|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
10-1423 |
0e+00 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 2080.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 10 SNSMRRNSS------VWKKD----SGREIFSRSSREEDDEEALRWAALEKLPTFDRLRKGILTA----SHAGGPI--NEI 73
Cdd:PLN03140 5 GGSMRRSISrsvsrsSRNMEdvfsGGSQSRRRTSSVDEDEEALKWAAIEKLPTYSRLRTSIMKSfvenDVYGNQLlhKEV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 74 DIQKLGFQDTKKLLERLIKVGDDEHEKLLWKLKKRIDRVGIDLPTIEVRFDHLKVEAEVHVGGRALPTFVNFISNFADKF 153
Cdd:PLN03140 85 DVTKLDGNDRQKFIDMVFKVAEEDNEKFLKKFRNRIDRVGIKLPTVEVRFEHLTVEADCYIGSRALPTLPNAARNIAESA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 154 LNTLHLVPNRKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQELKQTGRVTYNGHGMNEFVPQRTAAYI 233
Cdd:PLN03140 165 LGMLGINLAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKVSGEITYNGYRLNEFVPRKTSAYI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 234 GQNDVHIGEMTVRETFAYAARFQGVGSRYDMLTELARREKEANIKPDPDIDIFMKAMSTAGEKTNVMTDYILKILGLEVC 313
Cdd:PLN03140 245 SQNDVHVGVMTVKETLDFSARCQGVGTRYDLLSELARREKDAGIFPEAEVDLFMKATAMEGVKSSLITDYTLKILGLDIC 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 314 ADTMVGDDMLRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIFNGTALISLLQPAPETFNL 393
Cdd:PLN03140 325 KDTIVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFDL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 394 FDDIILIAEGEIIYEGPRDHVVEFFETMGFKCPPRKGVADFLQEVTSKKDQMQYWARRDEPYRFIRVREFAEAFQSFHVG 473
Cdd:PLN03140 405 FDDIILLSEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKKDQEQYWADRNKPYRYISVSEFAERFKSFHVG 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 474 RRIGDELALPFDKTKSHPAALTTKKYGVGIKELVKTSFSREYLLMKRNSFVYYFKFGQLLVMAFLTMTLFFRTEMQKKTE 553
Cdd:PLN03140 485 MQLENELSVPFDKSQSHKAALVFSKYSVPKMELLKACWDKEWLLMKRNAFVYVFKTVQIIIVAAIASTVFLRTEMHTRNE 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 554 VDGSLYTGALFFILMMLMFNGMSELSMTIAKLPVFYKQRDLLFYPAWVYSLPPWLLKIPISFMEAALTTFITYYVIGFDP 633
Cdd:PLN03140 565 EDGALYIGALLFSMIINMFNGFAELALMIQRLPVFYKQRDLLFHPPWTFTLPTFLLGIPISIIESVVWVVITYYSIGFAP 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 634 NVGRLFKQYILLVLMNQMASALFKMVAALGRNMIVANTFGAFAMLVFFALGGVVLSRDDIKKWWIWGYWISPIMYGQNAI 713
Cdd:PLN03140 645 EASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEWAYWVSPLSYGFNAL 724
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 714 LANEFFGHSW-SRAVENSSETLGVTFLKSRGFLPHAYWYWIGTGALLGFVVLFNFGFTLALTFLNSLGKPQAVIAEEPAS 792
Cdd:PLN03140 725 AVNEMFAPRWmNKMASDNSTRLGTAVLNIFDVFTDKNWYWIGVGALLGFTILFNVLFTLALTYLNPLGKKQAIISEETAE 804
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 793 DETELQSARSEGVVEAGANK-------------------------------KRGMVLPFEPHSITFDNVVYSVDMPQEMI 841
Cdd:PLN03140 805 EMEGEEDSIPRSLSSADGNNtrevaiqrmsnpeglsknrdssleaangvapKRGMVLPFTPLAMSFDDVNYFVDMPAEMK 884
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 842 EQGTQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIDGNITISGYPKNQQTFARISGYCEQTDIH 921
Cdd:PLN03140 885 EQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKKQETFARISGYCEQNDIH 964
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 922 SPHVTVYESLVYSAWLRLPKEVDKNKRKIFIEEVMELVELTPLRQALVGLPGESGLSTEQRKRLTIAVELVANPSIIFMD 1001
Cdd:PLN03140 965 SPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMD 1044
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1002 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELFLLKRGGEEIYVGPLGHESTHLINYFESIQGINK 1081
Cdd:PLN03140 1045 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYSGPLGRNSHKIIEYFEAIPGVPK 1124
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1082 ITEGYNPATWMLEVSTTSQEAALGVDFAQVYKNSELYKRNKELIKELSQPAPGSKDLYFPTQYSQSFLTQCMASLWKQHW 1161
Cdd:PLN03140 1125 IKEKYNPATWMLEVSSLAAEVKLGIDFAEHYKSSSLYQRNKALVKELSTPPPGASDLYFATQYSQSTWGQFKSCLWKQWW 1204
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1162 SYWRNPPYTAVRFLFTIGIALMFGTMFWDLGGKTKTRQDLSNAMGSMYTAVLFLGLQNAASVQPVVNVERTVFYREQAAG 1241
Cdd:PLN03140 1205 TYWRSPDYNLVRFFFTLAAALMVGTIFWKVGTKRSNANDLTMVIGAMYAAVLFVGINNCSTVQPMVAVERTVFYRERAAG 1284
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1242 MYSAMPYAFAQVFIEIPYVLVQAIVYGLIVYAMIGFEWTAVKFFWYLFFMYGSFLTFTFYGMMAVAMTPNHHIASVVSSA 1321
Cdd:PLN03140 1285 MYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMMTVSLTPNQQVAAIFAAA 1364
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1322 FYGIWNLFSGFLIPRPSMPVWWEWYYWLCPVAWTLYGLIASQFGDITEPMA----DSNMSVKQFIREFYGYREGFLGVVA 1397
Cdd:PLN03140 1365 FYGLFNLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIVSQYGDVEDTIKvpggAPDPTIKWYIQDHYGYDPDFMGPVA 1444
|
1450 1460
....*....|....*....|....*.
gi 257669152 1398 AMNVIFPLLFAVIFAIGIKSFNFQKR 1423
Cdd:PLN03140 1445 AVLVGFTVFFAFIFAFCIRTLNFQTR 1470
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
99-1366 |
0e+00 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 1214.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 99 EKLLWKLKKRIDRVGIDLP--TIEVRFDHLKVEAeVHVGGRALPTFVNFISNFADKFLNTLHLvPNRKKKFTILNDVSGI 176
Cdd:TIGR00956 6 KAWVKNFRKLIDSDPIYYKpyKLGVAYKNLSAYG-VAADSDYQPTFPNALLKILTRGFRKLKK-FRDTKTFDILKPMDGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 177 VKPGRMALLLGPPSSGKTTLLLALAGKLDQELKQ-TGRVTYNGHGMNEFVPQRTA--AYIGQNDVHIGEMTVRETFAYAA 253
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGvEGVITYDGITPEEIKKHYRGdvVYNAETDVHFPHLTVGETLDFAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 254 RFQGVGSRYDMLTELARREKeanikpdpdidifmkamstagektnvMTDYILKILGLEVCADTMVGDDMLRGISGGQKKR 333
Cdd:TIGR00956 164 RCKTPQNRPDGVSREEYAKH--------------------------IADVYMATYGLSHTRNTKVGNDFVRGVSGGERKR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 334 VTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIFNGTALISLLQPAPETFNLFDDIILIAEGEIIYEGPRDH 413
Cdd:TIGR00956 218 VSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 414 VVEFFETMGFKCPPRKGVADFLQEVTSKKdQMQYWARRDEPYrFIRVREFAEAFQSFHVGRRIGDELALPFDKT------ 487
Cdd:TIGR00956 298 AKQYFEKMGFKCPDRQTTADFLTSLTSPA-ERQIKPGYEKKV-PRTPQEFETYWRNSPEYAQLMKEIDEYLDRCsesdtk 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 488 --------KSHP-AALTTKKYGVGIKELVKTSFSREYLLMKRNSFVYYFKFGQLLVMAFLTMTLFFRTEMqkkTEVDGSL 558
Cdd:TIGR00956 376 eayreshvAKQSkRTRPSSPYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPK---NTSDFYS 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 559 YTGALFFILMMLMFNGMSELSMTIAKLPVFYKQRDLLFYPAWVYSLPPWLLKIPISFMEAALTTFITYYVIGFDPNVGRL 638
Cdd:TIGR00956 453 RGGALFFAILFNAFSSLLEIASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRF 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 639 FKQYILLVLMNQMASALFKMVAALGRNMIVANTFGAFAMLVFFALGGVVLSRDDIKKWWIWGYWISPIMYGQNAILANEF 718
Cdd:TIGR00956 533 FFYLLILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEF 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 719 FGHSW-------------SRAVENSSETL-----GVTFLKSRGFLPHAY-----WYWIGTGALLGFVVLFNFGFTLALTF 775
Cdd:TIGR00956 613 HGRRFecsqyvpsgggydNLGVTNKVCTVvgaepGQDYVDGDDYLKLSFqyynsHKWRNFGIIIGFTVFFFFVYILLTEF 692
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 776 LNSLGKPQAVIAEEpasdETELQSARSEGvVEAGANK---KRGMVLPFEPHSITFDNVVYSVDMPQEM-----------I 841
Cdd:TIGR00956 693 NKGAKQKGEILVFR----RGSLKRAKKAG-ETSASNKndiEAGEVLGSTDLTDESDDVNDEKDMEKESgedifhwrnltY 767
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 842 EQGTQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIDGNITISGYPKNQQTFARISGYCEQTDIH 921
Cdd:TIGR00956 768 EVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLH 847
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 922 SPHVTVYESLVYSAWLRLPKEVDKNKRKIFIEEVMELVELTPLRQALVGLPGEsGLSTEQRKRLTIAVELVANP-SIIFM 1000
Cdd:TIGR00956 848 LPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGE-GLNVEQRKRLTIGVELVAKPkLLLFL 926
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1001 DEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELFLLKRGGEEIYVGPLGHESTHLINYFEsIQGIN 1080
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGGQTVYFGDLGENSHTIINYFE-KHGAP 1005
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1081 KITEGYNPATWMLEVSTTSQEAALGVDFAQVYKNSELYKRNKELIKELSQPAPGSKDLYFPT---QYSQSFLTQCMASLW 1157
Cdd:TIGR00956 1006 KCPEDANPAEWMLEVIGAAPGAHANQDYHEVWRNSSEYQAVKNELDRLEAELSKAEDDNDPDalsKYAASLWYQFKLVLW 1085
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1158 KQHWSYWRNPPYTAVRFLFTIGIALMFGTMFWDLGgktKTRQDLSNAMGSMYTAVLFLGLQNAASVQPVVNVERTVFYRE 1237
Cdd:TIGR00956 1086 RTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVG---TSLQGLQNQMFAVFMATVLFNPLIQQYLPPFVAQRDLYEVRE 1162
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1238 QAAGMYSAMPYAFAQVFIEIPYVLVQAIVYGLIVYAMIGFEWTAVK-------FFWYLFFMYGSFLTFTFYGMMAVAMTP 1310
Cdd:TIGR00956 1163 RPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFYWNASKtgqvherGVLFWLLSTMFFLYFSTLGQMVISFNP 1242
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*.
gi 257669152 1311 NHHIASVVSSAFYGIWNLFSGFLIPRPSMPVWWEWYYWLCPVAWTLYGLIASQFGD 1366
Cdd:TIGR00956 1243 NADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLAD 1298
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
846-1370 |
3.18e-104 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 345.49 E-value: 3.18e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 846 QEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGY-IDGNITISGYPKNQQTFARISGYCEQTDIHSPH 924
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 925 VTVYESLVYSAWLRLPKEVDKNKRKIFIEEVMELVELTPLRQALVGLPGE-SGLSTEQRKRLTIAVELVANPSIIFMDEP 1003
Cdd:TIGR00955 114 LTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvKGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1004 TSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELFLLKrGGEEIYVGPlgheSTHLINYFESIqGINkIT 1083
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMA-EGRVAYLGS----PDQAVPFFSDL-GHP-CP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1084 EGYNPATWMLEVSTTSQ--EAALGVDFAQVYKNSELYKRNKELIKELSQPAPGSKDLYFPTQ------YSQSFLTQCMAS 1155
Cdd:TIGR00955 267 ENYNPADFYVQVLAVIPgsENESRERIEKICDSFAVSDIGRDMLVNTNLWSGKAGGLVKDSEnmegigYNASWWTQFYAL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1156 LWKQHWSYWRNPPYTAVRFLFTIGIALMFGTMFWDLGGKTKTRQDLSnamGSMYTAVLFLGLQNAASVQPVVNVERTVFY 1235
Cdd:TIGR00955 347 LKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNIN---GALFLFLTNMTFQNVFPVINVFTAELPVFL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1236 REQAAGMYSAMPYAFAQVFIEIPYVLVQAIVYGLIVYAMIGFEWTAVKFFWYLFFMYGSFLTFTFYGMMAVAMTPNHHIA 1315
Cdd:TIGR00955 424 RETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMA 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 257669152 1316 SVVSSAFYGIWNLFSGFLIPRPSMPVWWEWYYWLcpvAWTLY---GLIASQFGDITEP 1370
Cdd:TIGR00955 504 LTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYL---SWFRYgneGLLINQWSDVDNI 558
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
822-1060 |
1.45e-99 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 316.11 E-value: 1.45e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 822 PHSITFDNVVYSVDMPQemieqgtqeDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIDGNITISGY 901
Cdd:cd03232 1 GSVLTWKNLNYTVPVKG---------GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 902 PKNQqTFARISGYCEQTDIHSPHVTVYESLVYSAWLRlpkevdknkrkifieevmelveltplrqalvglpgesGLSTEQ 981
Cdd:cd03232 72 PLDK-NFQRSTGYVEQQDVHSPNLTVREALRFSALLR-------------------------------------GLSVEQ 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257669152 982 RKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELFLLKRGGEEIYVG 1060
Cdd:cd03232 114 RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRGGKTVYFG 192
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
824-1060 |
1.39e-72 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 240.15 E-value: 1.39e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 824 SITFDNVVYSVDmpqemieQGTQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIDGNITISGYPK 903
Cdd:cd03213 3 TLSFRNLTVTVK-------SSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 904 NQQTFARISGYCEQTDIHSPHVTVYESLVYSAWLRlpkevdknkrkifieevmelveltplrqalvglpgesGLSTEQRK 983
Cdd:cd03213 76 DKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------------GLSGGERK 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257669152 984 RLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELFLLKRgGEEIYVG 1060
Cdd:cd03213 119 RVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQ-GRVIYFG 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
162-773 |
2.72e-69 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 245.73 E-value: 2.72e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 162 NRKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQELKQTGRVTYNGHGMNEFVPQRTAAYIGQNDVHIG 241
Cdd:TIGR00955 33 RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 242 EMTVRETFAYAARFQgvgsrydmltelarrekeanikpdpdidifMKAMSTAGEKTNvMTDYILKILGLEVCADTMVGD- 320
Cdd:TIGR00955 113 TLTVREHLMFQAHLR------------------------------MPRRVTKKEKRE-RVDEVLQALGLRKCANTRIGVp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 321 DMLRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRnyvHIFNG--TALISLLQPAPETFNLFDDII 398
Cdd:TIGR00955 162 GRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLK---GLAQKgkTIICTIHQPSSELFELFDKII 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 399 LIAEGEIIYEGPRDHVVEFFETMGFKCPPRKGVADFLQEVTSkkdqmqywarrDEPYRFIRVREFAEA-FQSFHVGRRIG 477
Cdd:TIGR00955 239 LMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLA-----------VIPGSENESRERIEKiCDSFAVSDIGR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 478 DELALPFdkTKSHPAALTTKKYGVGIKELVKTSFSRE-YLLMKR-------NSFVYYFKFGQLLVMAFLTMTLFFRTEMQ 549
Cdd:TIGR00955 308 DMLVNTN--LWSGKAGGLVKDSENMEGIGYNASWWTQfYALLKRswlsvlrDPLLLKVRLIQTMMTAILIGLIYLGQGLT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 550 KKTEVDGSlytGALFFILMMLMF-NGMSELSMTIAKLPVFYKQRDLLFYPAWVYSLPPWLLKIPISFMEAALTTFITYYV 628
Cdd:TIGR00955 386 QKGVQNIN---GALFLFLTNMTFqNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWM 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 629 IGFDPNVGRLFKQYILLVLMNQMASALFKMVAALGRNMIVANTFGAFAMLVFFALGGVVLSRDDIKKWWIWGYWISPIMY 708
Cdd:TIGR00955 463 IGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRY 542
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257669152 709 GQNAILANEFFGHSWSRAVENSSETL----GVTFLKSRGFlpHAYWYWIGTGALLGFVVLFNFGFTLAL 773
Cdd:TIGR00955 543 GNEGLLINQWSDVDNIECTSANTTGPcpssGEVILETLSF--RNADLYLDLIGLVILIFFFRLLAYFAL 609
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
159-409 |
4.42e-67 |
|
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: 224.83 E-value: 4.42e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 159 LVPNRKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQELKQTGRVTYNGHGMNEF--VPQRTAAYIGQN 236
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYKEFaeKYPGEIIYVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 237 DVHIGEMTVRETFAYAARFQGvgsrydmltelarrekeanikpdpdidifmkamstagektnvmtdyilkilglevcadt 316
Cdd:cd03233 92 DVHFPTLTVRETLDFALRCKG----------------------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 317 mvgDDMLRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIFNGTALISLLQPAPETFNLFDD 396
Cdd:cd03233 113 ---NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDK 189
|
250
....*....|...
gi 257669152 397 IILIAEGEIIYEG 409
Cdd:cd03233 190 VLVLYEGRQIYYG 202
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
1156-1362 |
4.99e-59 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 201.73 E-value: 4.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1156 LWKQHWSYWRNPPYTAVRFLFTIGIALMFGTMFWDLGgktkTRQDLSNAMGSMYTAVLFLGLQNAASVQPVVNVERTVFY 1235
Cdd:pfam01061 2 LKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG----NQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1236 REQAAGMYSAMPYAFAQVFIEIPYVLVQAIVYGLIVYAMIGFEWTAVKFFWYLFFMYGSFLTFTFYGMMAVAMTPNHHIA 1315
Cdd:pfam01061 78 RELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 257669152 1316 SVVSSAFYGIWNLFSGFLIPRPSMPVWWEWYYWLCPVAWTLYGLIAS 1362
Cdd:pfam01061 158 SQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
852-1060 |
1.48e-55 |
|
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: 192.87 E-value: 1.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYI-DGNITISGYPKNQQTFARISGYCEQTDIHSPHVTVYES 930
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTtSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 931 LVYSAWLRLPKEV-DKNKRKIFIEEVMELVELTPLRQALVglpgeSGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1009
Cdd:cd03234 102 LTYTAILRLPRKSsDAIRKKRVEDVLLRDLALTRIGGNLV-----KGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 257669152 1010 RAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELFLLKRgGEEIYVG 1060
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSS-GEIVYSG 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
837-1366 |
1.56e-49 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 188.16 E-value: 1.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 837 PQEMIEQGTQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIDGNITISGYPKNQQTFARIsGYCE 916
Cdd:PLN03211 68 KPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRT-GFVT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 917 QTDIHSPHVTVYESLVYSAWLRLPKEVDKNKRKIFIEEVMELVELTPLRQALVGLPGESGLSTEQRKRLTIAVELVANPS 996
Cdd:PLN03211 147 QDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 997 IIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELFLLKRgGEEIYVGPlGHESthlINYFESI 1076
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSE-GRCLFFGK-GSDA---MAYFESV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1077 qginKITEGY--NPATWMLEVS---------------------TTSQEAALGVDFAQVYKNSELYKRNKELIKELSQPAP 1133
Cdd:PLN03211 302 ----GFSPSFpmNPADFLLDLAngvcqtdgvserekpnvkqslVASYNTLLAPKVKAAIEMSHFPQANARFVGSASTKEH 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1134 GSKD-LYFPTQYSQ-SFLTQcmaSLWKQHwsywRNPPYTAVRFLFTIGIALMFGTMFWDlggktKTRQDLSNAMGSMYTA 1211
Cdd:PLN03211 378 RSSDrISISTWFNQfSILLQ---RSLKER----KHESFNTLRVFQVIAAALLAGLMWWH-----SDFRDVQDRLGLLFFI 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1212 VLFLGLQNAASVQPVVNVERTVFYREQAAGMYSAMPYAFAQVFIEIPYVLVQAIVYGLIVYAMIGFEWTAVKFFWYLFFM 1291
Cdd:PLN03211 446 SIFWGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVL 525
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257669152 1292 YGSFLTFTFYGMMAVAMTPNHHIASVVSSAFYGIWNLFSGFLIPR-PSMPVWWEWyywlcpVAWTLYG---LIASQFGD 1366
Cdd:PLN03211 526 LGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYVHKlPSCMAWIKY------ISTTFYSyrlLINVQYGE 598
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
511-716 |
8.59e-48 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 169.76 E-value: 8.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 511 FSREYLLMKRNSFVYYFKFGQLLVMAFLTMTLFFRTemqkKTEVDGSLYTGALFFILMMLMFNGMSELSMTIAK-LPVFY 589
Cdd:pfam01061 2 LKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNL----GNQQGGLNRPGLLFFSILFNAFSALSGISPVFEKeRGVLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 590 KQRDLLFYPAWVYSLPPWLLKIPISFMEAALTTFITYYVIGFDPNVGRLFKQYILLVLMNQMASALFKMVAALGRNMIVA 669
Cdd:pfam01061 78 RELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 257669152 670 NTFGAFAMLVFFALGGVVLSRDDIKKWWIWGYWISPIMYGQNAILAN 716
Cdd:pfam01061 158 SQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
164-409 |
4.89e-45 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 161.56 E-value: 4.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 164 KKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDqELKQTGRVTYNGHGMNEFVPQRTAAYIGQNDVHIGEM 243
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRT-GLGVSGEVLINGRPLDKRSFRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 244 TVRETFAYAARfqgvgsrydmltelarrekeanikpdpdidifmkamstagektnvmtdyilkilglevcadtmvgddmL 323
Cdd:cd03213 98 TVRETLMFAAK--------------------------------------------------------------------L 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 324 RGISGGQKKRVTTG-EMLVGPSrALFMDEISTGLDSSTTYQIVNSLRNYVHIfNGTALISLLQPAPETFNLFDDIILIAE 402
Cdd:cd03213 110 RGLSGGERKRVSIAlELVSNPS-LLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSSEIFELFDKLLLLSQ 187
|
....*..
gi 257669152 403 GEIIYEG 409
Cdd:cd03213 188 GRVIYFG 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
160-409 |
3.59e-44 |
|
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: 160.13 E-value: 3.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 160 VPNRKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQELKQTGRVTYNGHGMNEFVPQRTAAYIGQNDVH 239
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQFQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 240 IGEMTVRETFAYAARFQgvgsrydmlteLARREKEANIKP-DPDidifmkamstagektnvmtdyilkiLGLEVCADTMV 318
Cdd:cd03234 93 LPGLTVRETLTYTAILR-----------LPRKSSDAIRKKrVED-------------------------VLLRDLALTRI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 319 GDDMLRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIfNGTALISLLQPAPETFNLFDDII 398
Cdd:cd03234 137 GGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQPRSDLFRLFDRIL 215
|
250
....*....|.
