVAG--EGLNVEQRKRLTIGVELVAKPKLLlFLDEPTSGLD 1031
Cdd:TIGR00955 120 LMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGrvKGLSGGERKRLAFASELLTDPPLL-FCDEPTSGLD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1032 SQTAWSICKLMRKLADHGQAILCTIHQPSALIMAEFDKLLFLQKgGRTAYFGELGENCQtminYFEKYGAdPCPKEANPA 1111
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAE-GRVAYLGSPDQAVP----FFSDLGH-PCPENYNPA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1112 EWMLQVVGAAPGS--------HAKQDYFEVwrnSSEYQAVREEINRMEAELSKLPRDNDPEALLKYAAPLWKQYLLVSWR 1183
Cdd:TIGR00955 273 DFYVQVLAVIPGSenesreriEKICDSFAV---SDIGRDMLVNTNLWSGKAGGLVKDSENMEGIGYNASWWTQFYALLKR 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1184 TIVQDWRSPGYIYSKLILVISSSLFIGFSFFKSKNNLQGLQSQMLAVFmFFVPFTTFIDQM--LPYFVKHRAVYeVREAP 1261
Cdd:TIGR00955 350 SWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALF-LFLTNMTFQNVFpvINVFTAELPVF-LRETR 427
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 353526216 1262 SRTFSWFAFIAGQITSEIPFQIVVGTISYFCWYYPVGLYANA 1303
Cdd:TIGR00955 428 SGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGA 469
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
153-384 |
4.86e-78 |
|
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: 256.42 E-value: 4.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 153 INKLKKPDDSKyFDILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAVNTYGFhIGKESQITYDGLSPHDIERHYRGDVI 232
Cdd:cd03233 9 ISFTTGKGRSK-IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGN-VSVEGDIHYNGIPYKEFAEKYPGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 233 YSAETDVHFPHLSVGDTLEFAARLRtpqnrgegidretyakhmasvymatyglshtrntnvGNDFVRGVSGGERKRVSIA 312
Cdd:cd03233 87 YVSEEDVHFPTLTVRETLDFALRCK------------------------------------GNEFVRGISGGERKRVSIA 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 353526216 313 EASLSGANIQCWDNATRGLDSATALEFIRALKTSATILDTTPLIAIYQCSQDAYELFDNVVVLYEGYQIFFG 384
Cdd:cd03233 131 EALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
857-1083 |
1.37e-66 |
|
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: 223.20 E-value: 1.37e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 857 FFWRDLTYQVKIK--KEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTGIITdGERLVNGHALD-SSFQR 933
Cdd:cd03213 4 LSFRNLTVTVKSSpsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVS-GEVLINGRPLDkRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 934 SIGYVQQQDVHLETTTVREALQFSAYLRqsnkiskkekddyvdyvidllemtdyadalvgvageGLNVEQRKRLTIGVEL 1013
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKLR------------------------------------GLSGGERKRVSIALEL 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1014 VAKPkLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSALIMAEFDKLLFLQKgGRTAYFG 1083
Cdd:cd03213 127 VSNP-SLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQ-GRVIYFG 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
167-780 |
3.74e-65 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 233.79 E-value: 3.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAV-NTYGFHIGkeSQITYDGlspHDIER-HYRGDVIYSAETDVHFPHL 244
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrSPKGVKGS--GSVLLNG---MPIDAkEMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 245 SVGDTLEFAARLRTPqnrgegiDRETYAKHMASV--YMATYGLSHTRNTNVGN-DFVRGVSGGERKRVSIAEASLSGANI 321
Cdd:TIGR00955 115 TVREHLMFQAHLRMP-------RRVTKKEKRERVdeVLQALGLRKCANTRIGVpGRVKGLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 322 QCWDNATRGLDSATALEFIRALKTSATiLDTTPLIAIYQCSQDAYELFDNVVVLYEGYQIFFGKASKAKEYFENMGWKCP 401
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQ-KGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 402 QRQTTADFLTSLTnpAErepLPGYEDKVPRTAQefetfwknspeyaeltKEIDEYFV-ECERSNTGETYRESHVAK---Q 477
Cdd:TIGR00955 267 ENYNPADFYVQVL--AV---IPGSENESRERIE----------------KICDSFAVsDIGRDMLVNTNLWSGKAGglvK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 478 SNNTRPSSPYTVSFFMQVRYVIARNFLRMKGDPSIPLISILSQLVMGLILASVFFNLRKSTDTFYFRGGALFFSVLFNAF 557
Cdd:TIGR00955 326 DSENMEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFLTNMTF 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 558 SSLLEILSLYEA-RPIVEKHRKYALYRPSADALASIISELPVKLLMTMSFNIVYYFMVNLRRTAGNFFFYWLMCASCTLV 636
Cdd:TIGR00955 406 QNVFPVINVFTAeLPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANV 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 637 MSHMFRSIGAVTTTIATAMSLSTVFLLAMIIYAGFVLPIPYILGWSRWIRYINPVTYIFESLMVNEFHG-REFECGQyip 715
Cdd:TIGR00955 486 ATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDvDNIECTS--- 562
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 353526216 716 sgpgfenlpvenkvCTTVGSTPGSTVVqgteyIKLAYQFYSSHKWRNFGITVAFAVFF-LGVYVAL 780
Cdd:TIGR00955 563 --------------ANTTGPCPSSGEV-----ILETLSFRNADLYLDLIGLVILIFFFrLLAYFAL 609
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
498-701 |
3.13e-53 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 185.55 E-value: 3.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 498 VIARNFLRMKGDPSIPLISILSQLVMGLILASVFFNLrKSTDTFYFRGGALFFSVLFNAFSSLLEILSLYEA-RPIVEKH 576
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNL-GNQQGGLNRPGLLFFSILFNAFSALSGISPVFEKeRGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 577 RKYALYRPSADALASIISELPVKLLMTMSFNIVYYFMVNLRRTAGNFFFYWLMCASCTLVMSHMFRSIGAVTTTIATAMS 656
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 353526216 657 LSTVFLLAMIIYAGFVLPIPYILGWSRWIRYINPVTYIFESLMVN 701
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
859-1083 |
6.50e-51 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 179.39 E-value: 6.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 859 WRDLTYQVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTGIITDGERLVNGHALD-SSFQRSIGY 937
Cdd:cd03234 6 WWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKpDQFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 938 VQQQDVHLETTTVREALQFSAYLRQSNKISKKEKDDYV-DYVIDLLEMTDYADALVgvagEGLNVEQRKRLTIGVELVAK 1016
Cdd:cd03234 86 VRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVeDVLLRDLALTRIGGNLV----KGISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 353526216 1017 PKLLlFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSALIMAEFDKLLFLQKgGRTAYFG 1083
Cdd:cd03234 162 PKVL-ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSS-GEIVYSG 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
167-705 |
7.05e-48 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 183.16 E-value: 7.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAVNTYGFHIGKESQITYDGLSPHDIERhyrgdVIYSAETDVHFPHLSV 246
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKR-----TGFVTQDDILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 247 GDTLEFAARLRTPQNrgegIDRETYAKHMASVyMATYGLSHTRNTNVGNDFVRGVSGGERKRVSIAEASLSGANIQCWDN 326
Cdd:PLN03211 158 RETLVFCSLLRLPKS----LTKQEKILVAESV-ISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 327 ATRGLDSATALEFIRALKTSATiLDTTPLIAIYQCSQDAYELFDNVVVLYEGYQIFFGKASKAKEYFENMGWKCPQRQTT 406
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 407 ADFLTSLTNP-------AEREPlpgyedkvPRTAQEFETFWKN--SPEYAeltkeideyfvECERSNTGETYRESHVAKQ 477
Cdd:PLN03211 312 ADFLLDLANGvcqtdgvSEREK--------PNVKQSLVASYNTllAPKVK-----------AAIEMSHFPQANARFVGSA 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 478 SNNTRPSSPYT--VSFFMQVRYVIARNfLRMKGDPSIPLISIlSQLVMGLILASVFF---NLRKSTDtfyfRGGALFF-S 551
Cdd:PLN03211 373 STKEHRSSDRIsiSTWFNQFSILLQRS-LKERKHESFNTLRV-FQVIAAALLAGLMWwhsDFRDVQD----RLGLLFFiS 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 552 VLFNAFSSLLEILSLYEARPIVEKHRKYALYRPSADALASIISELPVKLLMTMSFNIVYYFMVNLRRTAGNFFFYWLMCA 631
Cdd:PLN03211 447 IFWGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLL 526
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 353526216 632 SCTLVMSHMFRSIGAVTTTIATAMSLSTVFLLAMIIYAGF-VLPIPYILGwsrWIRYINPVTYIFEsLMVNEFHG 705
Cdd:PLN03211 527 GYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFyVHKLPSCMA---WIKYISTTFYSYR-LLINVQYG 597
|
|
| PDR_CDR |
pfam06422 |
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters ... |
714-805 |
2.40e-45 |
|
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: 158.39 E-value: 2.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 714 IPSGPGFENLPVENKVCTTVGSTPGSTVVQGTEYIKLAYQFYSSHKWRNFGITVAFAVFFLGVYVALTEFNKGAMQKGEI 793
Cdd:pfam06422 1 VPSGPGYENVSGANQVCAVVGAVPGQTFVSGDDYLAASYGYSYSHLWRNFGILIAFWIFFLALYLIATEYNSAAKSKGEV 80
|
90
....*....|..
gi 353526216 794 VLFLKGSLKKHK 805
Cdd:pfam06422 81 LVFKRGKAPKLK 92
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
1180-1391 |
3.55e-42 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 153.58 E-value: 3.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1180 VSWRTIVQDWRSPGYIYSKLILVISSSLFIGFSFFKSKNNLQGLQSQMLAVFMFFVPFTTFIDQMLPYFVKHRAVYEvRE 1259
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLY-RE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1260 APSRTFSWFAFIAGQITSEIPFQIVVGTISYFCWYYPVGLYANAeptdsvnSRGVLMWMLLTAFYVYTSTMGQLAISLNE 1339
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSA-------GRFFLFLLVLLLTALAASSLGLFISALAP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 353526216 1340 LIDNAANLATTLFTLCLMFCGVLAGPNVIPGFWIFMYRCNPFTYLIQAILST 1391
Cdd:pfam01061 153 SFEDASQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
872-1076 |
1.11e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.82 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLservtTGII--TDGERLVNGHALDSSFQ---RSIGYVQQQDVHLE 946
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRML-----LGLLrpTSGEVRVLGEDVARDPAevrRRIGYVPQEPALYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 947 TTTVREALQFSAYLRqsnKISKKEKDDYVDYVIDLLEMTDYADALVGvageGLNVEQRKRLTIGVELVAKPKLLlFLDEP 1026
Cdd:COG1131 87 DLTVRENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVG----TLSGGMKQRLGLALALLHDPELL-ILDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 353526216 1027 TSGLDSQTAWSICKLMRKLADHGQAILCTIHqpsalIMAE----FDKLLFLQKG 1076
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTH-----YLEEaerlCDRVAIIDKG 207
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
871-1117 |
3.36e-37 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 150.42 E-value: 3.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 871 EDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTGIITdGERLVNGHALDSSFQRSIGYVQQQDVHLETTTV 950
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFT-GTILANNRKPTKQILKRTGFVTQDDILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 951 REALQFSAYLRQSNKISKKEKDDYVDYVIDLLEMTDYADALVGVAG-EGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 1029
Cdd:PLN03211 158 RETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFiRGISGGERKRVSIAHEMLINPSLLI-LDEPTSG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1030 LDSQTAWSICKLMRKLADHGQAILCTIHQPSALIMAEFDKLLFLQKgGRTAYFGELGEncqtMINYFEKYGADPcPKEAN 1109
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSE-GRCLFFGKGSD----AMAYFESVGFSP-SFPMN 310
|
....*...
gi 353526216 1110 PAEWMLQV 1117
Cdd:PLN03211 311 PADFLLDL 318
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
856-1083 |
3.84e-37 |
|
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: 138.93 E-value: 3.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 856 IFFWRDLTYQVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTGIITDGERLVNGHALD---SSFQ 932
Cdd:cd03233 3 TLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYKefaEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 933 RSIGYVQQQDVHLETTTVREALQFSAYLRqsnkiskkeKDDYVdyvidllemtdyadalvgvagEGLNVEQRKRLTIGVE 1012
Cdd:cd03233 83 GEIIYVSEEDVHFPTLTVRETLDFALRCK---------GNEFV---------------------RGISGGERKRVSIAEA 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 353526216 1013 LVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLAD-HGQAILCTIHQPSALIMAEFDKLLFLqKGGRTAYFG 1083
Cdd:cd03233 133 LVSRASVLCW-DNSTRGLDSSTALEILKCIRTMADvLKTTTFVSLYQASDEIYDLFDKVLVL-YEGRQIYYG 202
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
155-384 |
4.24e-37 |
|
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: 138.84 E-value: 4.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 155 KLKKPDDSKYFDILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAVNTYGFHIgkESQITYDGLSPHDIErhYRGDVIYS 234
Cdd:cd03213 12 TVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGV--SGEVLINGRPLDKRS--FRKIIGYV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 235 AETDVHFPHLSVGDTLEFAARLRtpqnrgegidretyakhmasvymatyglshtrntnvgndfvrGVSGGERKRVSIAEA 314
Cdd:cd03213 88 PQDDILHPTLTVRETLMFAAKLR------------------------------------------GLSGGERKRVSIALE 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 315 SLSGANIQCWDNATRGLDSATALEFIRALKTSATiLDTTPLIAIYQCSQDAYELFDNVVVLYEGYQIFFG 384
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
872-1090 |
6.68e-35 |
|
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: 134.21 E-value: 6.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIIT-DGErlvNGHALDSSFQRSIGYVQQQDVHLETT 948
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAglLKPDSGSILiDGE---DVRKEPREARRQIGVLPDERGLYDRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 949 TVREALQFSAYLRQSNKISKKEKddyVDYVIDLLEMTDYADALVGvageGLNVEQRKRLTIGVELVAKPKLLLfLDEPTS 1028
Cdd:COG4555 90 TVRENIRYFAELYGLFDEELKKR---IEELIELLGLEEFLDRRVG----ELSTGMKKKVALARALVHDPKVLL-LDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 353526216 1029 GLDSQTAWSICKLMRKLADHGQAILCTIHQPSaLIMAEFDKLLFLQKgGRTAYFGELGENCQ 1090
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGKTVLFSSHIMQ-EVEALCDRVVILHK-GKVVAQGSLDELRE 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
860-1076 |
4.18e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 125.54 E-value: 4.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTG-IITDGERLvngHALDSSfQRS-- 934
Cdd:COG1136 8 RNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGglDRPTSGeVLIDGQDI---SSLSER-ELArl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 935 ----IGYVQQQdvH--LETTTVREALQFSAYLRqsnKISKKEKDDYVDYVIDLLEMTDYADALVGvageglnvE----QR 1004
Cdd:COG1136 84 rrrhIGFVFQF--FnlLPELTALENVALPLLLA---GVSRKERRERARELLERVGLGDRLDHRPS--------QlsggQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353526216 1005 KRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIHQPSalIMAEFDKLLFLQKG 1076
Cdd:COG1136 151 QRVAIARALVNRPKLIL-ADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPE--LAARADRVIRLRDG 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
860-1076 |
4.50e-31 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 121.81 E-value: 4.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKikKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLservtTGII--TDGERLVNGHALDSS----FQR 933
Cdd:cd03225 3 KNLSFSYP--DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLL-----NGLLgpTSGEVLVDGKDLTKLslkeLRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 934 SIGYV-QQQDVHLETTTVREALQFSayLRQsNKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVE 1012
Cdd:cd03225 76 KVGLVfQNPDDQFFGPTVEEEVAFG--LEN-LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGG----QKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 353526216 1013 LVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSaLIMAEFDKLLFLQKG 1076
Cdd:cd03225 149 LAMDPDILL-LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDG 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
871-1076 |
4.82e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.89 E-value: 4.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 871 EDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLservtTGII--TDGERLVNGHALDSSFQRsIGYV-QQQDVHLET 947
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAI-----LGLLppTSGTVRLFGKPPRRARRR-IGYVpQRAEVDWDF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 948 -TTVREALQFSAYLRQS--NKISKKEKDDyVDYVIDLLEMTDYADALVGvageglnvE----QRKRLTIGVELVAKPKLL 1020
Cdd:COG1121 91 pITVRDVVLMGRYGRRGlfRRPSRADREA-VDEALERVGLEDLADRPIG--------ElsggQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 353526216 1021 LfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAlIMAEFDKLLFLQKG 1076
Cdd:COG1121 162 L-LDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRG 215
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
869-1388 |
6.98e-31 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 133.05 E-value: 6.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 869 KKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTGIITDGERLVNGHALDSSF-QRSIGYVQQQDVHLET 947
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKVSGEITYNGYRLNEFVpRKTSAYISQNDVHVGV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 948 TTVREALQFSAYLRQS-------NKISKKEKDD------------------------YVDYVIDLLEMTDYADALVG-VA 995
Cdd:PLN03140 254 MTVKETLDFSARCQGVgtrydllSELARREKDAgifpeaevdlfmkatamegvksslITDYTLKILGLDICKDTIVGdEM 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 996 GEGLNVEQRKRLTIGvELVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQA-ILCTIHQPSALIMAEFDKLLFLQ 1074
Cdd:PLN03140 334 IRGISGGQKKRVTTG-EMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEAtVLMSLLQPAPETFDLFDDIILLS 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1075 KgGRTAYFGELgencQTMINYFEKYGADpCPKEANPAEWMLQVVgaapgshAKQDYFEVWRNSSE---YQAVREEINR-- 1149
Cdd:PLN03140 413 E-GQIVYQGPR----DHILEFFESCGFK-CPERKGTADFLQEVT-------SKKDQEQYWADRNKpyrYISVSEFAERfk 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1150 -------MEAELSkLPRDND---PEALL--KYAAPLwKQYLLVSWRtivQDW---RSPGYIY----SKLILV--ISSSLF 1208
Cdd:PLN03140 480 sfhvgmqLENELS-VPFDKSqshKAALVfsKYSVPK-MELLKACWD---KEWllmKRNAFVYvfktVQIIIVaaIASTVF 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1209 IGfSFFKSKNNLQG-------LQSQMLAVFMFFVPFTTFIdQMLPYFVKHRavyEVREAPSRTFSWFAFIAGqitseIPF 1281
Cdd:PLN03140 555 LR-TEMHTRNEEDGalyigalLFSMIINMFNGFAELALMI-QRLPVFYKQR---DLLFHPPWTFTLPTFLLG-----IPI 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1282 QIVVGTISYFCWYYPVGLYANAeptdsvnSRgvLMWMLLTAFYVYtstmgQLAISLNELIDNA------ANLATTLfTLC 1355
Cdd:PLN03140 625 SIIESVVWVVITYYSIGFAPEA-------SR--FFKQLLLVFLIQ-----QMAAGIFRLIASVcrtmiiANTGGAL-VLL 689
|
570 580 590
....*....|....*....|....*....|....*
gi 353526216 1356 LMFC--GVLAGPNVIPGFWIFMYRCNPFTYLIQAI 1388
Cdd:PLN03140 690 LVFLlgGFILPKGEIPNWWEWAYWVSPLSYGFNAL 724
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
869-1057 |
1.41e-30 |
|
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: 120.69 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 869 KKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLservtTGII--TDGERLVNGHALDSSF---QRSIGYVQQQDV 943
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKML-----TGELrpTSGTAYINGYSIRTDRkaaRQSLGYCPQFDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 944 HLETTTVREALQFSAYLRqsnKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELVAKPKlLLFL 1023
Cdd:cd03263 86 LFDELTVREHLRFYARLK---GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGG----MKRKLSLAIALIGGPS-VLLL 157
|
170 180 190
....*....|....*....|....*....|....
gi 353526216 1024 DEPTSGLDSQTAWSICKLMRKLAdHGQAILCTIH 1057
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVR-KGRSIILTTH 190
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
167-778 |
2.14e-30 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 131.51 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAVNTYGFHIgkESQITYDGLsPHDIERHYR--GdviYSAETDVHFPHL 244
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYI--EGDIRISGF-PKKQETFARisG---YCEQNDIHSPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 245 SVGDTLEFAARLRTPQNrgegIDRETYAKHMASVyMATYGLSHTRNTNVGNDFVRGVSGGERKRVSIAEASLSGANIQCW 324
Cdd:PLN03140 969 TVRESLIYSAFLRLPKE----VSKEEKMMFVDEV-MELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 325 DNATRGLDSATALEFIRALKTSatiLDT--TPLIAIYQCSQDAYELFDNVVVLYEGYQIFF----GKAS-KAKEYFENmg 397
Cdd:PLN03140 1044 DEPTSGLDARAAAIVMRTVRNT---VDTgrTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYsgplGRNShKIIEYFEA-- 1118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 398 wkcpqrqttadfltsltnpaerepLPGyedkVPRTAQEFE-TFW--KNSPEYAELTKEIDeyFVECERSNTgeTYRESHV 474
Cdd:PLN03140 1119 ------------------------IPG----VPKIKEKYNpATWmlEVSSLAAEVKLGID--FAEHYKSSS--LYQRNKA 1166
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 475 AKQSNNTRP--------SSPYTVSFFMQVRYVIARNFLRMKGDPSIPLISILSQLVMGLILASVFFNL---RKSTDTFYF 543
Cdd:PLN03140 1167 LVKELSTPPpgasdlyfATQYSQSTWGQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFWKVgtkRSNANDLTM 1246
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 544 RGGALFFSVLF---NAFSSLLEILSLyeARPIVEKHRKYALYRPSADALASIISELPVKLLMTMSFNIVYYFMVNLRRTA 620
Cdd:PLN03140 1247 VIGAMYAAVLFvgiNNCSTVQPMVAV--ERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTA 1324
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 621 GNFFFYWLMCASCTLVMSHMFRSIGAVTTTIATAMSLSTVFLLAMIIYAGFVLPIPYILGWSRWIRYINPVTYIFESLMV 700
Cdd:PLN03140 1325 AKFFWFYFISFFSFLYFTYYGMMTVSLTPNQQVAAIFAAAFYGLFNLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIV 1404
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 353526216 701 NEFHGrefecgqyipsgpgfenlpVENKVcTTVGSTPGSTVVQgteYIKLAYQFYSSHKWRNFGITVAFAVFFLGVYV 778
Cdd:PLN03140 1405 SQYGD-------------------VEDTI-KVPGGAPDPTIKW---YIQDHYGYDPDFMGPVAAVLVGFTVFFAFIFA 1459
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
154-384 |
1.96e-29 |
|
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: 117.76 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 154 NKLKKPDDSKYFDILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIA------VNTYGfhigkesQITYDG--LSPHDIER 225
Cdd:cd03234 9 VGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrveggGTTSG-------QILFNGqpRKPDQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 226 HyrgdVIYSAETDVHFPHLSVGDTLEFAARLRTPQNRGEGIDRETyakhmasvyMATYGLSHTRNTNVGNDFVRGVSGGE 305
Cdd:cd03234 82 C----VAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKR---------VEDVLLRDLALTRIGGNLVKGISGGE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 353526216 306 RKRVSIAEASLSGANIQCWDNATRGLDSATALEFIRALKTSATiLDTTPLIAIYQCSQDAYELFDNVVVLYEGYQIFFG 384
Cdd:cd03234 149 RRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLAR-RNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
876-1028 |
2.48e-28 |
|
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: 111.97 E-value: 2.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIItdgerLVNGHALDS----SFQRSIGYVQQQDVHLETTT 949
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAglLSPTEGTI-----LLDGQDLTDderkSLRKEIGYVFQDPQLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 353526216 950 VREALQFSAYLRqsnKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTS 1028
Cdd:pfam00005 76 VRENLRLGLLLK---GLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLL-LDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
860-1076 |
2.68e-28 |
|
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: 114.12 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIIT-DGERLVN--GHALDSSFQRS 934
Cdd:cd03255 4 KNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGglDRPTSGEVRvDGTDISKlsEKELAAFRRRH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 935 IGYVQQQDVHLETTTVREALQFSAYLRqsnKISKKEKDDYVDYVIDLLEMTDYADALVGvageGLNVEQRKRLTIGVELV 1014
Cdd:cd03255 84 IGFVFQSFNLLPDLTALENVELPLLLA---GVPKKERRERAEELLERVGLGDRLNHYPS----ELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353526216 1015 AKPKLLLfLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIHQPSalIMAEFDKLLFLQKG 1076
Cdd:cd03255 157 NDPKIIL-ADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPE--LAEYADRIIELRDG 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
168-328 |
2.79e-28 |
|
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: 111.97 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 168 LKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIER-HYRGDVIYSAETDVHFPHLSV 246
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIA----GLLSPTEGTILLDGQDLTDDERkSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 247 GDTLEFAARLRTPQNRGEGIDretyakhmASVYMATYGLSHTRNTNVGNdFVRGVSGGERKRVSIAEASLSGANIQCWDN 326
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDAR--------AEEALEKLGLGDLADRPVGE-RPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
..
gi 353526216 327 AT 328
Cdd:pfam00005 148 PT 149
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
860-1076 |
9.97e-28 |
|
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: 112.81 E-value: 9.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKikkEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLServttGII--TDGERLVNGHALD----SSFQR 933
Cdd:COG1122 4 ENLSFSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN-----GLLkpTSGEVLVDGKDITkknlRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 934 SIGYV-QQQDVHLETTTVREALQFSayLRQSnKISKKEKDDYVDYVIDLLEMTDYAD----ALVGvaGeglnveQRKRLT 1008
Cdd:COG1122 76 KVGLVfQNPDDQLFAPTVEEDVAFG--PENL-GLPREEIRERVEEALELVGLEHLADrpphELSG--G------QKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 353526216 1009 I-GVeLVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSaLIMAEFDKLLFLQKG 1076
Cdd:COG1122 145 IaGV-LAMEPEVLV-LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLD-LVAELADRVIVLDDG 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
872-1062 |
5.30e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 110.26 E-value: 5.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLServttGII--TDGERLVNGHALDS---SFQRSIGYVQQQDVHLE 946
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILA-----GLLppSAGEVLWNGEPIRDareDYRRRLAYLGHADGLKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 947 TTTVREALQFSAYLRQsnkisKKEKDDYVDYVIDLLEMTDYADALVGV--AGeglnveQRKRLTIGVELVAKPKLLLfLD 1024
Cdd:COG4133 89 ELTVRENLRFWAALYG-----LRADREAIDEALEAVGLAGLADLPVRQlsAG------QKRRVALARLLLSPAPLWL-LD 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 353526216 1025 EPTSGLDSQT-AWsICKLMRKLADHGQAILCTIHQPSAL 1062
Cdd:COG4133 157 EPFTALDAAGvAL-LAELIAAHLARGGAVLLTTHQPLEL 194
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
872-1076 |
1.35e-26 |
|
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: 109.16 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLservtTGII--TDGERLVNGHALDSSfQRSIGYVQQQDvHLETT- 948
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAI-----LGLLkpTSGSIRVFGKPLEKE-RKRIGYVPQRR-SIDRDf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 949 --TVRE--ALQFSAYLRQSNKISKKEKDDyVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELVAKPKLLLfLD 1024
Cdd:cd03235 84 piSVRDvvLMGLYGHKGLFRRLSKADKAK-VDEALERVGLSELADRQIGELSGG----QQQRVLLARALVQDPDLLL-LD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 353526216 1025 EPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSaLIMAEFDKLLFLQKG 1076
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLG-LVLEYFDRVLLLNRT 208
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
874-1076 |
3.37e-26 |
|
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: 107.99 E-value: 3.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 874 VILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIITDGERLVNGHALDssfQRSIGYVQQQDV---HLett 948
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAglERPDSGEILIDGRDVTGVPPE---RRNIGMVFQDYAlfpHL--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 949 TVREALQFSAYLRqsnKISKKEKDDYVDYVIDLLEMTDYADALVgvagEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTS 1028
Cdd:cd03259 88 TVAENIAFGLKLR---GVPKAEIRARVRELLELVGLEGLLNRYP----HELSGGQQQRVALARALAREPSLLL-LDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 353526216 1029 GLDSQTAWSICKLMRKL-ADHG-QAILCTIHQPSALIMAefDKLLFLQKG 1076
Cdd:cd03259 160 ALDAKLREELREELKELqRELGiTTIYVTHDQEEALALA--DRIAVMNEG 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
872-1076 |
3.82e-26 |
|
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: 106.33 E-value: 3.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLservtTGII--TDGERLVNGHALDS---SFQRSIGYVQQQDVHLE 946
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKII-----LGLLkpDSGEIKVLGKDIKKepeEVKRRIGYLPEEPSLYE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 947 TTTVREALQFSAylrqsnkiskkekddyvdyvidllemtdyadalvGvageglnveQRKRLTIGVELVAKPKlLLFLDEP 1026
Cdd:cd03230 87 NLTVRENLKLSG----------------------------------G---------MKQRLALAQALLHDPE-LLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 353526216 1027 TSGLDSQTAWSICKLMRKLADHGQAILCTIHqpsalIMAE----FDKLLFLQKG 1076
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSH-----ILEEaerlCDRVAILNNG 171
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
876-1053 |
3.04e-25 |
|
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: 105.98 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTG-IITDGERlVNGHALDSSFQRSIGYVQQQDVHLETTTVRE 952
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISgfLRPTSGsVLFDGED-ITGLPPHEIARLGIGRTFQIPRLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 953 ALQFSAYLRQSNKI-------SKKEKDDYVDYVIDLLEMTDYADALVGvageGLNVEQRKRLTIGVELVAKPKLLLfLDE 1025
Cdd:cd03219 95 NVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAG----ELSYGQQRRLEIARALATDPKLLL-LDE 169
|
170 180
....*....|....*....|....*...