gi 257669152 399 LIAEGEIIYEG 409
Cdd:cd03234 216 LLSSGEIVYSG 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
168-708 |
5.01e-36 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 146.95 E-value: 5.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLdQELKQTGRVTYNGHGMNEFVPQRTAaYIGQNDVHIGEMTVRE 247
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRI-QGNNFTGTILANNRKPTKQILKRTG-FVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 248 TFAYAArfqgvgsrydmlteLARREKEAnikpdpdidifmkamsTAGEKTNVmTDYILKILGLEVCADTMVGDDMLRGIS 327
Cdd:PLN03211 160 TLVFCS--------------LLRLPKSL----------------TKQEKILV-AESVISELGLTKCENTIIGNSFIRGIS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 328 GGQKKRVTTG-EMLVGPSrALFMDEISTGLDSSTTYQIVNSLRNYVHIfNGTALISLLQPAPETFNLFDDIILIAEGEII 406
Cdd:PLN03211 209 GGERKRVSIAhEMLINPS-LLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPSSRVYQMFDSVLVLSEGRCL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 407 YEGPRDHVVEFFETMGFKCPPRKGVADFLQEVTSKKDQMQYWARRDEPyrfiRVRE-FAEAFQSFHVGR-RIGDELALPF 484
Cdd:PLN03211 287 FFGKGSDAMAYFESVGFSPSFPMNPADFLLDLANGVCQTDGVSEREKP----NVKQsLVASYNTLLAPKvKAAIEMSHFP 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 485 DKTKSHPAALTTKKYGVGIKELVKTSFSREYLLMKR-------NSFvYYFKFGQLLVMAFLTMTLFFRTEMQkktEVDGS 557
Cdd:PLN03211 363 QANARFVGSASTKEHRSSDRISISTWFNQFSILLQRslkerkhESF-NTLRVFQVIAAALLAGLMWWHSDFR---DVQDR 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 558 LytGALFFilmMLMFNGMSELSMTIAKLP----VFYKQRDLLFYPAWVYSLPPWLLKIPISFMEAALTTFITYYVIGFDP 633
Cdd:PLN03211 439 L--GLLFF---ISIFWGVFPSFNSVFVFPqeraIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKP 513
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257669152 634 NVGRLFKQYILLVLMNQMASALFKMVAALGRNMIVANTFGAFAMLVFFALGGVVLSRddIKKWWIWGYWISPIMY 708
Cdd:PLN03211 514 ELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYVHK--LPSCMAWIKYISTTFY 586
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
853-1053 |
8.08e-35 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 133.65 E-value: 8.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyidgNITISGYP---KNQQTFARIsGYCEQTDIHSPHVTV 927
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGllRPTSG----EVRVLGEDvarDPAEVRRRI-GYVPQEPALYPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 928 YESLVYSAWLRlpkEVDKNKRKIFIEEVMELVELTPLRQALVGlpgesGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1007
Cdd:COG1131 91 RENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVG-----TLSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 257669152 1008 DARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELFLLKRG 1053
Cdd:COG1131 163 DPEARRELWELLRELAAEGKTVLLSTHYLE-EAERLCDRVAIIDKG 207
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
848-1053 |
1.24e-31 |
|
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: 123.46 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 848 DRLVLLKGVNGAFRPGVlTALMGVSGAGKTTLMDVLAGRKTGGYidGNITISGYP--KNQQTFARISGYCEQTDIHSPHV 925
Cdd:cd03264 11 GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSS--GTIRIDGQDvlKQPQKLRRRIGYLPQEFGVYPNF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 926 TVYESLVYSAWLrlpKEVDKNKRKIFIEEVMELVELTPLRQALVGlpgesGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1005
Cdd:cd03264 88 TVREFLDYIAWL---KGIPSKEVKARVDEVLELVNLGDRAKKKIG-----SLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 257669152 1006 GLDArAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELFLLKRG 1053
Cdd:cd03264 160 GLDP-EERIRFRNLLSELGEDRIVILSTHIVE-DVESLCNQVAVLNKG 205
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
852-1060 |
2.57e-31 |
|
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: 122.37 E-value: 2.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRkTGGY--IDGNITISGYP--KNQQTFARISGYCEQTDIHSPHVTV 927
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR-TEGNvsVEGDIHYNGIPykEFAEKYPGEIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 928 YESLVYSAWLRlpkeVDKNKRkifieevmelveltplrqalvglpgesGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1007
Cdd:cd03233 101 RETLDFALRCK----GNEFVR---------------------------GISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 257669152 1008 DARAAAIVMRTVRNTVD-TGRTVVCTIHQPSIDIFEAFDELFLLkRGGEEIYVG 1060
Cdd:cd03233 150 DSSTALEILKCIRTMADvLKTTTFVSLYQASDEIYDLFDKVLVL-YEGRQIYYG 202
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
853-1034 |
9.89e-31 |
|
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: 121.07 E-value: 9.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyidgNITISGYPKNQQTFA--RISGYCEQTDIHSPHVTVY 928
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGelRPTSG----TAYINGYSIRTDRKAarQSLGYCPQFDALFDELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 929 ESLVYSAWLR-LPK-EVDKNkrkifIEEVMELVELTPLRQALVGlpgesGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1006
Cdd:cd03263 94 EHLRFYARLKgLPKsEIKEE-----VELLLRVLGLTDKANKRAR-----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180
....*....|....*....|....*...
gi 257669152 1007 LDARAAAIVMRTVrNTVDTGRTVVCTIH 1034
Cdd:cd03263 164 LDPASRRAIWDLI-LEVRKGRSIILTTH 190
|
|
| PDR_assoc |
pfam08370 |
Plant PDR ABC transporter associated; This domain is found on the C-terminus of ABC-2 type ... |
723-786 |
1.05e-30 |
|
Plant PDR ABC transporter associated; This domain is found on the C-terminus of ABC-2 type transporter domains (pfam01061). It seems to be associated with the plant pleiotropic drug resistance (PDR) protein family of ABC transporters. Like in yeast, plant PDR ABC transporters may also play a role in the transport of antifungal agents [also pfam06422]. The PDR family is characterized by a configuration in which the ABC domain is nearer the N-terminus of the protein than the transmembrane domain.
Pssm-ID: 462450 [Multi-domain] Cd Length: 65 Bit Score: 115.29 E-value: 1.05e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257669152 723 WSRAVE-NSSETLGVTFLKSRGFLPHAYWYWIGTGALLGFVVLFNFGFTLALTFLNSLGKPQAVI 786
Cdd:pfam08370 1 WMKPTAsNGNTTLGVAVLKSRGLFTEAYWYWIGVGALLGFTILFNILFTLALTYLNPLGKSQAII 65
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
853-1053 |
1.63e-29 |
|
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: 118.42 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKtggYID-GNITISGYPK---NQQTFARIsGYCEQTDIHSPHVTVY 928
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLL---KPDsGSILIDGEDVrkePREARRQI-GVLPDERGLYDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 929 ESLVYSAWLRLPKEVDKNKRkifIEEVMELVELTPLRQALVGlpgesGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1008
Cdd:COG4555 93 ENIRYFAELYGLFDEELKKR---IEELIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 257669152 1009 ARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELFLLKRG 1053
Cdd:COG4555 165 VMARRLLREILRALKKEGKTVLFSSHIMQ-EVEALCDRVVILHKG 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
848-1061 |
2.57e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.88 E-value: 2.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 848 DRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGgyidGNITISGYPKNQQTfARIsGYCEQT---DIHS 922
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGllPPTS----GTVRLFGKPPRRAR-RRI-GYVPQRaevDWDF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 923 PhVTVYEsLVYSA------WLRLPKEVDKNKrkifIEEVMELVELTPLRQALVGLpgesgLSTEQRKRLTIAVELVANPS 996
Cdd:COG1121 91 P-ITVRD-VVLMGrygrrgLFRRPSRADREA----VDEALERVGLEDLADRPIGE-----LSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257669152 997 IIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELFLLKRGGeeIYVGP 1061
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRGL--VAHGP 221
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
160-409 |
6.79e-29 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 115.03 E-value: 6.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 160 VPNRKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQELKqTGRVTYNGHGMNE-FvpQRTAAYIGQNDV 238
Cdd:cd03232 13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVI-TGEILINGRPLDKnF--QRSTGYVEQQDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 239 HIGEMTVRETFAYAArfqgvgsrydmltelarrekeanikpdpdidifmkamstagektnvmtdyilkilglevcadtmv 318
Cdd:cd03232 90 HSPNLTVREALRFSA----------------------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 319 gddMLRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHifNGTALI-SLLQPAPETFNLFDDI 397
Cdd:cd03232 105 ---LLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLAD--SGQAILcTIHQPSASIFEKFDRL 179
|
250
....*....|...
gi 257669152 398 ILIAE-GEIIYEG 409
Cdd:cd03232 180 LLLKRgGKTVYFG 192
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
851-1054 |
2.72e-28 |
|
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: 115.14 E-value: 2.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGnITISGYPKNQqtFARISGYCEQTDIHSPHVT 926
Cdd:COG1120 15 PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGllKPSSGevLLDG-RDLASLSRRE--LARRIAYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 927 VYEsLV------YSAWLRLPKEVDKNKrkifIEEVMELVELTPLRQALVglpgeSGLSTEQRKRLTIAVELVANPSIIFM 1000
Cdd:COG1120 92 VRE-LValgrypHLGLFGRPSAEDREA----VEEALERTGLEHLADRPV-----DELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 257669152 1001 DEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSIdifeAF---DELFLLKRGG 1054
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRlARERGRTVVMVLHDLNL----AAryaDRLVLLKDGR 215
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
852-1053 |
2.25e-27 |
|
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: 111.40 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKtgGYIDGNITISGYPKNQQT---FARISGYCEQtdihSP----- 923
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL--GPTSGEVLVDGKDLTKLSlkeLRRKVGLVFQ----NPddqff 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 924 HVTVYESLVYSawLR---LPKEVDKNKrkifIEEVMELVELTPLRQALVglpgeSGLSTEQRKRLTIAVELVANPSIIFM 1000
Cdd:cd03225 90 GPTVEEEVAFG--LEnlgLPEEEIEER----VEEALELVGLEGLRDRSP-----FTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 257669152 1001 DEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELFLLKRG 1053
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDG 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
853-1053 |
3.87e-27 |
|
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: 110.70 E-value: 3.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyidgNITISGYPKnQQTFARIsGYCEQT---DIHSPhVTV 927
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGllKPTSG----SIRVFGKPL-EKERKRI-GYVPQRrsiDRDFP-ISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 928 YEsLV------YSAWLRLPKEVDKNKrkifIEEVMELVELTPLRQALVGLpgesgLSTEQRKRLTIAVELVANPSIIFMD 1001
Cdd:cd03235 88 RD-VVlmglygHKGLFRRLSKADKAK----VDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 257669152 1002 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELFLLKRG 1053
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLNRT 208
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
851-1053 |
8.55e-27 |
|
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: 107.72 E-value: 8.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIDGNITISGYPKNQqtfarisgyceqtdihsphvtvyes 930
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK--PTSGEILIDGKDIAK------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 931 lvysawlrlpkevdknkrkifieevmelVELTPLRQALVGLPGesgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1010
Cdd:cd00267 66 ----------------------------LPLEELRRRIGYVPQ---LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 257669152 1011 AAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELFLLKRG 1053
Cdd:cd00267 115 SRERLLELLRELAEEGRTVIIVTHDPE-LAELAADRVIVLKDG 156
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
825-1053 |
1.11e-25 |
|
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: 106.42 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 825 ITFDNVVYSVdmpqemieqGTQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGnITISG 900
Cdd:cd03255 1 IELKNLSKTY---------GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGldRPTSGevRVDG-TDISK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 901 YPKNQQTFAR---IsGYCEQTdiHS--PHVTVYESLvysawlRLPKEVDKNKRKIFIEEVMELVELTPLRQALVGLPGEs 975
Cdd:cd03255 71 LSEKELAAFRrrhI-GFVFQS--FNllPDLTALENV------ELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSE- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257669152 976 gLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHQPsiDIFEAFDELFLLKRG 1053
Cdd:cd03255 141 -LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDP--ELAEYADRIIELRDG 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
853-1005 |
2.76e-24 |
|
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: 100.41 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIDGNITISGYPKNQQT---FARISGYCEQTDIHSPHVTVYE 929
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS--PTEGTILLDGQDLTDDErksLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257669152 930 SLVYSAWLRLPKEVDKNKRkifIEEVMELVELTPLRQALVGLPGeSGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1005
Cdd:pfam00005 79 NLRLGLLLKGLSKREKDAR---AEEALEKLGLGDLADRPVGERP-GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
851-1036 |
3.62e-24 |
|
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: 101.79 E-value: 3.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyidgNITISGYPKNQQ--TFARISGYCEQTDIHSPHVT 926
Cdd:COG4133 16 LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGllPPSAG----EVLWNGEPIRDAreDYRRRLAYLGHADGLKPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 927 VYESLVYSAWLRlPKEVDKNKrkifIEEVMELVELTPLRQALVGLpgesgLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1006
Cdd:COG4133 92 VRENLRFWAALY-GLRADREA----IDEALEAVGLAGLADLPVRQ-----LSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190
....*....|....*....|....*....|
gi 257669152 1007 LDARAAAIVMRTVRNTVDTGRTVVCTIHQP 1036
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
851-1053 |
1.40e-23 |
|
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: 100.29 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGNiTISGYPKNQqtfaRISGYCEQTDIHSPHVT 926
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGleRPDSGeiLIDGR-DVTGVPPER----RNIGMVFQDYALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 927 VYESLVYSawLRLpKEVDKNKRKIFIEEVMELVELTPLRQALVglpgeSGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1006
Cdd:cd03259 89 VAENIAFG--LKL-RGVPKAEIRARVRELLELVGLEGLLNRYP-----HELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 257669152 1007 LDARAAAIVMRTVRNT-VDTGRTVVCTIHqpsiDIFEAF---DELFLLKRG 1053
Cdd:cd03259 161 LDAKLREELREELKELqRELGITTIYVTH----DQEEALalaDRIAVMNEG 207
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
825-1053 |
5.65e-23 |
|
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: 98.94 E-value: 5.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 825 ITFDNVVYSVdmpqemieqgtqEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyidgNITISGYP 902
Cdd:COG1122 1 IELENLSFSY------------PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGllKPTSG----EVLVDGKD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 903 KNQQTFARIS---GYCEQ---TDIHSPhvTVYESLVYSawLR---LPK-EVDKNkrkifIEEVMELVELTPLRQALVglp 972
Cdd:COG1122 65 ITKKNLRELRrkvGLVFQnpdDQLFAP--TVEEDVAFG--PEnlgLPReEIRER-----VEEALELVGLEHLADRPP--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 973 geSGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELFLLKR 1052
Cdd:COG1122 133 --HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLD-LVAELADRVIVLDD 209
|
.
gi 257669152 1053 G 1053
Cdd:COG1122 210 G 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
853-1053 |
6.34e-23 |
|
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: 97.08 E-value: 6.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyidgNITISGYP--KNQQTFARISGYCEQTDIHSPHVTVY 928
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGllKPDSG----EIKVLGKDikKEPEEVKRRIGYLPEEPSLYENLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 929 ESLVYSawlrlpkevdknkrkifieevmelveltplrqalvglpgeSGlsteQRKRLTIAVELVANPSIIFMDEPTSGLD 1008
Cdd:cd03230 92 ENLKLS----------------------------------------GG----MKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 257669152 1009 ARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELFLLKRG 1053
Cdd:cd03230 128 PESRREFWELLRELKKEGKTILLSSHILE-EAERLCDRVAILNNG 171
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
853-1053 |
2.63e-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: 95.72 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGnITISGYPKNQQTFARISGYCEQTDIHSPHVTVY 928
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGleEPDSGsiLIDG-EDLTDLEDELPPLRRRIGMVFQDFALFPHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 929 ESLVYsawlrlpkevdknkrkifieevmelveltplrqalvglpgesGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1008
Cdd:cd03229 95 ENIAL------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 257669152 1009 ARAAAIVMRTVRNTVDT-GRTVVCTIHqpsiDIFEAF---DELFLLKRG 1053
Cdd:cd03229 133 PITRREVRALLKSLQAQlGITVVLVTH----DLDEAArlaDRVVVLRDG 177
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
844-1038 |
5.01e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 96.27 E-value: 5.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 844 GTQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGnITISGYPKNQQTFAR---IsGYCE 916
Cdd:COG1136 15 GTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGldRPTSGevLIDG-QDISSLSERELARLRrrhI-GFVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 917 QtDIH-SPHVTVYESLVYSAWLRlpkEVDKNKRKIFIEEVMELVELTPLRQAlvgLPGEsgLSTEQRKRLTIAVELVANP 995
Cdd:COG1136 93 Q-FFNlLPELTALENVALPLLLA---GVSRKERRERARELLERVGLGDRLDH---RPSQ--LSGGQQQRVAIARALVNRP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 257669152 996 SIIFMDEPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHQPSI 1038
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPEL 207
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
165-422 |
1.31e-21 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 95.52 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 165 KKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDqelKQTGRVTYNGHGMNEFVPQ--RTAAYIGQNDVHIGE 242
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLR---PTSGEVRVLGEDVARDPAEvrRRIGYVPQEPALYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 243 MTVRETFAYAARFQGVGsrydmltelaRREKEANIkpdpdidifmkamstagektnvmtDYILKILGLEVCADTMVGDdm 322
Cdd:COG1131 88 LTVRENLRFFARLYGLP----------RKEARERI------------------------DELLELFGLTDAADRKVGT-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 323 lrgISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHifNGTA-LIS--LLqpaPETFNLFDDIIL 399
Cdd:COG1131 132 ---LSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAA--EGKTvLLSthYL---EEAERLCDRVAI 203
|
250 260
....*....|....*....|....*....
gi 257669152 400 IAEGEIIYEGPRDHVVE------FFETMG 422
Cdd:COG1131 204 IDKGRIVADGTPDELKArlledvFLELTG 232
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
853-1034 |
1.92e-21 |
|
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: 96.69 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyidgNITISGYP--KNQQTFARISGYCEQtdihspHVTVY 928
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTllRPTSG----TARVAGYDvvREPRKVRRSIGIVPQ------YASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 929 ESLvySAW---------LRLPKEVdKNKRkifIEEVMELVELTPLRQALVGlpgesGLSTEQRKRLTIAVELVANPSIIF 999
Cdd:TIGR01188 79 EDL--TGRenlemmgrlYGLPKDE-AEER---AEELLELFELGEAADRPVG-----TYSGGMRRRLDIAASLIHQPDVLF 147
|
170 180 190
....*....|....*....|....*....|....*
gi 257669152 1000 MDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1034
Cdd:TIGR01188 148 LDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTH 182
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
821-1053 |
3.22e-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: 99.84 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 821 EPHSITFDNVVYSVDmpqemieqgtQEDRLVLlKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGrktggYID---GNIT 897
Cdd:COG4987 330 GGPSLELEDVSFRYP----------GAGRPVL-DGLSLTLPPGERVAIVGPSGSGKSTLLALLLR-----FLDpqsGSIT 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 898 ISGYPK---NQQTFARISGYCEQtdihSPHV---TVYESLvysawlRLPK-EVDKNKrkifIEEVMELVELTPLRQALV- 969
Cdd:COG4987 394 LGGVDLrdlDEDDLRRRIAVVPQ----RPHLfdtTLRENL------RLARpDATDEE----LWAALERVGLGDWLAALPd 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 970 GL---PGESG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDtGRTVVCTIHQPSidIFEAF 1044
Cdd:COG4987 460 GLdtwLGEGGrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLA--GLERM 536
|
....*....
gi 257669152 1045 DELFLLKRG 1053
Cdd:COG4987 537 DRILVLEDG 545
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
851-1054 |
5.81e-21 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 91.73 E-value: 5.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG-RKTGGyidGNITISGYPKNQ---QTFARISGYCEQtdihsphvt 926
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGlLKPSS---GEILLDGKDLASlspKELARKIAYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 927 vyeslvysawlrlpkevdknkrkifieeVMELVELTPLRQALVglpgeSGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1006
Cdd:cd03214 81 ----------------------------ALELLGLAHLADRPF-----NELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 257669152 1007 LDARAAAIVMRTVRNTVD-TGRTVVCTIHQPSIdIFEAFDELFLLKRGG 1054
Cdd:cd03214 128 LDIAHQIELLELLRRLAReRGKTVVMVLHDLNL-AARYADRVILLKDGR 175
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
851-1053 |
1.37e-20 |
|
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: 92.18 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGNITISGYPKNQQTFARISGYCEQ-----TDIh 921
Cdd:cd03261 14 TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGllRPDSGevLIDGEDISGLSEAELYRLRRRMGMLFQsgalfDSL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 922 sphvTVYESLVYsaWLR----LPKEVdknkrkifIEE-VMELVELTPLRQALVGLPGEsgLSTEQRKRLTIAVELVANPS 996
Cdd:cd03261 93 ----TVFENVAF--PLRehtrLSEEE--------IREiVLEKLEAVGLRGAEDLYPAE--LSGGMKKRVALARALALDPE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 257669152 997 IIFMDEPTSGLDARAAAIVMRTVRNTVDT-GRTVVCTIHQPSiDIFEAFDELFLLKRG 1053
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLD-TAFAIADRIAVLYDG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
852-1034 |
1.50e-20 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 91.55 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiDGNITISGYPKNQQTFARISGYCEQT-DIHSPHVTVY 928
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGliKES----SGSILLNGKPIKAKERRKSIGYVMQDvDYQLFTDSVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 929 ESLVYSAwlrlpKEVDKNKRKIfiEEVMELVELTPLRQALvglPGEsgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1008
Cdd:cd03226 91 EELLLGL-----KELDAGNEQA--ETVLKDLDLYALKERH---PLS--LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180
....*....|....*....|....*.
gi 257669152 1009 ARAAAIVMRTVRNTVDTGRTVVCTIH 1034
Cdd:cd03226 159 YKNMERVGELIRELAAQGKAVIVITH 184
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
824-1053 |
1.57e-20 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 97.98 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 824 SITFDNVVYSVDmpqemieqgtqEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGrktgGYI--DGNITISGY 901
Cdd:COG2274 473 DIELENVSFRYP-----------GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG----LYEptSGRILIDGI 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 902 PKNQ---QTFARISGYCEQtDIHSPHVTVYESLVYSAwlrlpKEVDknkrkifIEEVMELVELTPLRQALVGLP------ 972
Cdd:COG2274 538 DLRQidpASLRRQIGVVLQ-DVFLFSGTIRENITLGD-----PDAT-------DEEIIEAARLAGLHDFIEALPmgydtv 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 973 -GESG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRnTVDTGRTVVCTIHQPSidIFEAFDELFL 1049
Cdd:COG2274 605 vGEGGsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLR-RLLKGRTVIIIAHRLS--TIRLADRIIV 681
|
....
gi 257669152 1050 LKRG 1053
Cdd:COG2274 682 LDKG 685
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
850-1030 |
1.82e-20 |
|
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: 92.11 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 850 LVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGNiTISGYPKNQ-------QTFARISGYceqt 918
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGflRPTSGsvLFDGE-DITGLPPHEiarlgigRTFQIPRLF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 919 dihsPHVTVYESLV----------YSAWLRLPKEVDKNKRkifIEEVMELVELTPLRQALVGLpgesgLSTEQRKRLTIA 988
Cdd:cd03219 88 ----PELTVLENVMvaaqartgsgLLLARARREEREARER---AEELLERVGLADLADRPAGE-----LSYGQQRRLEIA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 257669152 989 VELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVV 1030
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVL 197
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
821-1053 |
5.45e-20 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 95.60 E-value: 5.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 821 EPHSITFDNVVYSvdmpqemieqgtQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIDGNITISG 900
Cdd:COG4988 333 GPPSIELEDVSFS------------YPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP--YSGSILING 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 901 YP----KNQQTFARISgYCEQTdihsPHV---TVYEslvysaWLRLPK-EVDKnkrkifiEEVMELVELTPLRQALVGLP 972
Cdd:COG4988 399 VDlsdlDPASWRRQIA-WVPQN----PYLfagTIRE------NLRLGRpDASD-------EELEAALEAAGLDEFVAALP 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 973 -------GE--SGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNtVDTGRTVVCTIHQPSIDifEA 1043
Cdd:COG4988 461 dgldtplGEggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR-LAKGRTVILITHRLALL--AQ 537
|
250
....*....|
gi 257669152 1044 FDELFLLKRG 1053
Cdd:COG4988 538 ADRILVLDDG 547
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
853-1034 |
8.78e-20 |
|
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: 89.74 E-value: 8.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyidgNITISGYP--KNQQTFARISGYCEQTDIHSPHVTVY 928
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTllKPTSG----RATVAGHDvvREPREVRRRIGIVFQDLSVDDELTGW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 929 ESLVYSAWLR-LPKEVDKNKrkifIEEVMELVELTPLRQALVglpgeSGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1007
Cdd:cd03265 92 ENLYIHARLYgVPGAERRER----IDELLDFVGLLEAADRLV-----KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180
....*....|....*....|....*...