gi 353526216 1026 PTSGLDSQTAWSICKLMRKLADHGQAIL 1053
Cdd:cd03219 170 PAAGLNPEETEELAELIRELRERGITVL 197
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
871-1076 |
3.11e-25 |
|
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: 112.16 E-value: 3.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 871 EDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLServttGII--TDGERLVNGHALDS----SFQRSIGYVQQQDvH 944
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL-----GFLppYSGSILINGVDLSDldpaSWRRQIAWVPQNP-Y 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 945 LETTTVREALQFSAylrqsNKISKKEkddyVDYVIDLLEMTDYADAL-------VGVAGEGLNVEQRKRLTIGVELVAKP 1017
Cdd:COG4988 422 LFAGTIRENLRLGR-----PDASDEE----LEAALEAAGLDEFVAALpdgldtpLGEGGRGLSGGQAQRLALARALLRDA 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 353526216 1018 KLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTiHQPSAliMAEFDKLLFLQKG 1076
Cdd:COG4988 493 PLLL-LDEPTAHLDAETEAEILQALRRLAKGRTVILIT-HRLAL--LAQADRILVLDDG 547
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
860-1084 |
5.46e-25 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 105.90 E-value: 5.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKikkeDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLServttGII--TDGERLVNGHALDS----SFQR 933
Cdd:COG1120 5 ENLSVGYG----GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALA-----GLLkpSSGEVLLDGRDLASlsrrELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 934 SIGYVQQQDVHLETTTVREALQFSAYLRQSNKISKKEKD-DYVDYVIDLLEMTDYADALV-----GvageglnveQRKRL 1007
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDrEAVEEALERTGLEHLADRPVdelsgG---------ERQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 353526216 1008 TIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIHQPS-ALIMAefDKLLFLqKGGRTAYFGE 1084
Cdd:COG1120 147 LIARALAQEPPLLL-LDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNlAARYA--DRLVLL-KDGRIVAQGP 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
860-1083 |
2.22e-24 |
|
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: 102.83 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLnclseRVTTGII--TDGERLVNGHALDSS---FQRS 934
Cdd:cd03266 5 DALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTL-----RMLAGLLepDAGFATVDGFDVVKEpaeARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 935 IGYVQQQDVHLETTTVREALQFSAYLrqsNKISKKEKDDYVDYVIDLLEMTDYADALVGvageGLNVEQRKRLTIGVELV 1014
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGL---YGLKGDELTARLEELADRLGMEELLDRRVG----GFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353526216 1015 AKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHqpsalIMAEF----DKLLFLQKgGRTAYFG 1083
Cdd:cd03266 153 HDPPVLL-LDEPTTGLDVMATRALREFIRQLRALGKCILFSTH-----IMQEVerlcDRVVVLHR-GRVVYEG 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
872-1076 |
2.83e-24 |
|
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: 103.14 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIIT-DGERLvngHALDSS----FQRSIGYVQQQDVH 944
Cdd:COG1127 17 DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIglLRPDSGEILvDGQDI---TGLSEKelyeLRRRIGMLFQGGAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 945 LETTTVREALQFsaYLRQSNKISKKEKDDYVDYVIDLLEMTDYAD----ALVGvageGlnveQRKRLTIGVELVAKPKLL 1020
Cdd:COG1127 94 FDSLTVFENVAF--PLREHTDLSEAEIRELVLEKLELVGLPGAADkmpsELSG----G----MRKRVALARALALDPEIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 353526216 1021 lFLDEPTSGLDSQTAWSICKLMRKLADHGQA--ILCTiHQ-PSALIMAefDKLLFLQKG 1076
Cdd:COG1127 164 -LYDEPTAGLDPITSAVIDELIRELRDELGLtsVVVT-HDlDSAFAIA--DRVAVLADG 218
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
876-1070 |
3.78e-24 |
|
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: 104.78 E-value: 3.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTLLnclseRVTTGII--TDGERLVNGHALDSS---FQRSIGYVQQQDVHLETTTV 950
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTI-----RMLTTLLrpTSGTARVAGYDVVREprkVRRSIGIVPQYASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 951 REALQFSAYLRqsnKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELVAKPKLLlFLDEPTSGL 1030
Cdd:TIGR01188 84 RENLEMMGRLY---GLPKDEAEERAEELLELFELGEAADRPVGTYSGG----MRRRLDIAASLIHQPDVL-FLDEPTTGL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 353526216 1031 DSQTAWSICKLMRKLADHGQAILCTIHQpsaliMAEFDKL 1070
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHY-----MEEADKL 190
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
870-1076 |
4.86e-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: 4.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 870 KEDRVILDHVDGWVKPGQITALMGASGAGKTTLLnclseRVTTGII--TDGERLVNGHALDSS-FQRSIGYVQQQ-DVHL 945
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLA-----KILAGLIkeSSGSILLNGKPIKAKeRRKSIGYVMQDvDYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 946 ETTTVREALQFSAylrqsnkiskKEKDDY---VDYVIDLLEMTDYAD----ALVGvageGlnveQRKRLTIGVELVAKPK 1018
Cdd:cd03226 85 FTDSVREELLLGL----------KELDAGneqAETVLKDLDLYALKErhplSLSG----G----QKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 353526216 1019 LLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSaLIMAEFDKLLFLQKG 1076
Cdd:cd03226 147 LLIF-DEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYE-FLAKVCDRVLLLANG 202
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
872-1070 |
7.37e-24 |
|
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: 101.68 E-value: 7.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLServTTGIITDGERLVNGHALDS---SFQRSIGYVQQQDVHLETT 948
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLT---TLLKPTSGRATVAGHDVVReprEVRRRIGIVFQDLSVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 949 TVREALQFSAYLRqsnKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGLnveqRKRLTIGVELVAKPKLLlFLDEPTS 1028
Cdd:cd03265 89 TGWENLYIHARLY---GVPGAERRERIDELLDFVGLLEAADRLVKTYSGGM----RRRLEIARSLVHRPEVL-FLDEPTI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 353526216 1029 GLDSQTAWSICKLMRKL-ADHGQAILCTIHQpsaliMAEFDKL 1070
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLkEEFGMTILLTTHY-----MEEAEQL 198
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
860-1076 |
1.27e-23 |
|
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: 98.86 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKikkeDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIIT-DGERLvnGHALDSSFQRSIG 936
Cdd:cd00267 3 ENLSFRYG----GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAglLKPTSGEILiDGKDI--AKLPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 937 YVqqqdvhletttvreaLQFSAylrqsnkiskkekddyvdyvidllemtdyadalvgvageGlnveQRKRLTIGVELVAK 1016
Cdd:cd00267 77 YV---------------PQLSG---------------------------------------G----QRQRVALARALLLN 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1017 PKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSaLIMAEFDKLLFLQKG 1076
Cdd:cd00267 99 PDLLL-LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPE-LAELAADRVIVLKDG 156
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
871-1076 |
2.44e-23 |
|
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: 98.22 E-value: 2.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 871 EDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLservtTGI--ITDGERLVNGHALD----SSFQRSIGYVqQQDVH 944
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLL-----LRLydPTSGEILIDGVDLRdldlESLRKNIAYV-PQDPF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 945 LETTTVREalqfsaylrqsNKISkkekddyvdyvidllemtdyadalvgvAGeglnveQRKRLTIGVELVAKPKLLLfLD 1024
Cdd:cd03228 87 LFSGTIRE-----------NILS---------------------------GG------QRQRIAIARALLRDPPILI-LD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 353526216 1025 EPTSGLDSQTAWSICKLMRKLADHGQAILCTiHQPSALIMAefDKLLFLQKG 1076
Cdd:cd03228 122 EATSALDPETEALILEALRALAKGKTVIVIA-HRLSTIRDA--DRIIVLDDG 170
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
866-1087 |
1.65e-22 |
|
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: 98.23 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 866 VKIKKEDRVILDHVDgW-VKPGQITALMGASGAGKTTLLNCLSERV--TTGIITD--GERL--VNGHALdssfQRSIGYV 938
Cdd:COG1119 9 VTVRRGGKTILDDIS-WtVKPGEHWAILGPNGAGKSTLLSLITGDLppTYGNDVRlfGERRggEDVWEL----RKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 939 --QQQDVHLETTTVREALQ--FSAYLRQSNKISKKEKDdYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELV 1014
Cdd:COG1119 84 spALQLRFPRDETVLDVVLsgFFDSIGLYREPTDEQRE-RARELLELLGLAHLADRPFGTLSQG----EQRRVLIARALV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 353526216 1015 AKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHG--QAILCTiHQPSAlIMAEFDKLLFLqKGGRTAYFGELGE 1087
Cdd:COG1119 159 KDPELLI-LDEPTAGLDLGARELLLALLDKLAAEGapTLVLVT-HHVEE-IPPGITHVLLL-KDGRVVAAGPKEE 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
885-1083 |
1.88e-22 |
|
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: 97.37 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 885 PGQITALMGASGAGKTTLLNCLS--ERVTTGIITdgerlVNGHALDSS--------FQRSIGYVQQQDV---HLettTVR 951
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAglEKPDGGTIV-----LNGTVLFDSrkkinlppQQRKIGLVFQQYAlfpHL---NVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 952 EALQFSAylrqsNKISKKEKDDYVDYVIDLLEMTDYADALVGvageGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 1031
Cdd:cd03297 94 ENLAFGL-----KRKRNREDRISVDELLDLLGLDHLLNRYPA----QLSGGEKQRVALARALAAQPELLL-LDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 353526216 1032 SQTAWSICKLMRKLADHGQ--AILCTiHQPS-ALIMAEfdkLLFLQKGGRTAYFG 1083
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNipVIFVT-HDLSeAEYLAD---RIVVMEDGRLQYIG 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
860-1081 |
3.65e-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: 95.19 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKikkeDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLServttGIIT--DGERLVNGHALdssfqrsigy 937
Cdd:cd03214 3 ENLSVGYG----GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA-----GLLKpsSGEILLDGKDL---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 938 vqqqdvhlETTTVREALQFSAYLRQsnkiskkekddyvdyVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELVAKP 1017
Cdd:cd03214 64 --------ASLSPKELARKIAYVPQ---------------ALELLGLAHLADRPFNELSGG----ERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 353526216 1018 KLLLfLDEPTSGLDSQTAWSICKLMRKLAD-HGQAILCTIHQPS-ALIMAefDKLLFLQKGGRTAY 1081
Cdd:cd03214 117 PILL-LDEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNlAARYA--DRVILLKDGRIVAQ 179
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
872-1076 |
6.49e-22 |
|
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: 94.56 E-value: 6.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIIT-DGERLVNGHALDSSFQRSIGYVQQQDVHLETT 948
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAglEEPDSGSILiDGEDLTDLEDELPPLRRRIGMVFQDFALFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 949 TVREALQFsaylrqsnkiskkekddyvdyvidllemtdyadalvgvageGLNVEQRKRLTIGVELVAKPKLLLfLDEPTS 1028
Cdd:cd03229 92 TVLENIAL-----------------------------------------GLSGGQQQRVALARALAMDPDVLL-LDEPTS 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 353526216 1029 GLDSQTAWSICKLMRKLAD-HGQAILCTIHQPS-ALIMAefDKLLFLQKG 1076
Cdd:cd03229 130 ALDPITRREVRALLKSLQAqLGITVVLVTHDLDeAARLA--DRVVVLRDG 177
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
871-1076 |
1.58e-21 |
|
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: 101.45 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 871 EDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIItdgerLVNGHALD----SSFQRSIGYVqQQDVH 944
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLglYEPTSGRI-----LIDGIDLRqidpASLRRQIGVV-LQDVF 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 945 LETTTVREALQFSAYlrqsnKISkkekDDYVDYVIDLLEMTDYADAL-------VGVAGEGLNVEQRKRLTIGVELVAKP 1017
Cdd:COG2274 560 LFSGTIRENITLGDP-----DAT----DEEIIEAARLAGLHDFIEALpmgydtvVGEGGSNLSGGQRQRLAIARALLRNP 630
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 353526216 1018 KLLLfLDEPTSGLDSQTAWSICKLMRKLAdHGQAILCTIHQPSALIMAefDKLLFLQKG 1076
Cdd:COG2274 631 RILI-LDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLA--DRIIVLDKG 685
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
860-1053 |
3.02e-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: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLT--YQVKiKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLservtTGII--TDGERLVNGHALDS------ 929
Cdd:COG1123 264 RNLSkrYPVR-GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLL-----LGLLrpTSGSILFDGKDLTKlsrrsl 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 930 -SFQRSIGYVqQQDVHL---ETTTVREALQFSayLRQSNKISKKEKDDYVDYVIDLLEM-TDYAD----ALVGvaGegln 1000
Cdd:COG1123 338 rELRRRVQMV-FQDPYSslnPRMTVGDIIAEP--LRLHGLLSRAERRERVAELLERVGLpPDLADryphELSG--G---- 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 353526216 1001 veQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLAD-HGQAIL 1053
Cdd:COG1123 409 --QRQRVAIARALALEPKLLI-LDEPTSALDVSVQAQILNLLRDLQReLGLTYL 459
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
874-1053 |
3.07e-21 |
|
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: 94.72 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 874 VILDHVDGWVKPGQITALMGASGAGKTTLLNCLservtTGII--TDGERLVNGHALDS-------------SFQRsigyv 938
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLI-----TGFYrpTSGRILFDGRDITGlpphriarlgiarTFQN----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 939 qqqdVHL-ETTTVREALQFSAYLRQSNKI------------SKKEKDDYVDYVIDLLEMTDYADALVGvageGLNVEQRK 1005
Cdd:COG0411 88 ----PRLfPELTVLENVLVAAHARLGRGLlaallrlprarrEEREARERAEELLERVGLADRADEPAG----NLSYGQQR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 353526216 1006 RLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAIL 1053
Cdd:COG0411 160 RLEIARALATEPKLLL-LDEPAAGLNPEETEELAELIRRLrDERGITIL 207
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
860-1078 |
3.85e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 94.77 E-value: 3.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIIT-DGERlVNGHALDssfqrsIG 936
Cdd:COG1116 11 RGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAglEKPTSGEVLvDGKP-VTGPGPD------RG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 937 YVQQQDVHLETTTVREALQFSAYLRqsnKISKKEKDDYVDYVIDLLEMTDYADA----LVGvaGeglnveQRKRLTIGVE 1012
Cdd:COG1116 84 VVFQEPALLPWLTVLDNVALGLELR---GVPKAERRERARELLELVGLAGFEDAyphqLSG--G------MRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 353526216 1013 LVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQPS-ALIMAefDKLLFLQKG-GR 1078
Cdd:COG1116 153 LANDPEVLL-MDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDeAVFLA--DRVVVLSARpGR 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
874-1045 |
4.25e-21 |
|
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: 93.80 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 874 VILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTG-IITDGERL--VNGHALdSSFQRSIGYVQQQDVHLETT 948
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINglERPTSGsVLVDGTDLtlLSGKEL-RKARRRIGMIFQHFNLLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 949 TVREALqfsAYLRQSNKISKKEKDDYVDYVIDLLEMTDYADA----LVGvaGeglnveQRKRLTIGVELVAKPKLLLfLD 1024
Cdd:cd03258 98 TVFENV---ALPLEIAGVPKAEIEERVLELLELVGLEDKADAypaqLSG--G------QKQRVGIARALANNPKVLL-CD 165
|
170 180
....*....|....*....|.
gi 353526216 1025 EPTSGLDSQTAWSICKLMRKL 1045
Cdd:cd03258 166 EATSALDPETTQSILALLRDI 186
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
873-1073 |
4.54e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 98.90 E-value: 4.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 873 RVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTtgiITDGERLVNG----HALDSSFQRSIGYVQQQDvHLETT 948
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD---PTEGSIAVNGvplaDADADSWRDQIAWVPQHP-FLFAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 949 TVREALQFSAylrqsnkisKKEKDDYVDYVIDLLEMTDYADAL-------VGVAGEGLNVEQRKRLTIGVELVAKPKLLL 1021
Cdd:TIGR02857 411 TIAENIRLAR---------PDASDAEIREALERAGLDEFVAALpqgldtpIGEGGAGLSGGQAQRLALARAFLRDAPLLL 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 353526216 1022 fLDEPTSGLDSQTAWSICKLMRKLADhGQAILCTIHQPSalIMAEFDKLLFL 1073
Cdd:TIGR02857 482 -LDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLA--LAALADRIVVL 529
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
871-1076 |
6.67e-21 |
|
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: 98.68 E-value: 6.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 871 EDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLservtTGII--TDGERLVNGHALD----SSFQRSIGYVQQqDVH 944
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALL-----LRFLdpQSGSITLGGVDLRdldeDDLRRRIAVVPQ-RPH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 945 LETTTVREALqfsaylrqsnKISKKEKDDyvDYVIDLLE---MTDYADAL-------VGVAGEGLNVEQRKRLTIGVELV 1014
Cdd:COG4987 420 LFDTTLRENL----------RLARPDATD--EELWAALErvgLGDWLAALpdgldtwLGEGGRRLSGGERRRLALARALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 353526216 1015 AKPKLLLfLDEPTSGLDSQTAWSICKLMRKLAdHGQAILCTIHQPSALimAEFDKLLFLQKG 1076
Cdd:COG4987 488 RDAPILL-LDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGL--ERMDRILVLEDG 545
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
872-1081 |
6.95e-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: 6.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLnclseRVTTGII--TDGERLVNGHALDSSFQRSIGYVQQQDVHLETTT 949
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTI-----RMILGIIlpDSGEVLFDGKPLDIAARNRIGYLPEERGLYPKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 950 VREALQFSAYLRqsnKISKKEKDDYVDYVIDLLEMTDYADALVgvagEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 1029
Cdd:cd03269 87 VIDQLVYLAQLK---GLKKEEARRRIDEWLERLELSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLI-LDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 353526216 1030 LDSQTAWSICKLMRKLADHGQAILCTIHQpsaliMAEF----DKLLFLQKGGRTAY 1081
Cdd:cd03269 159 LDPVNVELLKDVIRELARAGKTVILSTHQ-----MELVeelcDRVLLLNKGRAVLY 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
866-1087 |
8.90e-21 |
|
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: 92.95 E-value: 8.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 866 VKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLservtTGII--TDGERLVNGHALDS-------SFQRSIG 936
Cdd:cd03261 6 LTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLI-----VGLLrpDSGEVLIDGEDISGlseaelyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 937 YVQQQDVHLETTTVREALQFsaYLRQSNKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELVAK 1016
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAF--PLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGG----MKKRVALARALALD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353526216 1017 PKlLLFLDEPTSGLDSQTAWSICKLMRKLADHGQA--ILCTIHQPSALIMAefDKLLFLqKGGRTAYFGELGE 1087
Cdd:cd03261 155 PE-LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLtsIMVTHDLDTAFAIA--DRIAVL-YDGKIVAEGTPEE 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
875-1053 |
1.06e-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: 92.50 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 875 ILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTG-IITDGERlVNGHALDSSFQRSIGYVQQ-QDV--HLett 948
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMglLPPRSGsIRFDGRD-ITGLPPHERARAGIGYVPEgRRIfpEL--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 949 TVREALQFSAYLRqsnkiSKKEKDDYVDYVID----LLEMTD-YADALVGvaGEglnveqRKRLTIGVELVAKPKLLLfL 1023
Cdd:cd03224 91 TVEENLLLGAYAR-----RRAKRKARLERVYElfprLKERRKqLAGTLSG--GE------QQMLAIARALMSRPKLLL-L 156
|
170 180 190
....*....|....*....|....*....|
gi 353526216 1024 DEPTSGLDSQTAWSICKLMRKLADHGQAIL 1053
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEGVTIL 186
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
872-1031 |
1.09e-20 |
|
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: 91.87 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGqITALMGASGAGKTTLLnclseRVTTGII--TDGERLVNGH---ALDSSFQRSIGYVQQQDVHLE 946
Cdd:cd03264 12 KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLM-----RILATLTppSSGTIRIDGQdvlKQPQKLRRRIGYLPQEFGVYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 947 TTTVREALQFSAYLRqsnKISKKEKDDYVDYVIDLLEMTDYADALVGvageGLNVEQRKRLTIGVELVAKPKLLLfLDEP 1026
Cdd:cd03264 86 NFTVREFLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIG----SLSGGMRRRVGIAQALVGDPSILI-VDEP 157
|
....*
gi 353526216 1027 TSGLD 1031
Cdd:cd03264 158 TAGLD 162
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
860-1053 |
2.05e-20 |
|
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: 91.38 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIIT-DGERlVNGHaldssfQRSIG 936
Cdd:cd03293 4 RNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAglERPTSGEVLvDGEP-VTGP------GPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 937 YVQQQDVHLETTTVREALqfsAYLRQSNKISKKEKDDYVDYVIDLLEMTDYADA----LVGvaGeglnveQRKRLTIGVE 1012
Cdd:cd03293 77 YVFQQDALLPWLTVLDNV---ALGLELQGVPKAEARERAEELLELVGLSGFENAyphqLSG--G------MRQRVALARA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 353526216 1013 LVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAIL 1053
Cdd:cd03293 146 LAVDPDVLL-LDEPFSALDALTREQLQEELLDIwRETGKTVL 186
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
863-1070 |
3.18e-20 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 90.74 E-value: 3.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 863 TYQVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIITDgerlvnghaLDSSFQRSIGYVQQ 940
Cdd:cd03268 3 TNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILglIKPDSGEITF---------DGKSYQKNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 941 QDVHLET------TTVREALQFSAYLRQsnkISKKEkddyVDYVIDLLEMTDYADALVGvageGLNVEQRKRLTIGVELV 1014
Cdd:cd03268 74 IGALIEApgfypnLTARENLRLLARLLG---IRKKR----IDEVLDVVGLKDSAKKKVK----GFSLGMKQRLGIALALL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 353526216 1015 AKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHqpsalIMAEFDKL 1070
Cdd:cd03268 143 GNPDLLI-LDEPTNGLDPDGIKELRELILSLRDQGITVLISSH-----LLSEIQKV 192
|
|
| ABC_trans_N |
pfam14510 |
ABC-transporter N-terminal; This domain is found at the N-terminus of ABC-transporter proteins ... |
61-144 |
3.36e-20 |
|
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: 86.22 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 61 DLARYLSHMSDIPGVSPFNGNISHEqlDPDSEnFNAKYWVKNLKKLFESDsDYYKPSKLGVAYRNLRAYGIANDSDYQPT 140
Cdd:pfam14510 1 ELARILTRQSSSSSSSSSPESTDPD--EEDSE-FDLRKWLKNLRRLIDED-GYIKPRKLGVAFKNLTVSGVGAGADYQPT 76
|
....
gi 353526216 141 VTNA 144
Cdd:pfam14510 77 VGNA 80
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
870-1077 |
1.05e-19 |
|
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: 89.98 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 870 KEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSE--RVTTGIItdgerLVNGHALD----SSFQRSIGYVqQQDV 943
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRfyDVDSGRI-----LIDGHDVRdytlASLRRQIGLV-SQDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 944 HLETTTVREALQFSAYLRQSNKISKKEKDDYVDYVIDllEMTDYADALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfL 1023
Cdd:cd03251 86 FLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIM--ELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILI-L 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 353526216 1024 DEPTSGLDSQTAWSICKLMRKLADHGQAI-----LCTIHQPsalimaefDKLLFLQKGG 1077
Cdd:cd03251 163 DEATSALDTESERLVQAALERLMKNRTTFviahrLSTIENA--------DRIVVLEDGK 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
872-1031 |
1.22e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 92.44 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIITDGERLVNGhaLDSSfQRSIGYVQQQDV---HLe 946
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAglEDPTSGEILIGGRDVTD--LPPK-DRNIAMVFQSYAlypHM- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 947 ttTVREALQFSayLRQSnKISKKEKDDYVDYVIDLLEMTDYAD----ALVGvaGeglnveQRKRLTIGVELVAKPKLLLF 1022
Cdd:COG3839 91 --TVYENIAFP--LKLR-KVPKAEIDRRVREAAELLGLEDLLDrkpkQLSG--G------QRQRVALGRALVREPKVFLL 157
|
....*....
gi 353526216 1023 lDEPTSGLD 1031
Cdd:COG3839 158 -DEPLSNLD 165
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
869-1076 |
1.65e-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: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 869 KKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNcLSERVTtgIITDGERLVNGHAL----DSSFQRSIGYVQQQDVh 944
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTK-LIQRFY--VPENGRVLVDGHDLaladPAWLRRQVGVVLQENV- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 945 LETTTVREALQFsaylrqSNKISKKEKDDYVDYVID----LLEMTDYADALVGVAGEGLNVEQRKRLTIGVELVAKPKLL 1020
Cdd:cd03252 87 LFNRSIRDNIAL------ADPGMSMERVIEAAKLAGahdfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 353526216 1021 LFlDEPTSGLDSQTAWSICKLMRKLADhGQAILCTIHQPSALIMAefDKLLFLQKG 1076
Cdd:cd03252 161 IF-DEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNA--DRIIVMEKG 212
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
872-1076 |
1.66e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.94 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLnclseRVTTGII--TDGERLVNGHALDSSFQRSIGYVqqqdvhLET-- 947
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTI-----RIILGILapDSGEVLWDGEPLDPEDRRRIGYL------PEErg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 948 ----TTVREALQFSAYLRQsnkISKKEKDDYVDYVIDLLEMTDYADALVgvagEGL---NveQRKrLTIGVELVAKPKLL 1020
Cdd:COG4152 82 lypkMKVGEQLVYLARLKG---LSKAEAKRRADEWLERLGLGDRANKKV----EELskgN--QQK-VQLIAALLHDPELL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1021 LfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsaliMA---EF-DKLLFLQKG 1076
Cdd:COG4152 152 I-LDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQ-----MElveELcDRIVIINKG 205
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
863-1045 |
1.77e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 91.68 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 863 TYQVKikKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTG-IITDGERLVnghALDSS----FQRSI 935
Cdd:COG1135 10 TFPTK--GGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINllERPTSGsVLVDGVDLT---ALSERelraARRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 936 GYVQQQDVHLETTTVRE--ALQfsayLRQSnKISKKEKDDYVDYVIDLLEMTDYADA----LVGvageglnvEQRKRLTI 1009
Cdd:COG1135 85 GMIFQHFNLLSSRTVAEnvALP----LEIA-GVPKAEIRKRVAELLELVGLSDKADAypsqLSG--------GQKQRVGI 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 353526216 1010 GVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 1045
Cdd:COG1135 152 ARALANNPKVLL-CDEATSALDPETTRSILDLLKDI 186
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
872-1076 |
2.21e-19 |
|
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: 88.36 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTG-IITDGERLVNGHALDSSFQRSIGYVQQQD---VHL 945
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINllEEPDSGtIIIDGLKLTDDKKNINELRQKVGMVFQQFnlfPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 946 ettTVREALQFSayLRQSNKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELVAKPKLLLFlDE 1025
Cdd:cd03262 92 ---TVLENITLA--PIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGG----QQQRVAIARALAMNPKVMLF-DE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 353526216 1026 PTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsaliMAeF-----DKLLFLQKG 1076
Cdd:cd03262 162 PTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE-----MG-FarevaDRVIFMDDG 211
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
871-1076 |
3.05e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 93.69 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 871 EDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSeR---VTTGIItdgerLVNGHALD----SSFQRSIGYVqQQDV 943
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLL-RfydPTSGRI-----LIDGVDIRdltlESLRRQIGVV-PQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 944 HLETTTVREALQFSAylrqsNKISKKE-----KDDYVDYVIDLLEMtDYaDALVGVAGEGLNVEQRKRLTIGVELVAKPK 1018
Cdd:COG1132 424 FLFSGTIRENIRYGR-----PDATDEEveeaaKAAQAHEFIEALPD-GY-DTVVGERGVNLSGGQRQRIAIARALLKDPP 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 353526216 1019 LLLfLDEPTSGLDSQTAWSICKLMRKLAdHGQAILcTI-HQPSALIMAefDKLLFLQKG 1076
Cdd:COG1132 497 ILI-LDEATSALDTETEALIQEALERLM-KGRTTI-VIaHRLSTIRNA--DRILVLDDG 550
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
867-1083 |
4.44e-19 |
|
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: 88.01 E-value: 4.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 867 KIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTtgiITDGERLVNGHALDS-------SFQRSIGYVQ 939
Cdd:cd03256 8 KTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE---PTSGSVLIDGTDINKlkgkalrQLRRQIGMIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 940 QQDVHLETTTVRE-----ALQFSAYLRQ-SNKISKKEKDDyvdyVIDLLE---MTDYA----DALVGvaGeglnveQRKR 1006
Cdd:cd03256 85 QQFNLIERLSVLEnvlsgRLGRRSTWRSlFGLFPKEEKQR----ALAALErvgLLDKAyqraDQLSG--G------QQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 353526216 1007 LTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIHQPSaLIMAEFDKLLFLqKGGRTAYFG 1083
Cdd:cd03256 153 VAIARALMQQPKLIL-ADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVD-LAREYADRIVGL-KDGRIVFDG 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
860-1076 |
5.22e-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: 92.27 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTyqVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTGIITDGERLVNGHALD--SSFQRS--I 935
Cdd:COG1123 8 RDLS--VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLelSEALRGrrI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 936 GYV-QQQDVHLETTTVREALQFSAYLRqsnKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELV 1014
Cdd:COG1123 86 GMVfQDPMTQLNPVTVGDQIAEALENL---GLSRAEARARVLELLEAVGLERRLDRYPHQLSGG----QRQRVAIAMALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353526216 1015 AKPKLLLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQPsALIMAEFDKLLFLQKG 1076
Cdd:COG1123 159 LDPDLLI-ADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDL-GVVAEIADRVVVMDDG 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
872-1047 |
7.53e-19 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 87.24 E-value: 7.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCL--------SERVTTGIITDGERLVNGHALDSSFQRSIGYVQQQDV 943
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndlipGAPDEGEVLLDGKDIYDLDVDVLELRRRVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 944 HLEtTTVREALQFSAYLRQSNKisKKEKDDYVDYVIDLLEMTDY-ADALvgvAGEGLNVEQRKRLTIGVELVAKPKLLLf 1022
Cdd:cd03260 92 PFP-GSIYDNVAYGLRLHGIKL--KEELDERVEEALRKAALWDEvKDRL---HALGLSGGQQQRLCLARALANEPEVLL- 164
|
170 180
....*....|....*....|....*
gi 353526216 1023 LDEPTSGLDSQTAWSICKLMRKLAD 1047
Cdd:cd03260 165 LDEPTSALDPISTAKIEELIAELKK 189
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
860-1076 |
1.01e-18 |
|
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: 87.17 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIIT-DGERLvnGHALDSSFQRSIG 936
Cdd:COG1124 5 RNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAglERPWSGEVTfDGRPV--TRRRRKAFRRRVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 937 YVQQQ---DVH----LETTtVREALQFsaylrqsnkISKKEKDDYVDYVIDLLEMTD-----YADALVGvageGlnveQR 1004
Cdd:COG1124 83 MVFQDpyaSLHprhtVDRI-LAEPLRI---------HGLPDREERIAELLEQVGLPPsfldrYPHQLSG----G----QR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 353526216 1005 KRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQPsALI--MAefDKLLFLQKG 1076
Cdd:COG1124 145 QRVAIARALILEPELLL-LDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDL-AVVahLC--DRVAVMQNG 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
860-1076 |
1.09e-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: 86.79 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTG-IITDGERLVN-GHALDSSFQRSI 935
Cdd:cd03257 5 KNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILglLKPTSGsIIFDGKDLLKlSRRLRKIRRKEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 936 GYV-QQQDVHLETT-TVREALQ--FSAYLRQSNKISKKEKDDYVDYVIDLLE--MTDYADALVGvageGlnveQRKRLTI 1009
Cdd:cd03257 85 QMVfQDPMSSLNPRmTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEevLNRYPHELSG----G----QRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 353526216 1010 GVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLAD-HGQAILCTIHQPSALimAEF-DKLLFLQKG 1076
Cdd:cd03257 157 ARALALNPKLLI-ADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVV--AKIaDRVAVMYAG 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
872-1031 |
1.44e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 89.00 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIITDGERLVNGHAldsSFQRSIGYVQQQDV---HLe 946
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAgfETPDSGRILLDGRDVTGLP---PEKRNVGMVFQDYAlfpHL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 947 ttTVREALQFSayLRQSnKISKKEKDDYVDYVIDLLEMTDYADALV----GvageglnvEQRKRLTIGVELVAKPKLLLf 1022
Cdd:COG3842 93 --TVAENVAFG--LRMR-GVPKAEIRARVAELLELVGLEGLADRYPhqlsG--------GQQQRVALARALAPEPRVLL- 158
|
....*....
gi 353526216 1023 LDEPTSGLD 1031
Cdd:COG3842 159 LDEPLSALD 167
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
885-1033 |
2.54e-18 |
|
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: 88.62 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 885 PGQ-ITALMGASGAGKTTLLNCLS--ERVTTGIIT-DGERLVNGHAldSSF----QRSIGYVQQQDV---HLettTVREA 953
Cdd:COG4148 23 PGRgVTALFGPSGSGKTTLLRAIAglERPDSGRIRlGGEVLQDSAR--GIFlpphRRRIGYVFQEARlfpHL---SVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 954 LQFSayLRQSNKISKKEKddyVDYVIDLLEMTD----YADALVGvaGEglnveqRKRLTIGVELVAKPKLLLfLDEPTSG 1029
Cdd:COG4148 98 LLYG--RKRAPRAERRIS---FDEVVELLGIGHlldrRPATLSG--GE------RQRVAIGRALLSSPRLLL-MDEPLAA 163
|
....
gi 353526216 1030 LDSQ 1033
Cdd:COG4148 164 LDLA 167
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
162-378 |
3.01e-18 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 85.68 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 162 SKYFD---ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIERHYRGDVIYSAETD 238
Cdd:COG4555 8 SKKYGkvpALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLA----GLLKPDSGSILIDGEDVRKEPREARRQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 239 VHFPHLSVGDTLEFAARLRtpqnrgeGIDRETYAKHMASvYMATYGLSHTRNTNVGndfvrGVSGGERKRVSIAEASLSG 318
Cdd:COG4555 84 GLYDRLTVRENIRYFAELY-------GLFDEELKKRIEE-LIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 353526216 319 ANIQCWDNATRGLD--SATAL-EFIRALKTS-ATILDTTPLIaiyqcsQDAYELFDNVVVLYEG 378
Cdd:COG4555 151 PKVLLLDEPTNGLDvmARRLLrEILRALKKEgKTVLFSSHIM------QEVEALCDRVVILHKG 208
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
867-1076 |
3.62e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 85.10 E-value: 3.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 867 KIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLN--CLSERVTTGIITdgerlVNGHALDS-------SFQRSIGY 937
Cdd:COG2884 9 KRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKllYGEERPTSGQVL-----VNGQDLSRlkrreipYLRRRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 938 VqQQDVHL-ETTTVRE----ALQFSaylrqsnKISKKEKDDYVDYVIDLLEMTDYADALVGV--AGEglnveqRKRLTIG 1010
Cdd:COG2884 84 V-FQDFRLlPDRTVYEnvalPLRVT-------GKSRKEIRRRVREVLDLVGLSDKAKALPHElsGGE------QQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 353526216 1011 VELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSalIMAEFDK-LLFLQKG 1076
Cdd:COG2884 150 RALVNRPELLL-ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE--LVDRMPKrVLELEDG 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
875-1053 |
4.65e-18 |
|
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: 85.03 E-value: 4.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 875 ILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIIT-DGERLVNghalDSSFQRS---IGYVQQ-QDV--HL 945
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISglLPPRSGSIRfDGEDITG----LPPHRIArlgIGYVPEgRRIfpSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 946 ettTVREALQFSAYLRQSNKISKKEKDDYVDYVIDLLEMTD-YADALVGvaGEglnveqRKRLTIGVELVAKPKLLLfLD 1024
Cdd:COG0410 94 ---TVEENLLLGAYARRDRAEVRADLERVYELFPRLKERRRqRAGTLSG--GE------QQMLAIGRALMSRPKLLL-LD 161
|
170 180 190
....*....|....*....|....*....|...
gi 353526216 1025 EPTSGLdsqtAWSICKLM----RKLADHGQAIL 1053
Cdd:COG0410 162 EPSLGL----APLIVEEIfeiiRRLNREGVTIL 190
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
873-1057 |
1.01e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 84.13 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 873 RVILDHVDGWVKPGQITALMGASGAGKTTLLNclserVTTGII--TDGERLVNGHALDSS--FQRS---IGYVQQQDVHL 945
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFY-----MIVGLVkpDSGKILLDGQDITKLpmHKRArlgIGYLPQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 946 ETTTVREALqfSAYLRQSNKiSKKEKDDYVDYVIDLLEMT----DYADALVGvaGEglnveqRKRLTIGVELVAKPKLLL 1021
Cdd:cd03218 88 RKLTVEENI--LAVLEIRGL-SKKEREEKLEELLEEFHIThlrkSKASSLSG--GE------RRRVEIARALATNPKFLL 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 353526216 1022 fLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 1057
Cdd:cd03218 157 -LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDH 191
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
874-1077 |
2.28e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 83.22 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 874 VILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTG-IITDGERLVNGHALDSSFQRSIGYVQQQDVHLETTTV 950
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINklEEITSGdLIVDGLKVNDPKVDERLIRQEAGMVFQQFYLFPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 951 REALQFSAylRQSNKISKKEKDDYVdyvIDLLemtdyadALVGVAGEG------LNVEQRKRLTIGVELVAKPKLLLFlD 1024
Cdd:PRK09493 95 LENVMFGP--LRVRGASKEEAEKQA---RELL-------AKVGLAERAhhypseLSGGQQQRVAIARALAVKPKLMLF-D 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 353526216 1025 EPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsalimAEF-----DKLLFLQKGG 1077
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE------IGFaekvaSRLIFIDKGR 213
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
875-1057 |
2.90e-17 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 81.70 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 875 ILDHVDGWVKPGQITALMGASGAGKTTLLNCLSE--RVTTG-IITDGERLVNGHALDSSFQRSIGYV-QQQDVHLETTTV 950
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGllRPQSGaVLIDGEPLDYSRKGLLERRQRVGLVfQDPDDQLFAADV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 951 REALQFSAylrQSNKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELVAKPKLLLfLDEPTSGL 1030
Cdd:TIGR01166 87 DQDVAFGP---LNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGG----EKKRVAIAGAVAMRPDVLL-LDEPTAGL 158
|
170 180
....*....|....*....|....*..
gi 353526216 1031 DSQTAWSICKLMRKLADHGQAILCTIH 1057
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
870-1076 |
3.15e-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: 82.66 E-value: 3.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 870 KEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSE--RVTTG-IITDGerlVNGHALD-SSFQRSIGYVqQQDVHL 945
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfyDPQKGqILIDG---IDIRDISrKSLRSMIGVV-LQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 946 ETTTVREALQFSAYLRQSNKISKKEKDDYVDYVIDLLEmTDYaDALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfLDE 1025
Cdd:cd03254 89 FSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLP-NGY-DTVLGENGGNLSQGERQLLAIARAMLRDPKILI-LDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 353526216 1026 PTSGLDSQTAWSICKLMRKLAdHGQAILCTIHQPSALIMAefDKLLFLQKG 1076
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKNA--DKILVLDDG 213
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
167-384 |
8.73e-17 |
|
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: 79.98 E-value: 8.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAVNTYGFHIgkESQITYDGlSPHDIErhYRGDVIYSAETDVHFPHLSV 246
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVI--TGEILING-RPLDKN--FQRSTGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 247 GDTLEFAARLRtpqnrgegidretyakhmasvymatyglshtrntnvgndfvrGVSGGERKRVSIAEASLSGANIQCWDN 326
Cdd:cd03232 97 REALRFSALLR------------------------------------------GLSVEQRKRLTIGVELAAKPSILFLDE 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353526216 327 ATRGLDSATALEFIRALKTSA----TILDTtpliaIYQCSQDAYELFDNVVVLYEGYQ-IFFG 384
Cdd:cd03232 135 PTSGLDSQAAYNIVRFLKKLAdsgqAILCT-----IHQPSASIFEKFDRLLLLKRGGKtVYFG 192
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
860-1076 |
1.55e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 81.32 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKikkeDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTgiiTDGERLVNGHALDS------SFQR 933
Cdd:COG4559 5 ENLSVRLG----GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTP---SSGEVRLNGRPLAAwspwelARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 934 SigyVQQQDVHLE-TTTVREALQFSAYLRQSnkiSKKEKDDYVDYVIDLLEMTDYAD----ALVGvaGEglnvEQRkrlt 1008
Cdd:COG4559 78 A---VLPQHSSLAfPFTVEEVVALGRAPHGS---SAAQDRQIVREALALVGLAHLAGrsyqTLSG--GE----QQR---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1009 igVEL----------VAKPKLLLFLDEPTSGLD----SQTAwsicKLMRKLADHGQAILCTIHQPSalIMAEF-DKLLFL 1073
Cdd:COG4559 142 --VQLarvlaqlwepVDGGPRWLFLDEPTSALDlahqHAVL----RLARQLARRGGGVVAVLHDLN--LAAQYaDRILLL 213
|
...
gi 353526216 1074 QKG 1076
Cdd:COG4559 214 HQG 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
876-1076 |
1.94e-16 |
|
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: 80.46 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTG-IITDGERLVNGHALDssfqRSIGYVQQQDVHLETTTVRE 952
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAglERPDSGtILFGGEDATDVPVQE----RNVGFVFQHYALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 953 ALQFSAYLR-QSNKISKKEKDDYVDYVIDLLEMTDYADALvgvaGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 1031
Cdd:cd03296 94 NVAFGLRVKpRSERPPEAEIRAKVHELLKLVQLDWLADRY----PAQLSGGQRQRVALARALAVEPKVLL-LDEPFGALD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 353526216 1032 SQTAWSICKLMRKLAD--HGQAILCTIHQPSALIMAefDKLLFLQKG 1076
Cdd:cd03296 169 AKVRKELRRWLRRLHDelHVTTVFVTHDQEEALEVA--DRVVVMNKG 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
876-1057 |
2.49e-16 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 79.37 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTLLN--CLSERVTTGIItdgerLVNGHALDS-------SFQRSIGYVQQQDVHLE 946
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKliYKEELPTSGTI-----RVNGQDVSDlrgraipYLRRKIGVVFQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 947 TTTVREALQFSayLRQSNKiSKKEKDDYVDYVIDLLEMTDYADALvgvaGEGLNVEQRKRLTIGVELVAKPKLLLfLDEP 1026
Cdd:cd03292 92 DRNVYENVAFA--LEVTGV-PPREIRKRVPAALELVGLSHKHRAL----PAELSGGEQQRVAIARAIVNSPTILI-ADEP 163
|
170 180 190
....*....|....*....|....*....|.
gi 353526216 1027 TSGLDSQTAWSICKLMRKLADHGQAILCTIH 1057
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
854-1057 |
3.96e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 79.30 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 854 REIFFWRDLTYQVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLServttGII--TDGERLVNGHAldsSF 931
Cdd:cd03267 15 KEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILS-----GLLqpTSGEVRVAGLV---PW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 932 QRSIGYVQQQDVHLETTT-------VREALQFsayLRQSNKISKKEKDDYVDYVIDLLEMTDYADALVgvagEGLNVEQR 1004
Cdd:cd03267 87 KRRKKFLRRIGVVFGQKTqlwwdlpVIDSFYL---LAAIYDLPPARFKKRLDELSELLDLEELLDTPV----RQLSLGQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 353526216 1005 KRLTIGVELVAKPKlLLFLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIH 1057
Cdd:cd03267 160 MRAEIAAALLHEPE-ILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSH 212
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
865-1103 |
4.17e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.00 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 865 QVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVT--TGIITDGERLVNGHALDSsfQRSIGYVQQQD 942
Cdd:PRK13537 12 NVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHpdAGSISLCGEPVPSRARHA--RQRVGVVPQFD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 943 VHLETTTVREALQ-FSAYLrqsnKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGLnveqRKRLTIGVELVAKPKLLL 1021
Cdd:PRK13537 90 NLDPDFTVRENLLvFGRYF----GLSAAAARALVPPLLEFAKLENKADAKVGELSGGM----KRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1022 fLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHqpsalIMAEFDKL---LFLQKGGRTAYFGELGENCQTMI--NYF 1096
Cdd:PRK13537 162 -LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH-----FMEEAERLcdrLCVIEEGRKIAEGAPHALIESEIgcDVI 235
|
....*..
gi 353526216 1097 EKYGADP 1103
Cdd:PRK13537 236 EIYGPDP 242
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
872-1059 |
4.73e-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: 83.18 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLservtTGIIT--DGERLVNG---HALDSSFQRSIGYVQQQDVHLE 946
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATL-----AGLLDplQGEVTLDGvpvSSLDQDEVRRRVSVCAQDAHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 947 TTTVREALqfsaylrqsnKISKKEKDDyvDYVIDLLE---MTDYADALVG----VAGEG---LNVEQRKRLTIGVELVAK 1016
Cdd:TIGR02868 422 DTTVRENL----------RLARPDATD--EELWAALErvgLADWLRALPDgldtVLGEGgarLSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 353526216 1017 PKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQP 1059
Cdd:TIGR02868 490 APILL-LDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
883-1076 |
5.18e-16 |
|
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: 78.79 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 883 VKPGQITALMGASGAGKTTLLNCLServttG--IITDGERLVNGHALD----SSFQRSIGYVqQQDVHLETTTVREALQF 956
Cdd:cd03245 27 IRAGEKVAIIGRVGSGKSTLLKLLA-----GlyKPTSGSVLLDGTDIRqldpADLRRNIGYV-PQDVTLFYGTLRDNITL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 957 SAYLRQSNKISKkekddyvdyVIDLLEMTDYA-------DALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 1029
Cdd:cd03245 101 GAPLADDERILR---------AAELAGVTDFVnkhpnglDLQIGERGRGLSGGQRQAVALARALLNDPPILL-LDEPTSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 353526216 1030 LDSQTAWSICKLMRKLADHGQAILCTiHQPSALIMAefDKLLFLQKG 1076
Cdd:cd03245 171 MDMNSEERLKERLRQLLGDKTLIIIT-HRPSLLDLV--DRIIVMDSG 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
872-1080 |
8.81e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.90 E-value: 8.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTgiiTDGERLVNGHAL----DSSFQRSIGYVQQQDVHLET 947
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP---QSGTVFLGDKPIsmlsSRQLARRLALLPQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 948 TTVREALQF--SAYLRQSNKISKKEKdDYVDYVIDLLEMTDYADALVgvagEGLNVEQRKRLTIGVELvAKPKLLLFLDE 1025
Cdd:PRK11231 91 ITVRELVAYgrSPWLSLWGRLSAEDN-ARVNQAMEQTRINHLADRRL----TDLSGGQRQRAFLAMVL-AQDTPVVLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 353526216 1026 PTSGLDSQTAWSICKLMRKLADHGQAILCTIH---QPSALImaefDKLLFLQKGGRTA 1080
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQASRYC----DHLVVLANGHVMA 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
872-1034 |
1.38e-15 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 77.97 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLsERVTTgiITDGERLVNGHALDS----SFQRSIGYVQQQDVhLET 947
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL-ERFYD--PTSGEILLDGVDIRDlnlrWLRSQIGLVSQEPV-LFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 948 TTVREALQFSAYLRQSNKISKKEKDDYVDYVIDLLEmtDYADALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPT 1027
Cdd:cd03249 91 GTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLP--DGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILL-LDEAT 167
|
....*..
gi 353526216 1028 SGLDSQT 1034
Cdd:cd03249 168 SALDAES 174
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
883-1057 |
2.31e-15 |
|
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: 82.37 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 883 VKPGQITALMGASGAGKTTLLNCLSERVTtgiITDGERLVNGHAL---DSSFQRSIGYVQQQDVHLETTTVREALQFSAY 959
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTT---VTSGDATVAGKSIltnISDVHQNMGYCPQFDAIDDLLTGREHLYLYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 960 LRqsnKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSIC 1039
Cdd:TIGR01257 2039 LR---GVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGG----NKRKLSTAIALIGCPPLVL-LDEPTTGMDPQARRMLW 2110
|
170
....*....|....*...
gi 353526216 1040 KLMRKLADHGQAILCTIH 1057
Cdd:TIGR01257 2111 NTIVSIIREGRAVVLTSH 2128
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
167-343 |
2.37e-15 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 80.87 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDI-ERHYRGDVIYSAEtDVHFPHLS 245
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLA----GLLDPLQGEVTLDGVPVSSLdQDEVRRRVSVCAQ-DAHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 246 VGDTLEFAarlrtpqnRGEGIDRETYAKhMASVYMATY--GLSHTRNTNVGNDFVRgVSGGERKRVSIAEASLSGANIQC 323
Cdd:TIGR02868 425 VRENLRLA--------RPDATDEELWAA-LERVGLADWlrALPDGLDTVLGEGGAR-LSGGERQRLALARALLADAPILL 494
|
170 180
....*....|....*....|
gi 353526216 324 WDNATRGLDSATALEFIRAL 343
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDL 514
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
863-1045 |
3.79e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 78.69 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 863 TYQVKIKKedRVILDHVDGWVKPGQITALMGASGAGKTTLLNC--LSERVTTG-IITDGERLVnghALDSS----FQRSI 935
Cdd:PRK11153 10 VFPQGGRT--IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCinLLERPTSGrVLVDGQDLT---ALSEKelrkARRQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 936 GYVQQqdvH---LETTTVREALQFSayLRQSNKiSKKEKDDYVDYVIDLLEMTDYADA----LVGvaGeglnveQRKRLT 1008
Cdd:PRK11153 85 GMIFQ---HfnlLSSRTVFDNVALP--LELAGT-PKAEIKARVTELLELVGLSDKADRypaqLSG--G------QKQRVA 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 353526216 1009 IGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 1045
Cdd:PRK11153 151 IARALASNPKVLL-CDEATSALDPATTRSILELLKDI 186
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
872-1076 |
6.48e-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: 75.73 E-value: 6.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSeR---VTTGIIT-DGE--RLVNGHaldsSFQRSIGYVqQQDVHL 945
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF-RfydVSSGSILiDGQdiREVTLD----SLRRAIGVV-PQDTVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 946 ETTTVREALQF---SAYLRQSNKISKKEKddyVDYVIdlLEMTDYADALVGVAGEGLNVEQRKRLTIGVELVAKPkLLLF 1022
Cdd:cd03253 87 FNDTIGYNIRYgrpDATDEEVIEAAKAAQ---IHDKI--MRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP-PILL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 353526216 1023 LDEPTSGLDSQTAWSICKLMRKLADHGQAILCTiHQPSALIMAefDKLLFLQKG 1076
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIA-HRLSTIVNA--DKIIVLKDG 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
177-343 |
6.98e-15 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 75.21 E-value: 6.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 177 PGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIERHYRGDVIYSAETDVHFPHLSVGDTLEFAARL 256
Cdd:COG4133 27 AGEALALTGPNGSGKTTLLRILA----GLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADGLKPELTVRENLRFWAAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 257 rtpqnRGEGIDRETYAKHMASVymatyGLSHTRNTnvgndFVRGVSGGERKRVSIAEASLSGANIqcW--DNATRGLDSA 334
Cdd:COG4133 103 -----YGLRADREAIDEALEAV-----GLAGLADL-----PVRQLSAGQKRRVALARLLLSPAPL--WllDEPFTALDAA 165
|
....*....
gi 353526216 335 TALEFIRAL 343
Cdd:COG4133 166 GVALLAELI 174
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
877-1076 |
1.23e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.41 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 877 DHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIIT-DGERL-------VNGHALDSSFQ-----RSIGYVQQ- 940
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTgfYKPTGGTILlRGQHIeglpghqIARMGVVRTFQhvrlfREMTVIENl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 941 ---QDVHLETTTVREALQFSAYLRqsnkiSKKEKDDYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELVAKP 1017
Cdd:PRK11300 102 lvaQHQQLKTGLFSGLLKTPAFRR-----AESEALDRAATWLERVGLLEHANRQAGNLAYG----QQRRLEIARCMVTQP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1018 KLLLfLDEPTSGLDSQTAWSICKLMRKLAD-HGQAILCTIHQPSaLIMAEFDKLLFLQKG 1076
Cdd:PRK11300 173 EILM-LDEPAAGLNPKETKELDELIAELRNeHNVTVLLIEHDMK-LVMGISDRIYVVNQG 230
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
871-1076 |
1.53e-14 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 73.02 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 871 EDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLservtTGII--TDGERLVNGHALDS----SFQRSIGYVQQqDVH 944
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLI-----LGLLrpTSGRVRLDGADISQwdpnELGDHVGYLPQ-DDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 945 LETTTVREalqfsaylrqsNKISkkekddyvdyvidllemtdyadalvgvAGeglnveQRKRLTIGVELVAKPKLLlFLD 1024
Cdd:cd03246 87 LFSGSIAE-----------NILS---------------------------GG------QRQRLGLARALYGNPRIL-VLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 353526216 1025 EPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSALIMAefDKLLFLQKG 1076
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASA--DRILVLEDG 171
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
871-1076 |
3.27e-14 |
|
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: 73.44 E-value: 3.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 871 EDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIITDGERLVNGhaLDSSfQRSIGYVQQQDVHLETT 948
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAglEEPTSGRIYIGGRDVTD--LPPK-DRDIAMVFQNYALYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 949 TVREALQFSAYLRqsnKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELVAKPKLLLfLDEPTS 1028
Cdd:cd03301 88 TVYDNIAFGLKLR---KVPKDEIDERVREVAELLQIEHLLDRKPKQLSGG----QRQRVALGRAIVREPKVFL-MDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 353526216 1029 GLDS----QTAWSICKLMRKLadhGQAILCTIH-QPSALIMAefDKLLFLQKG 1076
Cdd:cd03301 160 NLDAklrvQMRAELKRLQQRL---GTTTIYVTHdQVEAMTMA--DRIAVMNDG 207
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
870-1059 |
3.36e-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: 72.91 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 870 KEDRVILDHVDGWVKPGQITALMGASGAGKTTLLnclseRVTTGII--TDGERLVNGHALD---SSFQRSIGYVQQQDVH 944
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLL-----RILAGLSppLAGRVLLNGGPLDfqrDSIARGLLYLGHAPGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 945 LETTTVREALQFSAYLrqsnkiskkEKDDYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELVAKPKLLLfLD 1024
Cdd:cd03231 85 KTTLSVLENLRFWHAD---------HSDEQVEEALARVGLNGFEDRPVAQLSAG----QQRRVALARLLLSGRPLWI-LD 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 353526216 1025 EPTSGLDSQtawSICKLMRKLADH---GQAILCTIHQP 1059
Cdd:cd03231 151 EPTTALDKA---GVARFAEAMAGHcarGGMVVLTTHQD 185
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
872-1083 |
4.09e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 75.84 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIITDGERLVNGhaLDSSfQRSIGYVQQQDV---HLe 946
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAglEDITSGDLFIGEKRMND--VPPA-ERGVGMVFQSYAlypHL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 947 ttTVREALQFSAYLrqsNKISKKEKDDYVDYVIDLLEMtdyaDALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfLDEP 1026
Cdd:PRK11000 91 --SVAENMSFGLKL---AGAKKEEINQRVNQVAEVLQL----AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL-LDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 353526216 1027 TSGLDS----QTAWSICKLMRKLADhgQAILCTIHQPSALIMAefDKLLFLQkGGRTAYFG 1083
Cdd:PRK11000 161 LSNLDAalrvQMRIEISRLHKRLGR--TMIYVTHDQVEAMTLA--DKIVVLD-AGRVAQVG 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
867-1057 |
4.99e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.39 E-value: 4.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 867 KIKKEDRVILDhVDGWVKPGQITALMGASGAGKTT---LLNCLSERVTTGIITDGERlVNGHALDSSFQRSIGYVQQQDV 943
Cdd:PRK10895 11 KAYKGRRVVED-VSLTVNSGEIVGLLGPNGAGKTTtfyMVVGIVPRDAGNIIIDDED-ISLLPLHARARRGIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 944 HLETTTVREALQfsAYLRQSNKISKKEKDDYVDYVIDLLEMTDYADALvgvaGEGLNVEQRKRLTIGVELVAKPKLLLfL 1023
Cdd:PRK10895 89 IFRRLSVYDNLM--AVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM----GQSLSGGERRRVEIARALAANPKFIL-L 161
|
170 180 190
....*....|....*....|....*....|....
gi 353526216 1024 DEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 1057
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDH 195
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
866-1076 |
5.93e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.81 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 866 VKIKKEDRVILDHvDGWV---------KPGQITALMGASGAGKTTLLNCLServttGIIT-DGERLVNG---HALD-SSF 931
Cdd:PRK11174 348 VTIEAEDLEILSP-DGKTlagplnftlPAGQRIALVGPSGAGKTSLLNALL-----GFLPyQGSLKINGielRELDpESW 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 932 QRSIGYVqQQDVHLETTTVREALQFSAYLRQSNKISKKEKDDYVDYVIDLLEM-TDYAdalVGVAGEGLNVEQRKRLTIG 1010
Cdd:PRK11174 422 RKHLSWV-GQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQgLDTP---IGDQAAGLSVGQAQRLALA 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 353526216 1011 VELVAKPKLLLfLDEPTSGLDSQtawSICKLMRKL--ADHGQAILCTIHQPSALimAEFDKLLFLQKG 1076
Cdd:PRK11174 498 RALLQPCQLLL-LDEPTASLDAH---SEQLVMQALnaASRRQTTLMVTHQLEDL--AQWDQIWVMQDG 559
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
860-1057 |
6.69e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 73.27 E-value: 6.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKikkeDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTgiiTDGERLVNGHALDS------SFQR 933
Cdd:PRK13548 6 RNLSVRLG----GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSP---DSGEVRLNGRPLADwspaelARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 934 SigyVQQQDVHLE-TTTVREALQFSAYLRQSnkiSKKEKDDYVDYVIDLLEMTDYAD----ALVGvaGEglnvEQRkrlt 1008
Cdd:PRK13548 79 A---VLPQHSSLSfPFTVEEVVAMGRAPHGL---SRAEDDALVAAALAQVDLAHLAGrdypQLSG--GE----QQR---- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 353526216 1009 igVEL---------VAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIH 1057
Cdd:PRK13548 143 --VQLarvlaqlwePDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLH 199
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
175-378 |
9.42e-14 |
|
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: 72.15 E-value: 9.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 175 MRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIERHYRGDVIYSAETDVHFPHLSVGDTLEFAA 254
Cdd:cd03263 25 VYKGEIFGLLGHNGAGKTTTLKMLT----GELRPTSGTAYINGYSIRTDRKAARQSLGYCPQFDALFDELTVREHLRFYA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 255 RLRtpqnrgeGIdRETYAKHMASVYMATYGLSHTRNTnvgndFVRGVSGGERKRVSIAEASLSGANIQCWDNATRGLDSA 334
Cdd:cd03263 101 RLK-------GL-PKSEIKEEVELLLRVLGLTDKANK-----RARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 353526216 335 T---ALEFIRALKTSATILDTTPLIaiyqcsQDAYELFDNVVVLYEG 378
Cdd:cd03263 168 SrraIWDLILEVRKGRSIILTTHSM------DEAEALCDRIAIMSDG 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
872-1103 |
1.70e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 73.71 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLlnclsERVTTGIIT--DGERLVNGHALDS---SFQRSIGYVQQQDVHLE 946
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTI-----ARMILGMTSpdAGKITVLGVPVPArarLARARIGVVPQFDNLDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 947 TTTVREALQ-FSAYLRqsnkISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGLnveqRKRLTIGVELVAKPKLLLfLDE 1025
Cdd:PRK13536 128 EFTVRENLLvFGRYFG----MSTREIEAVIPSLLEFARLESKADARVSDLSGGM----KRRLTLARALINDPQLLI-LDE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1026 PTSGLDSQTAWSICKLMRKLADHGQAILCTIHqpsalIMAEF----DKLLFLQKG-----GRTAYFGELGENCQTMinyf 1096
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLARGKTILLTTH-----FMEEAerlcDRLCVLEAGrkiaeGRPHALIDEHIGCQVI---- 269
|
....*..