gi 257669152 1008 DARAAAIVMRTVRNTVDT-GRTVVCTIH 1034
Cdd:cd03265 163 DPQTRAHVWEYIEKLKEEfGMTILLTTH 190
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
862-1050 |
1.15e-19 |
|
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: 89.28 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 862 PGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIDGNITI---SGYPKNQQTFARISGYCEQTDIHSPHVTVYESLVYSAw 936
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGleKPDGGTIVLNGTVlfdSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGL- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 937 lrlpKEVDKNKRKIFIEEVMELVELTPLRQALVGlpgesGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVM 1016
Cdd:cd03297 101 ----KRKRNREDRISVDELLDLLGLDHLLNRYPA-----QLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190
....*....|....*....|....*....|....
gi 257669152 1017 RTVRNTVDtgrtvvcTIHQPSIDIFEAFDELFLL 1050
Cdd:cd03297 172 PELKQIKK-------NLNIPVIFVTHDLSEAEYL 198
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
853-1038 |
3.15e-19 |
|
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: 87.85 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRK--TGGYIDGN-ITISGYPKNQQTFARIS-GYCEQTDIHSPHVTVY 928
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEElpTSGTIRVNgQDVSDLRGRAIPYLRRKiGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 929 ESLVysawlrLPKEVDKNKRKIFIEEVMELVELTPLRQALVGLPgeSGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1008
Cdd:cd03292 97 ENVA------FALEVTGVPPREIRKRVPAALELVGLSHKHRALP--AELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190
....*....|....*....|....*....|
gi 257669152 1009 ARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1038
Cdd:cd03292 169 PDTTWEIMNLLKKINKAGTTVVVATHAKEL 198
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
165-424 |
3.36e-19 |
|
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: 88.38 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 165 KKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDqelKQTGRVTYNGHGMNE----------FVPQRTAAYIG 234
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLK---PDSGSILIDGEDVRKeprearrqigVLPDERGLYDR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 235 qndvhigeMTVRETFAYAARFQGvgsrydmlteLARREKEANIkpdpdidifmkamstagektnvmtDYILKILGLEVCA 314
Cdd:COG4555 89 --------LTVRENIRYFAELYG----------LFDEELKKRI------------------------EELIELLGLEEFL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 315 DTMVGddmlrGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIfNGTALIS--LLQpapETFN 392
Cdd:COG4555 127 DRRVG-----ELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSshIMQ---EVEA 197
|
250 260 270
....*....|....*....|....*....|..
gi 257669152 393 LFDDIILIAEGEIIYEGPRDHVVEFFETMGFK 424
Cdd:COG4555 198 LCDRVVILHKGKVVAQGSLDELREEIGEENLE 229
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
847-1034 |
4.09e-19 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 86.71 E-value: 4.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 847 EDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGNITisGYPKNQQTFARIS-GYCEQT--- 918
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGllRPQSGavLIDGEPL--DYSRKGLLERRQRvGLVFQDpdd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 919 DIHSPhvTVYESLVYSAwLRLPKEVDKNKRKIfiEEVMELVELTPLRQALVGLpgesgLSTEQRKRLTIAVELVANPSII 998
Cdd:TIGR01166 80 QLFAA--DVDQDVAFGP-LNLGLSEAEVERRV--REALTAVGASGLRERPTHC-----LSGGEKKRVAIAGAVAMRPDVL 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 257669152 999 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1034
Cdd:TIGR01166 150 LLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
817-1038 |
4.28e-19 |
|
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: 92.73 E-value: 4.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 817 VLPFEPHSITFDNVVYsvdmpqemieqgTQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYID- 893
Cdd:TIGR02857 314 VTAAPASSLEFSGVSV------------AYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGfvDPTEGSIAv 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 894 GNITISGYpkNQQTFARISGYCEQTdihsPHVtVYESLVYSAWLRLPKEVDKNkrkifIEEVMELVELTPLRQAL-VGL- 971
Cdd:TIGR02857 382 NGVPLADA--DADSWRDQIAWVPQH----PFL-FAGTIAENIRLARPDASDAE-----IREALERAGLDEFVAALpQGLd 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257669152 972 ----PGESGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNtVDTGRTVVCTIHQPSI 1038
Cdd:TIGR02857 450 tpigEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA-LAQGRTVLLVTHRLAL 519
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
849-1034 |
4.69e-19 |
|
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: 87.42 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 849 RLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiDGNITISGYPKNQQTFA---RISGYCEQTDIHsPHV 925
Cdd:cd03266 17 TVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD--AGFATVDGFDVVKEPAEarrRLGFVSDSTGLY-DRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 926 TVYESLVYSAWLRLPKEVDKNKRkifIEEVMELVELTPLRQALVGlpgesGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1005
Cdd:cd03266 94 TARENLEYFAGLYGLKGDELTAR---LEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
170 180
....*....|....*....|....*....
gi 257669152 1006 GLDARAAAIVMRTVRNTVDTGRTVVCTIH 1034
Cdd:cd03266 166 GLDVMATRALREFIRQLRALGKCILFSTH 194
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
163-413 |
7.11e-19 |
|
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: 86.79 E-value: 7.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 163 RKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkldQELKQTGRVTYNGHGMNEfvpQRTAAY--IG---QND 237
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTG---ELRPTSGTAYINGYSIRT---DRKAARqsLGycpQFD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 238 VHIGEMTVRETFAYAARFQGVGsrydmltelaRREKEANIkpdpdidifmkamstagektnvmtDYILKILGLEVCADTM 317
Cdd:cd03263 85 ALFDELTVREHLRFYARLKGLP----------KSEIKEEV------------------------ELLLRVLGLTDKANKR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 318 VGDdmlrgISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHifNGTALISLLQPApETFNLFDDI 397
Cdd:cd03263 131 ART-----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMD-EAEALCDRI 202
|
250
....*....|....*.
gi 257669152 398 ILIAEGEIIYEGPRDH 413
Cdd:cd03263 203 AIMSDGKLRCIGSPQE 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
853-1036 |
1.19e-18 |
|
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: 91.27 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGrktggYID---GNITISGYP---KNQQTFARISGYCEQtDIHSPHVT 926
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAG-----LLDplqGEVTLDGVPvssLDQDEVRRRVSVCAQ-DAHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 927 VYESLVYSAwlrlpKEVDKnkrkifiEEVMELVELTPLRQALVGLP-------GESG--LSTEQRKRLTIAVELVANPSI 997
Cdd:TIGR02868 425 VRENLRLAR-----PDATD-------EELWAALERVGLADWLRALPdgldtvlGEGGarLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*....
gi 257669152 998 IFMDEPTSGLDARAAAIVMRTVRNtVDTGRTVVCTIHQP 1036
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
853-1015 |
1.58e-18 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 86.08 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLM-------DVLAGRKTGG--YIDGNiTISGYPKNQQTFARISGYCEQtdihSP 923
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLrllnrlnDLIPGAPDEGevLLDGK-DIYDLDVDVLELRRRVGMVFQ----KP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 924 ---HVTVYESLVYSAWLRLPKEvdknkrkifIEEVMELVEltplrQAL--VGLPGE-------SGLSTEQRKRLTIAVEL 991
Cdd:cd03260 91 npfPGSIYDNVAYGLRLHGIKL---------KEELDERVE-----EALrkAALWDEvkdrlhaLGLSGGQQQRLCLARAL 156
|
170 180
....*....|....*....|....
gi 257669152 992 VANPSIIFMDEPTSGLDARAAAIV 1015
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKI 180
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
853-1061 |
1.71e-18 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 86.47 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGNITISGYPKNQQTFARISGYCEQTDIHSPHVTVY 928
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGlvEPTSGsvLIDGTDINKLKGKALRQLRRQIGMIFQQFNLIERLSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 929 ESLV---------YSAWLRLPKEVDKNKRKIFIEEVmELVELTPLRQalvglpgeSGLSTEQRKRLTIAVELVANPSIIF 999
Cdd:cd03256 97 ENVLsgrlgrrstWRSLFGLFPKEEKQRALAALERV-GLLDKAYQRA--------DQLSGGQQQRVAIARALMQQPKLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257669152 1000 MDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPsiDIFEAFDELFLLKRGGEEIYVGP 1061
Cdd:cd03256 168 ADEPVASLDPASSRQVMDLLKRiNREEGITVIVSLHQV--DLAREYADRIVGLKDGRIVFDGP 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
853-1030 |
2.16e-18 |
|
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: 90.35 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGNITISGYPKNQQTFARISGYCEQTDIHS--PHVT 926
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGllRPTSGsiLFDGKDLTKLSRRSLRELRRRVQMVFQDPYSSlnPRMT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 927 VYESLvySAWLRLPKEVDKNKRKIFIEEVMELVELTP-LRQALvglPGEsgLSTEQRKRLTIAVELVANPSIIFMDEPTS 1005
Cdd:COG1123 361 VGDII--AEPLRLHGLLSRAERRERVAELLERVGLPPdLADRY---PHE--LSGGQRQRVAIARALALEPKLLILDEPTS 433
|
170 180
....*....|....*....|....*.
gi 257669152 1006 GLDARAAAIVMRTVRNTVD-TGRTVV 1030
Cdd:COG1123 434 ALDVSVQAQILNLLRDLQReLGLTYL 459
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
853-1035 |
4.18e-18 |
|
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: 84.19 E-value: 4.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIdgNITISGYPKNQQTFARISGYCEQTDIHsPHVTVYES 930
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGliKPDSGEI--TFDGKSYQKNIEALRRIGALIEAPGFY-PNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 931 LVYSA-WLRLPKEVdknkrkifIEEVMELVELTPLRQALVGlpgesGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1009
Cdd:cd03268 93 LRLLArLLGIRKKR--------IDEVLDVVGLKDSAKKKVK-----GFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180
....*....|....*....|....*.
gi 257669152 1010 RAAAIVMRTVRNTVDTGRTVVCTIHQ 1035
Cdd:cd03268 160 DGIKELRELILSLRDQGITVLISSHL 185
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
170-351 |
5.26e-18 |
|
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: 82.31 E-value: 5.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 170 LNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDqelKQTGRVTYNGHGMNEFVPQRTA---AYIGQNDVHIGEMTVR 246
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS---PTEGTILLDGQDLTDDERKSLRkeiGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 247 ETFAYAARFQGVGSRYDmlteLARREKeanikpdpdidifmkamstagektnvmtdyILKILGLEVCADTMVGDDMlRGI 326
Cdd:pfam00005 78 ENLRLGLLLKGLSKREK----DARAEE------------------------------ALEKLGLGDLADRPVGERP-GTL 122
|
170 180
....*....|....*....|....*
gi 257669152 327 SGGQKKRVTTGEMLVGPSRALFMDE 351
Cdd:pfam00005 123 SGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
823-1038 |
5.26e-18 |
|
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: 84.56 E-value: 5.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 823 HSITFDNVVYSVDmpqemieqgtqEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGnITI 898
Cdd:cd03245 1 GRIEFRNVSFSYP-----------NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGlyKPTSGsvLLDG-TDI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 899 SGYPKnqQTFARISGYCEQtDIHSPHVTVYESLVYSAwlrlPKEVDknkrkifiEEVMELVELTPLRQALVGLP------ 972
Cdd:cd03245 69 RQLDP--ADLRRNIGYVPQ-DVTLFYGTLRDNITLGA----PLADD--------ERILRAAELAGVTDFVNKHPngldlq 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257669152 973 -GESG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVdTGRTVVCTIHQPSI 1038
Cdd:cd03245 134 iGERGrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSL 201
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
825-1053 |
8.66e-18 |
|
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: 82.43 E-value: 8.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 825 ITFDNVVYSvdmpqemieqgTQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGrktggYID---GNITISGY 901
Cdd:cd03228 1 IEFKNVSFS-----------YPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLR-----LYDptsGEILIDGV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 902 PK---NQQTFARISGYCEQtdihSPHV---TVYESLvysawlrlpkevdknkrkifieevmelveltplrqalvglpges 975
Cdd:cd03228 65 DLrdlDLESLRKNIAYVPQ----DPFLfsgTIRENI-------------------------------------------- 96
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257669152 976 gLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNtVDTGRTVVCTIHQPSidIFEAFDELFLLKRG 1053
Cdd:cd03228 97 -LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRA-LAKGKTVIVIAHRLS--TIRDADRIIVLDDG 170
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
168-357 |
1.27e-17 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 82.91 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkldQELKQTGRVTYNGHGMNEFVPQ--RTAAYIGQNDVHIGEMTV 245
Cdd:COG4133 16 LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAG---LLPPSAGEVLWNGEPIRDAREDyrRRLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 246 RETFAYAARFQGVGSRYDMLTELarrekeanikpdpdidifmkamstagektnvmtdyiLKILGLEVCADTMVGddMLrg 325
Cdd:COG4133 93 RENLRFWAALYGLRADREAIDEA------------------------------------LEAVGLAGLADLPVR--QL-- 132
|
170 180 190
....*....|....*....|....*....|..
gi 257669152 326 iSGGQKKRVTTGEMLVGPSRALFMDEISTGLD 357
Cdd:COG4133 133 -SAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
825-1052 |
1.43e-17 |
|
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: 83.29 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 825 ITFDNVVYSVdmpqemieqGTQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyidgNITISGYP 902
Cdd:cd03293 1 LEVRNVSKTY---------GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGleRPTSG----EVLVDGEP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 903 KNQQTFARisGYCEQTDIHSPHVTVYESLVYSawLRLpKEVDKNKRKIFIEEVMELVELTPLRQALvglPGEsgLSTEQR 982
Cdd:cd03293 68 VTGPGPDR--GYVFQQDALLPWLTVLDNVALG--LEL-QGVPKAEARERAEELLELVGLSGFENAY---PHQ--LSGGMR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257669152 983 KRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHqpsiDIFEAF---DELFLLKR 1052
Cdd:cd03293 138 QRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWrETGKTVLLVTH----DIDEAVflaDRVVVLSA 207
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
851-1053 |
6.59e-17 |
|
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: 82.05 E-value: 6.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGR--KTGGyidGNITISGypknqQTFARIS--------GYC--EQT 918
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlpPTYG---NDVRLFG-----ERRGGEDvwelrkriGLVspALQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 919 DIHSPHVTVYEsLVYSAW---LRLPKEVDKNKRKIfIEEVMELVELTPLRQALVGlpgesGLSTEQRKRLTIAVELVANP 995
Cdd:COG1119 89 LRFPRDETVLD-VVLSGFfdsIGLYREPTDEQRER-ARELLELLGLAHLADRPFG-----TLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257669152 996 SIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTvvcTI----HQPSiDIFEAFDELFLLKRG 1053
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGAP---TLvlvtHHVE-EIPPGITHVLLLKDG 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
168-414 |
3.03e-16 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 79.75 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkldqELK-QTGRVTYNGHGMNE------FVPQRTAAyigQNDVHI 240
Cdd:COG1121 20 PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILG----LLPpTSGTVRLFGKPPRRarrrigYVPQRAEV---DWDFPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 241 gemTVRETFAyAARFQGVGsrydmlteLARREKEAnikpdpDIDIFMKAMSTAGektnvMTDYilkilglevcADTMVGD 320
Cdd:COG1121 93 ---TVRDVVL-MGRYGRRG--------LFRRPSRA------DREAVDEALERVG-----LEDL----------ADRPIGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 321 dmlrgISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTT---YQIVNSLRNYvhifNGTALISL--LQPAPEtfnLFD 395
Cdd:COG1121 140 -----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEealYELLRELRRE----GKTILVVThdLGAVRE---YFD 207
|
250
....*....|....*....
gi 257669152 396 DIILIAeGEIIYEGPRDHV 414
Cdd:COG1121 208 RVLLLN-RGLVAHGPPEEV 225
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
851-1043 |
3.17e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.76 E-value: 3.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI---DGNITISGYPknqqtfarisgyceqTDIH---- 921
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGllPPAAGTIkldGGDIDDPDVA---------------EACHylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 922 ----SPHVTVYESLVYsaWLRLpkevdKNKRKIFIEEVMELVELtplrQALVGLPGeSGLSTEQRKRLTIAVELVANPSI 997
Cdd:PRK13539 81 rnamKPALTVAENLEF--WAAF-----LGGEELDIAAALEAVGL----APLAHLPF-GYLSAGQKRRVALARLLVSNRPI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 257669152 998 IFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPsIDIFEA 1043
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHIP-LGLPGA 193
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
848-1030 |
3.73e-16 |
|
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: 79.64 E-value: 3.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 848 DRLVLlKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDG-NITISGYPKNQQTFARIsGYCEQ----- 917
Cdd:COG1127 17 DRVVL-DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGllRPDSGeiLVDGqDITGLSEKELYELRRRI-GMLFQggalf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 918 TDIhsphvTVYESLVYsaWLR----LPKEVdknKRKIfIEEVMELVELtplRQALVGLPGEsgLSTEQRKRLTIAVELVA 993
Cdd:COG1127 95 DSL-----TVFENVAF--PLRehtdLSEAE---IREL-VLEKLELVGL---PGAADKMPSE--LSGGMRKRVALARALAL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 257669152 994 NPSIIFMDEPTSGLDARAAAIVMRTVRNTVDT-GRTVV 1030
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSV 196
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
844-1021 |
3.76e-16 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 79.09 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 844 GTQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGNITISGYPKNQQTFARISGYCEQTD 919
Cdd:cd03257 12 PTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGllKPTSGsiIFDGKDLLKLSRRLRKIRRKEIQMVFQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 920 IHS--PHVTVYESLVYSAWLRLpKEVDKNKRKIFIEEVMELVELTP--LRQalvgLPGEsgLSTEQRKRLTIAVELVANP 995
Cdd:cd03257 92 MSSlnPRMTIGEQIAEPLRIHG-KLSKKEARKEAVLLLLVGVGLPEevLNR----YPHE--LSGGQRQRVAIARALALNP 164
|
170 180
....*....|....*....|....*.
gi 257669152 996 SIIFMDEPTSGLDARAAAIVMRTVRN 1021
Cdd:cd03257 165 KLLIADEPTSALDVSVQAQILDLLKK 190
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
169-404 |
4.20e-16 |
|
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: 78.66 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 169 ILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkldQELKQTGRVTYNGHGMNEFVPQRTAAYIG---QN-DVHIGEMT 244
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNG---LLGPTSGEVLVDGKDLTKLSLKELRRKVGlvfQNpDDQFFGPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 245 VRETFAYAARFQGVgSRYDMltelARREKEAnikpdpdidifmkamstagektnvmtdyiLKILGLEVCADTMVgdDMLr 324
Cdd:cd03225 93 VEEEVAFGLENLGL-PEEEI----EERVEEA-----------------------------LELVGLEGLRDRSP--FTL- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 325 giSGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHifNGTALI------SLLqpapetFNLFDDII 398
Cdd:cd03225 136 --SGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA--EGKTIIivthdlDLL------LELADRVI 205
|
....*.
gi 257669152 399 LIAEGE 404
Cdd:cd03225 206 VLEDGK 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
823-1053 |
8.38e-16 |
|
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: 78.42 E-value: 8.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 823 HSITFDNVVYSVDmpqemieqgtqEDRLVLlKGVNGAFRPGVLTALMGVSGAGKTTLMDVLagrkTGGYI--DGNITISG 900
Cdd:cd03254 1 GEIEFENVNFSYD-----------EKKPVL-KDINFSIKPGETVAIVGPTGAGKTTLINLL----MRFYDpqKGQILIDG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 901 YPKNQQTFARIS---GYCEQtDIHSPHVTVYESLVYSawlrlpkevDKNKRKifiEEVMELVELTPLRQALVGLP----- 972
Cdd:cd03254 65 IDIRDISRKSLRsmiGVVLQ-DTFLFSGTIMENIRLG---------RPNATD---EEVIEAAKEAGAHDFIMKLPngydt 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 973 --GESG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDtGRTVVCTIHQPSIdIFEAfDELF 1048
Cdd:cd03254 132 vlGENGgnLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLST-IKNA-DKIL 208
|
....*
gi 257669152 1049 LLKRG 1053
Cdd:cd03254 209 VLDDG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
168-415 |
9.23e-16 |
|
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: 78.55 E-value: 9.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkldqELK-QTGRVTYNGHGMNEFVPQ---RTAAYIGQNDVHIGEM 243
Cdd:COG1120 15 PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAG----LLKpSSGEVLLDGRDLASLSRRelaRRIAYVPQEPPAPFGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 244 TVRETFAYAarfqgvgsRYDMLTELARREKEanikpdpDIDIFMKAMSTAGektnvmtdyilkILGLevcADTMVGDdml 323
Cdd:COG1120 91 TVRELVALG--------RYPHLGLFGRPSAE-------DREAVEEALERTG------------LEHL---ADRPVDE--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 324 rgISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIFNGTALISL--LQPApetFNLFDDIILIA 401
Cdd:COG1120 138 --LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLhdLNLA---ARYADRLVLLK 212
|
250
....*....|....
gi 257669152 402 EGEIIYEGPRDHVV 415
Cdd:COG1120 213 DGRIVAQGPPEEVL 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
850-1030 |
1.16e-15 |
|
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: 78.54 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 850 LVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGNiTISGYPKNQ-------QTFARISGYceqt 918
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGfyRPTSGriLFDGR-DITGLPPHRiarlgiaRTFQNPRLF---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 919 dihsPHVTVYESL-----------VYSAWLRLPKEVDKNKRKI-FIEEVMELVELTPLRQALVGlpgesGLSTEQRKRLT 986
Cdd:COG0411 92 ----PELTVLENVlvaaharlgrgLLAALLRLPRARREEREAReRAEELLERVGLADRADEPAG-----NLSYGQQRRLE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 257669152 987 IAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVV 1030
Cdd:COG0411 163 IARALATEPKLLLLDEPAAGLNPEETEELAELIRRlRDERGITIL 207
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
853-1034 |
3.13e-15 |
|
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: 76.81 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGNiTISGYPKNQQtfARIS-GYCEQTDIHSPHVTV 927
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGlvKPDSGkiLLDGQ-DITKLPMHKR--ARLGiGYLPQEASIFRKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 928 YESLvySAWLRLPKeVDKNKRKIFIEEVMELVELTPLRQALVglpgeSGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1007
Cdd:cd03218 93 EENI--LAVLEIRG-LSKKEREEKLEELLEEFHITHLRKSKA-----SSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180
....*....|....*....|....*..
gi 257669152 1008 DARAAAIVMRTVRNTVDTGRTVVCTIH 1034
Cdd:cd03218 165 DPIAVQDIQKIIKILKDRGIGVLITDH 191
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
851-1037 |
3.91e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 76.71 E-value: 3.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLMDV--LAGRKTGGYID-GNITI-SGYPKNQQ-----TFARISGYCEQTDIH 921
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinLLEQPEAGTIRvGDITIdTARSLSQQkglirQLRQHVGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 922 SPHVTVYESLVYSawlrlPKEVDKNKRKIFIEEVMELVeltplrqALVGLPGESG-----LSTEQRKRLTIAVELVANPS 996
Cdd:PRK11264 97 FPHRTVLENIIEG-----PVIVKGEPKEEATARARELL-------AKVGLAGKETsyprrLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 257669152 997 IIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPS 1037
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
169-416 |
4.19e-15 |
|
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: 80.65 E-value: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 169 ILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQelkQTGRVTYNGHGMNEFVPQ---RTAAYIGQnDVHIGEMTV 245
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP---TSGRILIDGIDLRQIDPAslrRQIGVVLQ-DVFLFSGTI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 246 REtfayaarfqgvgsrydmltelarrekeaNI---KPDPDIDIFMKAMSTAGektnvMTDYILKI-LGLevcaDTMVGDd 321
Cdd:COG2274 566 RE----------------------------NItlgDPDATDEEIIEAARLAG-----LHDFIEALpMGY----DTVVGE- 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 322 MLRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHifNGTALISllqpA--PETFNLFDDIIL 399
Cdd:COG2274 608 GGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIII----AhrLSTIRLADRIIV 681
|
250
....*....|....*..