gi 353526216 1097 EKYGADP 1103
Cdd:PRK13536 270 EIYGGDP 276
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
860-1057 |
2.34e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 72.03 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKikkEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLServttGII--TDGERLVNGHALDSS------F 931
Cdd:PRK13639 5 RDLKYSYP---DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFN-----GILkpTSGEVLIKGEPIKYDkkslleV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 932 QRSIGYV-QQQDVHLETTTVREALQFSAYlrqSNKISKKEKDDYVDYVIDLLEMTDYADAlvgvAGEGLNVEQRKRLTIG 1010
Cdd:PRK13639 77 RKTVGIVfQNPDDQLFAPTVEEDVAFGPL---NLGLSKEEVEKRVKEALKAVGMEGFENK----PPHHLSGGQKKRVAIA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 353526216 1011 VELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 1057
Cdd:PRK13639 150 GILAMKPEIIV-LDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
868-1058 |
3.47e-13 |
|
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: 70.73 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 868 IKKE--DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIIT-DGERLVNGHAldssFQRSIGYVQQQD 942
Cdd:cd03300 6 VSKFygGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAgfETPTSGEILlDGKDITNLPP----HKRPVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 943 V---HLettTVREALQFSAYLRqsnKISKKEKDDYVDYVIDLLEMTDYA----DALVGvaGeglnveQRKRLTIGVELVA 1015
Cdd:cd03300 82 AlfpHL---TVFENIAFGLRLK---KLPKAEIKERVAEALDLVQLEGYAnrkpSQLSG--G------QQQRVAIARALVN 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 353526216 1016 KPKLLLfLDEPTSGLDsqtawsicklmRKLADHGQAILCTIHQ 1058
Cdd:cd03300 148 EPKVLL-LDEPLGALD-----------LKLRKDMQLELKRLQK 178
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
165-331 |
4.58e-13 |
|
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: 70.16 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 165 FDILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDG-----LSPHDIERhyRGdVIYSAETDV 239
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIM----GLLPPRSGSIRFDGrditgLPPHERAR--AG-IGYVPEGRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 240 HFPHLSVGDTLEFAARLRTPQNRGEGIDRetyakhmasVYMATYGLSHTRNTNVGNdfvrgVSGGERKRVSIAEASLSGA 319
Cdd:cd03224 86 IFPELTVEENLLLGAYARRRAKRKARLER---------VYELFPRLKERRKQLAGT-----LSGGEQQMLAIARALMSRP 151
|
170
....*....|..
gi 353526216 320 NIQCWDNATRGL 331
Cdd:cd03224 152 KLLLLDEPSEGL 163
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
860-1059 |
4.94e-13 |
|
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: 69.31 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQvkikKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLnclseRVTTGII--TDGERLVNGHALD---SSFQRS 934
Cdd:TIGR01189 4 RNLACS----RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLL-----RILAGLLrpDSGEVRWNGTPLAeqrDEPHEN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 935 IGYVQQQDVHLETTTVREALQFSAYLRQSnkiskkeKDDYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELV 1014
Cdd:TIGR01189 75 ILYLGHLPGLKPELSALENLHFWAAIHGG-------AQRTIEDALAAVGLTGFEDLPAAQLSAG----QQRRLALARLWL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 353526216 1015 AKPKLLLfLDEPTSGLDSQtawSICKLMRKLADH---GQAILCTIHQP 1059
Cdd:TIGR01189 144 SRRPLWI-LDEPTTALDKA---GVALLAGLLRAHlarGGIVLLTTHQD 187
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
863-1057 |
5.86e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 71.66 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 863 TYQVKIKKED-------------RVI--LDHVDGWVKPGQITALMGASGAGKTTLLNCLservtTGII--TDGERLVNGH 925
Cdd:COG4586 10 TYRVYEKEPGlkgalkglfrreyREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKML-----TGILvpTSGEVRVLGY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 926 ---ALDSSFQRSIGYV----QQQDVHLettTVREALQfsaYLRQSNKISKKEKDDYVDYVIDLLEMTDYadalvgvageg 998
Cdd:COG4586 85 vpfKRRKEFARRIGVVfgqrSQLWWDL---PAIDSFR---LLKAIYRIPDAEYKKRLDELVELLDLGEL----------- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 999 LNVEQRKrLTIG----VELVA----KPKlLLFLDEPTSGLD--SQTAwsICKLMRKL-ADHGQAILCTIH 1057
Cdd:COG4586 148 LDTPVRQ-LSLGqrmrCELAAallhRPK-ILFLDEPTIGLDvvSKEA--IREFLKEYnRERGTTILLTSH 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
176-378 |
9.05e-13 |
|
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: 69.09 E-value: 9.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 176 RPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDG-----LSPHdierhyRGDVIYSAETDVHFPHLSVGDTL 250
Cdd:cd03259 24 EPGEFLALLGPSGCGKTTLLRLIA----GLERPDSGEILIDGrdvtgVPPE------RRNIGMVFQDYALFPHLTVAENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 251 EFAARLRtpqnrgeGIDRETYAKHMASVymatygLSHTRNTNVGNDFVRGVSGGERKRVSIAEASLSGANIQCWDNATRG 330
Cdd:cd03259 94 AFGLKLR-------GVPKAEIRARVREL------LELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 353526216 331 LDSATALEFIRALKtsaTILDTTPLIAIY----QcsQDAYELFDNVVVLYEG 378
Cdd:cd03259 161 LDAKLREELREELK---ELQRELGITTIYvthdQ--EEALALADRIAVMNEG 207
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
872-1057 |
9.82e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 69.73 E-value: 9.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSeRVTTgiITDGERLVNGHALDSSFQR------SIgyvQQQDVHL 945
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIS-RLLP--PDSGEVLVDGLDVATTPSRelakrlAI---LRQENHI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 946 ETT-TVREALQFSAYLRQSNKISKKEKdDYVDYVIDLLEMTDYA----DALVGvaGeglnveQRKRLTIGVELVAKPKLL 1020
Cdd:COG4604 87 NSRlTVRELVAFGRFPYSKGRLTAEDR-EIIDEAIAYLDLEDLAdrylDELSG--G------QRQRAFIAMVLAQDTDYV 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 353526216 1021 LfLDEPTSGLDSQTAWSICKLMRKLAD-HGQAILCTIH 1057
Cdd:COG4604 158 L-LDEPLNNLDMKHSVQMMKLLRRLADeLGKTVVIVLH 194
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
860-1076 |
1.12e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 69.78 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKikkeDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIITDGERLVNGhaldssfQRSIGy 937
Cdd:PRK11264 7 KNLVKKFH----GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINllEQPEAGTIRVGDITIDT-------ARSLS- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 938 vQQQdvhletTTVREALQFSAYLRQS-----------NKIS-----KKE-KDDYVDYVIDLLemtdyadALVGVAGEG-- 998
Cdd:PRK11264 75 -QQK------GLIRQLRQHVGFVFQNfnlfphrtvleNIIEgpvivKGEpKEEATARARELL-------AKVGLAGKEts 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 999 ----LNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPS-ALIMAefDKLLFL 1073
Cdd:PRK11264 141 yprrLSGGQQQRVAIARALAMRPEVILF-DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSfARDVA--DRAIFM 217
|
...
gi 353526216 1074 QKG 1076
Cdd:PRK11264 218 DQG 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
876-1033 |
1.35e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.40 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTG-IITDGERLvnghALDSSFQRSIGYVQQQDVHLETTTVRE 952
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAgfEQPTAGqIMLDGVDL----SHVPPYQRPINMMFQSYALFPHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 953 ALQFSayLRQsNKISKKEKDDYVDYVIDLLEMTDYAdalvGVAGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS 1032
Cdd:PRK11607 111 NIAFG--LKQ-DKLPKAEIASRVNEMLGLVHMQEFA----KRKPHQLSGGQRQRVALARSLAKRPKLLL-LDEPMGALDK 182
|
.
gi 353526216 1033 Q 1033
Cdd:PRK11607 183 K 183
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
860-1076 |
1.45e-12 |
|
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: 67.72 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKikKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLservtTGII--TDGERLVNGH---ALDSSFQRS 934
Cdd:cd03247 4 NNVSFSYP--EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLL-----TGDLkpQQGEITLDGVpvsDLEKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 935 IGYVQQQdVHLETTTVREAL--QFSaylrqsnkiskkekddyvdyvidllemtdyadalvgvAGEglnveqRKRLTIGVE 1012
Cdd:cd03247 77 ISVLNQR-PYLFDTTLRNNLgrRFS-------------------------------------GGE------RQRLALARI 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 353526216 1013 LVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADhGQAILCTIHQPSAliMAEFDKLLFLQKG 1076
Cdd:cd03247 113 LLQDAPIVL-LDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTG--IEHMDKILFLENG 172
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
873-1057 |
1.68e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 68.90 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 873 RVILDHVDGWVKPGQITALMGASGAGKTTLLNClservTTGII--TDGERLVNGHalDSS----FQRS---IGYVQQqdv 943
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYM-----IVGLVkpDSGRIFLDGE--DIThlpmHKRArlgIGYLPQ--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 944 hlETT-----TVREALQfsAYLRQSnKISKKEKDDYVDYVIDLLEMTD----YADALVGvaGEglnveqRKRLTIGVELV 1014
Cdd:COG1137 86 --EASifrklTVEDNIL--AVLELR-KLSKKEREERLEELLEEFGITHlrksKAYSLSG--GE------RRRVEIARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 353526216 1015 AKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 1057
Cdd:COG1137 153 TNPKFIL-LDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDH 194
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
883-1057 |
1.83e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.49 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 883 VKPGQITALMGASGAGKTTLLNCLServttGII--TDGERLVNGHALDSS------FQRSIGYV-QQQDVHLETTTVREA 953
Cdd:PRK13636 29 IKKGEVTAILGGNGAGKSTLFQNLN-----GILkpSSGRILFDGKPIDYSrkglmkLRESVGMVfQDPDNQLFSASVYQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 954 LQFSAYlrqSNKISKKEKDDYVDYVidlLEMTDYADaLVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQ 1033
Cdd:PRK13636 104 VSFGAV---NLKLPEDEVRKRVDNA---LKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV-LDEPTAGLDPM 175
|
170 180
....*....|....*....|....*
gi 353526216 1034 TAWSICKLMRKLADH-GQAILCTIH 1057
Cdd:PRK13636 176 GVSEIMKLLVEMQKElGLTIIIATH 200
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
856-1057 |
1.90e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.43 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 856 IFFWRDLTYQVKikkeDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTgiiTDGERLVNGHALDS----SF 931
Cdd:PRK10575 11 TFALRNVSFRVP----GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPP---SEGEILLDAQPLESwsskAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 932 QRSIGYVQQQDVHLETTTVREALQFSAYLRQSN----KISKKEKddyVDYVIDLLEMTDYADALVgvagEGLNVEQRKRL 1007
Cdd:PRK10575 84 ARKVAYLPQQLPAAEGMTVRELVAIGRYPWHGAlgrfGAADREK---VEEAISLVGLKPLAHRLV----DSLSGGERQRA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 353526216 1008 TIGVeLVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIH 1057
Cdd:PRK10575 157 WIAM-LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLH 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
876-1053 |
2.76e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.20 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIIT-DGERLVNGHALDsSFQRSIGYVqQQDVHL-ETTTVR 951
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSgvYQPDSGEILlDGEPVRFRSPRD-AQAAGIAII-HQELNLvPNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 952 EALQFSAYLRQSNKISKKE--KD-----DYVDYVIDLlemtdyaDALVGvageGLNVEQRKRLTIGVELVAKPKLLLfLD 1024
Cdd:COG1129 98 ENIFLGREPRRGGLIDWRAmrRRarellARLGLDIDP-------DTPVG----DLSVAQQQLVEIARALSRDARVLI-LD 165
|
170 180
....*....|....*....|....*....
gi 353526216 1025 EPTSGLDSQTAWSICKLMRKLADHGQAIL 1053
Cdd:COG1129 166 EPTASLTEREVERLFRIIRRLKAQGVAII 194
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
883-1094 |
3.36e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 71.29 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 883 VKPGQITALMGASGAGKTT---LLNCLSERVTTGIITDGERLV--NGHALdssfQRSIGYVQQQDVhLETTTVREALQFS 957
Cdd:TIGR00958 504 LHPGEVVALVGPSGSGKSTvaaLLQNLYQPTGGQVLLDGVPLVqyDHHYL----HRQVALVGQEPV-LFSGSVRENIAYG 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 958 AYLRQSNKISKKEKDDYVDYVIdlLEMTDYADALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWS 1037
Cdd:TIGR00958 579 LTDTPDEEIMAAAKAANAHDFI--MEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLI-LDEATSALDAECEQL 655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 353526216 1038 ICKLMRKladHGQAILCTIHQPSALIMAefDKLLFLQKGGrtayFGELGENCQTMIN 1094
Cdd:TIGR00958 656 LQESRSR---ASRTVLLIAHRLSTVERA--DQILVLKKGS----VVEMGTHKQLMED 703
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
883-1057 |
7.45e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.17 E-value: 7.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 883 VKPGQITALMGASGAGKTTLLNCLServttGIIT-DGERLVNGHALDS------SFQRsiGYVQQQDVHLETTTVREALQ 955
Cdd:COG4138 19 VNAGELIHLIGPNGAGKSTLLARMA-----GLLPgQGEILLNGRPLSDwsaaelARHR--AYLSQQQSPPFAMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 956 fsayLRQSNKISKKEKDDYVDYVIDLLEMTDYAD----ALVGvaGEglnvEQRKRLTiGVELVAKPKL-----LLFLDEP 1026
Cdd:COG4138 92 ----LHQPAGASSEAVEQLLAQLAEALGLEDKLSrpltQLSG--GE----WQRVRLA-AVLLQVWPTInpegqLLLLDEP 160
|
170 180 190
....*....|....*....|....*....|...
gi 353526216 1027 TSGLD--SQTAwsICKLMRKLADHGQAILCTIH 1057
Cdd:COG4138 161 MNSLDvaQQAA--LDRLLRELCQQGITVVMSSH 191
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
875-1076 |
8.46e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.73 E-value: 8.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 875 ILDHVDGWVKPGQITALMGASGAGKTTLLnclservttGII------TDGERLVNGHALDSSFQ--------RSIGYVQQ 940
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLL---------AILaglddgSSGEVSLVGQPLHQMDEearaklraKHVGFVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 941 QDVHLETTTVREALQFSAYLRQSNKISKKEKddyvdyVIDLLEMTDYADALVGVAGEGLNVEQrKRLTIGVELVAKPKlL 1020
Cdd:PRK10584 96 SFMLIPTLNALENVELPALLRGESSRQSRNG------AKALLEQLGLGKRLDHLPAQLSGGEQ-QRVALARAFNGRPD-V 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 353526216 1021 LFLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQPSalIMAEFDKLLFLQKG 1076
Cdd:PRK10584 168 LFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQ--LAARCDRRLRLVNG 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
860-1036 |
8.95e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 69.32 E-value: 8.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVkikkEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLServttGII--TDGERLVNGHAldssfqrSIGY 937
Cdd:COG0488 2 ENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILA-----GELepDSGEVSIPKGL-------RIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 938 VQQQDVHLETTTVREALQ-----FSAYLRQSNKISKKEkDDYVDYVIDLLEMTDYADALVGVAGE--------GLNVE-- 1002
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVLdgdaeLRALEAELEELEAKL-AEPDEDLERLAELQEEFEALGGWEAEaraeeilsGLGFPee 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 353526216 1003 ------------QRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT-AW 1036
Cdd:COG0488 145 dldrpvselsggWRRRVALARALLSEPDLLL-LDEPTNHLDLESiEW 190
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
874-1053 |
1.38e-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: 64.37 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 874 VILDHVDGWVKPGQITALMGASGAGKTTLLNCLServttGII--TDGERLVNGHALDS-----SFQRSIGYVQQqdvhle 946
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILS-----GLYkpDSGEILVDGKEVSFasprdARRAGIAMVYQ------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 947 tttvrealqfsaylrqsnkiskkekddyvdyvidllemtdyadalvgvagegLNVEQRKRLTIGVELVAKPKLLLfLDEP 1026
Cdd:cd03216 83 ----------------------------------------------------LSVGERQMVEIARALARNARLLI-LDEP 109
|
170 180
....*....|....*....|....*..
gi 353526216 1027 TSGLDSQTAWSICKLMRKLADHGQAIL 1053
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVI 136
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
866-1079 |
1.48e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.75 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 866 VKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVttgiitdgerlvnghaldsSFQRSIGYVQQQDVHL 945
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL-------------------KGTPVAGCVDVPDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 946 -ETTTVREALqfsaylrqsnkiskkEKDDYVDYVIDLLEMTDYADALVGVA--GEgLNVEQRKRLTIGVELVAKPKLLLf 1022
Cdd:COG2401 97 gREASLIDAI---------------GRKGDFKDAVELLNAVGLSDAVLWLRrfKE-LSTGQKFRFRLALLLAERPKLLV- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 353526216 1023 LDEPTSGLDSQTAWSICKLMRKLAD-HG-QAILCTIHQP--SALIMaefDKLLFLQKGGRT 1079
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKLARrAGiTLVVATHHYDviDDLQP---DLLIFVGYGGVP 217
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
876-1087 |
1.56e-11 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 65.82 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTLLNCLservtTGIIT--DGERLVNGHALD--SSFQRSIGYVQQQDVHLETTTVR 951
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETI-----AGFIKpdSGKILLNGKDITnlPPEKRDISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 952 EALQFSAYLRqsnKISKKEKDDYVDYVIDLLEMtdyaDALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 1031
Cdd:cd03299 90 KNIAYGLKKR---KVDKKEIERKVLEIAEMLGI----DHLLNRKPETLSGGEQQRVAIARALVVNPKILL-LDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1032 SQTAWSICKLMRKLadHGQAILCTIH----QPSALIMAefDKLLFLqKGGRTAYFGELGE 1087
Cdd:cd03299 162 VRTKEKLREELKKI--RKEFGVTVLHvthdFEEAWALA--DKVAIM-LNGKLIQVGKPEE 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
872-1080 |
1.58e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.94 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLnclseRVTTGIITD--GERLVNGHALDSSFQRSIGYvQQQDVHLETT- 948
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLL-----RAINGTLTPtaGTVLVAGDDVEALSARAASR-RVASVPQDTSl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 949 ----TVREALQFSAYLRQSNKISKKEKDD-YVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELV-AKPKLLlf 1022
Cdd:PRK09536 89 sfefDVRQVVEMGRTPHRSRFDTWTETDRaAVERAMERTGVAQFADRPVTSLSGG----ERQRVLLARALAqATPVLL-- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1023 LDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsaLIMAE--FDKLLFLQKGGRTA 1080
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHD---LDLAAryCDELVLLADGRVRA 219
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
883-1076 |
1.80e-11 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 65.18 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 883 VKPGQITALMGASGAGKTTLLNCLServttgiitdGE-RLVNGHaldSSFQRSIGYVQQQDvHLETTTVREALQFSAYLr 961
Cdd:cd03250 28 VPKGELVAIVGPVGSGKSSLLSALL----------GElEKLSGS---VSVPGSIAYVSQEP-WIQNGTIRENILFGKPF- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 962 qsnkiskkEKDDYvDYVIDL------LEMTDYADA-LVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 1034
Cdd:cd03250 93 --------DEERY-EKVIKAcalepdLEILPDGDLtEIGEKGINLSGGQKQRISLARAVYSDADIYL-LDDPLSAVDAHV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 353526216 1035 AWSICK--LMRKLADHGQAILCTiHQPSALimAEFDKLLFLQKG 1076
Cdd:cd03250 163 GRHIFEncILGLLLNNKTRILVT-HQLQLL--PHADQIVVLDNG 203
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
873-1045 |
2.06e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 66.26 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 873 RVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVttgIITDGERLVNGHALD--SSFQRS--IGYVqQQDVHLETT 948
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSL---PPDSGSILIDGKDVTklPEYKRAkyIGRV-FQDPMMGTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 949 ---TVRE--ALqfsAYLRQSNK-----ISKKEKDDYVDYVIDL---LE--MTDYADALVGvaGeglnveQRKRLTIGVEL 1013
Cdd:COG1101 95 psmTIEEnlAL---AYRRGKRRglrrgLTKKRRELFRELLATLglgLEnrLDTKVGLLSG--G------QRQALSLLMAT 163
|
170 180 190
....*....|....*....|....*....|..
gi 353526216 1014 VAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 1045
Cdd:COG1101 164 LTKPKLLL-LDEHTAALDPKTAALVLELTEKI 194
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
846-1076 |
2.70e-11 |
|
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: 65.18 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 846 GSVDFpenreiffwRDLTYQVKiKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLsERVTTgiITDGERLVNGH 925
Cdd:cd03248 10 GIVKF---------QNVTFAYP-TRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALL-ENFYQ--PQGGQVLLDGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 926 ALDS----SFQRSIGYVQQQDVhLETTTVREALQFSAYLRQSNKISKKEKDDYVDYVIDLLEMTDYADalVGVAGEGLNV 1001
Cdd:cd03248 77 PISQyehkYLHSKVSLVGQEPV-LFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTE--VGEKGSQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 353526216 1002 EQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPSALIMAefDKLLFLQKG 1076
Cdd:cd03248 154 GQKQRVAIARALIRNPQVLI-LDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVERA--DQILVLDGG 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
167-344 |
3.32e-11 |
|
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: 64.48 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDiERHYRGDVIYSAETDVHFPhLSV 246
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL----GLLKPTSGSIRVFGKPLEK-ERKRIGYVPQRRSIDRDFP-ISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 247 gdtLEFAARLRTPQNRGEG-IDRETYAKHMASvyMATYGLSHTRNTNVGNdfvrgVSGGERKRVSIAEASLSGANIQCWD 325
Cdd:cd03235 88 ---RDVVLMGLYGHKGLFRrLSKADKAKVDEA--LERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPDLLLLD 157
|
170
....*....|....*....
gi 353526216 326 NATRGLDSATALEFIRALK 344
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLR 176
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
860-1059 |
4.26e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 64.70 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVkikkEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCL----SERVTTG-IITDGERLVNghalDSSFQRS 934
Cdd:COG0396 4 KNLHVSV----EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghpKYEVTSGsILLDGEDILE----LSPDERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 935 ---IGYVQQQDVHLETTTVREALQFSAYLRQSNKISKKEKDDYVDYVIDLLEM-TDYADalvgvagEGLNVE----QRKR 1006
Cdd:COG0396 76 ragIFLAFQYPVEIPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLdEDFLD-------RYVNEGfsggEKKR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 353526216 1007 LTIGVELVAKPKLLLfLDEPTSGLDsqtAWS---ICKLMRKLADHGQAILCTIHQP 1059
Cdd:COG0396 149 NEILQMLLLEPKLAI-LDETDSGLD---IDAlriVAEGVNKLRSPDRGILIITHYQ 200
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
850-1092 |
6.53e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.73 E-value: 6.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 850 FPENREIF--FWRDLTYQVK-IKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCL---SERVTTGIITDGERLVN 923
Cdd:PRK09700 250 FNAMKENVsnLAHETVFEVRnVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLfgvDKRAGGEIRLNGKDISP 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 924 GHALDSsFQRSIGYVqqqdvhleTTTVREALQFSAY-LRQSNKISKKEKDDYVDYVIDLLEMTD---YADAlvgvAGEGL 999
Cdd:PRK09700 330 RSPLDA-VKKGMAYI--------TESRRDNGFFPNFsIAQNMAISRSLKDGGYKGAMGLFHEVDeqrTAEN----QRELL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1000 N-----VEQ---------RKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTihqPSAL--I 1063
Cdd:PRK09700 397 AlkchsVNQnitelsggnQQKVLISKWLCCCPEVIIF-DEPTRGIDVGAKAEIYKVMRQLADDGKVILMV---SSELpeI 472
|
250 260
....*....|....*....|....*....
gi 353526216 1064 MAEFDKLLFLQKGGRTAYFgelgENCQTM 1092
Cdd:PRK09700 473 ITVCDRIAVFCEGRLTQIL----TNRDDM 497
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
860-1076 |
8.51e-11 |
|
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: 62.93 E-value: 8.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVkikkEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCL----SERVTTGIIT-DGERLVNgHALDSSFQRS 934
Cdd:cd03217 4 KDLHVSV----GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghpKYEVTEGEILfKGEDITD-LPPEERARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 935 IGYVQQQDVHLETTTVREalqfsaYLRqsnkiskkekddYVDyvidllemtdyadalvgvagEGLNVEQRKRLTIGVELV 1014
Cdd:cd03217 79 IFLAFQYPPEIPGVKNAD------FLR------------YVN--------------------EGFSGGEKKRNEILQLLL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 353526216 1015 AKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSALIMAEFDKLLFLQKG 1076
Cdd:cd03217 121 LEPDLAI-LDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYDG 181
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
875-1076 |
9.60e-11 |
|
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: 63.28 E-value: 9.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 875 ILDHVDGWVKPGQITALMGASGAGKTTLLNCL---SERVTTGIITDGERL--VNGHALdssfQRSIGYVqQQDVHLETTT 949
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALfrlVELSSGSILIDGVDIskIGLHDL----RSRISII-PQDPVLFSGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 950 VREAL----QFS-AYLRQSNKISKkeKDDYVDYVIDLLemtdyaDALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfLD 1024
Cdd:cd03244 94 IRSNLdpfgEYSdEELWQALERVG--LKEFVESLPGGL------DTVVEEGGENLSVGQRQLLCLARALLRKSKILV-LD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 353526216 1025 EPTSGLDSQTAWSICKLMR-KLADHgqAILCTIHQPSALImaEFDKLLFLQKG 1076
Cdd:cd03244 165 EATASVDPETDALIQKTIReAFKDC--TVLTIAHRLDTII--DSDRILVLDKG 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
875-1076 |
1.13e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 63.78 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 875 ILDHVDGWVKPGQITALMGASGAGKTTLLNCLSE--------RVTTGIITDGERLVNghaLD-SSFQRSIGYVQQQDVHL 945
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielypeaRVSGEVYLDGQDIFK---MDvIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 946 ETTTVREALQFSAYLRQSNKiSKKEKDDYVDYVIDLLEMTDYADALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfLDE 1025
Cdd:PRK14247 95 PNLSIFENVALGLKLNRLVK-SKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLL-ADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 353526216 1026 PTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSALIMAefDKLLFLQKG 1076
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARIS--DYVAFLYKG 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
875-1076 |
1.27e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.00 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 875 ILDHVDGWVKPGQITALMGASGAGKTTLLNCLSeR---VTTGIItdgerLVNGHAL----DSSFQRSIGYVQQQdVHLet 947
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT-RawdPQQGEI-----LLNGQPIadysEAALRQAISVVSQR-VHL-- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 948 ttvrealqFSAYLRQSNKISKKEKDDyvDYVIDLLEMTDYADALVGvaGEGLNV------------EQRkRLTIGVELVA 1015
Cdd:PRK11160 426 --------FSATLRDNLLLAAPNASD--EALIEVLQQVGLEKLLED--DKGLNAwlgeggrqlsggEQR-RLGIARALLH 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 353526216 1016 KPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTiHQPSAliMAEFDKLLFLQKG 1076
Cdd:PRK11160 493 DAPLLL-LDEPTEGLDAETERQILELLAEHAQNKTVLMIT-HRLTG--LEQFDRICVMDNG 549
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
861-1057 |
1.58e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.98 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 861 DLTYQVKIKKEDRVILDhVDGWVKPGQITALMGASGAGKTTLLNCLSE--RVTTGIITDGERLVNGHALDSSFQ---RSI 935
Cdd:PRK13643 8 NYTYQPNSPFASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGllQPTEGKVTVGDIVVSSTSKQKEIKpvrKKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 936 GYVQQ--QDVHLETTTVREAlqfsAYLRQSNKISKKEKDDYVdyvIDLLEMTDYADALVGVAGEGLNVEQRKRLTIGVEL 1013
Cdd:PRK13643 87 GVVFQfpESQLFEETVLKDV----AFGPQNFGIPKEKAEKIA---AEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 353526216 1014 VAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 1057
Cdd:PRK13643 160 AMEPEVLV-LDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
825-1045 |
1.67e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.43 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 825 LDYQDEAeavNNEKFTEKGSTGSVDFpenREIFFwrdlTYQVKikkeDRVILDHVDGWVKPGQITALMGASGAGKTTLLN 904
Cdd:PRK11176 322 LDLEQEK---DEGKRVIERAKGDIEF---RNVTF----TYPGK----EVPALRNINFKIPAGKTVALVGRSGSGKSTIAN 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 905 CLSERVTtgiITDGERLVNGHALD----SSFQRSIGYVQQQdVHLETTTVREALqfsAYLRQsNKISKK--EKDDYVDYV 978
Cdd:PRK11176 388 LLTRFYD---IDEGEILLDGHDLRdytlASLRNQVALVSQN-VHLFNDTIANNI---AYART-EQYSREqiEEAARMAYA 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 353526216 979 IDLLE-MTDYADALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 1045
Cdd:PRK11176 460 MDFINkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILI-LDEATSALDTESERAIQAALDEL 526
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
871-1034 |
1.69e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.47 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 871 EDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERV--TTGIITDGERLvnghaldssfqrSIGYV-QQQDVHLET 947
Cdd:COG0488 326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELepDSGTVKLGETV------------KIGYFdQHQEELDPD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 948 TTVREALQfsaylRQSNKISKKEkddyvdyVIDLLEM----TDYADALVGV--AGEglnveqRKRLTIGVELVAKPKLLL 1021
Cdd:COG0488 394 KTVLDELR-----DGAPGGTEQE-------VRGYLGRflfsGDDAFKPVGVlsGGE------KARLALAKLLLSPPNVLL 455
|
170
....*....|...
gi 353526216 1022 fLDEPTSGLDSQT 1034
Cdd:COG0488 456 -LDEPTNHLDIET 467
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
167-378 |
1.98e-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: 62.10 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIERHYRGDVIYSA--ETDVHFPHL 244
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLN----GLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVfqNPDDQFFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 245 SVGDTLEFAarlrtPQNRgeGIDRETyAKHMASVYMATYGLSHTRNTNVGNdfvrgVSGGERKRVSIAEASLSGANIQCW 324
Cdd:cd03225 92 TVEEEVAFG-----LENL--GLPEEE-IEERVEEALELVGLEGLRDRSPFT-----LSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 353526216 325 DNATRGLDSATALEFIRALKTSATiLDTTPLIAIYQcSQDAYELFDNVVVLYEG 378
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHD-LDLLLELADRVIVLEDG 210
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
867-1045 |
2.22e-10 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 62.70 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 867 KIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTgiiTDGERLVNGH---ALD-SSFQRSIGYVQQQD 942
Cdd:cd03295 8 KRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEP---TSGEIFIDGEdirEQDpVELRRKIGYVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 943 VHLETTTVREALqfsAYLRQSNKISKKEKDDYVDYVIDLLEMTD------YADALVGvageglnvEQRKRLTIGVELVAK 1016
Cdd:cd03295 85 GLFPHMTVEENI---ALVPKLLKWPKEKIRERADELLALVGLDPaefadrYPHELSG--------GQQQRVGVARALAAD 153
|
170 180
....*....|....*....|....*....
gi 353526216 1017 PKLLLfLDEPTSGLDSQTAWSICKLMRKL 1045
Cdd:cd03295 154 PPLLL-MDEPFGALDPITRDQLQEEFKRL 181
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
876-1076 |
3.63e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 64.60 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTLLNCLsERV---TTGIIT-DGE--RLVNghalDSSFQRSIGYVqQQDVHLETTT 949
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLL-QRVfdpQSGRILiDGTdiRTVT----RASLRRNIAVV-FQDAGLFNRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 950 VREALQF------SAYLRQSNKISkkEKDDYVdyvidlLEMTDYADALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfL 1023
Cdd:PRK13657 425 IEDNIRVgrpdatDEEMRAAAERA--QAHDFI------ERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILI-L 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1024 DEPTSGLDSQTAwsicklmRKLAdhgQAILCTIHQPSALIMA-------EFDKLLFLQKG 1076
Cdd:PRK13657 496 DEATSALDVETE-------AKVK---AALDELMKGRTTFIIAhrlstvrNADRILVFDNG 545
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
160-384 |
4.07e-10 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 61.23 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 160 DDSKYFDILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIERHYRGDV-IYSAETD 238
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLA----GLLEPDAGFATVDGFDVVKEPAEARRRLgFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 239 VhFPHLSVGDTLEFAARLRtpqnrgeGIDRETyAKHMASVYMATYGLSHTRNTNVGndfvrGVSGGERKRVSIAEASLSG 318
Cdd:cd03266 89 L-YDRLTARENLEYFAGLY-------GLKGDE-LTARLEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 319 ANIQCWDNATRGLD---SATALEFIRALKTSA-TILDTTPLIaiyqcsQDAYELFDNVVVLYEGYQIFFG 384
Cdd:cd03266 155 PPVLLLDEPTTGLDvmaTRALREFIRQLRALGkCILFSTHIM------QEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
883-1057 |
4.24e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.87 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 883 VKPGQITALMGASGAGKTTLLNCLServttGIIT-DGERLVNGHALD----SSFQRSIGYVQQQDVHLETTTVREALQfs 957
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMA-----GLLPgSGSIQFAGQPLEawsaAELARHRAYLSQQQTPPFAMPVFQYLT-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 958 ayLRQSNKISKKEKDDYVDYVIDLLEMTDY----ADALVGvaGEGlnveQRKRLTiGVELVAKPKL-----LLFLDEPTS 1028
Cdd:PRK03695 92 --LHQPDKTRTEAVASALNEVAEALGLDDKlgrsVNQLSG--GEW----QRVRLA-AVVLQVWPDInpagqLLLLDEPMN 162
|
170 180 190
....*....|....*....|....*....|
gi 353526216 1029 GLD-SQTAWsICKLMRKLADHGQAILCTIH 1057
Cdd:PRK03695 163 SLDvAQQAA-LDRLLSELCQQGIAVVMSSH 191
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
158-378 |
4.49e-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: 61.73 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 158 KPDDSkyfDILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGlspHDI----ERHYRGDVIY 233
Cdd:cd03252 11 KPDGP---VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQ----RFYVPENGRVLVDG---HDLaladPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 234 SAETDVHFpHLSVGDTLEFAarlrtpqNRGEGIDRETYAKHMASVYMATYGLSHTRNTNVGNDFVrGVSGGERKRVSIAE 313
Cdd:cd03252 81 VLQENVLF-NRSIRDNIALA-------DPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGA-GLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 314 ASLSGANIQCWDNATRGLDSATALEFIRALKtsaTILDTTPLIAIyqcsqdAYEL-----FDNVVVLYEG 378
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMH---DICAGRTVIII------AHRLstvknADRIIVMEKG 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
176-378 |
5.16e-10 |
|
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: 59.57 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 176 RPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIERH-YRGDVIYsaetdvhfphlsvgdtlefaa 254
Cdd:cd00267 23 KAGEIVALVGPNGSGKSTLLRAIA----GLLKPTSGEILIDGKDIAKLPLEeLRRRIGY--------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 255 rlrTPQnrgegidretyakhmasvymatyglshtrntnvgndfvrgVSGGERKRVSIAEASLSGANIQCWDNATRGLDSA 334
Cdd:cd00267 78 ---VPQ----------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 353526216 335 TA---LEFIRAL-KTSATILDTTPLIaiyqcsQDAYELFDNVVVLYEG 378
Cdd:cd00267 115 SRerlLELLRELaEEGRTVIIVTHDP------ELAELAADRVIVLKDG 156
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
885-1087 |
5.19e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.95 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 885 PGQITALMGASGAGKTTLLNCLServttGII--TDGERLVNGHALDSSfQRSIGYVQQQ--------DVHLETTTVREAL 954
Cdd:PRK13638 26 LSPVTGLVGANGCGKSTLFMNLS-----GLLrpQKGAVLWQGKPLDYS-KRGLLALRQQvatvfqdpEQQIFYTDIDSDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 955 QFSayLRQSNkISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 1034
Cdd:PRK13638 100 AFS--LRNLG-VPEAEITRRVDEALTLVDAQHFRHQPIQCLSHG----QKKRVAIAGALVLQARYLL-LDEPTAGLDPAG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 353526216 1035 AWSICKLMRKLADHGQAILCTIHQPSaLIMAEFDKLLFLQKGGRTAYfGELGE 1087
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNHVIISSHDID-LIYEISDAVYVLRQGQILTH-GAPGE 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
167-378 |
8.19e-10 |
|
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: 59.51 E-value: 8.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDG---LSPHDIERHYRGDVIYSAETDVHFPH 243
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIA----GLEEPDSGSILIDGedlTDLEDELPPLRRRIGMVFQDFALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 244 LSVGDTLefaarlrtpqnrgegidretyakhmasvymaTYGLShtrntnvgndfvrgvsGGERKRVSIAEASLSGANIQC 323
Cdd:cd03229 91 LTVLENI-------------------------------ALGLS----------------GGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 353526216 324 WDNATRGLDSATALEFIRALKTSATILDTTPLIAIYQCSqDAYELFDNVVVLYEG 378
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLD-EAARLADRVVVLRDG 177
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
884-1049 |
8.68e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 60.80 E-value: 8.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 884 KPGQITALMGASGAGKTTL---LNCLServttgIITDGERLVNGHALDSS----------FQRSIGYVQQQdVHL-ETTT 949
Cdd:PRK11124 26 PQGETLVLLGPSGAGKSSLlrvLNLLE------MPRSGTLNIAGNHFDFSktpsdkaireLRRNVGMVFQQ-YNLwPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 950 VREALqFSAYLRQSnKISKKEKDDYVDYVIDLLEMTDYADA----LVGvageglnvEQRKRLTIGVELVAKPKLLLFlDE 1025
Cdd:PRK11124 99 VQQNL-IEAPCRVL-GLSKDQALARAEKLLERLRLKPYADRfplhLSG--------GQQQRVAIARALMMEPQVLLF-DE 167
|
170 180
....*....|....*....|....
gi 353526216 1026 PTSGLDSQTAWSICKLMRKLADHG 1049
Cdd:PRK11124 168 PTAALDPEITAQIVSIIRELAETG 191
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
162-384 |
8.89e-10 |
|
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: 60.59 E-value: 8.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 162 SKYFD---ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFhIGKES-QITYDG-----LSPHDIERHYR--GD 230
Cdd:cd03261 7 TKSFGgrtVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIV----GL-LRPDSgEVLIDGedisgLSEAELYRLRRrmGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 231 VIYSAETdvhFPHLSVGDTLEFaaRLRTPQNRGEGIDRETYAKHMASVymatyGLSHTRNTNVGNdfvrgVSGGERKRVS 310
Cdd:cd03261 82 LFQSGAL---FDSLTVFENVAF--PLREHTRLSEEEIREIVLEKLEAV-----GLRGAEDLYPAE-----LSGGMKKRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 353526216 311 IAEASLSGANIQCWDNATRGLDSATALEF---IRALKTSatiLDTTPLIAIYQCSqDAYELFDNVVVLYEGYQIFFG 384
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIddlIRSLKKE---LGLTSIMVTHDLD-TAFAIADRIAVLYDGKIVAEG 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
872-1048 |
9.00e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 61.21 E-value: 9.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCL--------SERVTTGIITDGE----RLVNGHALdssfQRSIGYVQ 939
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlipGARVEGEILLDGEdiydPDVDVVEL----RRRVGMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 940 QQDVHLeTTTVREALqfsAY-LRQSNKISKKEKDDYVDyvidllemtdyaDALVGVA------------GEGLNVEQRKR 1006
Cdd:COG1117 99 QKPNPF-PKSIYDNV---AYgLRLHGIKSKSELDEIVE------------ESLRKAAlwdevkdrlkksALGLSGGQQQR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 353526216 1007 LTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADH 1048
Cdd:COG1117 163 LCIARALAVEPEVLL-MDEPTSALDPISTAKIEELILELKKD 203
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
885-1031 |
1.17e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.81 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 885 PGQ-ITALMGASGAGKTTLLNCLServttGIIT--DGERLVNGHAL-DSS-------FQRSIGYVqQQDVHL-ETTTVRE 952
Cdd:PRK11144 22 PAQgITAIFGRSGAGKTSLINAIS-----GLTRpqKGRIVLNGRVLfDAEkgiclppEKRRIGYV-FQDARLfPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 953 ALQFSAylrqsnkisKKEKDDYVDYVIDLLE----MTDYADALVGvaGEglnveqRKRLTIGVELVAKPKLLLfLDEPTS 1028
Cdd:PRK11144 96 NLRYGM---------AKSMVAQFDKIVALLGieplLDRYPGSLSG--GE------KQRVAIGRALLTAPELLL-MDEPLA 157
|
...
gi 353526216 1029 GLD 1031
Cdd:PRK11144 158 SLD 160
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
176-378 |
1.26e-09 |
|
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: 58.95 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 176 RPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIERHYRGDVIYSAETDVHFPHLSVGDTLEFaar 255
Cdd:cd03230 24 EKGEIYGLLGPNGAGKTTLIKIIL----GLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPEEPSLYENLTVRENLKL--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 256 lrtpqnrgegidretyakhmasvymatyglshtrntnvgndfvrgvSGGERKRVSIAEASLSGANIQCWDNATRGLDSAT 335
Cdd:cd03230 97 ----------------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 353526216 336 ALEFIRALKTSA----TILDTTPLIaiyqcsQDAYELFDNVVVLYEG 378
Cdd:cd03230 131 RREFWELLRELKkegkTILLSSHIL------EEAERLCDRVAILNNG 171
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
885-1091 |
1.48e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.56 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 885 PGQITALMGASGAGKTTLLNCLS-------ERVTTGIITdgerlVNGHALDS------SFQRSIGYVQQQDvhletttvr 951
Cdd:PRK14239 30 PNEITALIGPSGSGKSTLLRSINrmndlnpEVTITGSIV-----YNGHNIYSprtdtvDLRKEIGMVFQQP--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 952 EALQFSAY------LRqSNKISKKEKDDYV-----------DYVIDLLEmtdyaDALVGVAGeglnvEQRKRLTIGVELV 1014
Cdd:PRK14239 96 NPFPMSIYenvvygLR-LKGIKDKQVLDEAvekslkgasiwDEVKDRLH-----DSALGLSG-----GQQQRVCIARVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1015 AKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCT--IHQPSALimaefdkllflqkGGRTAYF--GELGENCQ 1090
Cdd:PRK14239 165 TSPKIIL-LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTrsMQQASRI-------------SDRTGFFldGDLIEYND 230
|
.
gi 353526216 1091 T 1091
Cdd:PRK14239 231 T 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
887-1076 |
1.55e-09 |
|
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: 63.11 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 887 QITALMGASGAGKTTLLNCLservtTGII--TDGERLVNGHALDSSF---QRSIGYVQQQDVHLETTTVREALQFSAYLR 961
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSIL-----TGLLppTSGTVLVGGKDIETNLdavRQSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 962 -QSNKISKKEKDDYVDYVIDLLEMTDYADALVGvageGLnveQRKrLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICK 1040
Cdd:TIGR01257 1032 gRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSG----GM---QRK-LSVAIAFVGDAKVVV-LDEPTSGVDPYSRRSIWD 1102
|
170 180 190
....*....|....*....|....*....|....*.
gi 353526216 1041 LMRKLADHGQAILCTIHQPSALIMAefDKLLFLQKG 1076
Cdd:TIGR01257 1103 LLLKYRSGRTIIMSTHHMDEADLLG--DRIAIISQG 1136
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
874-1045 |
1.60e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 61.27 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 874 VILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTG-IITDGERLVnghalDSSFQ-RSIGYVQQQDVHLETTT 949
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAglEKPTEGqIFIDGEDVT-----HRSIQqRDICMVFQSYALFPHMS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 950 VREALqfsAYLRQSNKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELVAKPKLLLFlDEPTSG 1029
Cdd:PRK11432 95 LGENV---GYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGG----QQQRVALARALILKPKVLLF-DEPLSN 166
|
170
....*....|....*.
gi 353526216 1030 LDSQTAWSICKLMRKL 1045
Cdd:PRK11432 167 LDANLRRSMREKIREL 182
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
872-1078 |
1.62e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 62.52 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLnclseRVTTGIITDGERLVNGHALDSSF---QRSigYVQQqdvhletT 948
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLL-----RAIAGLWPYGSGRIARPAGARVLflpQRP--YLPL-------G 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 949 TVREALqfsAYLRQSNKISkkekDDYVDYVIDLLEMTDYADAlvgvagegLNVEQR--KRLTIGvE---------LVAKP 1017
Cdd:COG4178 441 TLREAL---LYPATAEAFS----DAELREALEAVGLGHLAER--------LDEEADwdQVLSLG-EqqrlafarlLLHKP 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 353526216 1018 KlLLFLDEPTSGLDSQTAWSICKLMRK-LADhgqailCTI----HQPSalIMAEFDKLLFLQKGGR 1078
Cdd:COG4178 505 D-WLFLDEATSALDEENEAALYQLLREeLPG------TTVisvgHRST--LAAFHDRVLELTGDGS 561
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
168-350 |
1.63e-09 |
|
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: 62.30 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 168 LKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIER-HYRGDVIYSAETdvhfPHLsV 246
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLL----GFVDPTEGSIAVNGVPLADADAdSWRDQIAWVPQH----PFL-F 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 247 GDTLEFAARLRTPQNRGEGIDRetyAKHMASVYMATYGLSHTRNTNVGNDfVRGVSGGERKRVSIAEASLSGANIQCWDN 326
Cdd:TIGR02857 409 AGTIAENIRLARPDASDAEIRE---ALERAGLDEFVAALPQGLDTPIGEG-GAGLSGGQAQRLALARAFLRDAPLLLLDE 484
|
170 180
....*....|....*....|....*..
gi 353526216 327 ATRGLDSATA---LEFIRALKTSATIL 350
Cdd:TIGR02857 485 PTAHLDAETEaevLEALRALAQGRTVL 511
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
884-1076 |
1.73e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 60.37 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 884 KPGQITALMGASGAGKTTLLNCLS--ERVTTGII------------TDGE-RLVNGHALDSSFQRSIGYVQQQDVHLETT 948
Cdd:PRK10619 29 NAGDVISIIGSSGSGKSTFLRCINflEKPSEGSIvvngqtinlvrdKDGQlKVADKNQLRLLRTRLTMVFQHFNLWSHMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 949 TVREALQFSAylrQSNKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGlnvEQRKRLTIGVELVAKPKLLLFlDEPTS 1028
Cdd:PRK10619 109 VLENVMEAPI---QVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSG---GQQQRVSIARALAMEPEVLLF-DEPTS 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 353526216 1029 GLDSQTAWSICKLMRKLADHGQAILCTIHQpsalimAEFDK-----LLFLQKG 1076
Cdd:PRK10619 182 ALDPELVGEVLRIMQQLAEEGKTMVVVTHE------MGFARhvsshVIFLHQG 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
872-1059 |
1.82e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 59.12 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLnclseRVTTGII--TDGERLVNGHAL-DSSFQRSIGYVQQQDVHLETT 948
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLL-----RLIAGLLppAAGTIKLDGGDIdDPDVAEACHYLGHRNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 949 TVREALQFSAYLRQSNkiskkekDDYVDYVIDLLEMTDYADALVGV--AGeglnveQRKRLTIGVELVAKPKLLLfLDEP 1026
Cdd:PRK13539 89 TVAENLEFWAAFLGGE-------ELDIAAALEAVGLAPLAHLPFGYlsAG------QKRRVALARLLVSNRPIWI-LDEP 154
|
170 180 190
....*....|....*....|....*....|....
gi 353526216 1027 TSGLDSQTAWSICKLMR-KLADHGQAILCTiHQP 1059
Cdd:PRK13539 155 TAALDAAAVALFAELIRaHLAQGGIVIAAT-HIP 187
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
876-1053 |
2.10e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.97 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTLLNCLServttGII--TDGERLVNGHALD-SSFQRS----IGYVQQqdvHL--- 945
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILY-----GLYqpDSGEILIDGKPVRiRSPRDAialgIGMVHQ---HFmlv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 946 ETTTVREALQFSAYLRQSNKISKKEkddyvdyVIDLLE--MTDY-----ADALVgvagEGLNVEQRKRltigVE----LV 1014
Cdd:COG3845 93 PNLTVAENIVLGLEPTKGGRLDRKA-------ARARIRelSERYgldvdPDAKV----EDLSVGEQQR----VEilkaLY 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 353526216 1015 AKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAIL 1053
Cdd:COG3845 158 RGARILI-LDEPTAVLTPQEADELFEILRRLAAEGKSII 195
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
870-1076 |
2.12e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.04 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 870 KEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTtgiITDGERLVNGHALDS----SFQRSIGYVQQQDVHL 945
Cdd:PRK10790 351 RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP---LTEGEIRLDGRPLSSlshsVLRQGVAMVQQDPVVL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 946 ETTtvrealqFSAYLRQSNKISKkekddyvDYVIDLLEMTDYAD----------ALVGVAGEGLNVEQRKRLTIGVELVA 1015
Cdd:PRK10790 428 ADT-------FLANVTLGRDISE-------EQVWQALETVQLAElarslpdglyTPLGEQGNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 353526216 1016 KPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHgqAILCTI-HQPSALIMAefDKLLFLQKG 1076
Cdd:PRK10790 494 TPQILI-LDEATANIDSGTEQAIQQALAAVREH--TTLVVIaHRLSTIVEA--DTILVLHRG 550
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
167-395 |
2.39e-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: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDG-----LSPHDIeRHYRGDVIY-------- 233
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLN----GLVEPTSGSVLIDGtdinkLKGKAL-RQLRRQIGMifqqfnli 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 234 ---SAETDVHFPHLSVGDTLEFAARLRTPQnrgegidretyAKHMASVYMATYGLSHTRNTNVGNdfvrgVSGGERKRVS 310
Cdd:cd03256 91 erlSVLENVLSGRLGRRSTWRSLFGLFPKE-----------EKQRALAALERVGLLDKAYQRADQ-----LSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 311 IAEASLSGANIQCWDNATRGLDSATALEFIRALKTSATILDTTPLIAIYQCsQDAYELFDNVVVLYEGYQIFFGKASKAK 390
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQV-DLAREYADRIVGLKDGRIVFDGPPAELT 233
|
....*
gi 353526216 391 EYFEN 395
Cdd:cd03256 234 DEVLD 238
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
870-1059 |
2.89e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.66 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 870 KEDRVILDHVDGWVKPGQITALMGASGAGKTTLLnclseRVTTGII--TDGERLVNG---HALDSSFQRSIGYVQQQD-V 943
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLL-----RILAGLArpDAGEVLWQGepiRRQRDEYHQDLLYLGHQPgI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 944 HLETTTVrEALQFSAYLRQsnkiskkEKDDyvDYVIDLLEMT---DYADALVGV--AGeglnveQRKRLTIGVELVAKPK 1018
Cdd:PRK13538 86 KTELTAL-ENLRFYQRLHG-------PGDD--EALWEALAQVglaGFEDVPVRQlsAG------QQRRVALARLWLTRAP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 353526216 1019 LLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQP 1059
Cdd:PRK13538 150 LWI-LDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
177-335 |
3.14e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 58.35 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 177 PGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDieRHYRGDVIYSAETDVHFPHLSVGDTLEFAARL 256
Cdd:PRK13539 27 AGEALVLTGPNGSGKTTLLRLIA----GLLPPAAGTIKLDGGDIDD--PDVAEACHYLGHRNAMKPALTVAENLEFWAAF 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 353526216 257 RtpqNRGEGIDRETyakhmasvyMATYGLSHTRNTNVGNdfvrgVSGGERKRVSIAEASLSGANIQCWDNATRGLDSAT 335
Cdd:PRK13539 101 L---GGEELDIAAA---------LEAVGLAPLAHLPFGY-----LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
885-1057 |
3.77e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.17 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 885 PGQITALMGASGAGKTTLLNCLSERVT--TGIITDGER---LVNGHALDSSFQRSI-----GYVQQQDvhletttvREAL 954
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSARLApdAGEVHYRMRdgqLRDLYALSEAERRRLlrtewGFVHQHP--------RDGL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 955 --QFSA---------------Y--LRQsnkiskkEKDDYVDYV-IDLLEMTDYADALVGvageGLnveqRKRLTIGVELV 1014
Cdd:PRK11701 103 rmQVSAggnigerlmavgarhYgdIRA-------TAGDWLERVeIDAARIDDLPTTFSG----GM----QQRLQIARNLV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 353526216 1015 AKPKlLLFLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIH 1057
Cdd:PRK11701 168 THPR-LVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTH 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
875-1065 |
3.81e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 59.33 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 875 ILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVT--TGIITDGERLVNGhaldSSFQRsiGYVQQQDVHLETTTVRE 952
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPyqHGSITLDGKPVEG----PGAER--GVVFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 953 ALQFSAYLRQSNKISKKEKddyvdyvidLLEMTdyadALVGVAGEG------LNVEQRKRLTIGVELVAKPKLLLfLDEP 1026
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRLEI---------AHQML----KKVGLEGAEkryiwqLSGGQRQRVGIARALAANPQLLL-LDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 353526216 1027 TSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQ-PSALIMA 1065
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLwQETGKQVLLITHDiEEAVFMA 196
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
869-1076 |
4.52e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.43 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 869 KKEDRVILDHVDGWVKPGQITALMGASGAGKTT---LLNCL---SERVTTGIITDGERLVNGHALDssFQRSIGYV-QQQ 941
Cdd:PRK13640 16 PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLllpDDNPNSKITVDGITLTAKTVWD--IREKVGIVfQNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 942 DVHLETTTVREALQFSAYLRQsnkISKKEKDDYVDYVIDLLEMTDYADAlvgvAGEGLNVEQRKRLTIGVELVAKPKLLL 1021
Cdd:PRK13640 94 DNQFVGATVGDDVAFGLENRA---VPRPEMIKIVRDVLADVGMLDYIDS----EPANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 353526216 1022 fLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIHQPSALIMAefDKLLFLQKG 1076
Cdd:PRK13640 167 -LDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEANMA--DQVLVLDDG 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
167-384 |
6.19e-09 |
|
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: 57.59 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGeLTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIERHYRGDVIYSAETDVHFPHLSV 246
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILA----TLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQEFGVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 247 GDTLEFAARLRtpqnrgeGI---DRETYAKHMasvymatygLSHTRNTNVGNDFVRGVSGGERKRVSIAEASLSGANIQC 323
Cdd:cd03264 90 REFLDYIAWLK-------GIpskEVKARVDEV---------LELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 353526216 324 WDNATRGLDSATALEF---IRALKTSATILDTTPLIaiyqcsQDAYELFDNVVVLYEGYQIFFG 384
Cdd:cd03264 154 VDEPTAGLDPEERIRFrnlLSELGEDRIVILSTHIV------EDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
883-1057 |
6.26e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 58.74 E-value: 6.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 883 VKPGQITALMGASGAGKTTLLNCLSERVTtgiITDGERLVNGHALDSSFQRS-IGYVQQQD-------VHLETTTVREAL 954
Cdd:PRK15056 30 VPGGSIAALVGVNGSGKSTLFKALMGFVR---LASGKISILGQPTRQALQKNlVAYVPQSEevdwsfpVLVEDVVMMGRY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 955 QFSAYLRqsnkISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGvELVAKPKLLLFLDEPTSGLDSQT 1034
Cdd:PRK15056 107 GHMGWLR----RAKKRDRQIVTAALARVDMVEFRHRQIGELSGG----QKKRVFLA-RAIAQQGQVILLDEPFTGVDVKT 177
|
170 180
....*....|....*....|...
gi 353526216 1035 AWSICKLMRKLADHGQAILCTIH 1057
Cdd:PRK15056 178 EARIISLLRELRDEGKTMLVSTH 200
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
176-344 |
8.00e-09 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 58.18 E-value: 8.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 176 RPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPhdieRHYRGDVIY---SAETDVHFPhLSVGDTLEF 252
Cdd:COG1121 30 PPGEFVAIVGPNGAGKSTLLKAIL----GLLPPTSGTVRLFGKPP----RRARRRIGYvpqRAEVDWDFP-ITVRDVVLM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 253 AARLRTPQNRgeGIDRETYAKHMASvyMATYGLSHTRNTNVGNdfvrgVSGGERKRVSIAEASLSGANIQCWDNATRGLD 332
Cdd:COG1121 101 GRYGRRGLFR--RPSRADREAVDEA--LERVGLEDLADRPIGE-----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVD 171
|
170
....*....|..
gi 353526216 333 SATALEFIRALK 344
Cdd:COG1121 172 AATEEALYELLR 183
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
159-378 |
8.24e-09 |
|
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: 56.62 E-value: 8.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 159 PDDSKYfdILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIERHYRGDVIYSAETD 238
Cdd:cd03228 11 PGRPKP--VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLL----RLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 239 VHFPHLSVGDtlefaarlrtpqnrgegidretyakhmasvymatyglshtrntNVgndfvrgVSGGERKRVSIAEASLSG 318
Cdd:cd03228 85 PFLFSGTIRE-------------------------------------------NI-------LSGGQRQRIAIARALLRD 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 353526216 319 ANIQCWDNATRGLDSATALEFIRALKTSA---TILdttpLIA-----IyqcsqdayELFDNVVVLYEG 378
Cdd:cd03228 115 PPILILDEATSALDPETEALILEALRALAkgkTVI----VIAhrlstI--------RDADRIIVLDDG 170
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
883-1073 |
9.11e-09 |
|
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: 56.67 E-value: 9.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 883 VKPGQITALMGASGAGKTTLLNCLS--ERVTTGIIT-DGERLVNGHALDSsFQRSIGYV----QQQDVHLETTtVREALQ 955
Cdd:cd03215 23 VRAGEIVGIAGLVGNGQTELAEALFglRPPASGEITlDGKPVTRRSPRDA-IRAGIAYVpedrKREGLVLDLS-VAENIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 956 FSAYLrqsnkiSkkekddyvdyvidllemtdyadalvgvageGLNveQRKrLTIGVELVAKPKLLLfLDEPTSGLDSQTA 1035
Cdd:cd03215 101 LSSLL------S------------------------------GGN--QQK-VVLARWLARDPRVLI-LDEPTRGVDVGAK 140
|
170 180 190
....*....|....*....|....*....|....*...