gi 257669152 400 IAEGEIIYEGPRDHVVE 416
Cdd:COG2274 682 LDKGRIVEDGTHEELLA 698
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
853-1030 |
4.37e-15 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 75.93 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI--DG-NITisgypkNQQTFARIS---GYCEQTDIHSPH 924
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGllPPRSGSIrfDGrDIT------GLPPHERARagiGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 925 VTVYESLVYSAWLRLPKEVDKNkrkifIEEVMELV-ELTPLRQALVGLpgesgLSTEQRKRLTIAVELVANPSIIFMDEP 1003
Cdd:cd03224 90 LTVEENLLLGAYARRRAKRKAR-----LERVYELFpRLKERRKQLAGT-----LSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180
....*....|....*....|....*..
gi 257669152 1004 TSGLDARAAAIVMRTVRNTVDTGRTVV 1030
Cdd:cd03224 160 SEGLAPKIVEEIFEAIRELRDEGVTIL 186
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
852-1034 |
5.16e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.73 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAgrktgGYI---DGNITISGYPKNQ---QTFARISGYCEQtdihSPHV 925
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS-----GELspdSGEVRLNGRPLADwspAELARRRAVLPQ----HSSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 926 ----TVYE--SLVYSAWLRLPKEVDknkrkIFIEEVMELVELTPLR----QALVGlpGEsglstEQRKRLtiAVELV--- 992
Cdd:PRK13548 88 sfpfTVEEvvAMGRAPHGLSRAEDD-----ALVAAALAQVDLAHLAgrdyPQLSG--GE-----QQRVQL--ARVLAqlw 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 257669152 993 ---ANPSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIH 1034
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALDLAHQHHVLRLARQlAHERGLAVIVVLH 199
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
852-1053 |
8.44e-15 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 73.79 E-value: 8.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGnitisgypknqqtfarisgyceqTDIHSphvtv 927
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGllRPTSGrvRLDG-----------------------ADISQ----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 928 yeslvysawlrlpkeVDKNKRKIFIEEVMELVELtplrqalvgLPG---ESGLSTEQRKRLTIAVELVANPSIIFMDEPT 1004
Cdd:cd03246 69 ---------------WDPNELGDHVGYLPQDDEL---------FSGsiaENILSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 257669152 1005 SGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSidIFEAFDELFLLKRG 1053
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDG 171
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
848-1053 |
1.13e-14 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 78.79 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 848 DRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGR-KTGGYIDGNITISGYPKNQQTFARIS---GYCEQTDIHS- 922
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlPHGGRISGEVLLDGRDLLELSEALRGrriGMVFQDPMTQl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 923 -PhVTVYESLVYSAWLRLpkeVDKNKRKIFIEEVMELVELTPLRQALvglPGEsgLSTEQRKRLTIAVELVANPSIIFMD 1001
Cdd:COG1123 97 nP-VTVGDQIAEALENLG---LSRAEARARVLELLEAVGLERRLDRY---PHQ--LSGGQRQRVAIAMALALDPDLLIAD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 257669152 1002 EPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSiDIFEAFDELFLLKRG 1053
Cdd:COG1123 168 EPTTALDVTTQAEILDLLRElQRERGTTVLLITHDLG-VVAEIADRVVVMDDG 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
851-1010 |
1.26e-14 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 74.97 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiDGNITISGYP-KNQQTFARISGYCEQTDIHSPHVTVYE 929
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPT--SGEILLDGKDiTNLPPHKRPVNTVFQNYALFPHLTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 930 SLVYSawLRLpKEVDKNKRKIFIEEVMELVELTPLRQALVglpgeSGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1009
Cdd:cd03300 92 NIAFG--LRL-KKLPKAEIKERVAEALDLVQLEGYANRKP-----SQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
.
gi 257669152 1010 R 1010
Cdd:cd03300 164 K 164
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
848-1061 |
1.71e-14 |
|
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: 74.68 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 848 DRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiDGNITISGYPKNQQTFA-RISGYCEQTDIHSPHVT 926
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPD--SGTILFGGEDATDVPVQeRNVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 927 VYESLVYSAWLRlPKEVDKNKRKIfIEEVMELVELTPLRQALVGLPGEsgLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1006
Cdd:cd03296 91 VFDNVAFGLRVK-PRSERPPEAEI-RAKVHELLKLVQLDWLADRYPAQ--LSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257669152 1007 LDARAAAIVMRTVRNTVD-TGRTVVCTIHQPSiDIFEAFDELFLLKRG-------GEEIYVGP 1061
Cdd:cd03296 167 LDAKVRKELRRWLRRLHDeLHVTTVFVTHDQE-EALEVADRVVVMNKGrieqvgtPDEVYDHP 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
161-405 |
1.77e-14 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 74.06 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 161 PNRKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTlLLALAGKLDQelKQTGRVTYNGHGMNEFVPQRTAAYIGQndvHI 240
Cdd:cd03255 11 GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKST-LLNILGGLDR--PTSGEVRVDGTDISKLSEKELAAFRRR---HI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 241 G----------EMTVRETFAYAARFQGVGSRydmltELARREKEAnikpdpdidifmkamstagektnvmtdyiLKILGL 310
Cdd:cd03255 85 GfvfqsfnllpDLTALENVELPLLLAGVPKK-----ERRERAEEL-----------------------------LERVGL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 311 EVCADTMVGDdmlrgISGGQKKRVTTGEMLVGPSRALFMDEiSTG-LDSSTTYQIVNSLRNYVHIFNGTALISLLQpaPE 389
Cdd:cd03255 131 GDRLNHYPSE-----LSGGQQQRVAIARALANDPKIILADE-PTGnLDSETGKEVMELLRELNKEAGTTIVVVTHD--PE 202
|
250
....*....|....*.
gi 257669152 390 TFNLFDDIILIAEGEI 405
Cdd:cd03255 203 LAEYADRIIELRDGKI 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
853-1053 |
1.95e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 73.85 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGrktggyI----DGNITISGYPKNQQTFARIsGYCEQTDIHSPHVTVY 928
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILG------IilpdSGEVLFDGKPLDIAARNRI-GYLPEERGLYPKMKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 929 ESLVYSAWLR-LPKEVDKNKrkifIEEVMELVELTPLRQALVglpgeSGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1007
Cdd:cd03269 89 DQLVYLAQLKgLKKEEARRR----IDEWLERLELSEYANKRV-----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 257669152 1008 DARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAF-DELFLLKRG 1053
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQ--MELVEELcDRVLLLNKG 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
163-414 |
2.26e-14 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 77.64 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 163 RKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQELKQTGRVTYNGH---GMNEFVPQRTAAYIGQN-DV 238
Cdd:COG1123 15 PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRdllELSEALRGRRIGMVFQDpMT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 239 HIGEMTVRETFAYAARFQGVGSRydmltELARREKEAnikpdpdidifmkamstagektnvmtdyiLKILGLEVCADTMV 318
Cdd:COG1123 95 QLNPVTVGDQIAEALENLGLSRA-----EARARVLEL-----------------------------LEAVGLERRLDRYP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 319 GDdmlrgISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNyVHIFNGTALISLLQPAPETFNLFDDII 398
Cdd:COG1123 141 HQ-----LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRE-LQRERGTTVLLITHDLGVVAEIADRVV 214
|
250
....*....|....*.
gi 257669152 399 LIAEGEIIYEGPRDHV 414
Cdd:COG1123 215 VMDDGRIVEDGPPEEI 230
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
853-1053 |
2.35e-14 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 72.08 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyidgNITISGypknqqtfarisgycEQTDIHSPHvtvyes 930
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGlyKPDSG----EILVDG---------------KEVSFASPR------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 931 lvysawlrlpkevDKNKRKIfieevmelveltplrqALVglpgeSGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1010
Cdd:cd03216 71 -------------DARRAGI----------------AMV-----YQLSVGERQMVEIARALARNARLLILDEPTAALTPA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 257669152 1011 AAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELFLLKRG 1053
Cdd:cd03216 117 EVERLFKVIRRLRAQGVAVIFISHRLD-EVFEIADRVTVLRDG 158
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
852-1053 |
2.83e-14 |
|
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: 74.26 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGAFRPGVLTALMGVSGAGKTTLMdvlagRKTGGYID---GNITISGYPKNQQT---FARISGYCEQTDIHSPHV 925
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTM-----KMINRLIEptsGEIFIDGEDIREQDpveLRRKIGYVIQQIGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 926 TVYESLVYsawlrLPK--EVDKNKRKIFIEEVMELVELTPlRQALVGLPGEsgLSTEQRKRLTIAVELVANPSIIFMDEP 1003
Cdd:cd03295 91 TVEENIAL-----VPKllKWPKEKIRERADELLALVGLDP-AEFADRYPHE--LSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 257669152 1004 TSGLDAraaaiVMRT------VRNTVDTGRTVVCTIHqpsiDIFEAF---DELFLLKRG 1053
Cdd:cd03295 163 FGALDP-----ITRDqlqeefKRLQQELGKTIVFVTH----DIDEAFrlaDRIAIMKNG 212
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
853-1030 |
3.63e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 76.98 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGN-ITISGyPKNQQTfARISGyceqtdIH-----S 922
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGvyQPDSGeiLLDGEpVRFRS-PRDAQA-AGIAI------IHqelnlV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 923 PHVTVYESLVYSAWLRLPKEVDKNKRKIFIEEVMELVELT-PLRqALVGlpgesGLSTEQRKRLTIAVELVANPSIIFMD 1001
Cdd:COG1129 92 PNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDiDPD-TPVG-----DLSVAQQQLVEIARALSRDARVLILD 165
|
170 180
....*....|....*....|....*....
gi 257669152 1002 EPTSGLDARAAAIVMRTVRNTVDTGRTVV 1030
Cdd:COG1129 166 EPTASLTEREVERLFRIIRRLKAQGVAII 194
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
853-1058 |
5.62e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 75.13 E-value: 5.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGNiTISGYPKNQ-------QTFARIsgyceqtdih 921
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfeTPDSGriLLDGR-DVTGLPPEKrnvgmvfQDYALF---------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 922 sPHVTVYESLVYSawLRLpKEVDKNKRKIFIEEVMELVELTPLRQALvglPGEsgLSTEQRKRLTIAVELVANPSIIFMD 1001
Cdd:COG3842 90 -PHLTVAENVAFG--LRM-RGVPKAEIRARVAELLELVGLEGLADRY---PHQ--LSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257669152 1002 EPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHQPSidifEAF---DELFLLKRG-----G--EEIY 1058
Cdd:COG3842 161 EPLSALDAKLREEMREELRRLQrELGITFIYVTHDQE----EALalaDRIAVMNDGrieqvGtpEEIY 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
853-1053 |
5.75e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 74.37 E-value: 5.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIdgniTISGYPKNQQTFARI-------SGYceqtdihsP 923
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGilAPDSGEV----LWDGEPLDPEDRRRIgylpeerGLY--------P 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 924 HVTVYESLVYSAWLR-LPKEVDKNKrkifIEEVMELVELTPLRQALVglpgESgLS-TEQRKrLTIAVELVANPSIIFMD 1001
Cdd:COG4152 85 KMKVGEQLVYLARLKgLSKAEAKRR----ADEWLERLGLGDRANKKV----EE-LSkGNQQK-VQLIAALLHDPELLILD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 257669152 1002 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAF-DELFLLKRG 1053
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQ--MELVEELcDRIVIINKG 205
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
853-1018 |
6.60e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 74.72 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGNITISGYPKNQ------QTFARisgYceqtdihs 922
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGleDPTSGeiLIGGRDVTDLPPKDRniamvfQSYAL---Y-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 923 PHVTVYESLVYSawLRLPKeVDKNKRKIFIEEVMELVELTPL--RqalvgLPGEsgLSTEQRKRLTIAVELVANPSIIFM 1000
Cdd:COG3839 88 PHMTVYENIAFP--LKLRK-VPKAEIDRRVREAAELLGLEDLldR-----KPKQ--LSGGQRQRVALGRALVREPKVFLL 157
|
170 180
....*....|....*....|
gi 257669152 1001 DEPTSGLDA--RAAaivMRT 1018
Cdd:COG3839 158 DEPLSNLDAklRVE---MRA 174
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
851-1034 |
7.81e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.48 E-value: 7.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiDGNITISGYP-KNQQTFARIS-GYCEQTDIHSPHVTVY 928
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD--AGKITVLGVPvPARARLARARiGVVPQFDNLDLEFTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 929 ESL-VYSAWLRLpkevdkNKRKIfiEEVM-ELVELTPL-RQALVGLpgeSGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1005
Cdd:PRK13536 133 ENLlVFGRYFGM------STREI--EAVIpSLLEFARLeSKADARV---SDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180
....*....|....*....|....*....
gi 257669152 1006 GLDARAAAIVMRTVRNTVDTGRTVVCTIH 1034
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
863-1042 |
8.13e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 72.62 E-value: 8.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 863 GVLTALMGVSGAGKTTLMDVLAG---RKTGGYIDGNITISGYPKNQQTFARIsGYCEQTDIHSPHVTVYESLVysAWLRL 939
Cdd:PRK10895 29 GEIVGLLGPNGAGKTTTFYMVVGivpRDAGNIIIDDEDISLLPLHARARRGI-GYLPQEASIFRRLSVYDNLM--AVLQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 940 PKEVDKNKRKIFIEEVMELVELTPLRQALvglpGESgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1019
Cdd:PRK10895 106 RDDLSAEQREDRANELMEEFHIEHLRDSM----GQS-LSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRII 180
|
170 180
....*....|....*....|....*
gi 257669152 1020 RNTVDTGRTVVCTIH--QPSIDIFE 1042
Cdd:PRK10895 181 EHLRDSGLGVLITDHnvRETLAVCE 205
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
154-412 |
9.31e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 73.32 E-value: 9.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 154 LNTLHLVPNRKKKfTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQELKQ-----TGRVTYNGHGMNEFVPQR 228
Cdd:PRK13547 2 LTADHLHVARRHR-AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPrgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 229 TA---AYIGQndvhigemTVRETFAYAARFQGVGSRYDMltelARREKEANIKpdpDIDIFMKAMSTAGektnvmtdyil 305
Cdd:PRK13547 81 LArlrAVLPQ--------AAQPAFAFSAREIVLLGRYPH----ARRAGALTHR---DGEIAWQALALAG----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 306 kilglevcADTMVGDDMLRgISGGQKKRVTTGEML---------VGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIFN 376
Cdd:PRK13547 135 --------ATALVGRDVTT-LSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWN 205
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 257669152 377 GTALISLLQPapetfNL----FDDIILIAEGEIIYEG-PRD 412
Cdd:PRK13547 206 LGVLAIVHDP-----NLaarhADRIAMLADGAIVAHGaPAD 241
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
168-421 |
1.15e-13 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 71.98 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkLdqeLK-QTGRVTYNGHGMNEFVPQRTAAYIG---QN-DVHIGE 242
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNG-L---LKpTSGEVLVDGKDITKKNLRELRRKVGlvfQNpDDQLFA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 243 MTVRETFAYAARFQGVGSRydmltELARREKEAnikpdpdidifmkamstagektnvmtdyiLKILGLEVCADTMVGDdm 322
Cdd:COG1122 91 PTVEEDVAFGPENLGLPRE-----EIRERVEEA-----------------------------LELVGLEHLADRPPHE-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 323 lrgISGGQKKRVTTGEMLV-GPsRALFMDEISTGLDSSTTYQIVNSLRNYvHIFNGTALIS--LLQPAPEtfnLFDDIIL 399
Cdd:COG1122 135 ---LSGGQKQRVAIAGVLAmEP-EVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVthDLDLVAE---LADRVIV 206
|
250 260
....*....|....*....|..
gi 257669152 400 IAEGEIIYEGPRDHVVEFFETM 421
Cdd:COG1122 207 LDDGRIVADGTPREVFSDYELL 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
844-1049 |
1.20e-13 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 72.43 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 844 GTQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyidgNITISGYPkNQQTFARIsGYCEQTDih 921
Cdd:COG1116 18 PTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGleKPTSG----EVLVDGKP-VTGPGPDR-GVVFQEP-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 922 S--PHVTVYESLVYSawLRLpKEVDKNKRKIFIEEVMELVELTPLRQALvglPGEsgLSTEQRKRLTIAVELVANPSIIF 999
Cdd:COG1116 90 AllPWLTVLDNVALG--LEL-RGVPKAERRERARELLELVGLAGFEDAY---PHQ--LSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 257669152 1000 MDEPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHqpsiDIFEAfdeLFL 1049
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWqETGKTVLFVTH----DVDEA---VFL 205
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
853-1034 |
1.29e-13 |
|
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: 71.98 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyidgNITISGY-P-KNQQTF-ARISGYCEQTDIHSPHVTV 927
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGllQPTSG----EVRVAGLvPwKRRKKFlRRIGVVFGQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 928 YESL-VYSAWLRLPKEVDKNKRKIFIEeVMELVEL--TPLRQalvglpgesgLSTEQRKRLTIAVELVANPSIIFMDEPT 1004
Cdd:cd03267 113 IDSFyLLAAIYDLPPARFKKRLDELSE-LLDLEELldTPVRQ----------LSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190
....*....|....*....|....*....|.
gi 257669152 1005 SGLDARAAAIVMRTVRNTV-DTGRTVVCTIH 1034
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNrERGTTVLLTSH 212
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
848-1034 |
1.51e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.30 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 848 DRLVLlKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiDGNITISGYP---KNQQTFARIsGYCEQTDIHSPH 924
Cdd:PRK13537 19 DKLVV-DGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPD--AGSISLCGEPvpsRARHARQRV-GVVPQFDNLDPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 925 VTVYESL-VYSAWLRLPKEVDKnkrkifiEEVMELVELTPLRQALVGLPGEsgLSTEQRKRLTIAVELVANPSIIFMDEP 1003
Cdd:PRK13537 95 FTVRENLlVFGRYFGLSAAAAR-------ALVPPLLEFAKLENKADAKVGE--LSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190
....*....|....*....|....*....|.
gi 257669152 1004 TSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1034
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
846-1036 |
1.59e-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: 70.85 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 846 QEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIDGNITISgyPKNQQTFARISGYCEQTDIHSP 923
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGllRPDSGEVRWNGTPL--AEQRDEPHENILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 924 HVTVYESLVYsaWLRLPKEVDKNkrkifIEEVMELVELTPLRQALVGLpgesgLSTEQRKRLTIAVELVANPSIIFMDEP 1003
Cdd:TIGR01189 87 ELSALENLHF--WAAIHGGAQRT-----IEDALAAVGLTGFEDLPAAQ-----LSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|...
gi 257669152 1004 TSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQP 1036
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
853-1073 |
1.83e-13 |
|
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: 71.60 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI--DGNiTISGYPKNQQTFarisGYCEQTDIHSPHVTVY 928
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGfiKPDSGKIllNGK-DITNLPPEKRDI----SYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 929 ESLVYSawLRLpKEVDKNKRKifiEEVMELVELTPLRQALVGLPGEsgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1008
Cdd:cd03299 90 KNIAYG--LKK-RKVDKKEIE---RKVLEIAEMLGIDHLLNRKPET--LSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257669152 1009 ARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELFLLkRGGEEIYVGPLGHESTHLINYF 1073
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIM-LNGKLIQVGKPEEVFKKPKNEF 225
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
863-1034 |
3.39e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 863 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiDGNITISGYPKNQQTFARISGYC---EQTDIHSPhvTVYESLV------Y 933
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLA--SGKISILGQPTRQALQKNLVAYVpqsEEVDWSFP--VLVEDVVmmgrygH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 934 SAWLRLPKEVDKNkrkiFIEEVMELVELTPLRQALVGlpgesGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA 1013
Cdd:PRK15056 109 MGWLRRAKKRDRQ----IVTAALARVDMVEFRHRQIG-----ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180
....*....|....*....|.
gi 257669152 1014 IVMRTVRNTVDTGRTVVCTIH 1034
Cdd:PRK15056 180 RIISLLRELRDEGKTMLVSTH 200
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
862-1014 |
5.04e-13 |
|
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: 72.44 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 862 PGVlTALMGVSGAGKTTLMDVLAG--RKTGGYI--DGNITisgypknQQTFARIS--------GYCEQTDIHSPHVTVYE 929
Cdd:COG4148 25 RGV-TALFGPSGSGKTTLLRAIAGleRPDSGRIrlGGEVL-------QDSARGIFlpphrrriGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 930 SLVYSAWlRLPKEvdknKRKIFIEEVMELVELTPL--RQAlvglpgeSGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1007
Cdd:COG4148 97 NLLYGRK-RAPRA----ERRISFDEVVELLGIGHLldRRP-------ATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
....*...
gi 257669152 1008 D-ARAAAI 1014
Cdd:COG4148 165 DlARKAEI 172
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
853-1015 |
5.31e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 70.45 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLM-------DVLAGRKtggyIDGNITISGypknqqtfarisgyceqTDIHSPHV 925
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPGAR----VEGEILLDG-----------------EDIYDPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 926 TVYEslvysawLR------------LPKEVDKN----------KRKifiEEVMELVElTPLRQAlvGLPGE--------- 974
Cdd:COG1117 86 DVVE-------LRrrvgmvfqkpnpFPKSIYDNvayglrlhgiKSK---SELDEIVE-ESLRKA--ALWDEvkdrlkksa 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 257669152 975 SGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIV 1015
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKI 193
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
851-1010 |
7.15e-13 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 69.21 E-value: 7.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGNITISGYPKNQ------QTFARisgYceqtdi 920
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGleEPTSGriYIGGRDVTDLPPKDRdiamvfQNYAL---Y------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 921 hsPHVTVYESLVYSAWLRLPKEVDKNKRkifIEEVMELVELTPLrqaLVGLPGEsgLSTEQRKRLTIAVELVANPSIIFM 1000
Cdd:cd03301 85 --PHMTVYDNIAFGLKLRKVPKDEIDER---VREVAELLQIEHL---LDRKPKQ--LSGGQRQRVALGRAIVREPKVFLM 154
|
170
....*....|
gi 257669152 1001 DEPTSGLDAR 1010
Cdd:cd03301 155 DEPLSNLDAK 164
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
168-418 |
7.58e-13 |
|
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: 69.62 E-value: 7.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkldQELKQTGRVTYNGH---GMNEFVPQRTAAYIG---QNDVHIG 241
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIG---LLRPDSGEILVDGQditGLSEKELYELRRRIGmlfQGGALFD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 242 EMTVRETFAYAARfqgvgsrydMLTELARREKEAnikpdpdidifmKAMstagEKtnvmtdyiLKILGLEVCADTMVGDd 321
Cdd:COG1127 96 SLTVFENVAFPLR---------EHTDLSEAEIRE------------LVL----EK--------LELVGLPGAADKMPSE- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 322 mlrgISGGQKKRvttgemlVGPSRAL-------FMDEISTGLDSSTTYQIVNSLRNYVHIFNGTALI---SLlqpaPETF 391
Cdd:COG1127 142 ----LSGGMRKR-------VALARALaldpeilLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVvthDL----DSAF 206
|
250 260 270
....*....|....*....|....*....|....*
gi 257669152 392 NLFDDIILIAEGEIIYEGPRD--------HVVEFF 418
Cdd:COG1127 207 AIADRVAVLADGKIIAEGTPEellasddpWVRQFL 241
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
852-1053 |
8.20e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.42 E-value: 8.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIDGNITISGYPKN-----QQTFARISGYCEQ----TDI 920
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGllRPQKGAVLWQGKPLDYSKRgllalRQQVATVFQDPEQqifyTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 921 HSphvtvyeSLVYSawLR-LPKEVDKNKRKIfiEEVMELVELTPLRQALVglpgeSGLSTEQRKRLTIAVELVANPSIIF 999
Cdd:PRK13638 96 DS-------DIAFS--LRnLGVPEAEITRRV--DEALTLVDAQHFRHQPI-----QCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 257669152 1000 MDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpSID-IFEAFDELFLLKRG 1053
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSH--DIDlIYEISDAVYVLRQG 212
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
825-1037 |
9.55e-13 |
|
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: 69.44 E-value: 9.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 825 ITFDNVV--YSVDMPqemieqgtqedrlVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRktggYI--DGNITISG 900
Cdd:cd03252 1 ITFEHVRfrYKPDGP-------------VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF----YVpeNGRVLVDG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 901 YP---KNQQTFARISGYCEQtdihsphvtvyESLVYSAWLRlpKEVDKNKRKIFIEEVMELVELTPLRQALVGLP----- 972
Cdd:cd03252 64 HDlalADPAWLRRQVGVVLQ-----------ENVLFNRSIR--DNIALADPGMSMERVIEAAKLAGAHDFISELPegydt 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257669152 973 --GE--SGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDtGRTVVCTIHQPS 1037
Cdd:cd03252 131 ivGEqgAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLS 198
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
836-1008 |
9.69e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.42 E-value: 9.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 836 MPQEMIEQ--------GTQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiDGNITISGYPKNQ-- 905
Cdd:PRK10584 1 MPAENIVEvhhlkksvGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGS--SGEVSLVGQPLHQmd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 906 -----QTFARISGYCEQTDIHSPHVTVYESLVYSAWLRlpKEVDKNKRkifiEEVMELVELTPLRQALVGLPGEsgLSTE 980
Cdd:PRK10584 79 eearaKLRAKHVGFVFQSFMLIPTLNALENVELPALLR--GESSRQSR----NGAKALLEQLGLGKRLDHLPAQ--LSGG 150
|
170 180
....*....|....*....|....*...
gi 257669152 981 QRKRLTIAVELVANPSIIFMDEPTSGLD 1008
Cdd:PRK10584 151 EQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
787-1034 |
9.95e-13 |
|
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: 73.51 E-value: 9.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 787 AEEPASDETELQSARSEGVVeAGANKKRGMVLpfepHSITfdnVVYSvdmpqemieqGTQE---DRLVLlkGVngafRPG 863
Cdd:TIGR01257 1910 AKEPIFDEDDDVAEERQRII-SGGNKTDILRL----NELT---KVYS----------GTSSpavDRLCV--GV----RPG 1965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 864 VLTALMGVSGAGKTTLMDVLAGRKTggYIDGNITISGypknQQTFARIS------GYCEQTDIHSPHVTVYESLVYSAWL 937
Cdd:TIGR01257 1966 ECFGLLGVNGAGKTTTFKMLTGDTT--VTSGDATVAG----KSILTNISdvhqnmGYCPQFDAIDDLLTGREHLYLYARL 2039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 938 R-LPKEVdknkrkifIEEV----MELVELTPLRQALVGLpgesgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA 1012
Cdd:TIGR01257 2040 RgVPAEE--------IEKVanwsIQSLGLSLYADRLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
250 260
....*....|....*....|..
gi 257669152 1013 AIVMRTVRNTVDTGRTVVCTIH 1034
Cdd:TIGR01257 2107 RMLWNTIVSIIREGRAVVLTSH 2128
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
167-415 |
1.06e-12 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 69.39 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 167 FTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKldqeLKQT-GRVTYNGH---GMNEFvpQRTAAYIG---QNDVH 239
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGF----LRPTsGSVLFDGEditGLPPH--EIARLGIGrtfQIPRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 240 IGEMTVRETFAYAARFQgvgSRYDMLTELARREKEANIKpdpdidifmKAMStagektnvmtdyILKILGLEVCADTMVG 319
Cdd:cd03219 87 FPELTVLENVMVAAQAR---TGSGLLLARARREEREARE---------RAEE------------LLERVGLADLADRPAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 320 DdmlrgISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNyVHIFNGTALI-----SLLqpapetFNLF 394
Cdd:cd03219 143 E-----LSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRE-LRERGITVLLvehdmDVV------MSLA 210
|
250 260
....*....|....*....|.
gi 257669152 395 DDIILIAEGEIIYEGPRDHVV 415
Cdd:cd03219 211 DRVTVLDQGRVIAEGTPDEVR 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
185-409 |
1.14e-12 |
|
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: 68.86 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 185 LLGPPSSGKTTLLLALAG--KLDQelkqtGRVTYNG-------HGMNEFVPQRTAAYIGQNDVHIGEMTVRETFAYAARF 255
Cdd:cd03297 28 IFGASGAGKSTLLRCIAGleKPDG-----GTIVLNGtvlfdsrKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 256 QGVGSRYDMLTElarrekeanikpdpdidifmkamstagektnvmtdyILKILGLEVCADTMVGddmlrGISGGQKKRVT 335
Cdd:cd03297 103 KRNREDRISVDE------------------------------------LLDLLGLDHLLNRYPA-----QLSGGEKQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257669152 336 TGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIFNGTALIsLLQPAPETFNLFDDIILIAEGEIIYEG 409
Cdd:cd03297 142 LARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIF-VTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
853-1038 |
1.43e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.94 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKtgGY--IDGNITISG---------------------YPknqqtfA 909
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHP--KYevTSGSILLDGedilelspderaragiflafqYP------V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 910 RISGyceqtdihsphVTVYESLVYSAWLRLPKEVDKNKRKIFIEEVMELVELTP--LRQAL-VGLPGesGlsteQRKRLT 986
Cdd:COG0396 88 EIPG-----------VSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEdfLDRYVnEGFSG--G----EKKRNE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 257669152 987 IAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1038
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRI 202
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
162-409 |
1.85e-12 |
|
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: 68.16 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 162 NRKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQElkqTGRVTYNGHGMNE----------FVPQRTAA 231
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD---AGFATVDGFDVVKepaearrrlgFVSDSTGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 232 YigqndvhiGEMTVRETFAYAARFQGvgsrydmlteLARREKEANIkpdpdidifmkamstagektnvmtDYILKILGLE 311
Cdd:cd03266 90 Y--------DRLTARENLEYFAGLYG----------LKGDELTARL------------------------EELADRLGME 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 312 VCADTMVGddmlrGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIfnGTALISLLQPAPETF 391
Cdd:cd03266 128 ELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL--GKCILFSTHIMQEVE 200
|
250
....*....|....*...
gi 257669152 392 NLFDDIILIAEGEIIYEG 409
Cdd:cd03266 201 RLCDRVVVLHRGRVVYEG 218
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
825-1054 |
2.34e-12 |
|
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: 68.41 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 825 ITFDNVVYsvdmpqemieqGTQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLM-------DVLAGRKTggyIDGnIT 897
Cdd:cd03251 1 VEFKNVTF-----------RYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVnliprfyDVDSGRIL---IDG-HD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 898 ISGYPKNQqtFARISGYCEQtDIHSPHVTVYESLVYSawlrlpkevdknKRKIFIEEVMELVELTPLRQALVGLP----- 972
Cdd:cd03251 66 VRDYTLAS--LRRQIGLVSQ-DVFLFNDTVAENIAYG------------RPGATREEVEEAARAANAHEFIMELPegydt 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 973 --GESG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDtGRTVVCTIHQPSIdIFEAfDELF 1048
Cdd:cd03251 131 viGERGvkLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLST-IENA-DRIV 207
|
....*.
gi 257669152 1049 LLKRGG 1054
Cdd:cd03251 208 VLEDGK 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
166-406 |
2.54e-12 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 68.15 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 166 KFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkLDQelKQTGRVTYNGH---GMNEfvPQRTA---AYIG---QN 236
Cdd:COG1136 20 EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG-LDR--PTSGEVLIDGQdisSLSE--RELARlrrRHIGfvfQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 237 dvH--IGEMTVRETFAYAARFQGVGSRydmltelaRREKEAnikpdpdidifmkamstagektnvmtDYILKILGLEVCA 314
Cdd:COG1136 95 --FnlLPELTALENVALPLLLAGVSRK--------ERRERA--------------------------RELLERVGLGDRL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 315 DTMVGDdmlrgISGGQKKRVTTGEMLVGPSRALFMDEIsTG-LDSSTTYQIVNSLRNYVHIFNGTALIsllqpA---PET 390
Cdd:COG1136 139 DHRPSQ-----LSGGQQQRVAIARALVNRPKLILADEP-TGnLDSKTGEEVLELLRELNRELGTTIVM-----VthdPEL 207
|
250
....*....|....*.
gi 257669152 391 FNLFDDIILIAEGEII 406
Cdd:COG1136 208 AARADRVIRLRDGRIV 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
851-1061 |
2.65e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.66 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLaGRKTGGYiDGNITISGYPK---NQQTFARISGYCEQTDIHSPHVTV 927
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPS-EGEILLDAQPLeswSSKAFARKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 928 YEsLV-------YSAWLRLPKEvDKNKrkifIEEVMELVELTPLRQALVglpgeSGLSTEQRKRLTIAVELVANPSIIFM 1000
Cdd:PRK10575 103 RE-LVaigrypwHGALGRFGAA-DREK----VEEAISLVGLKPLAHRLV-----DSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257669152 1001 DEPTSGLDARAAAIVMRTV-RNTVDTGRTVVCTIHqpsiDIFEAF---DELFLLkRGGEEIYVGP 1061
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVhRLSQERGLTVIAVLH----DINMAArycDYLVAL-RGGEMIAQGT 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
825-1034 |
2.67e-12 |
|
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: 68.34 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 825 ITFDNVVYSVDmpqemieqgTQEDRLVLlKGVNGAFRPGVLTALMGVSGAGKTTLM-------DVLAGRKTggyIDGnIT 897
Cdd:cd03249 1 IEFKNVSFRYP---------SRPDVPIL-KGLSLTIPPGKTVALVGSSGCGKSTVVsllerfyDPTSGEIL---LDG-VD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 898 ISGYpkNQQTFARISGYCEQtdihSPHV---TVYESLVYSAWLRLPKEVDKNKRKIFIEE-VMELveltPLR-QALVGlP 972
Cdd:cd03249 67 IRDL--NLRWLRSQIGLVSQ----EPVLfdgTIAENIRYGKPDATDEEVEEAAKKANIHDfIMSL----PDGyDTLVG-E 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257669152 973 GESGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIH 1034
Cdd:cd03249 136 RGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEAL-DRAMKGRTTIVIAH 196
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
160-409 |
3.25e-12 |
|
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: 67.39 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 160 VPNRKKK---FTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDqelKQTGRVTYNGHGM--NEFVPQRTAAYIG 234
Cdd:cd03265 3 VENLVKKygdFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLK---PTSGRATVAGHDVvrEPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 235 QNDVHIGEMTVRETFAYAARFQGVGSRydmltELARRekeanikpdpdidifmkamstagektnvmTDYILKILGLEVCA 314
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGA-----ERRER-----------------------------IDELLDFVGLLEAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 315 DTMVgddmlRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIFNGTALISlLQPAPETFNLF 394
Cdd:cd03265 126 DRLV-----KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLT-THYMEEAEQLC 199
|
250
....*....|....*
gi 257669152 395 DDIILIAEGEIIYEG 409
Cdd:cd03265 200 DRVAIIDHGRIIAEG 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
853-1053 |
3.33e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 68.72 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIDGNITISGYPKNQQTFARISGYCEQTDIHSP-HVTVY 928
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGilkPSSGRILFDGKPIDYSRKGLMKLRESVGMVFQDPDNQLfSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 929 ESLVYSAW-LRLPK-EVDKNkrkifIEEVMELVELTPLRQAlvglPGESgLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1006
Cdd:PRK13636 102 QDVSFGAVnLKLPEdEVRKR-----VDNALKRTGIEHLKDK----PTHC-LSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 257669152 1007 LDARAAAIVMRTVRNTV-DTGRTVVCTIHqpSIDIFEAF-DELFLLKRG 1053
Cdd:PRK13636 172 LDPMGVSEIMKLLVEMQkELGLTIIIATH--DIDIVPLYcDNVFVMKEG 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
844-1054 |
4.95e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.73 E-value: 4.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 844 GTQEDRLVllKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIDGNITISGYPKNQQT---FARISGYCEQTDI 920
Cdd:PRK11231 11 GYGTKRIL--NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP--QSGTVFLGDKPISMLSsrqLARRLALLPQHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 921 HSPHVTVYESLVY--SAWLRLPKEVDKNKRKIfIEEVMELVELTPLRQALVglpgeSGLSTEQRKRLTIAVELVANPSII 998
Cdd:PRK11231 87 TPEGITVRELVAYgrSPWLSLWGRLSAEDNAR-VNQAMEQTRINHLADRRL-----TDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 257669152 999 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpsiDIFEA---FDELFLLKRGG 1054
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLH----DLNQAsryCDHLVVLANGH 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
169-409 |
5.46e-12 |
|
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: 67.26 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 169 ILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDqelKQTGRVTYNGHGMNEFVPQRTAAYIG--QNDVHIGEMTVR 246
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYD---VDSGRILIDGHDVRDYTLASLRRQIGlvSQDVFLFNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 247 ETFAYAarfqgvgsrydmltelarrekeaniKPDPDIDIFMKAMSTAGektnvMTDYILKilgLEVCADTMVGDdmlRGI 326
Cdd:cd03251 94 ENIAYG-------------------------RPGATREEVEEAARAAN-----AHEFIME---LPEGYDTVIGE---RGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 327 --SGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHifNGTALI-----SLLQPApetfnlfDDIIL 399
Cdd:cd03251 138 klSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFViahrlSTIENA-------DRIVV 208
|
250
....*....|
gi 257669152 400 IAEGEIIYEG 409
Cdd:cd03251 209 LEDGKIVERG 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
853-1053 |
6.08e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.94 E-value: 6.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiDGNITISGYPknqQTFARISGYCEQ--TDIH-----SPHV 925
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD--AGSILIDGQE---MRFASTTAALAAgvAIIYqelhlVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 926 TVYESLvysaWL-RLPKEVDKNKRKIFIEEVME-LVEL-------TPLRQalvglpgesgLSTEQRKRLTIAVELVANPS 996
Cdd:PRK11288 95 TVAENL----YLgQLPHKGGIVNRRLLNYEAREqLEHLgvdidpdTPLKY----------LSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 257669152 997 IIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELFLLKRG 1053
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRME-EIFALCDAITVFKDG 216
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
166-406 |
6.35e-12 |
|
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: 66.39 E-value: 6.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 166 KFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAG--KLDQelkqtGRVTYNGHGMNEFVP-QRTAAYIGQNDVHIGE 242
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGleRPDS-----GEILIDGRDVTGVPPeRRNIGMVFQDYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 243 MTVRETFAYAARFQGVGSRydmltELARREKEanikpdpdidifmkamstagektnvmtdyILKILGLEVCADTMVgddm 322
Cdd:cd03259 87 LTVAENIAFGLKLRGVPKA-----EIRARVRE-----------------------------LLELVGLEGLLNRYP---- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 323 lRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDssttYQIVNSLRNYV-HIFNGTALISLL----QpaPETFNLFDDI 397
Cdd:cd03259 129 -HELSGGQQQRVALARALAREPSLLLLDEPLSALD----AKLREELREELkELQRELGITTIYvthdQ--EEALALADRI 201
|
....*....
gi 257669152 398 ILIAEGEII 406
Cdd:cd03259 202 AVMNEGRIV 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
844-1035 |
7.08e-12 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 66.84 E-value: 7.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 844 GTQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIDGNITISGY------PKNQQTFARISGYCEQ 917
Cdd:cd03258 12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLER--PTSGSVLVDGTdltllsGKELRKARRRIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 918 tdihspHV------TVYESLVYSawLRLPKeVDKNKRKIFIEEVMELVELTPLRQAlvgLPGEsgLSTEQRKRLTIAVEL 991
Cdd:cd03258 90 ------HFnllssrTVFENVALP--LEIAG-VPKAEIEERVLELLELVGLEDKADA---YPAQ--LSGGQKQRVGIARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 257669152 992 VANPSIIFMDEPTSGLDARAAAIVMRTVRNT-VDTGRTVVCTIHQ 1035
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHE 200
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
851-1011 |
7.97e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 69.71 E-value: 7.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIDGNITIsgyPKNqqtfARIsGYCEQTDIHSPHVTVYES 930
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELE--PDSGEVSI---PKG----LRI-GYLPQEPPLDDDLTVLDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 931 lVYSAWLRLpKEVDKNKRKI------FIEEVMELVELTP-------------LRQALVGLpgesGLSTE----------- 980
Cdd:COG0488 82 -VLDGDAEL-RALEAELEELeaklaePDEDLERLAELQEefealggweaearAEEILSGL----GFPEEdldrpvselsg 155
|
170 180 190
....*....|....*....|....*....|..
gi 257669152 981 -QRKRLTIAVELVANPSIIFMDEPTSGLDARA 1011
Cdd:COG0488 156 gWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
753-1030 |
9.92e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 69.42 E-value: 9.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 753 IGTGALLGFVVLFNFGFTLALTFLNSLGKPQAVIAeepASDE-TELQSARSEGVVEAGANKkrgmvLPFEPHSITFDNVV 831
Cdd:COG1132 275 LTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALA---SAERiFELLDEPPEIPDPPGAVP-----LPPVRGEIEFENVS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 832 YSVDmpqemieqgtqEDRLVLlKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGrktggYID---GNITISGYPKNQQTF 908
Cdd:COG1132 347 FSYP-----------GDRPVL-KDISLTIPPGETVALVGPSGSGKSTLVNLLLR-----FYDptsGRILIDGVDIRDLTL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 909 A----RIsGYCEQtDIHSPHVTVYESLVYSAwlrlpKEVDKnkrkifiEEVMELveltpLRQALV-----GLP------- 972
Cdd:COG1132 410 EslrrQI-GVVPQ-DTFLFSGTIRENIRYGR-----PDATD-------EEVEEA-----AKAAQAhefieALPdgydtvv 470
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 973 GESG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNtVDTGRTVV 1030
Cdd:COG1132 471 GERGvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALER-LMKGRTTI 529
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
852-1013 |
1.00e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 66.86 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLagrktggyidgNITISGYPKnqqtfARISG--YCEQTDIHS------- 922
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-----------NRLIELYPE-----ARVSGevYLDGQDIFKmdvielr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 923 -------------PHVTVYESLVYSawLRLPKEVdKNKRKIF--IEEVMELVELTPLRQALVGLPGESgLSTEQRKRLTI 987
Cdd:PRK14247 82 rrvqmvfqipnpiPNLSIFENVALG--LKLNRLV-KSKKELQerVRWALEKAQLWDEVKDRLDAPAGK-LSGGQQQRLCI 157
|
170 180
....*....|....*....|....*.
gi 257669152 988 AVELVANPSIIFMDEPTSGLDARAAA 1013
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTA 183
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
163-414 |
1.04e-11 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 69.16 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 163 RKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkLDQelKQTGRVTYNGHGMNEFVPQRTAA------YIGQN 236
Cdd:COG1123 274 GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG-LLR--PTSGSILFDGKDLTKLSRRSLRElrrrvqMVFQD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 237 DVH--IGEMTVRETFAYAARFQGVGSRydmltelARREKEAnikpdpdidifmkamstagektnvmtDYILKILGLevca 314
Cdd:COG1123 351 PYSslNPRMTVGDIIAEPLRLHGLLSR-------AERRERV--------------------------AELLERVGL---- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 315 dtmvGDDMLR----GISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIFNGTAL-----ISLLQ 385
Cdd:COG1123 394 ----PPDLADryphELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLfishdLAVVR 469
|
250 260
....*....|....*....|....*....
gi 257669152 386 papetfNLFDDIILIAEGEIIYEGPRDHV 414
Cdd:COG1123 470 ------YIADRVAVMYDGRIVEDGPTEEV 492
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
853-1037 |
1.38e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 66.34 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLagrKTGGYIDGNITISGypknQQTFARISGYCEQTD-----------IH 921
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSI---NRMNDLNPEVTITG----SIVYNGHNIYSPRTDtvdlrkeigmvFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 922 SPH---VTVYESLVYSawLRLPKEVDKNKrkifIEEVMElvelTPLRQALV------GLPGES-GLSTEQRKRLTIAVEL 991
Cdd:PRK14239 94 QPNpfpMSIYENVVYG--LRLKGIKDKQV----LDEAVE----KSLKGASIwdevkdRLHDSAlGLSGGQQQRVCIARVL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 257669152 992 VANPSIIFMDEPTSGLDARAAAIVMRTVRNTVD--TGRTVVCTIHQPS 1037
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRSMQQAS 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
167-412 |
1.44e-11 |
|
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: 66.05 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 167 FTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQElkqTGRVTYNGHGMNEFVPQ--RTA----AYIGQNDVHI 240
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT---SGSVLIDGTDINKLKGKalRQLrrqiGMIFQQFNLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 241 GEMTVRET-----FAYAARFQGVGSRYDmltelaRREKEANIkpdpdidifmkamstagektnvmtdYILKILGLEVCAD 315
Cdd:cd03256 91 ERLSVLENvlsgrLGRRSTWRSLFGLFP------KEEKQRAL-------------------------AALERVGLLDKAY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 316 TMVGDdmlrgISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIFNGTALISLLQPapetfNL-- 393
Cdd:cd03256 140 QRADQ-----LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQV-----DLar 209
|
250 260
....*....|....*....|.
gi 257669152 394 --FDDIILIAEGEIIYEGPRD 412
Cdd:cd03256 210 eyADRIVGLKDGRIVFDGPPA 230
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
169-369 |
1.59e-11 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 68.54 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 169 ILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDqelKQTGRVTYNG---HGMNEFVPQRTAAYIGQnDVHIGEMTV 245
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD---PLQGEVTLDGvpvSSLDQDEVRRRVSVCAQ-DAHLFDTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 246 RETFAYAarfqgvgsrydmltelarrekeaniKPDPDIDIFMKAMSTAGektnvMTDYilkILGLEVCADTMVGDDMLRg 325
Cdd:TIGR02868 426 RENLRLA-------------------------RPDATDEELWAALERVG-----LADW---LRALPDGLDTVLGEGGAR- 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 257669152 326 ISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLR 369
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLL 515
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
846-1012 |
1.90e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.61 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 846 QEDRLV--LLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIDGNITISGYPKNQQTFA-------RISGYCE 916
Cdd:PRK11629 16 QEGSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTP--TSGDVIFNGQPMSKLSSAakaelrnQKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 917 QTDIHSPHVTVYESLVysawlrLPKEVDKNKRKIFIEEVMELVELTPLRQALVGLPGEsgLSTEQRKRLTIAVELVANPS 996
Cdd:PRK11629 94 QFHHLLPDFTALENVA------MPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSE--LSGGERQRVAIARALVNNPR 165
|
170
....*....|....*.