gi 353526216 1036 WSICKLMRKLADHGQAILctihqpsaLIMAEFDKLLFL 1073
Cdd:cd03215 141 AEIYRLIRELADAGKAVL--------LISSELDELLGL 170
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
871-1076 |
1.05e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 57.75 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 871 EDRVILDHVDGWVKPGQITALMGASGAGKTTL---LNCLSERVTTGIITDGERLVNGH---ALDS-SFQRSIGYVQQQDV 943
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLlkvLNRLIEIYDSKIKVDGKVLYFGKdifQIDAiKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 944 HLETTTVREALqfsAYLRQSNKIskKEKDDYVDYVIDLLEMT----DYADALVGVAGEgLNVEQRKRLTIGVELVAKPKL 1019
Cdd:PRK14246 101 PFPHLSIYDNI---AYPLKSHGI--KEKREIKKIVEECLRKVglwkEVYDRLNSPASQ-LSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 353526216 1020 LLfLDEPTSGLDSQTAWSICKLMRKLADHgQAILCTIHQPSALIMAEfDKLLFLQKG 1076
Cdd:PRK14246 175 LL-MDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVA-DYVAFLYNG 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
176-314 |
1.12e-08 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 57.10 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 176 RPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIERhyrgDVIYSAETDVHFPHLSVGDTLEFAAR 255
Cdd:cd03293 28 EEGEFVALVGPSGCGKSTLLRIIA----GLERPTSGEVLVDGEPVTGPGP----DRGYVFQQDALLPWLTVLDNVALGLE 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 353526216 256 LRTPQNRgegiDRETYAKHmasvYMATYGLSHTRntnvgNDFVRGVSGGERKRVSIAEA 314
Cdd:cd03293 100 LQGVPKA----EARERAEE----LLELVGLSGFE-----NAYPHQLSGGMRQRVALARA 145
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
878-1083 |
1.24e-08 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 56.73 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 878 HVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIITDGErlVNGHALDSSfQRSIGYVQQQD---VHLET-TTVR 951
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAgfETPQSGRVLING--VDVTAAPPA-DRPVSMLFQENnlfAHLTVeQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 952 EALQFSAYLRQSNKiskkekddyvdyvidllEMTDYADALVGVAG------EGLNVEQRKRLTIGVELVaKPKLLLFLDE 1025
Cdd:cd03298 93 LGLSPGLKLTAEDR-----------------QAIEVALARVGLAGlekrlpGELSGGERQRVALARVLV-RDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 353526216 1026 PTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQPSAlIMAEFDKLLFLQKgGRTAYFG 1083
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPED-AKRLAQRVVFLDN-GRIAAQG 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
875-1057 |
1.31e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.13 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 875 ILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTgiiTDGERLVNGHALD--SSF------QRSIGYVQQQDVHLE 946
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTP---TSGDVIFNGQPMSklSSAakaelrNQKLGFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 947 TTTVREALQFSAYLRQSNKISKKEKddyvdyvidLLEMTdyadALVGVAGEG------LNVEQRKRLTIGVELVAKPKLL 1020
Cdd:PRK11629 101 DFTALENVAMPLLIGKKKPAEINSR---------ALEML----AAVGLEHRAnhrpseLSGGERQRVAIARALVNNPRLV 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 353526216 1021 LfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIH 1057
Cdd:PRK11629 168 L-ADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTH 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
176-386 |
1.37e-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: 59.15 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 176 RPGELTVVLGRPGAGCSTLLKtiAVNTYGFHIGKES-QITYDGLSPHDIERHYRGDVI--YSAETDVHFPHLSVGDTLEF 252
Cdd:COG1123 30 APGETVALVGESGSGKSTLAL--ALMGLLPHGGRISgEVLLDGRDLLELSEALRGRRIgmVFQDPMTQLNPVTVGDQIAE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 253 AARLRtpqnrgeGIDRETyAKHMASVYMATYGLSHtrntnVGNDFVRGVSGGERKRVSIAEASLSGANIQCWDNATRGLD 332
Cdd:COG1123 108 ALENL-------GLSRAE-ARARVLELLEAVGLER-----RLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 353526216 333 SATALEFIRALKTSATILDTTPLIaIYQCSQDAYELFDNVVVLYEGYQIFFGKA 386
Cdd:COG1123 175 VTTQAEILDLLRELQRERGTTVLL-ITHDLGVVAEIADRVVVMDDGRIVEDGPP 227
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
876-1058 |
1.39e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTLLNCL---SERVTTGIITDGERlVNGHALDSSFQRSIGYVQQQDVHLETTTVRE 952
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLfgiYQKDSGSILFQGKE-IDFKSSKEALENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 953 ALQFSAYLRQS-----NKISKKEKDDYVDYVIDLlemtdyaDALVGVAgeGLNVEQRKRLTIGVELVAKPKLLLfLDEPT 1027
Cdd:PRK10982 93 NMWLGRYPTKGmfvdqDKMYRDTKAIFDELDIDI-------DPRAKVA--TLSVSQMQMIEIAKAFSYNAKIVI-MDEPT 162
|
170 180 190
....*....|....*....|....*....|.
gi 353526216 1028 SGLDSQTAWSICKLMRKLADHGQAILCTIHQ 1058
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKERGCGIVYISHK 193
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
852-1057 |
1.43e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.03 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 852 ENREIFFWRDLTYQVkikkEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTgiiTDGERLVNGHALDS-- 929
Cdd:PRK10247 3 ENSPLLQLQNVGYLA----GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISP---TSGTLLFEGEDISTlk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 930 --SFQRSIGYVQQQDVhLETTTVREALQFSAYLRQSNKISKKEKDDYVDYVIDLLEMTDYADALVGvaGEglnveqRKRL 1007
Cdd:PRK10247 76 peIYRQQVSYCAQTPT-LFGDTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSG--GE------KQRI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 353526216 1008 TIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIH 1057
Cdd:PRK10247 147 SLIRNLQFMPKVLL-LDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTH 196
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
877-1031 |
1.69e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.37 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 877 DHVDGWVKPGQITALMGASGAGKTTLLNCLservtTGII--TDGERLVNGHALDS---SFQRSIGYVQQQDVHLETTTVR 951
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKML-----TGLLpaSEGEAWLFGQPVDAgdiATRRRVGYMSQAFSLYGELTVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 952 EALQFSAYLRQsnkISKKEKDDYVDYVIDLLEMTDYADALvgvaGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 1031
Cdd:NF033858 358 QNLELHARLFH---LPAAEIAARVAEMLERFDLADVADAL----PDSLPLGIRQRLSLAVAVIHKPELLI-LDEPTSGVD 429
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
162-350 |
2.08e-08 |
|
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: 56.68 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 162 SKYFDILKSMDAI---MRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDG-----LSPHDIERhyRGdVIY 233
Cdd:cd03219 7 TKRFGGLVALDDVsfsVRPGEIHGLIGPNGAGKTTLFNLIS----GFLRPTSGSVLFDGeditgLPPHEIAR--LG-IGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 234 SAETDVHFPHLSVGDTLEFAARLRTPQNRGEGIDRETYAKHMASV--YMATYGLSHTRNTNVGNdfvrgVSGGERKRVSI 311
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEREARERAeeLLERVGLADLADRPAGE-----LSYGQQRRLEI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 353526216 312 AEASLSGANIQCWDNATRGL---DSATALEFIRALKTS-ATIL 350
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLnpeETEELAELIRELRERgITVL 197
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
873-1072 |
2.21e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.03 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 873 RVILDHVDGWVKPGQITALMGASGAGKTTLL---NCLSERVTtGIITDGERLVNGHALDS-----SFQRSIGYVQQQDVH 944
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlNRMNDKVS-GYRYSGDVLLGGRSIFNyrdvlEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 945 LETTTVREALqfsAYLRQSNKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfLD 1024
Cdd:PRK14271 113 FPMSIMDNVL---AGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL-LD 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 353526216 1025 EPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSALIMAEFDKLLF 1072
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFF 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
870-1076 |
2.31e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 56.92 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 870 KEDRVILDHVDGWVKPGQITALMGASGAGKTTLlnclsERVTTGII--TDGERLVNGHALDSS----FQRSIGYV-QQQD 942
Cdd:PRK13632 19 NSENNALKNVSFEINEGEYVAILGHNGSGKSTI-----SKILTGLLkpQSGEIKIDGITISKEnlkeIRKKIGIIfQNPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 943 VHLETTTVREALQFSAylrQSNKISKKEKDDYVDYVIDLLEMTDYADAlvgvagEGLNVE--QRKRLTIGVELVAKPKLL 1020
Cdd:PRK13632 94 NQFIGATVEDDIAFGL---ENKKVPPKKMKDIIDDLAKKVGMEDYLDK------EPQNLSggQKQRVAIASVLALNPEII 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 353526216 1021 LFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTI-HQPSALIMAefDKLLFLQKG 1076
Cdd:PRK13632 165 IF-DESTSMLDPKGKREIKKIMVDLRKTRKKTLISItHDMDEAILA--DKVIVFSEG 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
176-378 |
2.44e-08 |
|
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: 56.06 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 176 RPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDG-----LSPHDIERHyrgdvIYSAETDVHFPHLSVGDTL 250
Cdd:cd03245 28 RAGEKVAIIGRVGSGKSTLLKLLA----GLYKPTSGSVLLDGtdirqLDPADLRRN-----IGYVPQDVTLFYGTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 251 EFAARLRTpqnrgegiDRETyakhMASVYMAtyGLshtrntnvgNDFV---------------RGVSGGERKRVSIAEAS 315
Cdd:cd03245 99 TLGAPLAD--------DERI----LRAAELA--GV---------TDFVnkhpngldlqigergRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353526216 316 LSGANIQCWDNATRGLDSATALEFIRALKtsATILDTTPLIAIYQCSqdAYELFDNVVVLYEG 378
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLR--QLLGDKTLIIITHRPS--LLDLVDRIIVMDSG 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
178-378 |
2.52e-08 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 55.96 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 178 GELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIERHYRGDVIYSAETDVhFPHLSVGDTLEFAarlR 257
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIA----GFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNL-FAHLTVEQNVGLG---L 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 258 TPQNRGEGIDRETYAKHMASVYMAtyGLSHTRntnvgndfVRGVSGGERKRVSIAEASLSGANIQCWDNATRGLDSATAL 337
Cdd:cd03298 96 SPGLKLTAEDRQAIEVALARVGLA--GLEKRL--------PGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 353526216 338 EFIRALKTSATILDTTPLIAIYQcSQDAYELFDNVVVLYEG 378
Cdd:cd03298 166 EMLDLVLDLHAETKMTVLMVTHQ-PEDAKRLAQRVVFLDNG 205
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
873-1076 |
4.04e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.37 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 873 RVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTGIITDGERLVNGHALDSSFQRSIGYVQ---------QQDV 943
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTLNGEPLAAIDAPRlarlravlpQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 944 HLETTTVREALQFSAY--LRQSNKISKKEKDdyvdyVID-LLEMTDyADALVG-----VAGEGLNVEQRKRLTIGV---E 1012
Cdd:PRK13547 94 PAFAFSAREIVLLGRYphARRAGALTHRDGE-----IAWqALALAG-ATALVGrdvttLSGGELARVQFARVLAQLwppH 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 353526216 1013 LVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIHQPSaLIMAEFDKLLFLQKG 1076
Cdd:PRK13547 168 DAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLArDWNLGVLAIVHDPN-LAARHADRIAMLADG 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
883-1045 |
4.40e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 57.02 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 883 VKPGQITALMGASGAGKTTLLNCLS--ERVTTGII----TDGERLvngHALDssfqRSIGYVQQQDVHLETTTVREALQF 956
Cdd:PRK10851 25 IPSGQMVALLGPSGSGKTTLLRIIAglEHQTSGHIrfhgTDVSRL---HARD----RKVGFVFQHYALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 957 SAYL-----RQSNKISKKEkddyvdyVIDLLEMTDYADaLVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 1031
Cdd:PRK10851 98 GLTVlprreRPNAAAIKAK-------VTQLLEMVQLAH-LADRYPAQLSGGQKQRVALARALAVEPQILL-LDEPFGALD 168
|
170
....*....|....
gi 353526216 1032 SQTAWSICKLMRKL 1045
Cdd:PRK10851 169 AQVRKELRRWLRQL 182
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
883-1087 |
5.30e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 55.53 E-value: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 883 VKPGQITALMGASGAGKTTLLNCLS--ERVTTGIItdgerLVNG--HALDSSFQRSIGYVQQQD---VHLettTVRE--A 953
Cdd:COG3840 22 IAAGERVAILGPSGAGKSTLLNLIAgfLPPDSGRI-----LWNGqdLTALPPAERPVSMLFQENnlfPHL---TVAQniG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 954 LQFSAYLRqsnkISKKEKDDyvdyVIDLLE---MTDYAD----ALVGvaGeglnveQRKRLTIGVELVAKPKLLLfLDEP 1026
Cdd:COG3840 94 LGLRPGLK----LTAEQRAQ----VEQALErvgLAGLLDrlpgQLSG--G------QRQRVALARCLVRKRPILL-LDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353526216 1027 TSGLDSQTAWSICKLMRKLAD-HGQAILCTIHQPS-ALIMAefDKLLFLqKGGRTAYFGELGE 1087
Cdd:COG3840 157 FSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEdAARIA--DRVLLV-ADGRIAADGPTAA 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
876-1058 |
5.41e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.79 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTLLNCLServttGIITdGERLVNGHA--LDSSFQRS-------------IGYVQQ 940
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLS-----GLIT-GDKSAGSHIelLGRTVQREgrlardirksranTGYIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 941 QDVHLETTTVRE-----ALQFSAYLRQSNKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELVA 1015
Cdd:PRK09984 94 QFNLVNRLSVLEnvligALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGG----QQQRVAIARALMQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 353526216 1016 KPKLLLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQ 1058
Cdd:PRK09984 170 QAKVIL-ADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQ 212
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
876-1053 |
7.72e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.89 E-value: 7.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTLLN--CLSERVTTGIITDGERLVNGHALDSSFQRSIGYVQQQDVHLETTTVREA 953
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGtlCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 954 LQFSAYLrqsnkISKKEKDDYVDYVIDLLEMtdYADALVGVAGEGLNVEQrKRLTIGVELVAKPKLLLfLDEPTSGLDSQ 1033
Cdd:PRK11614 101 LAMGGFF-----AERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQ-QMLAIGRALMSQPRLLL-LDEPSLGLAPI 171
|
170 180
....*....|....*....|
gi 353526216 1034 TAWSICKLMRKLADHGQAIL 1053
Cdd:PRK11614 172 IIQQIFDTIEQLREQGMTIF 191
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
872-1073 |
7.93e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.12 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLnclseRVTTGIITDGERLVnghalDSSFQRSIGYVQQQdVHLETTTvr 951
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLV-----RVVLGLVAPDEGVI-----KRNGKLRIGYVPQK-LYLDTTL-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 952 eALQFSAYLRQSNKISKKekddyvdyviDLLEMTDYADA--LVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 1029
Cdd:PRK09544 83 -PLTVNRFLRLRPGTKKE----------DILPALKRVQAghLIDAPMQKLSGGETQRVLLARALLNRPQLLV-LDEPTQG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 353526216 1030 LDSQTAWSICKLMRKLADH-GQAILCTIHQPSaLIMAEFDKLLFL 1073
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRElDCAVLMVSHDLH-LVMAKTDEVLCL 194
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
153-378 |
1.38e-07 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 54.05 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 153 INKLKK--PDDSKYFDILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDG---LSPHDIERHY 227
Cdd:cd03257 4 VKNLSVsfPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAIL----GLLKPTSGSIIFDGkdlLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 228 RGDVI-------YSAETdvhfPHLSVGDTLEFAARLRTPqNRGEGIDRETYAKHMASVymatyGLSHTRntnvGNDFVRG 300
Cdd:cd03257 80 RRKEIqmvfqdpMSSLN----PRMTIGEQIAEPLRIHGK-LSKKEARKEAVLLLLVGV-----GLPEEV----LNRYPHE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 301 VSGGERKRVSIAEA-SLSGANIQCwDNATRGLDSATALEFIRALKTSATILDTTpLIAIyqcSQD---AYELFDNVVVLY 376
Cdd:cd03257 146 LSGGQRQRVAIARAlALNPKLLIA-DEPTSALDVSVQAQILDLLKKLQEELGLT-LLFI---THDlgvVAKIADRVAVMY 220
|
..
gi 353526216 377 EG 378
Cdd:cd03257 221 AG 222
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
847-1087 |
1.38e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 54.32 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 847 SVDFP--ENREIFFWRDLTYQVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLServttGII--TDGERLV 922
Cdd:COG1134 11 SKSYRlyHEPSRSLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIA-----GILepTSGRVEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 923 NGH-----ALDSSFQRSIgyvqqqdvhlettTVREALQFSAYLrqsNKISKKEKDDYVDYVIDLLEMTDYADALVGV--A 995
Cdd:COG1134 86 NGRvsallELGAGFHPEL-------------TGRENIYLNGRL---LGLSRKEIDEKFDEIVEFAELGDFIDQPVKTysS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 996 GeglnveQRKRLTIGVELVAKPKLLLfLDEPTSGLD------SQtawsicKLMRKLADHGQAILCTIHQPSALimAEF-D 1068
Cdd:COG1134 150 G------MRARLAFAVATAVDPDILL-VDEVLAVGDaafqkkCL------ARIRELRESGRTVIFVSHSMGAV--RRLcD 214
|
250
....*....|....*....
gi 353526216 1069 KLLFLQKgGRTAYFGELGE 1087
Cdd:COG1134 215 RAIWLEK-GRLVMDGDPEE 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
876-1058 |
1.46e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.95 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIITdgerlVNGHALDS-----SFQRSIGYVQQQDVHLETT 948
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSgiHEPTKGTIT-----INNINYNKldhklAAQLGIGIIYQELSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 949 TVREALQFSAYLRQS----NKISKKEKDDYVDYVIDLLEMTDYADALVGvageGLNVEQRKRLTIGVELVAKPKLLLfLD 1024
Cdd:PRK09700 96 TVLENLYIGRHLTKKvcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVA----NLSISHKQMLEIAKTLMLDAKVII-MD 170
|
170 180 190
....*....|....*....|....*....|....
gi 353526216 1025 EPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 1058
Cdd:PRK09700 171 EPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK 204
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
860-1087 |
1.56e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.42 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKIKKEdrvILDHVDGWVKPGQITALMGASGAGKTTLLnclseRVTTGII--TDGERLVNGHALDSS----FQR 933
Cdd:PRK13652 7 RDLCYSYSGSKE---ALNNINFIAPRNSRIAVIGPNGAGKSTLF-----RHFNGILkpTSGSVLIRGEPITKEnireVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 934 SIGYV-QQQDVHLETTTVREALQFSAYLRQSNKISKKEKddyVDYVIDLLEMTDYADAlvgvAGEGLNVEQRKRLTIGVE 1012
Cdd:PRK13652 79 FVGLVfQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHR---VSSALHMLGLEELRDR----VPHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 353526216 1013 LVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLAD-HGQAILCTIHQPSalIMAEFDKLLFLQKGGRTAYFGELGE 1087
Cdd:PRK13652 152 IAMEPQVLV-LDEPTAGLDPQGVKELIDFLNDLPEtYGMTVIFSTHQLD--LVPEMADYIYVMDKGRIVAYGTVEE 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
178-353 |
1.64e-07 |
|
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: 53.57 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 178 GELTVVLGRPGAGCSTLLKTIavntYGFHIGKESQITYDGLSPHDIER----HYRGDVIYSAETDVHFPHLSVGDTLEFA 253
Cdd:cd03292 27 GEFVFLVGPSGAGKSTLLKLI----YKEELPTSGTIRVNGQDVSDLRGraipYLRRKIGVVFQDFRLLPDRNVYENVAFA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 254 ARLrtpqnrgEGIDRETYAKHMASVyMATYGLSHTRNTnvgndFVRGVSGGERKRVSIAEASLSGANIQCWDNATRGLDS 333
Cdd:cd03292 103 LEV-------TGVPPREIRKRVPAA-LELVGLSHKHRA-----LPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180
....*....|....*....|....
gi 353526216 334 ATALEFIRALKTS----ATILDTT 353
Cdd:cd03292 170 DTTWEIMNLLKKInkagTTVVVAT 193
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
876-1076 |
1.74e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 54.37 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIITDGERLVNGHALdSSFQRSIGYVQQQDvhlETTTVREA 953
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIgiEKVKSGEIFYNNQAITDDNF-EKLRKHIGIVFQNP---DNQFVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 954 LQFS-AYLRQSNKISKKEKDDYVDYVIDLLEMTDYADAlvgvAGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS 1032
Cdd:PRK13648 101 VKYDvAFGLENHAVPYDEMHRRVSEALKQVDMLERADY----EPNALSGGQKQRVAIAGVLALNPSVII-LDEATSMLDP 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 353526216 1033 QTAWSICKLMRKL-ADHGQAILCTIHQPSAliMAEFDKLLFLQKG 1076
Cdd:PRK13648 176 DARQNLLDLVRKVkSEHNITIISITHDLSE--AMEADHVIVMNKG 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
176-387 |
1.78e-07 |
|
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: 55.68 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 176 RPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDG-----LSPHDIeRHYRGDVIYsaetdVH-------FPH 243
Cdd:COG1123 289 RRGETLGLVGESGSGKSTLARLLL----GLLRPTSGSILFDGkdltkLSRRSL-RELRRRVQM-----VFqdpysslNPR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 244 LSVGDTLEFAARLRTPQNRGEGIDRetyakhmASVYMATYGLShtrnTNVGNDFVRGVSGGERKRVSIAEASLSGANIQC 323
Cdd:COG1123 359 MTVGDIIAEPLRLHGLLSRAERRER-------VAELLERVGLP----PDLADRYPHELSGGQRQRVAIARALALEPKLLI 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 324 WDNATRGLDSATA---LEFIRALKTSatiLDTTpLIAIyqcSQD---AYELFDNVVVLYEGYQIFFGKAS 387
Cdd:COG1123 428 LDEPTSALDVSVQaqiLNLLRDLQRE---LGLT-YLFI---SHDlavVRYIADRVAVMYDGRIVEDGPTE 490
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
860-1076 |
1.96e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 54.35 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKiKKEDRVILDHVDGWVKPGQITALMGASGAGKTT---LLNCLSERVTTGIITDGERLVNGHALDssFQRSIG 936
Cdd:PRK13650 8 KNLTFKYK-EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLEAESGQIIIDGDLLTEENVWD--IRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 937 YV-QQQDVHLETTTVREALQFSAylrqSNK-ISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELV 1014
Cdd:PRK13650 85 MVfQNPDNQFVGATVEDDVAFGL----ENKgIPHEEMKERVNEALELVGMQDFKEREPARLSGG----QKQRVAIAGAVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353526216 1015 AKPKLLLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQPSALIMAefDKLLFLQKG 1076
Cdd:PRK13650 157 MRPKIII-LDEATSMLDPEGRLELIKTIKGIrDDYQMTVISITHDLDEVALS--DRVLVMKNG 216
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
886-1045 |
2.11e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.22 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 886 GQITALMGASGAGKTTLLNCLSERVTTG---IITDGERLvnGHALDSSFQRSIGYVQQQDVHLETTTVREALQFSAYLRQ 962
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAhghVWLDGEHI--QHYASKEVARRIGLLAQNATTPGDITVQELVARGRYPHQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 963 SNKIS-KKEKDDYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKL 1041
Cdd:PRK10253 111 PLFTRwRKEDEEAVTKAMQATGITHLADQSVDTLSGG----QRQRAWIAMVLAQETAIML-LDEPTTWLDISHQIDLLEL 185
|
....
gi 353526216 1042 MRKL 1045
Cdd:PRK10253 186 LSEL 189
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
162-314 |
2.22e-07 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 53.39 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 162 SKYFD---ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIERHYRG-DVIYsaET 237
Cdd:cd03300 7 SKFYGgfvALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIA----GFETPTSGEILLDGKDITNLPPHKRPvNTVF--QN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 353526216 238 DVHFPHLSVGDTLEFAARLRtpqNRGEGIDRETYAKHMASVYMATYglshtrntnvGNDFVRGVSGGERKRVSIAEA 314
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLK---KLPKAEIKERVAEALDLVQLEGY----------ANRKPSQLSGGQQQRVAIARA 144
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
871-1069 |
2.38e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.03 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 871 EDRVILDHVDGWVKPGQITALMGASGAGKTTLLnclseRVTTGIIT--DGERLVNGHALD---SSFQRSIGYVQQQDVHL 945
Cdd:PRK13540 12 HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLL-----KLIAGLLNpeKGEILFERQSIKkdlCTYQKQLCFVGHRSGIN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 946 ETTTVREALQFSAYLRQSNKiskkekddYVDYVIDLLEMTDYADALVGVAGEGlnveQRKRLTIGVELVAKPKLLLfLDE 1025
Cdd:PRK13540 87 PYLTLRENCLYDIHFSPGAV--------GITELCRLFSLEHLIDYPCGLLSSG----QKRQVALLRLWMSKAKLWL-LDE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 353526216 1026 PTSGLDSQtawSICKLMRKLADH---GQAILCTIHQPSALIMAEFDK 1069
Cdd:PRK13540 154 PLVALDEL---SLLTIITKIQEHrakGGAVLLTSHQDLPLNKADYEE 197
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
861-1056 |
2.43e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 53.87 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 861 DLTYQVKikKEDRVILDHVDGWVKPGQITALMGASGAGKTTL---LNCLSeRVTTGIITdgerlVNGHALDSS----FQR 933
Cdd:PRK13635 10 HISFRYP--DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLaklLNGLL-LPEAGTIT-----VGGMVLSEEtvwdVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 934 SIGYV-QQQDVHLETTTVREALQFSAylrQSNKISKKEKDDYVDYVIDLLEMTDYAD----ALVGvageglnvEQRKRLT 1008
Cdd:PRK13635 82 QVGMVfQNPDNQFVGATVQDDVAFGL---ENIGVPREEMVERVDQALRQVGMEDFLNrephRLSG--------GQKQRVA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 353526216 1009 IGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTI 1056
Cdd:PRK13635 151 IAGVLALQPDIII-LDEATSMLDPRGRREVLETVRQLKEQKGITVLSI 197
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
167-384 |
2.47e-07 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 52.32 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIE---RHYRGdVIYSAetdvhfPH 243
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLT----GDLKPQQGEITLDGVPVSDLEkalSSLIS-VLNQR------PY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 244 LsvgdtleFAARLRTpqnrgegidretyakhmasvymatyglshtrntNVGNDFvrgvSGGERKRVSIAEASLSGANIQC 323
Cdd:cd03247 86 L-------FDTTLRN---------------------------------NLGRRF----SGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 353526216 324 WDNATRGLDSATALEFIR----ALKTSATILDTTPLIAIyqcsqdayELFDNVVVLYEGYQIFFG 384
Cdd:cd03247 122 LDEPTVGLDPITERQLLSlifeVLKDKTLIWITHHLTGI--------EHMDKILFLENGKIIMQG 178
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
865-940 |
2.78e-07 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 51.30 E-value: 2.78e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 353526216 865 QVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERV--TTGIITDGERLvnghaldssfqrSIGYVQQ 940
Cdd:cd03221 5 NLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELepDEGIVTWGSTV------------KIGYFEQ 70
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
888-1075 |
3.69e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 53.31 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 888 ITALMGASGAGKTTLL---NCLSE-----RVTTGIITDGERLVNGHALDSSFQRSIGYVQQQDVHLETTTVREALQFSAY 959
Cdd:PRK14267 32 VFALMGPSGCGKSTLLrtfNRLLElneeaRVEGEVRLFGRNIYSPDVDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 960 LRQSNKiSKKEKDDYVDYVID---LLE-----MTDYADALVGvageglnvEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 1031
Cdd:PRK14267 112 LNGLVK-SKKELDERVEWALKkaaLWDevkdrLNDYPSNLSG--------GQRQRLVIARALAMKPKILL-MDEPTANID 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 353526216 1032 SQTAWSICKLMRKLADHGQAILCTiHQPS-ALIMAEFDKLLFLQK 1075
Cdd:PRK14267 182 PVGTAKIEELLFELKKEYTIVLVT-HSPAqAARVSDYVAFLYLGK 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
866-1076 |
4.10e-07 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 54.42 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 866 VKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCL----SERVTTGIIT-----------------DGERL-VN 923
Cdd:TIGR03269 6 LTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdQYEPTSGRIIyhvalcekcgyverpskVGEPCpVC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 924 GHALDSS----------------------FQRSIGYVQQQDVhLETttVREALQFSAYlrqsnkiskkEKDDYVDYVIDL 981
Cdd:TIGR03269 86 GGTLEPEevdfwnlsdklrrrirkriaimLQRTFALYGDDTV-LDN--VLEALEEIGY----------EGKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 982 LEMTDYADALVGVAGEgLNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIHQPS 1060
Cdd:TIGR03269 153 IEMVQLSHRITHIARD-LSGGEKQRVVLARQLAKEP-FLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPE 230
|
250
....*....|....*..
gi 353526216 1061 alIMAEF-DKLLFLQKG 1076
Cdd:TIGR03269 231 --VIEDLsDKAIWLENG 245
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
868-1076 |
4.27e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 53.80 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 868 IKK--EDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTG-IITDGERLVNGHALdssfQRSIGYVQQQD 942
Cdd:PRK09452 20 ISKsfDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAgfETPDSGrIMLDGQDITHVPAE----NRHVNTVFQSY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 943 VHLETTTVREALQFSayLRqsnkISKKEKDDYVDYVIDLLEMT---DYAD----ALVGvaGeglnveQRKRLTIGVELVA 1015
Cdd:PRK09452 96 ALFPHMTVFENVAFG--LR----MQKTPAAEITPRVMEALRMVqleEFAQrkphQLSG--G------QQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 353526216 1016 KPKLLLfLDEPTSGLD----SQTAWSICKLMRKLadhGQA-ILCTIHQPSALIMAefDKLLFLQKG 1076
Cdd:PRK09452 162 KPKVLL-LDESLSALDyklrKQMQNELKALQRKL---GITfVFVTHDQEEALTMS--DRIVVMRDG 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
752-1063 |
4.28e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.92 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 752 YQFYSSHKWRNFGITVAFAVFFLGV-YVALTEFNKGAMQKGEIVLFLKGSLKKHKRKTAASNKGDIEAGPVAGKLDY--- 827
Cdd:TIGR01271 1102 FLYLSTLRWFQMRIDIIFVFFFIAVtFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFidl 1181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 828 -QDEAEAVNNEKFTEKGSTGSVDFPENREIffW--------RDLTyqVKIKKEDRVILDHVDGWVKPGQITALMGASGAG 898
Cdd:TIGR01271 1182 pQEEPRPSGGGGKYQLSTVLVIENPHAQKC--WpsggqmdvQGLT--AKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSG 1257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 899 KTTLLNCLSERVTtgiiTDGERLVNGHALDS----SFQRSIGYVQQQdVHLETTTVREALqfSAYLRQSNK-ISKKEKDD 973
Cdd:TIGR01271 1258 KSTLLSALLRLLS----TEGEIQIDGVSWNSvtlqTWRKAFGVIPQK-VFIFSGTFRKNL--DPYEQWSDEeIWKVAEEV 1330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 974 YVDYVIDllEMTDYADALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAIL 1053
Cdd:TIGR01271 1331 GLKSVIE--QFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILL-LDEPSAHLDPVTLQIIRKTLKQSFSNCTVIL 1407
|
330
....*....|
gi 353526216 1054 CTiHQPSALI 1063
Cdd:TIGR01271 1408 SE-HRVEALL 1416
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
165-379 |
5.79e-07 |
|
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: 52.23 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 165 FDILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIavntYGFHIGKESQITYDGLSPHDIERHY-RGDVIYSAETDVHFph 243
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL----FRFYDVSSGSILIDGQDIREVTLDSlRRAIGVVPQDTVLF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 244 lsvGDTLEFAARLRTPQNRGEGIDRETYAKHMASVYMatyGLSHTRNTNVGNdfvRGV--SGGERKRVSIAEASLSGANI 321
Cdd:cd03253 88 ---NDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIM---RFPDGYDTIVGE---RGLklSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353526216 322 QCWDNATRGLDSATALEFIRALKTSATiLDTTPLIA-----IYQCsqdayelfDNVVVLYEGY 379
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAhrlstIVNA--------DKIIVLKDGR 212
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
866-1031 |
6.11e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.49 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 866 VKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSER----VTTGIIT-DGERLVN-------GHALDSSFQR 933
Cdd:PRK09580 7 LHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedyeVTGGTVEfKGKDLLElspedraGEGIFMAFQY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 934 SI---GYVQQQDVHLETTTVREalqfsayLRQSNKISKKEKDDYVDYVIDLLEMTdyADALVGVAGEGLNVEQRKRLTIG 1010
Cdd:PRK09580 87 PVeipGVSNQFFLQTALNAVRS-------YRGQEPLDRFDFQDLMEEKIALLKMP--EDLLTRSVNVGFSGGEKKRNDIL 157
|
170 180
....*....|....*....|.