gi 257669152 997 IIFMDEPTSGLDARAA 1012
Cdd:PRK11629 166 LVLADEPTGNLDARNA 181
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
168-412 |
1.91e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 65.86 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQELKQtGRVTYNGhgmnefvpqrtaayigQNdvhIGEMTVRE 247
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTS-GSILLDG----------------ED---ILELSPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 248 --------TFAYAARFQGVGsrydmLTELARREKEANIKPDPDIDIFMKAMSTAgektnvmtdyiLKILGLEvcadtmvg 319
Cdd:COG0396 74 raragiflAFQYPVEIPGVS-----VSNFLRTALNARRGEELSAREFLKLLKEK-----------MKELGLD-------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 320 DDMLR-----GISGGQKKRVTTGEMLV-GPSRALFmDEISTGLD-------SsttyQIVNSLRNyvhifNGTALI----- 381
Cdd:COG0396 130 EDFLDryvneGFSGGEKKRNEILQMLLlEPKLAIL-DETDSGLDidalrivA----EGVNKLRS-----PDRGILiithy 199
|
250 260 270
....*....|....*....|....*....|....*
gi 257669152 382 ----SLLQPapetfnlfDDIILIAEGEIIYEGPRD 412
Cdd:COG0396 200 qrilDYIKP--------DFVHVLVDGRIVKSGGKE 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
848-1034 |
2.06e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 66.25 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 848 DRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGNiTISGYPKNQQTFARISGYCEQT---DI 920
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGilKPTSGevLIKGE-PIKYDKKSLLEVRKTVGIVFQNpddQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 921 HSPhvTVYESLVYSAW-LRLPKEVDKNKRKIFIEEV-MELVELTPLRQalvglpgesgLSTEQRKRLTIAVELVANPSII 998
Cdd:PRK13639 92 FAP--TVEEDVAFGPLnLGLSKEEVEKRVKEALKAVgMEGFENKPPHH----------LSGGQKKRVAIAGILAMKPEII 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 257669152 999 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1034
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
853-1089 |
2.34e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.80 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIDG-NITISGypKNQQTFARISGYCEQTDIHSPHV------ 925
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGsHIELLG--RTVQREGRLARDIRKSRANTGYIfqqfnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 926 ----TVYESLVYSA------W---LRLPKEVDKNKrkifieevmELVELTPLRQALVGLPGESGLSTEQRKRLTIAVELV 992
Cdd:PRK09984 98 vnrlSVLENVLIGAlgstpfWrtcFSWFTREQKQR---------ALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 993 ANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDT-GRTVVCTIHQpsIDIFEAFDELFLLKRGGEEIYVGPLGHESTHLIN 1071
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQ--VDYALRYCERIVALRQGHVFYDGSSQQFDNERFD 246
|
250
....*....|....*...
gi 257669152 1072 YFesIQGINKITEGYNPA 1089
Cdd:PRK09984 247 HL--YRSINRVEENAKAA 262
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
168-412 |
2.74e-11 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 65.22 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkldQELKQTGRVTYNGH---GMNEFVPQRTAAYIG---QNDVHIG 241
Cdd:cd03261 14 TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVG---LLRPDSGEVLIDGEdisGLSEAELYRLRRRMGmlfQSGALFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 242 EMTVRETFAYAARfqgvgsrydMLTELARREkeanikpdpdidIFMKAMSTagektnvmtdyiLKILGLEVCADTMVGDd 321
Cdd:cd03261 91 SLTVFENVAFPLR---------EHTRLSEEE------------IREIVLEK------------LEAVGLRGAEDLYPAE- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 322 mlrgISGGQKKRvttgemlVGPSRAL-------FMDEISTGLDSSTTYQIVNSLRNYVHIFNGTALI---SLlqpaPETF 391
Cdd:cd03261 137 ----LSGGMKKR-------VALARALaldpellLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMvthDL----DTAF 201
|
250 260
....*....|....*....|.
gi 257669152 392 NLFDDIILIAEGEIIYEGPRD 412
Cdd:cd03261 202 AIADRIAVLYDGKIVAEGTPE 222
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
853-1030 |
3.17e-11 |
|
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: 65.00 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI--DG-NITisgypkNQQTFARIS---GYCEQT-DIHsP 923
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGllPPRSGSIrfDGeDIT------GLPPHRIARlgiGYVPEGrRIF-P 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 924 HVTVYESLVYSAWLRLPKEVDKNKrkifIEEVMELV-ELTPLRQALVGLpgesgLSTEQRKRLTIAVELVANPSIIFMDE 1002
Cdd:COG0410 92 SLTVEENLLLGAYARRDRAEVRAD----LERVYELFpRLKERRRQRAGT-----LSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180
....*....|....*....|....*...
gi 257669152 1003 PTSGLDARAAAIVMRTVRNTVDTGRTVV 1030
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIRRLNREGVTIL 190
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
861-1053 |
3.57e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.91 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 861 RPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYID-GNITISGYPKNQQT--FARISGYCEQTdihsPHVTVYESLVYSA 935
Cdd:PRK13643 30 KKGSYTALIGHTGSGKSTLLQHLNGllQPTEGKVTvGDIVVSSTSKQKEIkpVRKKVGVVFQF----PESQLFEETVLKD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 936 WLRLPKE--VDKNKRKIFIEEVMELVELTplRQALVGLPGEsgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA 1013
Cdd:PRK13643 106 VAFGPQNfgIPKEKAEKIAAEKLEMVGLA--DEFWEKSPFE--LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 257669152 1014 IVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELFLLKRG 1053
Cdd:PRK13643 182 EMMQLFESIHQSGQTVVLVTHLMD-DVADYADYVYLLEKG 220
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
852-1058 |
4.75e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 65.94 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGrktggyID----GNITISGypknQQTFARIS------GYCEQtdiH 921
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAG------LEtpdsGRIVLNG----RDLFTNLPprerrvGFVFQ---H 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 922 S---PHVTVYESLVYSAWLRLPKEVDKNKRkifIEEVMELVELTPL--RqalvgLPGEsgLSTEQRKRLTIAVELVANPS 996
Cdd:COG1118 84 YalfPHMTVAENIAFGLRVRPPSKAEIRAR---VEELLELVQLEGLadR-----YPSQ--LSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257669152 997 IIFMDEPTSGLDARAAAIVMRTVRNTVD-TGRTVVCTIHqpsiDIFEAF---DELFLLKRG-------GEEIY 1058
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLHDeLGGTTVFVTH----DQEEALelaDRVVVMNQGrieqvgtPDEVY 222
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
847-1053 |
5.16e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 847 EDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIDGNITIsgypknqqtfarisgyceQTDIHSPHVT 926
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDV------------------PDNQFGREAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 927 VYESLvysawlrlPKEVDKNkrkifieEVMELVeltplrqALVGL---------PGEsgLSTEQRKRLTIAVELVANPSI 997
Cdd:COG2401 102 LIDAI--------GRKGDFK-------DAVELL-------NAVGLsdavlwlrrFKE--LSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257669152 998 IFMDEPTSGLDARAAAIVMRTVRNTVDTGRT--VVCTIH-------QPSIDIFEAFDELFLLKRG 1053
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLQKLARRAGItlVVATHHydviddlQPDLLIFVGYGGVPEEKRR 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
167-418 |
7.75e-11 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 63.90 E-value: 7.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 167 FTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkLDQelKQTGRVTYNGHGMNEFVPQ-RTAAYIGQNDVHIGEMTV 245
Cdd:cd03296 15 FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG-LER--PDSGTILFGGEDATDVPVQeRNVGFVFQHYALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 246 RETFAYAARFQGVgsrydmltelARREKEANIKPdpdidifmKAMStagektnvmtdyILKILGLEVCADTMVGDdmlrg 325
Cdd:cd03296 92 FDNVAFGLRVKPR----------SERPPEAEIRA--------KVHE------------LLKLVQLDWLADRYPAQ----- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 326 ISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSsttyQIVNSLRNY---VHIFNGTALISLLQPAPETFNLFDDIILIAE 402
Cdd:cd03296 137 LSGGQRQRVALARALAVEPKVLLLDEPFGALDA----KVRKELRRWlrrLHDELHVTTVFVTHDQEEALEVADRVVVMNK 212
|
250 260
....*....|....*....|....
gi 257669152 403 GEI--------IYEGPRDHVVEFF 418
Cdd:cd03296 213 GRIeqvgtpdeVYDHPASPFVYSF 236
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
851-1041 |
9.86e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 66.37 E-value: 9.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGrktggyI----DGNITisgYPKNQQTF-----ARIsgyceqtdih 921
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG------LwpygSGRIA---RPAGARVLflpqrPYL---------- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 922 sPHVTVYESLVYsawlrlPKEVDKNKRKIfIEEVMELVELTPLRQAL-VGLPGESGLSTEQRKRLTIAVELVANPSIIFM 1000
Cdd:COG4178 438 -PLGTLREALLY------PATAEAFSDAE-LREALEAVGLGHLAERLdEEADWDQVLSLGEQQRLAFARLLLHKPDWLFL 509
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 257669152 1001 DEPTSGLDARAAAIVMRTVRNTV-DTgrTVVCTIHQPSIDIF 1041
Cdd:COG4178 510 DEATSALDEENEAALYQLLREELpGT--TVISVGHRSTLAAF 549
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
168-409 |
1.18e-10 |
|
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: 62.07 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkldqELK-QTGRVTYNGHGMNEFVPQrtaayigqndvhigemtvr 246
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAG----LLKpSSGEILLDGKDLASLSPK------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 247 etfayaarfqgvgsrydmltELARRekeanikpdpdidifMKAMSTAgektnvmtdyiLKILGLEVCADTMVGDdmlrgI 326
Cdd:cd03214 70 --------------------ELARK---------------IAYVPQA-----------LELLGLAHLADRPFNE-----L 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 327 SGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIFNGTALISLLQPapetfNL----FDDIILIAE 402
Cdd:cd03214 99 SGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDL-----NLaaryADRVILLKD 173
|
....*..
gi 257669152 403 GEIIYEG 409
Cdd:cd03214 174 GRIVAQG 180
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
164-409 |
1.35e-10 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 62.62 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 164 KKKF---TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkLDQelKQTGRVTYNGHGM--NEFVPQRTAAYIgqnDV 238
Cdd:cd03268 7 TKTYgkkRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILG-LIK--PDSGEITFDGKSYqkNIEALRRIGALI---EA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 239 HI--GEMTVRETFAYAARFQGVgsrydmltelarREKEAnikpdpdidifmkamstagektnvmtDYILKILGLEVcadt 316
Cdd:cd03268 81 PGfyPNLTARENLRLLARLLGI------------RKKRI--------------------------DEVLDVVGLKD---- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 317 mVGDDMLRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHiFNGTALIS--LLQpapETFNLF 394
Cdd:cd03268 119 -SAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISshLLS---EIQKVA 193
|
250
....*....|....*
gi 257669152 395 DDIILIAEGEIIYEG 409
Cdd:cd03268 194 DRIGIINKGKLIEEG 208
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
168-409 |
3.10e-10 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 61.40 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDqelKQTGRVTYNGHGMNE------FVPQRTAAyigQNDVHIg 241
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK---PTSGSIRVFGKPLEKerkrigYVPQRRSI---DRDFPI- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 242 emTVRETFAyaarfQGVGSRYDMLTELARREKEAnikpdpdidifmkamstagektnvmTDYILKILGLEVCADtmvgdd 321
Cdd:cd03235 86 --SVRDVVL-----MGLYGHKGLFRRLSKADKAK-------------------------VDEALERVGLSELAD------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 322 mlRGI---SGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTT---YQIVNSLRNYvhifNGTALISL--LQPAPEtfnL 393
Cdd:cd03235 128 --RQIgelSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQediYELLRELRRE----GMTILVVThdLGLVLE---Y 198
|
250
....*....|....*.
gi 257669152 394 FDDIILIAeGEIIYEG 409
Cdd:cd03235 199 FDRVLLLN-RTVVASG 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
161-404 |
3.76e-10 |
|
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: 60.95 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 161 PNRKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDqelKQTGRVTYNGHgmNEFVPQrtAAYIgQNDvhi 240
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE---KLSGSVSVPGS--IAYVSQ--EPWI-QNG--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 241 gemTVRE--TFayaarfqgvGSRYDMltelaRREKEAnIKP---DPDIDIFMKamstagektnvmtdyilkilGLEvcad 315
Cdd:cd03250 81 ---TIREniLF---------GKPFDE-----ERYEKV-IKAcalEPDLEILPD--------------------GDL---- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 316 TMVGDdmlRGI--SGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNS-----LRNYVHIFNGTALISLLQPAp 388
Cdd:cd03250 119 TEIGE---KGInlSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENcilglLLNNKTRILVTHQLQLLPHA- 194
|
250
....*....|....*.
gi 257669152 389 etfnlfDDIILIAEGE 404
Cdd:cd03250 195 ------DQIVVLDNGR 204
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
839-1036 |
3.77e-10 |
|
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: 60.97 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 839 EMIEQGTQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyidgNITISGYPKNQQ--TFARISGY 914
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGlsPPLAG----RVLLNGGPLDFQrdSIARGLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 915 CEQTDIHSPHVTVYESLvysAWLRLPKEVDKnkrkifIEEVMELVELTPLRQALVGlpgesGLSTEQRKRLTIAVELVAN 994
Cdd:cd03231 78 LGHAPGIKTTLSVLENL---RFWHADHSDEQ------VEEALARVGLNGFEDRPVA-----QLSAGQQRRVALARLLLSG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 257669152 995 PSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQP 1036
Cdd:cd03231 144 RPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
853-1053 |
3.95e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 62.02 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIDGNITISGYPKNQQTFARisGYCEQTDIHSPHVTVYESLV 932
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVP--YQHGSITLDGKPVEGPGAER--GVVFQNEGLLPWRNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 933 YSAWLRlpkEVDKNKRKIFIEEVMelveltplrqALVGLPGESG-----LSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1007
Cdd:PRK11248 93 FGLQLA---GVEKMQRLEIAHQML----------KKVGLEGAEKryiwqLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 257669152 1008 DA--RAAaivMRTVRNTV--DTGRTVVCTIHqpsiDIFEAF---DELFLLKRG 1053
Cdd:PRK11248 160 DAftREQ---MQTLLLKLwqETGKQVLLITH----DIEEAVfmaTELVLLSPG 205
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
169-415 |
3.97e-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: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 169 ILNDVSGIVKPGRMALLLGPPSSGKTTLllalaGKLDQEL--KQTGRVTYNGHGMNEFVPqrtaayigqndvhigemtvr 246
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTL-----TKLIQRFyvPENGRVLVDGHDLALADP-------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 247 etfAYAARFQGVGSRYDMLTELARREKEANIKPDPDIDIFMKAMSTAGEKtnvmtDYILKilgLEVCADTMVGDDMLrGI 326
Cdd:cd03252 72 ---AWLRRQVGVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAH-----DFISE---LPEGYDTIVGEQGA-GL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 327 SGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIvnsLRNYVHIFNGTALIsLLQPAPETFNLFDDIILIAEGEII 406
Cdd:cd03252 140 SGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAI---MRNMHDICAGRTVI-IIAHRLSTVKNADRIIVMEKGRIV 215
|
....*....
gi 257669152 407 YEGPRDHVV 415
Cdd:cd03252 216 EQGSHDELL 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
170-435 |
4.20e-10 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 61.58 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 170 LNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQElkqTGRVTYNGHGMNEFVPQ-RTAAYIGQNDVHIGEMTVRET 248
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD---SGKILLNGKDITNLPPEkRDISYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 249 FAYAARFQGVgsrydMLTELARREKEanikpdpdidifmkamstagektnvmtdyILKILGLEVCADTMVgddmlRGISG 328
Cdd:cd03299 92 IAYGLKKRKV-----DKKEIERKVLE-----------------------------IAEMLGIDHLLNRKP-----ETLSG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 329 GQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNyVHIFNGTALISLLQPAPETFNLFDDIILIAEGEIIYE 408
Cdd:cd03299 133 GEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK-IRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV 211
|
250 260
....*....|....*....|....*..
gi 257669152 409 GPRDHVveffetmgFKCPPRKGVADFL 435
Cdd:cd03299 212 GKPEEV--------FKKPKNEFVAEFL 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
165-405 |
4.50e-10 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 60.10 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 165 KKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkldqELKQT-GRVTYNGHGMN---EFVPQRTaAYIGQNDVHI 240
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILG----LLKPDsGEIKVLGKDIKkepEEVKRRI-GYLPEEPSLY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 241 GEMTVRETFAYaarfqgvgsrydmltelarrekeanikpdpdidifmkamstagektnvmtdyilkilglevcadtmvgd 320
Cdd:cd03230 86 ENLTVRENLKL--------------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 321 dmlrgiSGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIfNGTALIS--LLQPAPEtfnLFDDII 398
Cdd:cd03230 97 ------SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSshILEEAER---LCDRVA 166
|
....*..
gi 257669152 399 LIAEGEI 405
Cdd:cd03230 167 ILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
163-404 |
4.52e-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: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 163 RKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDqelKQTGRVTYNGHGMNEFVPQRtaayigqndvhige 242
Cdd:cd00267 8 RYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK---PTSGEILIDGKDIAKLPLEE-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 243 mtVRETFAYaaRFQgvgsrydmltelarrekeanikpdpdidifmkamstagektnvmtdyilkilglevcadtmvgddm 322
Cdd:cd00267 71 --LRRRIGY--VPQ------------------------------------------------------------------ 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 323 lrgISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHifNGTALISLLQPAPETFNLFDDIILIAE 402
Cdd:cd00267 81 ---LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAE--EGRTVIIVTHDPELAELAADRVIVLKD 155
|
..
gi 257669152 403 GE 404
Cdd:cd00267 156 GK 157
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
170-409 |
4.57e-10 |
|
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: 61.07 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 170 LNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDqelKQTGRVTYNGHGMNEFVPQ---RTAAYIGQnDVHIGEMTVR 246
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYK---PTSGSVLLDGTDIRQLDPAdlrRNIGYVPQ-DVTLFYGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 247 ETFAYAArfqgvgsrydmltelarrekeanikPDPDIDIFMKAMSTAGektnvMTDYILKI-LGLevcaDTMVGDDMlRG 325
Cdd:cd03245 96 DNITLGA-------------------------PLADDERILRAAELAG-----VTDFVNKHpNGL----DLQIGERG-RG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 326 ISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVhifNGTALI------SLLQpapetfnLFDDIIL 399
Cdd:cd03245 141 LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL---GDKTLIiithrpSLLD-------LVDRIIV 210
|
250
....*....|
gi 257669152 400 IAEGEIIYEG 409
Cdd:cd03245 211 MDSGRIVADG 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
161-409 |
5.29e-10 |
|
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: 60.98 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 161 PNRKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkldQELKQTGRVTYNGHGMNEFVPQ------RTAAYIG 234
Cdd:cd03257 12 PTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILG---LLKPTSGSIIFDGKDLLKLSRRlrkirrKEIQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 235 Q------NDVhigeMTVRETFAYAARFQGVGSRYDMLtELARREKEANIKPDPDidifmkamstagektnVMTDYIlkil 308
Cdd:cd03257 89 QdpmsslNPR----MTIGEQIAEPLRIHGKLSKKEAR-KEAVLLLLVGVGLPEE----------------VLNRYP---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 309 glevcadtmvgddmlRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIFNGTAL-----ISL 383
Cdd:cd03257 144 ---------------HELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLfithdLGV 208
|
250 260
....*....|....*....|....*.
gi 257669152 384 LQpapetfNLFDDIILIAEGEIIYEG 409
Cdd:cd03257 209 VA------KIADRVAVMYAGKIVEEG 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
852-1058 |
6.16e-10 |
|
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: 60.23 E-value: 6.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIDGNITISGypknqqtfarisgyceqTDIhsPHVTVYESL 931
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKG-----------------EDI--TDLPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 932 ---VYSAWLRlPKEVDKNKRKIFIEEVMElveltplrqalvglpgesGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1008
Cdd:cd03217 76 rlgIFLAFQY-PPEIPGVKNADFLRYVNE------------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 257669152 1009 ARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELFLL------KRGGEEIY 1058
Cdd:cd03217 137 IDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLydgrivKSGDKELA 192
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
852-1054 |
7.10e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 62.94 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiDGNITISGYPKNQQTFA----RISGYCEQTDI------- 920
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT--AGTVLVAGDDVEALSARaasrRVASVPQDTSLsfefdvr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 921 ------HSPHVTvyeslvysawlRLPKEVDKNKRKIfiEEVMELVELTplrqALVGLPGESgLSTEQRKRLTIAVELVAN 994
Cdd:PRK09536 96 qvvemgRTPHRS-----------RFDTWTETDRAAV--ERAMERTGVA----QFADRPVTS-LSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257669152 995 PSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpSIDIFEAF-DELFLLKRGG 1054
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIH--DLDLAARYcDELVLLADGR 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
163-409 |
8.51e-10 |
|
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: 60.28 E-value: 8.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 163 RKKKftILNDVSGIVKPGrMALLLGPPSSGKTTLLLALAGKLDQElkqTGRVTYNGH----GMNEFvpQRTAAYIGQNDV 238
Cdd:cd03264 11 GKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPS---SGTIRIDGQdvlkQPQKL--RRRIGYLPQEFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 239 HIGEMTVRETFAYAARFQGVGSRydmltelaRREKEAnikpdpdidifmkamstagektnvmtDYILKILGLEVCADTMV 318
Cdd:cd03264 83 VYPNFTVREFLDYIAWLKGIPSK--------EVKARV--------------------------DEVLELVNLGDRAKKKI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 319 GddmlrGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLR----NYVHIFNgTALISLLQpapetfNLF 394
Cdd:cd03264 129 G-----SLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSelgeDRIVILS-THIVEDVE------SLC 196
|
250
....*....|....*
gi 257669152 395 DDIILIAEGEIIYEG 409
Cdd:cd03264 197 NQVAVLNKGKLVFEG 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
847-1038 |
9.09e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.20 E-value: 9.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 847 EDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLagrktgGYID----GNITISGY---PKNQQTFARIS----GYC 915
Cdd:PRK10535 18 EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL------GCLDkptsGTYRVAGQdvaTLDADALAQLRrehfGFI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 916 EQTDIHSPHVTVYESL----VYSAwlrlpkeVDKNKRKifiEEVMELVELTPLRQALVGLPGEsgLSTEQRKRLTIAVEL 991
Cdd:PRK10535 92 FQRYHLLSHLTAAQNVevpaVYAG-------LERKQRL---LRAQELLQRLGLEDRVEYQPSQ--LSGGQQQRVSIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 257669152 992 VANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1038
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQV 206
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
852-1027 |
1.15e-09 |
|
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: 62.51 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGA---FRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG---------YIDgnITISGyPKNQQTFARISGYCEQ 917
Cdd:TIGR03269 296 VVKAVDNVsleVKEGEIFGIVGTSGAGKTTLSKIIAGvlEPTSGevnvrvgdeWVD--MTKPG-PDGRGRAKRYIGILHQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 918 TDIHSPHVTVYESLVYSAWLRLPKEVdkNKRKIFIEEVMELVELTPLRQALVGLPGEsgLSTEQRKRLTIAVELVANPSI 997
Cdd:TIGR03269 373 EYDLYPHRTVLDNLTEAIGLELPDEL--ARMKAVITLKMVGFDEEKAEEILDKYPDE--LSEGERHRVALAQVLIKEPRI 448
|
170 180 190
....*....|....*....|....*....|
gi 257669152 998 IFMDEPTSGLDaraaAIVMRTVRNTVDTGR 1027
Cdd:TIGR03269 449 VILDEPTGTMD----PITKVDVTHSILKAR 474
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
853-1007 |
1.30e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.49 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiDGNITISG--YPKNQQTFARISG----YCEQTDIHspHVT 926
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT--KGTITINNinYNKLDHKLAAQLGigiiYQELSVID--ELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 927 VYESLVYSawlRLPKE-------VDKNKRKIFIEEVMELVELTPLRQALVGlpgesGLSTEQRKRLTIAVELVANPSIIF 999
Cdd:PRK09700 97 VLENLYIG---RHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVA-----NLSISHKQMLEIAKTLMLDAKVII 168
|
....*...