gi 353526216 1011 VELVAKPKLLLfLDEPTSGLD 1031
Cdd:PRK09580 158 QMAVLEPELCI-LDESDSGLD 177
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
860-1083 |
6.37e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 52.82 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKikkEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLServttGIIT--DGERLVNGHALDSSFQRSI-- 935
Cdd:PRK13647 8 EDLHFRYK---DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLN-----GIYLpqRGRVKVMGREVNAENEKWVrs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 936 --GYV-QQQDVHLETTTVREALQFSAylrQSNKISKKEKDDYVDYVIDLLEMTDYADAlvgvAGEGLNVEQRKRLTIGVE 1012
Cdd:PRK13647 80 kvGLVfQDPDDQVFSSTVWDDVAFGP---VNMGLDKDEVERRVEEALKAVRMWDFRDK----PPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 353526216 1013 LVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSalIMAEFDKLLFLQKGGRTAYFG 1083
Cdd:PRK13647 153 LAMDPDVIV-LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVD--LAAEWADQVIVLKEGRVLAEG 220
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
875-1046 |
6.73e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 53.31 E-value: 6.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 875 ILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIITDGERLVNghALDSSfQRSIGYVQQQDV---HLettT 949
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAglERITSGEIWIGGRVVN--ELEPA-DRDIAMVFQNYAlypHM---S 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 950 VREALqfsAYLRQSNKISKKEKDDYVDYVIDLLEMTDYAD----ALVGvaGeglnveQRKRLTIGVELVAKPKLLLFlDE 1025
Cdd:PRK11650 93 VRENM---AYGLKIRGMPKAEIEERVAEAARILELEPLLDrkprELSG--G------QRQRVAMGRAIVREPAVFLF-DE 160
|
170 180
....*....|....*....|....*
gi 353526216 1026 PTSGLDS----QTAWSICKLMRKLA 1046
Cdd:PRK11650 161 PLSNLDAklrvQMRLEIQRLHRRLK 185
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
876-1070 |
6.76e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIIT-DGERLVNGHALDsSFQRSIGyVQQQDVHL-ETTTVR 951
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSgnYQPDAGSILiDGQEMRFASTTA-ALAAGVA-IIYQELHLvPEMTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 952 EALqfsaYLRQ-SNKISkkekddyvdyVIDLLEMtdYADALVGVAGEGLNVE---QRKRLTIG----VElVAKPKLL--- 1020
Cdd:PRK11288 98 ENL----YLGQlPHKGG----------IVNRRLL--NYEAREQLEHLGVDIDpdtPLKYLSIGqrqmVE-IAKALARnar 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 353526216 1021 -LFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsaliMAEFDKL 1070
Cdd:PRK11288 161 vIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHR-----MEEIFAL 206
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
863-1057 |
7.27e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.44 E-value: 7.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 863 TYQVKIKKEDRVILDhVDGWVKPGQITALMGASGAGKTT---LLNCLSERvTTGIITDGERLVNGHALDS---SFQRSIG 936
Cdd:PRK13649 11 TYQAGTPFEGRALFD-VNLTIEDGSYTAFIGHTGSGKSTimqLLNGLHVP-TQGSVRVDDTLITSTSKNKdikQIRKKVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 937 YVQQ-QDVHLETTTVREALQFSAylrQSNKISKKEKDdyvdyvidllEMTDYADALVGVAGE-------GLNVEQRKRLT 1008
Cdd:PRK13649 89 LVFQfPESQLFEETVLKDVAFGP---QNFGVSQEEAE----------ALAREKLALVGISESlfeknpfELSGGQMRRVA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 353526216 1009 IGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 1057
Cdd:PRK13649 156 IAGILAMEPKILV-LDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
159-345 |
7.69e-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: 53.68 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 159 PDDSKYfdILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIE-RHYRGDVIYSAET 237
Cdd:COG2274 484 PGDSPP--VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL----GLYEPTSGRILIDGIDLRQIDpASLRRQIGVVLQD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 238 DVHF------------PHLSVgDTLEFAARLrtpqnrgEGIDRETYAKHMasvymatyGLshtrNTNVGnDFVRGVSGGE 305
Cdd:COG2274 558 VFLFsgtirenitlgdPDATD-EEIIEAARL-------AGLHDFIEALPM--------GY----DTVVG-EGGSNLSGGQ 616
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 353526216 306 RKRVSIAEASLSGANIQCWDNATRGLDSATALEFIRALKT 345
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRR 656
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
876-1051 |
1.02e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.01 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTG-----IITDGERLVNGHALDSSfQRSIGYVQQQDVHLETTTV 950
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyegeIIFEGEELQASNIRDTE-RAGIAIIHQELALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 951 REALqfsaYLrqSNKISKKEkddyvdyVIDLLEMTDYADALVGVAGEGLNVEQR-KRLTIG----VEL---VAKPKLLLF 1022
Cdd:PRK13549 100 LENI----FL--GNEITPGG-------IMDYDAMYLRAQKLLAQLKLDINPATPvGNLGLGqqqlVEIakaLNKQARLLI 166
|
170 180
....*....|....*....|....*....
gi 353526216 1023 LDEPTSGLDSQTAWSICKLMRKLADHGQA 1051
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDLKAHGIA 195
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
875-1076 |
1.12e-06 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 50.87 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 875 ILDHVDGWVKPGQITALMGASGAGKTTLLNCL---SERVTTGIITDGE--RLVNGHALdssfQRSIGYVqQQDVHLETTT 949
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALfrfLEAEEGKIEIDGIdiSTIPLEDL----RSSLTII-PQDPTLFSGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 950 VREALQfsaylrqsnkiskkEKDDYVDYVIdllemtdYADALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 1029
Cdd:cd03369 98 IRSNLD--------------PFDEYSDEEI-------YGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLV-LDEATAS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 353526216 1030 LDSQTAWSICKLMRKLADhGQAILCTIHQPSALImaEFDKLLFLQKG 1076
Cdd:cd03369 156 IDYATDALIQKTIREEFT-NSTILTIAHRLRTII--DYDKILVMDAG 199
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
167-378 |
1.29e-06 |
|
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: 50.95 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIA-VNTYgfhigKESQITYDGLSPH---DIER-HYRGD---VIYSaetd 238
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGgLDRP-----TSGEVRVDGTDISklsEKELaAFRRRhigFVFQ---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 239 vHF---PHLSVGDTLEFAARLRTPQNRgegiDRETYAKHMASVYmatyGLSHTRNTNVGNdfvrgVSGGERKRVSIAEAS 315
Cdd:cd03255 90 -SFnllPDLTALENVELPLLLAGVPKK----ERRERAEELLERV----GLGDRLNHYPSE-----LSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353526216 316 LSGANIQCWDNATRGLDSATALEFIRALKTSATILDTTPLIAIYqcSQDAYELFDNVVVLYEG 378
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTH--DPELAEYADRIIELRDG 216
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
167-378 |
1.44e-06 |
|
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: 51.07 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIERH-YRGDVIYSAETDVHFPhls 245
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLM----RFYDPQKGQILIDGIDIRDISRKsLRSMIGVVLQDTFLFS--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 246 vgDTLEFAARLRTPQNRGEGIDRETYAKHMASVYMAtygLSHTRNTNVGNdfvRG--VSGGERKRVSIAEASLSGANIQC 323
Cdd:cd03254 91 --GTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMK---LPNGYDTVLGE---NGgnLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 353526216 324 WDNATRGLDSAT------ALEFIRALKTSATI---LDTTpliaiyqcsQDAyelfDNVVVLYEG 378
Cdd:cd03254 163 LDEATSNIDTETekliqeALEKLMKGRTSIIIahrLSTI---------KNA----DKILVLDDG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
162-314 |
1.68e-06 |
|
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: 50.61 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 162 SKYFD---ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLsphdierhyrgdVIYSAETD 238
Cdd:cd03262 7 HKSFGdfhVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCIN----LLEEPDSGTIIIDGL------------KLTDDKKN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 239 VH---------------FPHLSVGDTLEFAARLRTPQNRGEGIDRetyakhmASVYMATYGLSHTRntnvgNDFVRGVSG 303
Cdd:cd03262 71 INelrqkvgmvfqqfnlFPHLTVLENITLAPIKVKGMSKAEAEER-------ALELLEKVGLADKA-----DAYPAQLSG 138
|
170
....*....|.
gi 353526216 304 GERKRVSIAEA 314
Cdd:cd03262 139 GQQQRVAIARA 149
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
860-1053 |
1.81e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 52.33 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLT--YQVKIKKEDRVILDhVDGW------------VKPGQITALMGASGAGKTTLLNCL--SERVTTGIIT-DGERLV 922
Cdd:COG1129 239 RELEdlFPKRAAAPGEVVLE-VEGLsvggvvrdvsfsVRAGEILGIAGLVGAGRTELARALfgADPADSGEIRlDGKPVR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 923 NGHALDSsFQRSIGYV----QQQDVHLETTtVREALQFSAYLRQSNK--ISKKEKDDYVDYVIDLLEM-TDYADALVGva 995
Cdd:COG1129 318 IRSPRDA-IRAGIAYVpedrKGEGLVLDLS-IRENITLASLDRLSRGglLDRRRERALAEEYIKRLRIkTPSPEQPVG-- 393
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 353526216 996 geGL---NveQRKRLtIGVELVAKPKLLLfLDEPTSGLD----SQtawsICKLMRKLADHGQAIL 1053
Cdd:COG1129 394 --NLsggN--QQKVV-LAKWLATDPKVLI-LDEPTRGIDvgakAE----IYRLIRELAAEGKAVI 448
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
167-317 |
1.93e-06 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 50.17 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHigkESQITYDG---LSPHDIER---HYRGdVIYSAETDVH 240
Cdd:COG4136 16 LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIA----GTL---SPAFSASGevlLNGRRLTAlpaEQRR-IGILFQDDLL 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 353526216 241 FPHLSVGDTLEFAarlrTPQNRGEGIDRETYAKHMASVymatyGLSHtrntnVGNDFVRGVSGGERKRVSIAEASLS 317
Cdd:COG4136 88 FPHLSVGENLAFA----LPPTIGRAQRRARVEQALEEA-----GLAG-----FADRDPATLSGGQRARVALLRALLA 150
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
863-1045 |
2.09e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 51.23 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 863 TYQVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIIT-DGERLVnghALDSS--------- 930
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVglESPSQGNVSwRGEPLA---KLNRAqrkafrrdi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 931 ---FQRSIGYVQQQdvhletTTVREALqfSAYLRQSNKISKKEKDDYVDyviDLLEMTDYADALVGVAGEGLNVEQRKRL 1007
Cdd:PRK10419 92 qmvFQDSISAVNPR------KTVREII--REPLRHLLSLDKAERLARAS---EMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 353526216 1008 TIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 1045
Cdd:PRK10419 161 CLARALAVEPKLLI-LDEAVSNLDLVLQAGVIRLLKKL 197
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
867-1057 |
2.22e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.24 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 867 KIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLnclseRVTTGIITDgerlVNGHALDSSfQRSIGYVQQQDVHLE 946
Cdd:TIGR03719 12 KVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLL-----RIMAGVDKD----FNGEARPQP-GIKVGYLPQEPQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 947 TTTVREALQFS-----AYLRQSNKISKK--EKDDYVDYVID----LLEMTDYADAL-----VGVAGEGL-------NVE- 1002
Cdd:TIGR03719 82 TKTVRENVEEGvaeikDALDRFNEISAKyaEPDADFDKLAAeqaeLQEIIDAADAWdldsqLEIAMDALrcppwdaDVTk 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1003 ----QRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT-AWsickLMRKLADHGQAILCTIH 1057
Cdd:TIGR03719 162 lsggERRRVALCRLLLSKPDMLL-LDEPTNHLDAESvAW----LERHLQEYPGTVVAVTH 216
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
176-396 |
2.32e-06 |
|
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: 50.41 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 176 RPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIE-RHYRGDVIYsaetdVH-FP-----HLSVGD 248
Cdd:COG1122 25 EKGEFVAIIGPNGSGKSTLLRLLN----GLLKPTSGEVLVDGKDITKKNlRELRRKVGL-----VFqNPddqlfAPTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 249 TLEFAarlrtPQNRgeGIDRETyAKHMASVYMATYGLSHTRNTNVGNdfvrgVSGGERKRVSIAeaslsGA-----NIQC 323
Cdd:COG1122 96 DVAFG-----PENL--GLPREE-IRERVEEALELVGLEHLADRPPHE-----LSGGQKQRVAIA-----GVlamepEVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 353526216 324 WDNATRGLDSATALEFIRALKTSATiLDTTPLIAiyqcSQD---AYELFDNVVVLYEGYQIFFGkasKAKEYFENM 396
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIV----THDldlVAELADRVIVLDDGRIVADG---TPREVFSDY 225
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
872-1031 |
3.33e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTGIITD----GERLVNGHAL-DssFQRSIGYVQQQdVHLE 946
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDltlfGRRRGSGETIwD--IKKHIGYVSSS-LHLD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 947 ---TTTVREALqFSAY-----LRQ--SNKISKKekddyVDYVIDLLEMTDY-ADALVgvagEGLNVEQRKRLTIGVELVA 1015
Cdd:PRK10938 349 yrvSTSVRNVI-LSGFfdsigIYQavSDRQQKL-----AQQWLDILGIDKRtADAPF----HSLSWGQQRLALIVRALVK 418
|
170
....*....|....*.
gi 353526216 1016 KPKLLLfLDEPTSGLD 1031
Cdd:PRK10938 419 HPTLLI-LDEPLQGLD 433
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
167-378 |
3.42e-06 |
|
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: 48.97 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIERHYRgdviysaetdvhfphlsv 246
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA----GLLKPSSGEILLDGKDLASLSPKEL------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 247 gdtlefaarlrtpqnrgegidretyAKHMASV--YMATYGLSHTRNTNVGNdfvrgVSGGERKRVSIAEASLSGANIQCW 324
Cdd:cd03214 72 -------------------------ARKIAYVpqALELLGLAHLADRPFNE-----LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 353526216 325 DNATRGLDSATALEFIRALKTSATILDTTPLIAIYQCSQdAYELFDNVVVLYEG 378
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNL-AARYADRVILLKDG 174
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
167-349 |
3.80e-06 |
|
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: 49.92 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIE----RHYRGDViysaETDVHFP 242
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIP----RFYDVDSGRILIDGHDVRDYTlaslRRQIGLV----SQDVFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 243 HLSVGDTLEFAarlrtpqNRGEGIDRETYAKHMASVYMATYGLSHTRNTNVGndfVRGV--SGGERKRVSIAEASLSGAN 320
Cdd:cd03251 89 NDTVAENIAYG-------RPGATREEVEEAARAANAHEFIMELPEGYDTVIG---ERGVklSGGQRQRIAIARALLKDPP 158
|
170 180 190
....*....|....*....|....*....|....*
gi 353526216 321 IQCWDNATRGLDSAT------ALEFIRALKTSATI 349
Cdd:cd03251 159 ILILDEATSALDTESerlvqaALERLMKNRTTFVI 193
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
168-388 |
4.33e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 50.23 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 168 LKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGlSPHDIER----HYRGDV-IYSAETDVHFP 242
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLN----GILKPSSGRILFDG-KPIDYSRkglmKLRESVgMVFQDPDNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 243 HLSVGDTLEFAA-RLRTPQNR-GEGIDREtyakhmasvyMATYGLSHTRNTNVgndfvRGVSGGERKRVSIAEASLSGAN 320
Cdd:PRK13636 97 SASVYQDVSFGAvNLKLPEDEvRKRVDNA----------LKRTGIEHLKDKPT-----HCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 353526216 321 IQCWDNATRGLDSATALEFIRALKTSATILDTTPLIAIYQCsqDAYELF-DNVVVLYEGYQIFFGKASK 388
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDI--DIVPLYcDNVFVMKEGRVILQGNPKE 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
847-1049 |
5.22e-06 |
|
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: 50.84 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 847 SVDFPENREIFFwrdltyqvkiKKEDRV-ILDHVDGWVKPGQITALMGASGAGKTTL----LNCLServTTGIIT-DGER 920
Cdd:COG4172 282 KVWFPIKRGLFR----------RTVGHVkAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP---SEGEIRfDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 921 LvngHALDSS------------FQ---------RSIGyvqqqdvhletTTVREALQFsaylrQSNKISKKEKDDYVdyvi 979
Cdd:COG4172 349 L---DGLSRRalrplrrrmqvvFQdpfgslsprMTVG-----------QIIAEGLRV-----HGPGLSAAERRARV---- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 980 dllemtdyADALVGVageGLNVE------------QRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL-A 1046
Cdd:COG4172 406 --------AEALEEV---GLDPAarhryphefsggQRQRIAIARALILEPKLLV-LDEPTSALDVSVQAQILDLLRDLqR 473
|
...
gi 353526216 1047 DHG 1049
Cdd:COG4172 474 EHG 476
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
177-314 |
5.31e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 49.70 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 177 PGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGlSPHDIERHYRGDVIysaETDVHFPHLSVGDTLEFAARL 256
Cdd:PRK11248 26 SGELLVVLGPSGCGKTTLLNLIA----GFVPYQHGSITLDG-KPVEGPGAERGVVF---QNEGLLPWRNVQDNVAFGLQL 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 353526216 257 RtpqnrgeGIDRETyAKHMASVYMATYGLShtrntNVGNDFVRGVSGGERKRVSIAEA 314
Cdd:PRK11248 98 A-------GVEKMQ-RLEIAHQMLKKVGLE-----GAEKRYIWQLSGGQRQRVGIARA 142
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
860-1031 |
5.82e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 49.70 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTYQVKIKKED--RVILDHVDGWVKPGQITALMGASGAGKTTL---LNCLServttgIITDGERLVNGhaLDSS---- 930
Cdd:PRK13633 8 KNVSYKYESNEESteKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALL------IPSEGKVYVDG--LDTSdeen 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 931 ---FQRSIGYV-QQQDVHLETTTVREALQFSAylrQSNKISKKEKDDYVDYVIDLLEMTDYADAlvgvAGEGLNVEQRKR 1006
Cdd:PRK13633 80 lwdIRNKAGMVfQNPDNQIVATIVEEDVAFGP---ENLGIPPEEIRERVDESLKKVGMYEYRRH----APHLLSGGQKQR 152
|
170 180
....*....|....*....|....*
gi 353526216 1007 LTIGVELVAKPKLLLFlDEPTSGLD 1031
Cdd:PRK13633 153 VAIAGILAMRPECIIF-DEPTAMLD 176
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
867-1057 |
6.41e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 867 KIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLnclseRVTTGIITD--GE-RLVNGHaldssfqrSIGYVQQQDV 943
Cdd:PRK11819 14 KVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLL-----RIMAGVDKEfeGEaRPAPGI--------KVGYLPQEPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 944 HLETTTVREALQFS-----AYLRQSNKISKK--EKDDYVDYVIDllEMTDY-------------------ADAL------ 991
Cdd:PRK11819 81 LDPEKTVRENVEEGvaevkAALDRFNEIYAAyaEPDADFDALAA--EQGELqeiidaadawdldsqleiaMDALrcppwd 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353526216 992 --VGVAGEGlnvEQRK----RLtigveLVAKPKLLLfLDEPTSGLDSQT-AWsickLMRKLADHGQAILCTIH 1057
Cdd:PRK11819 159 akVTKLSGG---ERRRvalcRL-----LLEKPDMLL-LDEPTNHLDAESvAW----LEQFLHDYPGTVVAVTH 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
847-1083 |
7.74e-06 |
|
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: 48.68 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 847 SVDFPENREIFFW--RDLTYQVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIITDGERLV 922
Cdd:cd03220 7 SKSYPTYKGGSSSlkKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAgiYPPDSGTVTVRGRVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 923 NGHALDSSFQRSIgyvqqqdvhlettTVREALQFSAYLrqsNKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGlnve 1002
Cdd:cd03220 87 SLLGLGGGFNPEL-------------TGRENIYLNGRL---LGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSG---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1003 QRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSALimAEF-DKLLFLQKgGRTAY 1081
Cdd:cd03220 147 MKARLAFAIATALEPDILL-IDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSI--KRLcDRALVLEK-GKIRF 222
|
..
gi 353526216 1082 FG 1083
Cdd:cd03220 223 DG 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
178-314 |
9.07e-06 |
|
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: 48.41 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 178 GELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIERHYRgDVIYSAETDVHFPHLSVGDTLEFAARLR 257
Cdd:cd03301 26 GEFVVLLGPSGCGKTTTLRMIA----GLEEPTSGRIYIGGRDVTDLPPKDR-DIAMVFQNYALYPHMTVYDNIAFGLKLR 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 353526216 258 tpqnrgeGIDRETYAKHMASVyMATYGLSHtrntnVGNDFVRGVSGGERKRVSIAEA 314
Cdd:cd03301 101 -------KVPKDEIDERVREV-AELLQIEH-----LLDRKPKQLSGGQRQRVALGRA 144
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
162-347 |
1.00e-05 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 48.55 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 162 SKYF---DILKSMDAIMRPGELTVVLGRPGAGCSTLLKTiavntygfhIGKESQIT-----YDGLS---PHDIERHYRGD 230
Cdd:PRK09493 8 SKHFgptQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRC---------INKLEEITsgdliVDGLKvndPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 231 VIYSAETDVHFPHLSVGDTLEFAARlrtpQNRGEGidRETyAKHMASVYMATYGLSHTrntnvGNDFVRGVSGGERKRVS 310
Cdd:PRK09493 79 AGMVFQQFYLFPHLTALENVMFGPL----RVRGAS--KEE-AEKQARELLAKVGLAER-----AHHYPSELSGGQQQRVA 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 353526216 311 IAEASLSGANIQCWDNATRGLDSATALEFIRALKTSA 347
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLA 183
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
866-1031 |
1.15e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 866 VKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLServttgiitdGERLVNGHALDSSFQRSIGYVQQQDVHL 945
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLK----------NEISADGGSYTFPGNWQLAWVNQETPAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 946 ETTTV-------REALQFSAYLRQSNKISKKEKDDYVDYVIDLLEM-TDYADALVGVAGEGLNVEQ------------RK 1005
Cdd:PRK10636 77 PQPALeyvidgdREYRQLEAQLHDANERNDGHAIATIHGKLDAIDAwTIRSRAASLLHGLGFSNEQlerpvsdfsggwRM 156
|
170 180
....*....|....*....|....*.
gi 353526216 1006 RLTIGVELVAKPKLLLfLDEPTSGLD 1031
Cdd:PRK10636 157 RLNLAQALICRSDLLL-LDEPTNHLD 181
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
850-1076 |
1.25e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 50.33 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 850 FPENREIFFwRDltYQVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCL---SERVTTGIITDGERLVNGHA 926
Cdd:TIGR00957 1279 WPPRGRVEF-RN--YCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLfriNESAEGEIIIDGLNIAKIGL 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 927 LDSSFQRSIgyvQQQDVHLETTTVREALQ-FSAYlrqsnkiskkeKDDYVDYVIDLLEMTDYADAL-------VGVAGEG 998
Cdd:TIGR00957 1356 HDLRFKITI---IPQDPVLFSGSLRMNLDpFSQY-----------SDEEVWWALELAHLKTFVSALpdkldheCAEGGEN 1421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 353526216 999 LNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADhgQAILCTIHQPSALIMaEFDKLLFLQKG 1076
Cdd:TIGR00957 1422 LSVGQRQLVCLARALLRKTKILV-LDEATAAVDLETDNLIQSTIRTQFE--DCTVLTIAHRLNTIM-DYTRVIVLDKG 1495
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
152-344 |
1.43e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 49.71 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 152 AINKLKKPDDSKyfDILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAVNtygFHIGkESQITYDGLSPHDIE-RHYRGD 230
Cdd:PRK10789 317 NIRQFTYPQTDH--PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRH---FDVS-EGDIRFHDIPLTKLQlDSWRSR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 231 VIYSAETDVHFphlsvGDTLEFAARLRTPQNRGEGIDRetyAKHMASVYMATYGLSHTRNTNVGNdfvRGV--SGGERKR 308
Cdd:PRK10789 391 LAVVSQTPFLF-----SDTVANNIALGRPDATQQEIEH---VARLASVHDDILRLPQGYDTEVGE---RGVmlSGGQKQR 459
|
170 180 190
....*....|....*....|....*....|....*.
gi 353526216 309 VSIAEASLSGANIQCWDNATRGLDSATALEFIRALK 344
Cdd:PRK10789 460 ISIARALLLNAEILILDDALSAVDGRTEHQILHNLR 495
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
167-378 |
1.62e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 49.72 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCST---LLKTIAVNTYGfhigkesQITYDGLSPHDIERHYrgdviysaetdVHFPH 243
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTvaaLLQNLYQPTGG-------QVLLDGVPLVQYDHHY-----------LHRQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 244 LSVG-DTLEFAARLRtpQNRGEGIDRETYAKHMASVYMA-----TYGLSHTRNTNVGNDFVRgVSGGERKRVSIAEASLS 317
Cdd:TIGR00958 558 ALVGqEPVLFSGSVR--ENIAYGLTDTPDEEIMAAAKAAnahdfIMEFPNGYDTEVGEKGSQ-LSGGQKQRIAIARALVR 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353526216 318 GANIQCWDNATRGLDSAT--ALEFIRALKTSATILDTTPLIAIYQCsqdayelfDNVVVLYEG 378
Cdd:TIGR00958 635 KPRVLILDEATSALDAECeqLLQESRSRASRTVLLIAHRLSTVERA--------DQILVLKKG 689
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
885-1076 |
1.73e-05 |
|
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: 46.21 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 885 PGQITALMGASGAGKTTLLNCLservttgiitdgerlvnghaldssfqrsigyvqqqdvhletttvrealqfsayLRQSN 964
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL-----------------------------------------------------ARELG 27
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 965 KISKKEKddYVDyVIDLLEMTDYADALVGVAGEGLNVEQRKRLTIGVELVAKPKL-LLFLDEPTSGLDSQTAWSI----- 1038
Cdd:smart00382 28 PPGGGVI--YID-GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPdVLILDEITSLLDAEQEALLlllee 104
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 353526216 1039 -CKLMRKLADHGQAILCTIHQP----SALIMAEFDKLLFLQKG 1076
Cdd:smart00382 105 lRLLLLLKSEKNLTVILTTNDEkdlgPALLRRRFDRRIVLLLI 147
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
861-1031 |
1.85e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 48.48 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 861 DLTYQVKIKKEDRVILDhVDGWVKPGQITALMGASGAGKTTLLNCLSERV--TTGIITDGERLVNGHALDS---SFQRSI 935
Cdd:PRK13634 9 EHRYQYKTPFERRALYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqpTSGTVTIGERVITAGKKNKklkPLRKKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 936 GYVQQQDVH-LETTTVREALQFSAylrQSNKISKKEKDDYVDYVIdllemtdyadALVGVAGEGLNVE-------QRKRL 1007
Cdd:PRK13634 88 GIVFQFPEHqLFEETVEKDICFGP---MNFGVSEEDAKQKAREMI----------ELVGLPEELLARSpfelsggQMRRV 154
|
170 180
....*....|....*....|....
gi 353526216 1008 TIGVELVAKPKLLLfLDEPTSGLD 1031
Cdd:PRK13634 155 AIAGVLAMEPEVLV-LDEPTAGLD 177
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
874-1076 |
2.14e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 48.31 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 874 VILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTT--GIITDGErLVNGHALDSSFQ----------------RSI 935
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSkyGTIQVGD-IYIGDKKNNHELitnpyskkiknfkelrRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 936 GYVQQ-QDVHLETTTVREALQFSAYLRQSNKISKKEKDDYvdyvidLLEMTDYADALVGVAGEGLNVEQRKRLTIGVELV 1014
Cdd:PRK13631 119 SMVFQfPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKF------YLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353526216 1015 AKPKLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ-PSALIMAefDKLLFLQKG 1076
Cdd:PRK13631 193 IQPEILIF-DEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTmEHVLEVA--DEVIVMDKG 252
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
863-1076 |
2.54e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.08 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 863 TYQVKIKKEDRViLDHVDGWVKPGQITALMGASGAGKTTLLnclseRVTTGIITD--GERLVNGHALDSS---------F 931
Cdd:PRK13645 15 TYAKKTPFEFKA-LNNTSLTFKKNKVTCVIGTTGSGKSTMI-----QLTNGLIISetGQTIVGDYAIPANlkkikevkrL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 932 QRSIGYV-QQQDVHLETTTVREALQFSAYLRQSNKISKKEKddyvdyVIDLLEMTDYADALVGVAGEGLNVEQRKRLTIG 1010
Cdd:PRK13645 89 RKEIGLVfQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKK------VPELLKLVQLPEDYVKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 353526216 1011 vELVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQPSALIMAEfDKLLFLQKG 1076
Cdd:PRK13645 163 -GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIA-DEVIVMHEG 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
176-314 |
3.92e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 48.09 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 176 RPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDG-----LSPHDIERHyrGDVIysaetdVH-----FPHLS 245
Cdd:COG1129 28 RPGEVHALLGENGAGKSTLMKILS----GVYQPDSGEILLDGepvrfRSPRDAQAA--GIAI------IHqelnlVPNLS 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353526216 246 VGDTLeFAARLrtPQNRGeGID-RETYAKhmASVYMATYGLS---HTRntnvgndfVRGVSGGERKRVSIAEA 314
Cdd:COG1129 96 VAENI-FLGRE--PRRGG-LIDwRAMRRR--ARELLARLGLDidpDTP--------VGDLSVAQQQLVEIARA 154
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
167-311 |
3.96e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 46.63 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDG-----LSPhdiERhYRGDVIYSAETDVHF 241
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVA----SLISPTSGTLLFEGedistLKP---EI-YRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 353526216 242 PHlSVGDTLEFaarlrtP-QNRGEGIDRETYAKHMASvymatYGL-SHTRNTNVgNDfvrgVSGGERKRVSI 311
Cdd:PRK10247 94 GD-TVYDNLIF------PwQIRNQQPDPAIFLDDLER-----FALpDTILTKNI-AE----LSGGEKQRISL 148
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
874-1058 |
4.81e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.74 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 874 VILDHVDGWVKPGQITALMGASGAGKTTLLnclseRVTTGIIT--DGERLVNGHAL-----DSSFQRSIGYVQQQDVHLE 946
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLM-----KIIAGIVPpdSGTLEIGGNPCarltpAKAHQLGIYLVPQEPLLFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 947 TTTVREALQFSAYLRQSNKISKKEKDDYVDYVIDLlemtdyaDALVGVagegLNVEQRKRLTIGVELVAKPKLLLfLDEP 1026
Cdd:PRK15439 100 NLSVKENILFGLPKRQASMQKMKQLLAALGCQLDL-------DSSAGS----LEVADRQIVEILRGLMRDSRILI-LDEP 167
|
170 180 190
....*....|....*....|....*....|..
gi 353526216 1027 TSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 1058
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLAQGVGIVFISHK 199
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
167-340 |
5.76e-05 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 45.60 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGK--ESQITYDG-----LSPHdiERHYRGdvIYSA-ETD 238
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIM----GHPKYEvtEGEILFKGeditdLPPE--ERARLG--IFLAfQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 239 VHFPHLSVGDTLefaarlrtpqnrgegidretyakhmasvymatyglshtRNTNVGndFvrgvSGGERKRVSIAEASLSG 318
Cdd:cd03217 87 PEIPGVKNADFL--------------------------------------RYVNEG--F----SGGEKKRNEILQLLLLE 122
|
170 180
....*....|....*....|..
gi 353526216 319 ANIQCWDNATRGLDsATALEFI 340
Cdd:cd03217 123 PDLAILDEPDSGLD-IDALRLV 143
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
162-378 |
1.10e-04 |
|
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: 45.41 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 162 SKYFDILKSMDAI---MRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDG--LSPHDIERHYRGDVI--YS 234
Cdd:cd03296 9 SKRFGDFVALDDVsldIPSGELVALLGPSGSGKTTLLRLIA----GLERPDSGTILFGGedATDVPVQERNVGFVFqhYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 235 AetdvhFPHLSVGDTLEFAARLRtpqNRGEGIDRETYAKHMASVymatygLSHTRNTNVGNDFVRGVSGGERKRVSIAEA 314
Cdd:cd03296 85 L-----FRHMTVFDNVAFGLRVK---PRSERPPEAEIRAKVHEL------LKLVQLDWLADRYPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 353526216 315 SLSGANIQCWDNATRGLDSATALEFIRALKTSATILDTTPLIAIYQcSQDAYELFDNVVVLYEG 378
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHD-QEEALEVADRVVVMNKG 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
933-1082 |
1.41e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 933 RSIGYVQQQDVHLETTTVREALQFSAYLRQSNKISKKEKDDYVDYVIDLLemTDYADALVGVAGEGLNVEQRKRLTIGVE 1012
Cdd:PTZ00265 1295 RNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESL--PNKYDTNVGPYGKSLSGGQKQRIAIARA 1372
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 1013 LVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSALIMAEfDKLLFLQKGGRTAYF 1082
Cdd:PTZ00265 1373 LLREPKILL-LDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRS-DKIVVFNNPDRTGSF 1440
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
290-349 |
1.46e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 46.49 E-value: 1.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 353526216 290 NTNVGNdfvRG--VSGGERKRVSIAEASLSGANIQCWDNATRGLDSAT------ALEFIRALKTSATI 349
Cdd:PRK13657 462 DTVVGE---RGrqLSGGERQRLAIARALLKDPPILILDEATSALDVETeakvkaALDELMKGRTTFII 526
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
875-1076 |
1.47e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 45.28 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 875 ILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTtgiITDGERLVNG--------HALDSSFqrsigyvqqqdvhle 946
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVD---IFDGKIVIDGidisklplHTLRSRL--------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 947 TTTVREALQFSAYLRQSNKISKKEKDDYVDYVIDLLEMTDYA-------DALVGVAGEGLNVEQRKRLTIGVELVAKPKL 1019
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVkslpgglDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 353526216 1020 LLfLDEPTSGLDSQTAWSICK-LMRKLADhgQAILCTIHQPSALIMAefDKLLFLQKG 1076
Cdd:cd03288 178 LI-MDEATASIDMATENILQKvVMTAFAD--RTVVTIAHRVSTILDA--DLVLVLSRG 230
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
546-698 |
1.55e-04 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 44.42 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 546 GALFFSVLFNAFSSLLeiLSLYEARpivEKHRKYALY----RPSADALASIISELPVKLLMTMSFNIVYYFMVNLRRTAG 621
Cdd:COG0842 8 GLLAMSLLFTALMLTA--LSIARER---EQGTLERLLvtpvSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 353526216 622 NFFFYWLMCASCTLVMSHMFRSIGAVTTTIATAMSLSTVFLLAMIIYAGFVLPIPYILGWSRWIRYINPVTYIFESL 698
Cdd:COG0842 83 SLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEAL 159
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
167-312 |
1.69e-04 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 45.15 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDG-----LSPHDIERHyRGdvIYSAETDVHF 241
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS----GELSPDSGEVRLNGrpladWSPAELARR-RA--VLPQHSSLSF 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 353526216 242 PhLSVGDTLEFAarlRTPQNRGEGIDRETYAKHMASVymatyGLSHTRNTnvgndFVRGVSGGERKRVSIA 312
Cdd:PRK13548 90 P-FTVEEVVAMG---RAPHGLSRAEDDALVAAALAQV-----DLAHLAGR-----DYPQLSGGEQQRVQLA 146
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
162-331 |
1.84e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.93 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 162 SKYF---DILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQIT-----YDGLSPHDIERHYRGdVIY 233
Cdd:PRK09700 12 GKSFgpvHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLS----GIHEPTKGTITinninYNKLDHKLAAQLGIG-IIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 234 SaetdvhfpHLSVGDTLEFAARL---RTPQNRGEGIDRETYAK--HMASVYMATYGLSHTRNTNVGNdfvrgVSGGERKR 308
Cdd:PRK09700 87 Q--------ELSVIDELTVLENLyigRHLTKKVCGVNIIDWREmrVRAAMMLLRVGLKVDLDEKVAN-----LSISHKQM 153
|
170 180
....*....|....*....|...
gi 353526216 309 VSIAEASLSGANIQCWDNATRGL 331
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSL 176
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
859-915 |
2.51e-04 |
|
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: 43.93 E-value: 2.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 859 WRDLTYQV-KIKKEDRVILDHVDGWVKpGQITALMGASGAGKTTLLNCL--SERVTTGII 915
Cdd:cd01854 58 YEKLGYPVlAVSAKTGEGLDELRELLK-GKTSVLVGQSGVGKSTLLNALlpELVLATGEI 116
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
167-343 |
2.68e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.43 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIA------VNTYGFHIGKESQITYDGLSPHDIERHYRGDVIYSAETDVH 240
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltggGAPRGARVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 241 FPhLSVGDTLEFAarlRTPQNRGEGI----DREtyakhMASVYMATYGLShtrnTNVGNDfVRGVSGGERKRVSIA---- 312
Cdd:PRK13547 96 FA-FSAREIVLLG---RYPHARRAGAlthrDGE-----IAWQALALAGAT----ALVGRD-VTTLSGGELARVQFArvla 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 353526216 313 -----EASLSGANIQCWDNATRGLDSA---TALEFIRAL 343
Cdd:PRK13547 162 qlwppHDAAQPPRYLLLDEPTAALDLAhqhRLLDTVRRL 200
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
536-699 |
3.28e-04 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 44.69 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 536 KSTDTFYFRGGALFFSVLFNAFSSLleILSLYEARPIVEKHRKYAL-YRPSADALASIISELPVKLLMTMsfnIVYYFMV 614
Cdd:pfam12698 155 PQSGYAYYLVGLILMIIILIGAAII--AVSIVEEKESRIKERLLVSgVSPLQYWLGKILGDFLVGLLQLL---IILLLLF 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 615 NLRRTAGNFFFYWLMCASCTLVMSHMFRSIGAVTTTIATAMSLSTVFLLAMIIYAGFVLPIPYILGWSRWIRYINPVTYI 694
Cdd:pfam12698 230 GIGIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSP 309
|
....*
gi 353526216 695 FESLM 699
Cdd:pfam12698 310 IDGLL 314
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
876-915 |
3.68e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 44.54 E-value: 3.68e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTLLNCL--SERVTTGII 915
Cdd:PRK01889 185 LDVLAAWLSGGKTVALLGSSGVGKSTLVNALlgEEVQKTGAV 226
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
860-1081 |
4.56e-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: 44.07 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 860 RDLTyqVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTtgiiTDGERLVNGHALDS----SFQRSI 935
Cdd:cd03289 6 KDLT--AKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN----TEGDIQIDGVSWNSvplqKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 936 GYVQQQdVHLETTTVREALqfSAYLRQSNK-ISKKEKDDYVDYVIDllEMTDYADALVGVAGEGLNVEQRKRLTIGVELV 1014
Cdd:cd03289 80 GVIPQK-VFIFSGTFRKNL--DPYGKWSDEeIWKVAEEVGLKSVIE--QFPGQLDFVLVDGGCVLSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 353526216 1015 AKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTiHQPSAliMAEFDKLLFLQKGGRTAY 1081
Cdd:cd03289 155 SKAKILL-LDEPSAHLDPITYQVIRKTLKQAFADCTVILSE-HRIEA--MLECQRFLVIEENKVRQY 217
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
162-314 |
4.82e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 44.17 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 162 SKYFD---ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGlspHDIERhyrgdviYSAET- 237
Cdd:PRK09452 21 SKSFDgkeVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIA----GFETPDSGRIMLDG---QDITH-------VPAENr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 238 DVH--------FPHLSVGDTLEFAARL-RTPQnrgegidRETYAKHMASVYMATygLSHTRNTNvgndfVRGVSGGERKR 308
Cdd:PRK09452 87 HVNtvfqsyalFPHMTVFENVAFGLRMqKTPA-------AEITPRVMEALRMVQ--LEEFAQRK-----PHQLSGGQQQR 152
|
....*.
gi 353526216 309 VSIAEA 314
Cdd:PRK09452 153 VAIARA 158
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
290-378 |
5.42e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 44.43 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 290 NTNVGNdfvRGV--SGGERKRVSIAEASLSGANIQCWDNATRGLDSATALEFIRALKtSATILDTTPLIA-----Iyqcs 362
Cdd:COG5265 485 DTRVGE---RGLklSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR-EVARGRTTLVIAhrlstI---- 556
|
90
....*....|....*.
gi 353526216 363 QDAyelfDNVVVLYEG 378
Cdd:COG5265 557 VDA----DEILVLEAG 568
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
876-1049 |
5.87e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTG-----IITDGErLVNGHALDSSFQRSIGYVQQQdvhletttv 950
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyegeILFDGE-VCRFKDIRDSEALGIVIIHQE--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 951 reaLQFSAYLrqS--------NKISKKEkddyvdyVIDLLEMTDYADALvgVAGEGLNVEQRKRLT-IGV---ELV---- 1014
Cdd:NF040905 87 ---LALIPYL--SiaeniflgNERAKRG-------VIDWNETNRRAREL--LAKVGLDESPDTLVTdIGVgkqQLVeiak 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 353526216 1015 --AKPKLLLFLDEPTSGL---DSQtawSICKLMRKLADHG 1049
Cdd:NF040905 153 alSKDVKLLILDEPTAALneeDSA---ALLDLLLELKAQG 189
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
966-1055 |
5.99e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 966 ISKKEKDDYVDYVIDLLEMTDYAdalvGVAGEGLNVEQRKRLTIGVELVAKPKLLlFLDEPTSGLDSQTAWSICKLMRKL 1045
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAA----GRAAAKYSGGMRRRLDLAASMIGRPAVL-YLDEPTTGLDPRTRNEVWDEVRSM 190
|
90
....*....|
gi 353526216 1046 ADHGQAILCT 1055
Cdd:NF000106 191 VRDGATVLLT 200
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
876-1057 |
6.18e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.54 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTTL---LNCL-----------------------SERVTTGII---TDGERLVNGHA 926
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALllpdtgtiewifkdeknkkktkeKEKVLEKLViqkTRFKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 927 LdssfQRSIGYVQQ-QDVHLETTTVREALQFSAylrQSNKISKKE-KDDYVDYvidlLEMTDYADALVGVAGEGLNVEQR 1004
Cdd:PRK13651 103 I----RRRVGVVFQfAEYQLFEQTIEKDIIFGP---VSMGVSKEEaKKRAAKY----IELVGLDESYLQRSPFELSGGQK 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 353526216 1005 KRLTIGVELVAKPKLLlFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 1057
Cdd:PRK13651 172 RRVALAGILAMEPDFL-VFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
167-410 |
9.13e-04 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 42.81 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAV--NTYGFHIgKESQITYDGLSP----HDIERHYRGDVIYSAETDVH 240
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLleQPEAGTI-RVGDITIDTARSlsqqKGLIRQLRQHVGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 241 FPHLSVGDTLEFAARLRTPQNRGEGIDRetyakhmASVYMATYGLSHTRNTnvgndFVRGVSGGERKRVSIAEASLSGAN 320
Cdd:PRK11264 97 FPHRTVLENIIEGPVIVKGEPKEEATAR-------ARELLAKVGLAGKETS-----YPRRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 321 IQCWDNATRGLDS---ATALEFIRALKTSatilDTTPLIAIYQCSQdAYELFDNVVVLYEGYQIFFGkasKAKEYFENmg 397
Cdd:PRK11264 165 VILFDEPTSALDPelvGEVLNTIRQLAQE----KRTMVIVTHEMSF-ARDVADRAIFMDQGRIVEQG---PAKALFAD-- 234
|
250
....*....|...
gi 353526216 398 wkcPQRQTTADFL 410
Cdd:PRK11264 235 ---PQQPRTRQFL 244
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
168-395 |
9.53e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 42.69 E-value: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 168 LKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIERHYR--GDVIYS-AETDVHFPH- 243
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLS----GLITGDKSAGSHIELLGRTVQREGRlaRDIRKSrANTGYIFQQf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 244 -----LSVGDTLEFAARLRTPQNRG-----EGIDRETYAKHMASVYMATYglSHTRntnvgndfVRGVSGGERKRVSIAE 313
Cdd:PRK09984 96 nlvnrLSVLENVLIGALGSTPFWRTcfswfTREQKQRALQALTRVGMVHF--AHQR--------VSTLSGGQQQRVAIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 314 ASLSGANIQCWDNATRGLDSATA---LEFIRALKTSATIldtTPLIAIYQCSQdAYELFDNVVVLYEGYqIFFGKASKAk 390
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESArivMDTLRDINQNDGI---TVVVTLHQVDY-ALRYCERIVALRQGH-VFYDGSSQQ- 239
|
....*
gi 353526216 391 eyFEN 395
Cdd:PRK09984 240 --FDN 242
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
167-314 |
9.70e-04 |
|
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: 42.76 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTI-AVN--TYGFHI-------GKES------QItydGLSPHDIERHYRG- 229
Cdd:COG1119 18 ILDDISWTVKPGEHWAILGPNGAGKSTLLSLItGDLppTYGNDVrlfgerrGGEDvwelrkRI---GLVSPALQLRFPRd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 230 ----DVIYSAETDvhfphlSVGdtlefaaRLRTPqnrgEGIDRETyAKHMasvyMATYGLSHTRNTNVGNdfvrgVSGGE 305
Cdd:COG1119 95 etvlDVVLSGFFD------SIG-------LYREP----TDEQRER-AREL----LELLGLAHLADRPFGT-----LSQGE 147
|
....*....
gi 353526216 306 RKRVSIAEA 314
Cdd:COG1119 148 QRRVLIARA 156
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
871-1093 |
1.03e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 871 EDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTtgiITDGERLVnghaldssfQRSIGYVQQQdVHLETTTV 950
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFE---ISEGRVWA---------ERSIAYVPQQ-AWIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 951 REALQF-----SAYLRQSNKISKKEKddyvdyviDLLEMTDYADALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLfLDE 1025
Cdd:PTZ00243 738 RGNILFfdeedAARLADAVRVSQLEA--------DLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYL-LDD 808
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 353526216 1026 PTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSALIMAefDKLLFLQkGGRTAYFGELGENCQTMI 1093
Cdd:PTZ00243 809 PLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRA--DYVVALG-DGRVEFSGSSADFMRTSL 873
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
876-1067 |
1.18e-03 |
|
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: 41.93 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 876 LDHVDGWVKPGQITALMGASGAGKTT-LLNCLSERVT-TGIITDGERLVNGHALDSSFQR---SIGYVQQQDvHLETTTV 950
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSlLLAILGEMQTlEGKVHWSNKNESEPSFEATRSRnrySVAYAAQKP-WLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 951 REALQF-SAYLRQSNKISKKEKDDYVDyvIDLLEMTDYADalVGVAGEGLNVEQRKRLTIGVELVAKPKlLLFLDEPTSG 1029
Cdd:cd03290 96 EENITFgSPFNKQRYKAVTDACSLQPD--IDLLPFGDQTE--IGERGINLSGGQRQRICVARALYQNTN-IVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 353526216 1030 LDSQTAWSICK--LMRKLADHGQAILCTIHQPSALIMAEF 1067
Cdd:cd03290 171 LDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHADW 210
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
879-926 |
1.21e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 41.60 E-value: 1.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 353526216 879 VDGWVKPGQITALMGASGAGKTTLLNCLSERVTTGIITDGERLVNGHA 926
Cdd:pfam13481 26 IKGLLPAGGLGLLAGAPGTGKTTLALDLAAAVATGKPWLGGPRVPEQG 73
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
167-388 |
1.24e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 42.34 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTI--AVNTYGFHIGKESQITYDGLSPHDIER-HYRGDVIYSAETDVHFPH 243
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrLIEIYDSKIKVDGKVLYFGKDIFQIDAiKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 244 LSVGDTLEFAArlrtpqnRGEGIDRETYAKHMASVYMATYGLSHTRNTNVgNDFVRGVSGGERKRVSIAEASLSGANIQC 323
Cdd:PRK14246 105 LSIYDNIAYPL-------KSHGIKEKREIKKIVEECLRKVGLWKEVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 353526216 324 WDNATRGLD--SATALE-FIRALKTSATIldttplIAIYQCSQDAYELFDNVVVLYEGYQIFFGKASK 388
Cdd:PRK14246 177 MDEPTSMIDivNSQAIEkLITELKNEIAI------VIVSHNPQQVARVADYVAFLYNGELVEWGSSNE 238
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
872-903 |
1.32e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 42.44 E-value: 1.32e-03
10 20 30
....*....|....*....|....*....|..
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLL 903
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLL 50
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
879-927 |
1.33e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 42.58 E-value: 1.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 353526216 879 VDGWVKPGQITALMGASGAGKTTLLNCLSERVTTGIITDGERLVNGHAL 927
Cdd:COG3598 6 VPGLLPEGGVTLLAGPPGTGKSFLALQLAAAVAAGGPWLGRRVPPGKVL 54
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
167-379 |
1.69e-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: 41.76 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIE-RHYRGDV-IYSAEtdvhfPHL 244
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLE----RFYDPTSGEILLDGVDIRDLNlRWLRSQIgLVSQE-----PVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 245 ---SVGDTLEFAARLRTPqnrgEGIDRetyAKHMASVYMATYGLSHTRNTNVGNdfvRGV--SGGERKRVSIAEASLSGA 319
Cdd:cd03249 89 fdgTIAENIRYGKPDATD----EEVEE---AAKKANIHDFIMSLPDGYDTLVGE---RGSqlSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 353526216 320 NIQCWDNATRGLDSAT------ALEfiRALKTSATILDTTPLIAIyqcsQDAyelfDNVVVLYEGY 379
Cdd:cd03249 159 KILLLDEATSALDAESeklvqeALD--RAMKGRTTIVIAHRLSTI----RNA----DLIAVLQNGQ 214
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
872-1034 |
1.75e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 42.61 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 872 DRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLS--ERVTTGIITDGERLVnghaldssfqrsIGYVQQQDVHLE-TT 948
Cdd:TIGR03719 334 DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITgqEQPDSGTIEIGETVK------------LAYVDQSRDALDpNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 949 TVREAL--------------QFSAYLRQSN-KISKKEKddyvdyvidllemtdyadaLVGVAGEGlnveQRKRLTIGVEL 1013
Cdd:TIGR03719 402 TVWEEIsggldiiklgkreiPSRAYVGRFNfKGSDQQK-------------------KVGQLSGG----ERNRVHLAKTL 458
|
170 180
....*....|....*....|.
gi 353526216 1014 VAKPKLLLfLDEPTSGLDSQT 1034
Cdd:TIGR03719 459 KSGGNVLL-LDEPTNDLDVET 478
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
167-354 |
1.94e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 41.37 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 167 ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIERHYRgdVIYSAetdvHFPHLSV 246
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLA----GLLHVESGQIQIDGKTATRGDRSRF--MAYLG----HLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 247 G-DTLEFAARLRTPQNRgegidretYAKHMASVYMATYGLSHTRNTnvgndFVRGVSGGERKRVSIAEASLSGANIQCWD 325
Cdd:PRK13543 96 DlSTLENLHFLCGLHGR--------RAKQMPGSALAIVGLAGYEDT-----LVRQLSAGQKKRLALARLWLSPAPLWLLD 162
|
170 180 190
....*....|....*....|....*....|...
gi 353526216 326 N--ATRGLDSATALEFIRA--LKTSATILDTTP 354
Cdd:PRK13543 163 EpyANLDLEGITLVNRMISahLRGGGAALVTTH 195
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
162-314 |
2.04e-03 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 42.13 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 162 SKYFDILKSMDAI---MRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGLSPHDIERhYRGDVIYSAETD 238
Cdd:PRK11607 26 TKSFDGQHAVDDVsltIYKGEIFALLGASGCGKSTLLRMLA----GFEQPTAGQIMLDGVDLSHVPP-YQRPINMMFQSY 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 353526216 239 VHFPHLSVGDTLEFAARL-RTPqnRGEGIDRetYAKHMASVYMATYGLSHTRNtnvgndfvrgVSGGERKRVSIAEA 314
Cdd:PRK11607 101 ALFPHMTVEQNIAFGLKQdKLP--KAEIASR--VNEMLGLVHMQEFAKRKPHQ----------LSGGQRQRVALARS 163
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
241-411 |
2.77e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 41.37 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 241 FPHLSVGDTLEFAARL-RTPQNRGEGIDRETYAKHMASVYMATyglshtrnTNVGNDFVRGVSGGERKRVSIAEASLSGA 319
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLnGLVKSKKELDERVEWALKKAALWDEV--------KDRLNDYPSNLSGGQRQRLVIARALAMKP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 320 NIQCWDNATRGLD---SATALEFIRALKTSATILDTTpliaiyQCSQDAYELFDNVVVLYEGYQIFFGKASKAkeyFENm 396
Cdd:PRK14267 169 KILLMDEPTANIDpvgTAKIEELLFELKKEYTIVLVT------HSPAQAARVSDYVAFLYLGKLIEVGPTRKV---FEN- 238
|
170
....*....|....*
gi 353526216 397 gwkcPQRQTTADFLT 411
Cdd:PRK14267 239 ----PEHELTEKYVT 249
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
272-386 |
3.00e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 41.37 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 272 AKHMASVYMATYGLshtrntnvGNDFVR----GVSGGERKRVSIAEASLSGANIQCWDNATRGLDSATALEFIRALKTSA 347
Cdd:PRK13631 152 AKKLAKFYLNKMGL--------DDSYLErspfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK 223
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 353526216 348 TILDTtpLIAIYQCSQDAYELFDNVVVLYEG--------YQIFFGKA 386
Cdd:PRK13631 224 ANNKT--VFVITHTMEHVLEVADEVIVMDKGkilktgtpYEIFTDQH 268
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1003-1045 |
3.03e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.00 E-value: 3.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 353526216 1003 QRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 1045
Cdd:PRK15134 430 QRQRIAIARALILKPSLII-LDEPTSSLDKTVQAQILALLKSL 471
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
860-906 |
3.57e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 39.83 E-value: 3.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 353526216 860 RDLTYQV-KIKKEDRVILDHVDGWVKpGQITALMGASGAGKTTLLNCL 906
Cdd:pfam03193 80 RAIGYPVlFVSAKTGEGIEALKELLK-GKTTVLAGQSGVGKSTLLNAL 126
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
162-226 |
4.85e-03 |
|
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: 39.33 E-value: 4.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 353526216 162 SKYFD---ILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDG-----LSPHDIERH 226
Cdd:cd03216 7 TKRFGgvkALDGVSLSVRRGEVHALLGENGAGKSTLMKILS----GLYKPDSGEILVDGkevsfASPRDARRA 75
|
|
| PDR_CDR |
pfam06422 |
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters ... |
1459-1482 |
5.54e-03 |
|
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: 37.44 E-value: 5.54e-03
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
175-338 |
6.50e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 39.88 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 175 MRPGELTVVLGRPGAGCSTLLKTIAvntyGFHIGKESQITYDGlspHDI------ERHYRGDVIYSAETDVhFPHLSVGD 248
Cdd:PRK10895 26 VNSGEIVGLLGPNGAGKTTTFYMVV----GIVPRDAGNIIIDD---EDIsllplhARARRGIGYLPQEASI-FRRLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 249 TLEFAARLRTPQNRGEGIDRetyakhmASVYMATYGLSHTRNtNVGndfvRGVSGGERKRVSIAEASLSGANIQCWDNAT 328
Cdd:PRK10895 98 NLMAVLQIRDDLSAEQREDR-------ANELMEEFHIEHLRD-SMG----QSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170
....*....|
gi 353526216 329 RGLDSATALE 338
Cdd:PRK10895 166 AGVDPISVID 175
|
|
| CpaF |
COG4962 |
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ... |
893-922 |
6.81e-03 |
|
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443988 [Multi-domain] Cd Length: 386 Bit Score: 40.53 E-value: 6.81e-03
10 20 30
....*....|....*....|....*....|
gi 353526216 893 GASGAGKTTLLNCLServttGIITDGERLV 922
Cdd:COG4962 189 GGTGSGKTTLLNALS-----GFIPPDERIV 213
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
888-1001 |
6.93e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.40 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 888 ITALMGASGAGKTTLLNCLSeRVTTGIITDGERLVNGHALDSSFQRSIGYVQQQDVHLETTTVREALQFSA-YLRQSNKI 966
Cdd:pfam13476 20 LTLITGPNGSGKTTILDAIK-LALYGKTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEITFENNDGRYTYAIeRSRELSKK 98
|
90 100 110
....*....|....*....|....*....|....*
gi 353526216 967 SKKEKDDYVDYVIDLLEMTDYADALVGVAGEGLNV 1001
Cdd:pfam13476 99 KGKTKKKEILEILEIDELQQFISELLKSDKIILPL 133
|
|
| TagG |
COG1682 |
ABC-type polysaccharide/teichoic acid/polyol phosphate export permease [Carbohydrate transport ... |
495-698 |
8.70e-03 |
|
ABC-type polysaccharide/teichoic acid/polyol phosphate export permease [Carbohydrate transport and metabolism];
Pssm-ID: 441288 [Multi-domain] Cd Length: 258 Bit Score: 39.78 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 495 VRYVIARNF-LRMKGDPSIPLISILSQLVMGLILASVFFNL-RKSTDTFYFrggALFFS---VLFNAFSSLLE--ILSLY 567
Cdd:COG1682 13 ILALVRRDLkARYRRSVLGLLWALLNPLLMLLVYTFVFGVLlRAPSGGVPY---ALFLLaglLPWNFFSEALNrgSGSIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353526216 568 EARPIVEKhrkyaLYRPSADA-LASIISELpVKLLMTMSFNIVYYFMVNLRRTAGNFFF------YWLMCASCTLVMS-- 638
Cdd:COG1682 90 ANAGLIKK-----VYFPREILpLARVLSAL-VNFLISLVVLLVVLLLFGVPPSWTLLLLplalllLLLFGLGLGLLLAal 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 353526216 639 -HMFRSIGAVTTTIATAMslstvFLLAMIIYagfvlPIPYILGWSRWIRYINPVTYIFESL 698
Cdd:COG1682 164 nVFFRDVQQIVGLLLQLL-----FFLSPVFY-----PLSTLPEPLRWLLLLNPLTHIIELF 214
|
|
| |