gi 257669152 1000 MDEPTSGL 1007
Cdd:PRK09700 169 MDEPTSSL 176
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
853-1034 |
1.42e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.26 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyidgNITISGY-P-KNQQTFAR-IS---GYCEQTdihSPH 924
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGilVPTSG----EVRVLGYvPfKRRKEFARrIGvvfGQRSQL---WWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 925 VTVYESL-----VYsawlRLPKEVDKNKRKIFIEeVMELVEL--TPLRQalvglpgesgLSTEQRKRLTIAVELVANPSI 997
Cdd:COG4586 111 LPAIDSFrllkaIY----RIPDAEYKKRLDELVE-LLDLGELldTPVRQ----------LSLGQRMRCELAAALLHRPKI 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 257669152 998 IFMDEPTSGLDaraaAIVMRTVRNTV-----DTGRTVVCTIH 1034
Cdd:COG4586 176 LFLDEPTIGLD----VVSKEAIREFLkeynrERGTTILLTSH 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
156-405 |
1.50e-09 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 59.58 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 156 TLHLVPNRKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkldQELKQTGRVTYNGHGMNEFVP-QRTAAYIG 234
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAG---LEEPTSGRIYIGGRDVTDLPPkDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 235 QNDVHIGEMTVRETFAYAARFQGVGSRydmltELARREKEAnikpdpdidifmkamstagektnvmtdyiLKILGLEVCA 314
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKD-----EIDERVREV-----------------------------AELLQIEHLL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 315 DTMVgddmlRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNyVHIFNGTALISLLQPAPETFNLF 394
Cdd:cd03301 125 DRKP-----KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKR-LQQRLGTTTIYVTHDQVEAMTMA 198
|
250
....*....|.
gi 257669152 395 DDIILIAEGEI 405
Cdd:cd03301 199 DRIAVMNDGQI 209
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
845-1053 |
1.64e-09 |
|
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: 59.79 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 845 TQEDRLVLlKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyidgNITISGYPknqqtfarISGYcEQTDIHS 922
Cdd:cd03248 23 TRPDTLVL-QDVSFTLHPGEVTALVGPSGSGKSTVVALLENfyQPQGG----QVLLDGKP--------ISQY-EHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 923 PHVTV-YESLVYSAWLRlpKEVDKNKRKIFIEEVMELVELTPLRQALVGLP-------GESG--LSTEQRKRLTIAVELV 992
Cdd:cd03248 89 KVSLVgQEPVLFARSLQ--DNIAYGLQSCSFECVKEAAQKAHAHSFISELAsgydtevGEKGsqLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257669152 993 ANPSIIFMDEPTSGLDARAAAIVMRTVRNTvDTGRTVVCTIHQpsIDIFEAFDELFLLKRG 1053
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDW-PERRTVLVIAHR--LSTVERADQILVLDGG 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
168-381 |
2.02e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.00 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPG-RMALLlGPPSSGKTTLLLALAGKLDQElkqTGRVTYNghgmnefvPQRTAAYIGQNDVHIGEMTVR 246
Cdd:COG0488 12 PLLDDVSLSINPGdRIGLV-GRNGAGKSTLLKILAGELEPD---SGEVSIP--------KGLRIGYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 247 ETFayaarFQGVGSRYDMLTELARREKEAnikPDPDIDifMKAMSTAGEKTNVMTDY--------ILKILGLEVC-ADTM 317
Cdd:COG0488 80 DTV-----LDGDAELRALEAELEELEAKL---AEPDED--LERLAELQEEFEALGGWeaearaeeILSGLGFPEEdLDRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257669152 318 VGDdmlrgISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTtyqiVNSLRNYVHIFNGTALI 381
Cdd:COG0488 150 VSE-----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEFLKNYPGTVLV 204
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
162-372 |
2.35e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 60.87 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 162 NRKKKF---TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkLDQElkQTGRVTYNGHGMNEF-VPQRTAAYIGQND 237
Cdd:PRK10851 7 NIKKSFgrtQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG-LEHQ--TSGHIRFHGTDVSRLhARDRKVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 238 VHIGEMTVRETFAYAarfqgvgsrydmLTELARREKeanikpdPDIDIFmkamstageKTNVMTdyILKILGLEVCADTM 317
Cdd:PRK10851 84 ALFRHMTVFDNIAFG------------LTVLPRRER-------PNAAAI---------KAKVTQ--LLEMVQLAHLADRY 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 257669152 318 VGDdmlrgISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSsttyQIVNSLRNYV 372
Cdd:PRK10851 134 PAQ-----LSGGQKQRVALARALAVEPQILLLDEPFGALDA----QVRKELRRWL 179
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
852-1061 |
2.37e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.86 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGAFRPGVLTALMGVSGAGKTTLM---DVLAGRKTGGYIDGNITISG---YPKNQQTFA--RISGYCEQTDIHSP 923
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfNRLLELNEEARVEGEVRLFGrniYSPDVDPIEvrREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 924 HVTVYES----LVYSAWLRLPKEVDKN-----KRKIFIEEVMELVELTPlrqalvglpgeSGLSTEQRKRLTIAVELVAN 994
Cdd:PRK14267 99 HLTIYDNvaigVKLNGLVKSKKELDERvewalKKAALWDEVKDRLNDYP-----------SNLSGGQRQRLVIARALAMK 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257669152 995 PSIIFMDEPTSGLDARAAAIVMRTVRNtVDTGRTVVCTIHQPS----IDIFEAFdeLFLlkrgGEEIYVGP 1061
Cdd:PRK14267 168 PKILLMDEPTANIDPVGTAKIEELLFE-LKKEYTIVLVTHSPAqaarVSDYVAF--LYL----GKLIEVGP 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
170-369 |
2.45e-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: 61.53 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 170 LNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQElkqTGRVTYNGHGMNEFVP---QRTAAYIGQNDvHIGEMTVR 246
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT---EGSIAVNGVPLADADAdswRDQIAWVPQHP-FLFAGTIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 247 ETFAYAARfqgvGSRYDMLTELARRekeanikpdPDIDIFMKAmstagektnvmtdyilkilgLEVCADTMVGDDMlRGI 326
Cdd:TIGR02857 414 ENIRLARP----DASDAEIREALER---------AGLDEFVAA--------------------LPQGLDTPIGEGG-AGL 459
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 257669152 327 SGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLR 369
Cdd:TIGR02857 460 SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALR 502
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
824-1053 |
2.66e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 60.23 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 824 SITFDNV--VYSVDMPQEmiEQGtqedrlvlLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiDGNITISGY 901
Cdd:PRK13641 2 SIKFENVdyIYSPGTPME--KKG--------LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPS--SGTITIAGY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 902 PKNQQTFARisgyceqtdihsphvtvyeslvysAWLRLPKEVDK----NKRKIFIEEVMELVELTPLR----------QA 967
Cdd:PRK13641 70 HITPETGNK------------------------NLKKLRKKVSLvfqfPEAQLFENTVLKDVEFGPKNfgfsedeakeKA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 968 L-----VGLPGESG------LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQP 1036
Cdd:PRK13641 126 LkwlkkVGLSEDLIskspfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNM 205
|
250
....*....|....*..
gi 257669152 1037 SiDIFEAFDELFLLKRG 1053
Cdd:PRK13641 206 D-DVAEYADDVLVLEHG 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
851-1035 |
2.69e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 59.34 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLM---DVLAGRKTGGYIDGNITISGYPKNQQTFARISGYCEQTDIHSPHVTV 927
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVFQQFYLFPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 928 YESLVYSawlrlPKEVDKNKRKIFIEEVMELVELTPLRQALVGLPGEsgLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1007
Cdd:PRK09493 95 LENVMFG-----PLRVRGASKEEAEKQARELLAKVGLAERAHHYPSE--LSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180
....*....|....*....|....*...
gi 257669152 1008 DARAAAIVMRTVRNTVDTGRTVVCTIHQ 1035
Cdd:PRK09493 168 DPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
824-1053 |
2.99e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 59.79 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 824 SITFDNVVYsvdmpqeMIEQGTQEDRlVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYID-GNITISG 900
Cdd:PRK13646 2 TIRFDNVSY-------TYQKGTPYEH-QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAllKPTTGTVTvDDITITH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 901 YPKNQ--QTFARISGYCEQTdihsPHVTVYESLVYSAWLRLPKEVDKNkrkifIEEVME-----LVELTPLRQALVGLPG 973
Cdd:PRK13646 74 KTKDKyiRPVRKRIGMVFQF----PESQLFEDTVEREIIFGPKNFKMN-----LDEVKNyahrlLMDLGFSRDVMSQSPF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 974 EsgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSiDIFEAFDELFLLKR 1052
Cdd:PRK13646 145 Q--MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlQTDENKTIILVSHDMN-EVARYADEVIVMKE 221
|
.
gi 257669152 1053 G 1053
Cdd:PRK13646 222 G 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
167-410 |
3.65e-09 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 58.78 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 167 FTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDqelKQTGRVTYNGHGMNEF-----------VPQRTAAYigq 235
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYD---VSSGSILIDGQDIREVtldslrraigvVPQDTVLF--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 236 NDvhigemTVRETFAYAarfqgvgsrydmltelarrekeaniKPDP-DIDIFmkamsTAGEKTNVMTdyilKILGLEVCA 314
Cdd:cd03253 88 ND------TIGYNIRYG-------------------------RPDAtDEEVI-----EAAKAAQIHD----KIMRFPDGY 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 315 DTMVGDdmlRG--ISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNyvhIFNGTALISLLQPAPETFN 392
Cdd:cd03253 128 DTIVGE---RGlkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRD---VSKGRTTIVIAHRLSTIVN 201
|
250
....*....|....*...
gi 257669152 393 LfDDIILIAEGEIIYEGP 410
Cdd:cd03253 202 A-DKIIVLKDGRIVERGT 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
837-1010 |
5.20e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 59.96 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 837 PQEMIEQGTQEDRLVLLKGVNGAF-------------RPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiDGNITISGypk 903
Cdd:PRK09452 1 SKKLNKQPSSLSPLVELRGISKSFdgkevisnldltiNNGEFLTLLGPSGCGKTTVLRLIAGFETPD--SGRIMLDG--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 904 nqQTFARISGycEQTDIHS--------PHVTVYESLVYSawLRLPKeVDKNKRKIFIEEVMELVELTPLRQALVglpgeS 975
Cdd:PRK09452 76 --QDITHVPA--ENRHVNTvfqsyalfPHMTVFENVAFG--LRMQK-TPAAEITPRVMEALRMVQLEEFAQRKP-----H 143
|
170 180 190
....*....|....*....|....*....|....*
gi 257669152 976 GLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1010
Cdd:PRK09452 144 QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
161-351 |
5.41e-09 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 57.87 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 161 PNRKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkLDQElkQTGRVTYNGHGMNEfvPQRTAAYIGQNDVHI 240
Cdd:cd03293 11 GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAG-LERP--TSGEVLVDGEPVTG--PGPDRGYVFQQDALL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 241 GEMTVRETFAYAARFQGVgsrydmltelARREKEAnikpdpdidifmKAMStagektnvmtdyILKILGLEVCADTMVGD 320
Cdd:cd03293 86 PWLTVLDNVALGLELQGV----------PKAEARE------------RAEE------------LLELVGLSGFENAYPHQ 131
|
170 180 190
....*....|....*....|....*....|....*
gi 257669152 321 dmlrgISGGQKKRV----TtgeMLVGPsRALFMDE 351
Cdd:cd03293 132 -----LSGGMRQRValarA---LAVDP-DVLLLDE 157
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
853-1017 |
5.44e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 59.86 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGNITISGYPKNQ------QTFARisgYceqtdihs 922
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGleRITSGeiWIGGRVVNELEPADRdiamvfQNYAL---Y-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 923 PHVTVYESLVYSAWLR-LPKEvDKNKRkifIEEVMELVELTPL-----RQalvglpgesgLSTEQRKRLTIAVELVANPS 996
Cdd:PRK11650 89 PHMSVRENMAYGLKIRgMPKA-EIEER---VAEAARILELEPLldrkpRE----------LSGGQRQRVAMGRAIVREPA 154
|
170 180
....*....|....*....|...
gi 257669152 997 IIFMDEPTSGLDA--RAAaivMR 1017
Cdd:PRK11650 155 VFLFDEPLSNLDAklRVQ---MR 174
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
845-1009 |
5.91e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 59.73 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 845 TQEDRLVLLKGVNGAF-------------RPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDG-NITISGypknqq 906
Cdd:PRK11432 1 MTQKNFVVLKNITKRFgsntvidnlnltiKQGTMVTLLGPSGCGKTTVLRLVAGleKPTEGqiFIDGeDVTHRS------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 907 tfarisgyCEQTDI----HS----PHVTVYESLVYSawLRLPKeVDKNKRKIFIEEVMELVELTPLRQALVglpgeSGLS 978
Cdd:PRK11432 75 --------IQQRDIcmvfQSyalfPHMSLGENVGYG--LKMLG-VPKEERKQRVKEALELVDLAGFEDRYV-----DQIS 138
|
170 180 190
....*....|....*....|....*....|.
gi 257669152 979 TEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1009
Cdd:PRK11432 139 GGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
167-410 |
6.30e-09 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 58.02 E-value: 6.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 167 FTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAG--KLDQelkqtGRVTYNGHGMNEFVP-QRTAAYIGQNDVHIGEM 243
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGfeTPTS-----GEILLDGKDITNLPPhKRPVNTVFQNYALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 244 TVRETFAYAARFQGVGSrydmlTELARREKEAnikpdpdidifmkamstagektnvmtdyiLKILGLEVCADTMVGDdml 323
Cdd:cd03300 88 TVFENIAFGLRLKKLPK-----AEIKERVAEA-----------------------------LDLVQLEGYANRKPSQ--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 324 rgISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNyVHIFNGTALISLLQPAPETFNLFDDIILIAEG 403
Cdd:cd03300 131 --LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKR-LQKELGITFVFVTHDQEEALTMSDRIAVMNKG 207
|
250
....*....|....*
gi 257669152 404 EI--------IYEGP 410
Cdd:cd03300 208 KIqqigtpeeIYEEP 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
162-410 |
7.38e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 59.35 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 162 NRKKKF---TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkldQELKQTGRVTYNGhgmnEFVPQRTaayIGQNDV 238
Cdd:PRK11432 11 NITKRFgsnTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAG---LEKPTEGQIFIDG----EDVTHRS---IQQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 239 HI--------GEMTVRETFAYAARFQGVGSrydmlTELARREKEAnikpdpdidifmkamstagektnvmtdyiLKILGL 310
Cdd:PRK11432 81 CMvfqsyalfPHMSLGENVGYGLKMLGVPK-----EERKQRVKEA-----------------------------LELVDL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 311 EVCADTMVGDdmlrgISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIFNGTALIsLLQPAPET 390
Cdd:PRK11432 127 AGFEDRYVDQ-----ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLY-VTHDQSEA 200
|
250 260
....*....|....*....|
gi 257669152 391 FNLFDDIILIAEGEIIYEGP 410
Cdd:PRK11432 201 FAVSDTVIVMNKGKIMQIGS 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
825-1053 |
7.46e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 60.51 E-value: 7.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 825 ITFDNVVYSvdMPqemieqgTQEDRLVLlKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyidgNITISGYP 902
Cdd:TIGR00958 479 IEFQDVSFS--YP-------NRPDVPVL-KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNlyQPTGG----QVLLDGVP 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 903 knqqtfarisgyCEQTDIHSPHVTV----YESLVYSAWLRlpKEVDKNKRKIFIEEVMELVELTPLRQALVGLP------ 972
Cdd:TIGR00958 545 ------------LVQYDHHYLHRQValvgQEPVLFSGSVR--ENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPngydte 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 973 -GESG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARaaaiVMRTVRNTVDT-GRTVVCTIHQPSidIFEAFDELF 1048
Cdd:TIGR00958 611 vGEKGsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAE----CEQLLQESRSRaSRTVLLIAHRLS--TVERADQIL 684
|
....*
gi 257669152 1049 LLKRG 1053
Cdd:TIGR00958 685 VLKKG 689
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
853-1030 |
1.02e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.66 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGnitisgypknqqtfarisgycEQTDIHSPHV--- 925
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGlyQPDSGeiLIDG---------------------KPVRIRSPRDaia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 926 ----------------TVYESLVYSawLRLPKEVDKNKRKIfIEEVMELVELTPLR---QALVG-LP-GEsglstEQRkr 984
Cdd:COG3845 80 lgigmvhqhfmlvpnlTVAENIVLG--LEPTKGGRLDRKAA-RARIRELSERYGLDvdpDAKVEdLSvGE-----QQR-- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 257669152 985 ltiaVE----LVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVV 1030
Cdd:COG3845 150 ----VEilkaLYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSII 195
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
154-370 |
1.02e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.86 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 154 LNTLHLVPNRKKKftiLNDVSGIVKPGRMALLLGPPSSGKTTLLLAL--AGKLDQELKQTGRVTYNGHgmNEFVPQRTAA 231
Cdd:PRK14239 8 VSDLSVYYNKKKA---LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGH--NIYSPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 232 YIGQndvHIG---------EMTVRETFAYAARFQGVgsrydmltelarREKEaniKPDPDIDIFMKAMSTAGEKTNVMTD 302
Cdd:PRK14239 83 DLRK---EIGmvfqqpnpfPMSIYENVVYGLRLKGI------------KDKQ---VLDEAVEKSLKGASIWDEVKDRLHD 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257669152 303 YILkilglevcadtmvgddmlrGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRN 370
Cdd:PRK14239 145 SAL-------------------GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLG 193
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
846-1053 |
1.07e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 58.71 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 846 QEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYidGNITISG-YPKNQQTFARISGYCEQTDIHS-- 922
Cdd:PRK13631 35 QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKY--GTIQVGDiYIGDKKNNHELITNPYSKKIKNfk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 923 ------------PHVTVYESLVYS------AWLRLPKEVDKNKRKIFIEEvMEL----VELTPLrqalvglpgesGLSTE 980
Cdd:PRK13631 113 elrrrvsmvfqfPEYQLFKDTIEKdimfgpVALGVKKSEAKKLAKFYLNK-MGLddsyLERSPF-----------GLSGG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257669152 981 QRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELFLLKRG 1053
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME-HVLEVADEVIVMDKG 252
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
849-1008 |
1.41e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 56.96 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 849 RLVLlKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDG-NITisGYPKNQQtfAR--IsGYCEQTdih 921
Cdd:COG1137 16 RTVV-KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGlvKPDSGriFLDGeDIT--HLPMHKR--ARlgI-GYLPQE--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 922 sPHV----TVYESLvySAWLRLpKEVDKNKRKIFIEEVMELVELTPLRQAlvglPGESgLSTEQRKRLTIAVELVANPSI 997
Cdd:COG1137 87 -ASIfrklTVEDNI--LAVLEL-RKLSKKEREERLEELLEEFGITHLRKS----KAYS-LSGGERRRVEIARALATNPKF 157
|
170
....*....|.
gi 257669152 998 IFMDEPTSGLD 1008
Cdd:COG1137 158 ILLDEPFAGVD 168
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
853-1034 |
1.44e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 57.82 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiDGNITISG---YPKNQQTFARISGYCEQT-DIHSPHVTVY 928
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQ--RGRVKVMGrevNAENEKWVRSKVGLVFQDpDDQVFSSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 929 ESLVYSAW-LRL-PKEVDKNkrkifIEEVMELVELTPLRQAlvglpGESGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1006
Cdd:PRK13647 99 DDVAFGPVnMGLdKDEVERR-----VEEALKAVRMWDFRDK-----PPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAY 168
|
170 180
....*....|....*....|....*...
gi 257669152 1007 LDARAAAIVMRTVRNTVDTGRTVVCTIH 1034
Cdd:PRK13647 169 LDPRGQETLMEILDRLHNQGKTVIVATH 196
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
854-1017 |
1.51e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.50 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 854 KGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRK--TGG--YIdGNITISGYPKNQqtfaRISGYCEQTDIHSPHVTVYE 929
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEdiTSGdlFI-GEKRMNDVPPAE----RGVGMVFQSYALYPHLSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 930 SLvySAWLRLPKeVDKNKRKIFIEEVMELVELTPL--RQalvglPGEsgLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1007
Cdd:PRK11000 95 NM--SFGLKLAG-AKKEEINQRVNQVAEVLQLAHLldRK-----PKA--LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170
....*....|
gi 257669152 1008 DArAAAIVMR 1017
Cdd:PRK11000 165 DA-ALRVQMR 173
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
851-1053 |
1.75e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.09 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG----RktggyidGNITISGYPKNQ---QTFARISGYCEQtDIHSP 923
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyQ-------GSLKINGIELREldpESWRKHLSWVGQ-NPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 924 HVTVYESLvysawlrLPKEVDKNKrkifiEEVMELVELTPLRQALVGLP-------GE--SGLSTEQRKRLTIAVELVAN 994
Cdd:PRK11174 436 HGTLRDNV-------LLGNPDASD-----EQLQQALENAWVSEFLPLLPqgldtpiGDqaAGLSVGQAQRLALARALLQP 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 257669152 995 PSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQpsIDIFEAFDELFLLKRG 1053
Cdd:PRK11174 504 CQLLLLDEPTASLDAHSEQLVMQAL-NAASRRQTTLMVTHQ--LEDLAQWDQIWVMQDG 559
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
154-364 |
1.79e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 57.18 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 154 LNTLHLV-PNRKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQElkqTGRVTYNGH---GmnefvPQRT 229
Cdd:COG4525 6 VRHVSVRyPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS---SGEITLDGVpvtG-----PGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 230 AAYIGQNDVHIGEMTVRETFAYAARFQGVGsrydmlteLARREKEAnikpdpdidifmkamstagektnvmtDYILKILG 309
Cdd:COG4525 78 RGVVFQKDALLPWLNVLDNVAFGLRLRGVP--------KAERRARA--------------------------EELLALVG 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 257669152 310 LEVCADTMVGDdmlrgISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQI 364
Cdd:COG4525 124 LADFARRRIWQ-----LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQM 173
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
856-1035 |
1.90e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 59.26 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 856 VNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIDGNITISG--YPKNQQTFARISGYCEQTDIHSPHVTVYESLVY 933
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPP--TSGTVLVGGkdIETNLDAVRQSLGMCPQHNILFHHLTVAEHILF 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 934 SAWLrlpKEVDKNKRKIFIEEVMELVELTPLRQAlvglpGESGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA---R 1010
Cdd:TIGR01257 1027 YAQL---KGRSWEEAQLEMEAMLEDTGLHHKRNE-----EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPysrR 1098
|
170 180
....*....|....*....|....*
gi 257669152 1011 AAAIVMRTVRntvdTGRTVVCTIHQ 1035
Cdd:TIGR01257 1099 SIWDLLLKYR----SGRTIIMSTHH 1119
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
166-414 |
1.94e-08 |
|
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: 56.42 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 166 KFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAG--KLDQELKQTGRVTYNGH----------------GMnefVPQ 227
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlnDLIPGAPDEGEVLLDGKdiydldvdvlelrrrvGM---VFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 228 RTAAYigqndvhigEMTVRETFAYAARFQGVGSRydmlTELARREKEAnikpdpdidifmkamstagektnvmtdyiLKI 307
Cdd:cd03260 89 KPNPF---------PGSIYDNVAYGLRLHGIKLK----EELDERVEEA-----------------------------LRK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 308 LGL--EVCADTMVgddmlRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHifNGTALI---S 382
Cdd:cd03260 127 AALwdEVKDRLHA-----LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIvthN 199
|
250 260 270
....*....|....*....|....*....|..
gi 257669152 383 LLQPApetfNLFDDIILIAEGEIIYEGPRDHV 414
Cdd:cd03260 200 MQQAA----RVADRTAFLLNGRLVEFGPTEQI 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
166-351 |
2.16e-08 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 57.78 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 166 KFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkLDqelKQT-GRVTYNGHGMNEFVPQ-RTAAYIGQNDV---Hi 240
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG-LE---DPTsGEILIGGRDVTDLPPKdRNIAMVFQSYAlypH- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 241 geMTVRETFAYAARFQGVGSRydmltELARREKEAnikpdpdidifmkamstagektnvmtdyiLKILGLEvcadtmvgd 320
Cdd:COG3839 90 --MTVYENIAFPLKLRKVPKA-----EIDRRVREA-----------------------------AELLGLE--------- 124
|
170 180 190
....*....|....*....|....*....|....*
gi 257669152 321 DML----RGISGGQKKRVTTGEMLVGPSRALFMDE 351
Cdd:COG3839 125 DLLdrkpKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
867-1036 |
2.47e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.59 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 867 ALMGVSGAGKTTLMDVLaGRKTGGY-----IDGNITISG---YPKNQQTFARISGYCEQTDIHSPHVTVYESLVYSawlr 938
Cdd:PRK14246 40 GIMGPSGSGKSTLLKVL-NRLIEIYdskikVDGKVLYFGkdiFQIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYP---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 939 LPKEVDKNKRKI--FIEEVMELVELTPLRQALVGLPGeSGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVM 1016
Cdd:PRK14246 115 LKSHGIKEKREIkkIVEECLRKVGLWKEVYDRLNSPA-SQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIE 193
|
170 180
....*....|....*....|
gi 257669152 1017 RTVrNTVDTGRTVVCTIHQP 1036
Cdd:PRK14246 194 KLI-TELKNEIAIVIVSHNP 212
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
852-1038 |
2.69e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.34 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIDGNITISGY------PKNQ---------QTFARISGYCE 916
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKdllelsPEDRagegifmafQYPVEIPGVSN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 917 QTDIHSPHVTVYEslvysawLRLPKEVDKNKRKIFIEEVMELVELTPlrqALVGLPGESGLSTEQRKRLTIAVELVANPS 996
Cdd:PRK09580 96 QFFLQTALNAVRS-------YRGQEPLDRFDFQDLMEEKIALLKMPE---DLLTRSVNVGFSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 257669152 997 IIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1038
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRI 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
853-1008 |
2.94e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 57.40 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGnITISGYPKNQ------------QTF----ARis 912
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLleRPTSGsvLVDG-VDLTALSERElraarrkigmifQHFnllsSR-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 913 gyceqtdihsphvTVYESLVYSawLRLPKeVDKNKRKifiEEVMELVELtplrqalVGLPGESG-----LSTEQRKRLTI 987
Cdd:COG1135 98 -------------TVAENVALP--LEIAG-VPKAEIR---KRVAELLEL-------VGLSDKADaypsqLSGGQKQRVGI 151
|
170 180
....*....|....*....|.
gi 257669152 988 AVELVANPSIIFMDEPTSGLD 1008
Cdd:COG1135 152 ARALANNPKVLLCDEATSALD 172
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
169-370 |
3.65e-08 |
|
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: 55.12 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 169 ILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDqelKQTGRVTYNG-------HGMNEFvpQRTAAYIGQN-DVHI 240
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLR---PQSGAVLIDGepldysrKGLLER--RQRVGLVFQDpDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 241 GEMTVRETFAYAARFQGVGSrydmlTELARREKEANIKpdpdidifmkamstagektnvmtdyiLKILGLEvcadtmvgD 320
Cdd:TIGR01166 82 FAADVDQDVAFGPLNLGLSE-----AEVERRVREALTA--------------------------VGASGLR--------E 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 257669152 321 DMLRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRN 370
Cdd:TIGR01166 123 RPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAILRR 172
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
856-1053 |
3.89e-08 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 55.99 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 856 VNGAFRPGVLTALMGVSGAGKTTLMDVLAGR-----KTGGYID---GNITISGYPKNQQTF-ARIS-GYCEQTDIHSPHV 925
Cdd:TIGR02323 22 VSFDLYPGEVLGIVGESGSGKSTLLGCLAGRlapdhGTATYIMrsgAELELYQLSEAERRRlMRTEwGFVHQNPRDGLRM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 926 TVyeSLVYSAWLRLPKEVDKNKRKIFIEEV--MELVELTPLRqaLVGLPgeSGLSTEQRKRLTIAVELVANPSIIFMDEP 1003
Cdd:TIGR02323 102 RV--SAGANIGERLMAIGARHYGNIRATAQdwLEEVEIDPTR--IDDLP--RAFSGGMQQRLQIARNLVTRPRLVFMDEP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 257669152 1004 TSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHQPSIDIFEAfDELFLLKRG 1053
Cdd:TIGR02323 176 TGGLDVSVQARLLDLLRGLVrDLGLAVIIVTHDLGVARLLA-QRLLVMQQG 225
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
824-1034 |
3.95e-08 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 55.58 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 824 SITFDNVV--YSVDMPqemieqgtqedrLVLlKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAgR---KTGG--YIDGnI 896
Cdd:cd03244 2 DIEFKNVSlrYRPNLP------------PVL-KNISFSIKPGEKVGIVGRTGSGKSSLLLALF-RlveLSSGsiLIDG-V 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 897 TISGYPKNQ--QTFARISgyceQtdihsphvtvyESLVYSAWLRL---PKEV--DknkrkifiEEVMELVELTPLRQALV 969
Cdd:cd03244 67 DISKIGLHDlrSRISIIP----Q-----------DPVLFSGTIRSnldPFGEysD--------EELWQALERVGLKEFVE 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257669152 970 GLPG-------ESG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRnTVDTGRTVVCTIH 1034
Cdd:cd03244 124 SLPGgldtvveEGGenLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIR-EAFKDCTVLTIAH 196
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
166-412 |
4.85e-08 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 55.13 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 166 KFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQelkQTGRVTYNGHGMNEFVPQRTA----AYIGQNDVHIG 241
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPP---RSGSIRFDGRDITGLPPHERAragiGYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 242 EMTVRETFAYAARFQGVGSR-------YDMLTELARREKEAnikpdpdidifmkamstagektnvmtdyilkilglevcA 314
Cdd:cd03224 89 ELTVEENLLLGAYARRRAKRkarlervYELFPRLKERRKQL--------------------------------------A 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 315 DTMvgddmlrgiSGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIfnGTALISLLQPAPETFNLF 394
Cdd:cd03224 131 GTL---------SGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE--GVTILLVEQNARFALEIA 199
|
250
....*....|....*...
gi 257669152 395 DDIILIAEGEIIYEGPRD 412
Cdd:cd03224 200 DRAYVLERGRVVLEGTAA 217
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
824-1084 |
4.98e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 55.91 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 824 SITFDNVVYSVdmpqemiEQGTQEDRLVLLkGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKT---GGYIDGNITISG 900
Cdd:PRK13649 2 GINLQNVSYTY-------QAGTPFEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVptqGSVRVDDTLITS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 901 YPKNQqtfarisgyceqtDIHSPHVTVyeSLVYsawlRLPKEvdknkrKIFIEEVMELVELTPL---------------R 965
Cdd:PRK13649 74 TSKNK-------------DIKQIRKKV--GLVF----QFPES------QLFEETVLKDVAFGPQnfgvsqeeaealareK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 966 QALVGL--------PGEsgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPS 1037
Cdd:PRK13649 129 LALVGIseslfeknPFE--LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMD 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 257669152 1038 iDIFEAFDELFLLKRGgeEIYVGPLGHESTHLINYFESIQ-GINKITE 1084
Cdd:PRK13649 207 -DVANYADFVYVLEKG--KLVLSGKPKDIFQDVDFLEEKQlGVPKITK 251
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
861-1038 |
5.73e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 55.45 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 861 RPGVLTALMGVSGAGKTTLMDVLAGR------KTGGYIDGNITISGYPKN--QQTFARISGycEQTD-IHSPHvtvYESL 931
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKlkpnlgKFDDPPDWDEILDEFRGSelQNYFTKLLE--GDVKvIVKPQ---YVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 932 vysawlrLPKEVDKNKRKI--------FIEEVMELVELTPLRQALVglpgeSGLSTEQRKRLTIAVELVANPSIIFMDEP 1003
Cdd:cd03236 99 -------IPKAVKGKVGELlkkkdergKLDELVDQLELRHVLDRNI-----DQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190
....*....|....*....|....*....|....*
gi 257669152 1004 TSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1038
Cdd:cd03236 167 SSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAV 201
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
843-1053 |
5.80e-08 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 54.78 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 843 QGTQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiDGNITISGypknqqtfaRISgYCEQTD- 919
Cdd:cd03250 11 DSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGelEKL----SGSVSVPG---------SIA-YVSQEPw 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 920 IHSphVTVYESLVYSawlrlpKEVDKNKrkifIEEVMELVELTP-LRQalvgLP-------GESG--LSTEQRKRLTIAV 989
Cdd:cd03250 77 IQN--GTIRENILFG------KPFDEER----YEKVIKACALEPdLEI----LPdgdlteiGEKGinLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257669152 990 ELVANPSIIFMDEPTSGLDAR-AAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAFDELFLLKRG 1053
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHvGRHIFENCILGLLLNNKTRILVTHQ--LQLLPHADQIVVLDNG 203
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
850-1008 |
6.46e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 55.38 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 850 LVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI--DGNiTISGYPKNQ-------QTFARISGYCEQT 918
Cdd:PRK11300 18 LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGfyKPTGGTIllRGQ-HIEGLPGHQiarmgvvRTFQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 919 DIHSPHVTVYESL---VYSAWLRLP----KEVDKNKRKIFIEEVMELVELTPlRQAlvglpgeSGLSTEQRKRLTIAVEL 991
Cdd:PRK11300 97 VIENLLVAQHQQLktgLFSGLLKTPafrrAESEALDRAATWLERVGLLEHAN-RQA-------GNLAYGQQRRLEIARCM 168
|
170
....*....|....*..
gi 257669152 992 VANPSIIFMDEPTSGLD 1008
Cdd:PRK11300 169 VTQPEILMLDEPAAGLN 185
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
168-231 |
7.63e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 55.16 E-value: 7.63e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkldqELK-QTGRVTYNGHGMNEFVPQRTAA 231
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG----ELSpDSGEVRLNGRPLADWSPAELAR 76
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
168-370 |
8.33e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.80 E-value: 8.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQELKQtGRVTYNGHGMNEFVPQRTAayigqndvhiGEmTVRE 247
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTG-GTVEFKGKDLLELSPEDRA----------GE-GIFM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 248 TFAYAARFQGVGSRYDMLTEL-ARREkeanIKPDPDIDIFMkamstagektnvMTDYI-LKILGLEVCADtMVGDDMLRG 325
Cdd:PRK09580 83 AFQYPVEIPGVSNQFFLQTALnAVRS----YRGQEPLDRFD------------FQDLMeEKIALLKMPED-LLTRSVNVG 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 257669152 326 ISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQI---VNSLRN 370
Cdd:PRK09580 146 FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVadgVNSLRD 193
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
168-412 |
9.97e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.58 E-value: 9.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkldQELKQTGRVTYNGhgmnEFVPQRtaayigqndvhigemtvre 247
Cdd:PRK13537 21 LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLG---LTHPDAGSISLCG----EPVPSR------------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 248 tfAYAARFQ-GVGSRYDmltelarrekeaNIKPD----PDIDIFMKAMSTAGEKTNVMTDYILKILGLEVCADTMVGDdm 322
Cdd:PRK13537 75 --ARHARQRvGVVPQFD------------NLDPDftvrENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 323 lrgISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYvhIFNGTALISLLQPAPETFNLFDDIILIAE 402
Cdd:PRK13537 139 ---LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSL--LARGKTILLTTHFMEEAERLCDRLCVIEE 213
|
250
....*....|.
gi 257669152 403 GEIIYEG-PRD 412
Cdd:PRK13537 214 GRKIAEGaPHA 224
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
1210-1366 |
1.10e-07 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 53.67 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1210 TAVLFLGLQNAASVqpvVNVERT--VFYREQAAGMySAMPYAFAQVFIEIPYVLVQAIVYGLIVYAMIGFEWTAVKFFWY 1287
Cdd:COG0842 12 MSLLFTALMLTALS---IAREREqgTLERLLVTPV-SRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLLLL 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257669152 1288 LFFMYGSFLTFTFYGMMAVAMTPNHHIASVVSSAFYGIWNLFSGFLIPRPSMPVWWEWYYWLCPVAWTLYGLIASQFGD 1366
Cdd:COG0842 88 LLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRALFLGG 166
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
166-425 |
1.90e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.22 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 166 KFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDqelKQTGRVTYNGHGMNEFVPQRTAAYIG---QNDVHIGE 242
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMT---PAHGHVWLDGEHIQHYASKEVARRIGllaQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 243 MTVRETFAYAarfqgvgsRYDMLTELARREKEanikpdpDIDIFMKAMSTAGektnvMTDYILKilglevCADTMvgddm 322
Cdd:PRK10253 96 ITVQELVARG--------RYPHQPLFTRWRKE-------DEEAVTKAMQATG-----ITHLADQ------SVDTL----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 323 lrgiSGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNyVHIFNGTALISLLQPAPETFNLFDDIILIAE 402
Cdd:PRK10253 145 ----SGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSE-LNREKGYTLAAVLHDLNQACRYASHLIALRE 219
|
250 260
....*....|....*....|....*.
gi 257669152 403 GEIIYEGPRDHVV--EFFETM-GFKC 425
Cdd:PRK10253 220 GKIVAQGAPKEIVtaELIERIyGLRC 245
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
168-360 |
2.33e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 52.95 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQElkqTGRVTYNGHGMNEFVPQRTAAYIGQNDVHIGEMTVRE 247
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPA---AGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 248 TFAYAARFQGvgsrydmltelarrekeaniKPDPDIDIFMKAMstagektnvmtdyilkilGLEVCADTMVGDdmlrgIS 327
Cdd:PRK13539 93 NLEFWAAFLG--------------------GEELDIAAALEAV------------------GLAPLAHLPFGY-----LS 129
|
170 180 190
....*....|....*....|....*....|...
gi 257669152 328 GGQKKRVTTGEMLVGPSRALFMDEISTGLDSST 360
Cdd:PRK13539 130 AGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
180-414 |
2.45e-07 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 54.73 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 180 GRMALLlGPPSSGKTTLLLALAGKLDqelKQTGRVTYNGHGMNE-----FVP--QRTAAYIGQNDVHIGEMTVRETFAYA 252
Cdd:TIGR02142 24 GVTAIF-GRSGSGKTTLIRLIAGLTR---PDEGEIVLNGRTLFDsrkgiFLPpeKRRIGYVFQEARLFPHLSVRGNLRYG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 253 ARFqgvgsrydmltelarrekeanikpdpdidifmkamsTAGEKTNVMTDYILKILGLEVCADTMVGDdmlrgISGGQKK 332
Cdd:TIGR02142 100 MKR------------------------------------ARPSERRISFERVIELLGIGHLLGRLPGR-----LSGGEKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 333 RVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIFNGTAL-IS-LLQpapETFNLFDDIILIAEGEIIYEGP 410
Cdd:TIGR02142 139 RVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILyVShSLQ---EVLRLADRVVVLEDGRVAAAGP 215
|
....
gi 257669152 411 RDHV 414
Cdd:TIGR02142 216 IAEV 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
825-1053 |
2.50e-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: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 825 ITFDNVVYSVDmpqemiEQGTQedrlvLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRktggyID---GNITISGY 901
Cdd:cd03247 1 LSINNVSFSYP------EQEQQ-----VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGD-----LKpqqGEITLDGV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 902 PknqqtfarisgyceqtdihsphVTVYESLVYSAWLRLPKEVdknkrKIFIeevmelvelTPLRQALvGLPgesgLSTEQ 981
Cdd:cd03247 65 P----------------------VSDLEKALSSLISVLNQRP-----YLFD---------TTLRNNL-GRR----FSGGE 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257669152 982 RKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNtVDTGRTVV-CTIHQPSIdifEAFDELFLLKRG 1053
Cdd:cd03247 104 RQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFE-VLKDKTLIwITHHLTGI---EHMDKILFLENG 172
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
862-1034 |
2.61e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.93 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 862 PGVLTALMGVSGAGKTTLMDVLAGRKTGGyiDGNITISGYPKNQQTFARISGYCEQTDIHSPHVTVYESLVYSAWL--RL 939
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVE--SGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLhgRR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 940 PKEVDKNkrkifieeVMELVELTPLRQALVglpgeSGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1019
Cdd:PRK13543 114 AKQMPGS--------ALAIVGLAGYEDTLV-----RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
170
....*....|....*
gi 257669152 1020 RNTVDTGRTVVCTIH 1034
Cdd:PRK13543 181 SAHLRGGGAALVTTH 195
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
852-1053 |
2.70e-07 |
|
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: 53.37 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGAFRPGVLTALMGVSGAGKTTL-------MDVLAGRKTggyIDGnITISGYPKnQQTFARISgyceqtdihsph 924
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIV---IDG-IDISKLPL-HTLRSRLS------------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 925 VTVYESLVYSAWLRLPKEVDKNKRKIFIEEVMELVELTPLRQALVG------LPGESGLSTEQRKRLTIAVELVANPSII 998
Cdd:cd03288 99 IILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGgldavvTEGGENFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 257669152 999 FMDEPTSGLDARAAAIVMRTVRnTVDTGRTVVCTIHQPSiDIFEAfDELFLLKRG 1053
Cdd:cd03288 179 IMDEATASIDMATENILQKVVM-TAFADRTVVTIAHRVS-TILDA-DLVLVLSRG 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
862-1034 |
3.04e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.39 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 862 PGVLTALMGVSGAGKTTLMDVLAGRKTGGyiDGNITISGYPKNQQTFARIS------------GYCEQ--TDIHSPHVT- 926
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSARLAPD--AGEVHYRMRDGQLRDLYALSeaerrrllrtewGFVHQhpRDGLRMQVSa 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 927 ---VYESLVYSAWlrlpkevdKNKRKIFIEEV--MELVELTPLRqaLVGLPgeSGLSTEQRKRLTIAVELVANPSIIFMD 1001
Cdd:PRK11701 109 ggnIGERLMAVGA--------RHYGDIRATAGdwLERVEIDAAR--IDDLP--TTFSGGMQQRLQIARNLVTHPRLVFMD 176
|
170 180 190
....*....|....*....|....*....|....
gi 257669152 1002 EPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIH 1034
Cdd:PRK11701 177 EPTGGLDVSVQARLLDLLRGLVrELGLAVVIVTH 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
170-382 |
3.11e-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: 52.80 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 170 LNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkldQELKQTGRVTYNGHGMNEFvPQRTAAYIGQndvHIG-------- 241
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYK---EELPTSGTIRVNGQDVSDL-RGRAIPYLRR---KIGvvfqdfrl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 242 --EMTVRETFAYAARFQGVGSRydmltELARREKEAnikpdpdidifmkamstagektnvmtdyiLKILGLEVCADTMVG 319
Cdd:cd03292 90 lpDRNVYENVAFALEVTGVPPR-----EIRKRVPAA-----------------------------LELVGLSHKHRALPA 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257669152 320 ddmlrGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNsLRNYVHIFNGTALIS 382
Cdd:cd03292 136 -----ELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMN-LLKKINKAGTTVVVA 192
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
160-409 |
3.12e-07 |
|
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: 52.67 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 160 VPNRKKKF---TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLdqeLKQTGRVTYNGHGMnEFVPQRTAAYIGQN 236
Cdd:cd03269 3 VENVTKRFgrvTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGII---LPDSGEVLFDGKPL-DIAARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 237 DVHIGEMTVRETFAYAARFQGVGSRYdmltelARREkeanikpdpdidifmkamstagektnvmTDYILKILGLEVCADT 316
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKGLKKEE------ARRR----------------------------IDEWLERLELSEYANK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 317 MVgddmlRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTT---YQIVNSLRNyvhifNGTALISLLQPAPETFNL 393
Cdd:cd03269 125 RV-----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVellKDVIRELAR-----AGKTVILSTHQMELVEEL 194
|
250
....*....|....*.
gi 257669152 394 FDDIILIAEGEIIYEG 409
Cdd:cd03269 195 CDRVLLLNKGRAVLYG 210
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
152-405 |
3.14e-07 |
|
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: 52.86 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 152 KFLNTLHLVPNRKKKfTILNDVSGIVKPGRMALLLGPPSSGKTTlLLALAGKLDQelKQTGRVTYNGHGMNEF---VPQR 228
Cdd:cd03248 13 KFQNVTFAYPTRPDT-LVLQDVSFTLHPGEVTALVGPSGSGKST-VVALLENFYQ--PQGGQVLLDGKPISQYehkYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 229 TAAYIGQNDVHIGEmTVRETFAYaarfqGVGS-RYDMLTELArrekeanikpdpdidifmkamSTAGEKTNVMtdyilki 307
Cdd:cd03248 89 KVSLVGQEPVLFAR-SLQDNIAY-----GLQScSFECVKEAA---------------------QKAHAHSFIS------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 308 lGLEVCADTMVGDdmlRG--ISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHifNGTAL----- 380
Cdd:cd03248 135 -ELASGYDTEVGE---KGsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLviahr 208
|
250 260
....*....|....*....|....*
gi 257669152 381 ISLLQPApetfnlfDDIILIAEGEI 405
Cdd:cd03248 209 LSTVERA-------DQILVLDGGRI 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
856-1053 |
3.22e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.01 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 856 VNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyiDGNITISG-----YPKNQQtfARISGYCEQTDIHSPHVTVYES 930
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG---SGSIQFAGqpleaWSAAEL--ARHRAYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 931 LVysawLRLPKEVDKNKRKIFIEEVMELVELTPL--R--QALVGlpGESglsteQRKRLTiAVEL----VANPS--IIFM 1000
Cdd:PRK03695 90 LT----LHQPDKTRTEAVASALNEVAEALGLDDKlgRsvNQLSG--GEW-----QRVRLA-AVVLqvwpDINPAgqLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 257669152 1001 DEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAfDELFLLKRG 1053
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHA-DRVWLLKQG 209
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
758-1053 |
3.92e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 54.72 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 758 LLGFVVLFNF------GFTLALTFLNSLGKpqaviAEEPASDETELQSARSEGVVEA--------GANKKRGM-VLPFEP 822
Cdd:PRK10790 264 LCGLLMLFGFsasgtiEVGVLYAFISYLGR-----LNEPLIELTTQQSMLQQAVVAGervfelmdGPRQQYGNdDRPLQS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 823 HSITFDNVVYSVDmpqemieqgtqEDRLVLlKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGrktggYI---DGNITIS 899
Cdd:PRK10790 339 GRIDIDNVSFAYR-----------DDNLVL-QNINLSVPSRGFVALVGHTGSGKSTLASLLMG-----YYpltEGEIRLD 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 900 GYPKNQQTFA--RISGYCEQTDihsPhVTVYESLVysAWLRLPKEVDKNKrkifIEEVMELVELTPLRQALV-GLP---G 973
Cdd:PRK10790 402 GRPLSSLSHSvlRQGVAMVQQD---P-VVLADTFL--ANVTLGRDISEEQ----VWQALETVQLAELARSLPdGLYtplG 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 974 ESG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRnTVDTGRTVVCTIHQPSIdIFEAfDELFLLK 1051
Cdd:PRK10790 472 EQGnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALA-AVREHTTLVVIAHRLST-IVEA-DTILVLH 548
|
..
gi 257669152 1052 RG 1053
Cdd:PRK10790 549 RG 550
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
853-1069 |
4.13e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 53.27 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiDGNITISGYP---KNQQTFARISGYCEQT---DIHSPhvT 926
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPT--SGSVLIRGEPitkENIREVRKFVGLVFQNpddQIFSP--T 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 927 VYESLVYSAW-LRLPKEVDKNKrkifIEEVMELVELTPLRQALvglpgESGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1005
Cdd:PRK13652 96 VEQDIAFGPInLGLDEETVAHR----VSSALHMLGLEELRDRV-----PHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257669152 1006 GLDARAAAIVMRTVRNTVDT-GRTVVCTIHQPSIdIFEAFDELFLLKRGG-------EEIYVGPLGHESTHL 1069
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRivaygtvEEIFLQPDLLARVHL 237
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
863-1076 |
4.80e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 53.69 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 863 GVLTALMGVSGAGKTTLMDVLAG--RKTGGYI--DGnITISGYPKNQ-------QTFARIsgyceqtdihsPHVTVYESL 931
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAGfeQPTAGQImlDG-VDLSHVPPYQrpinmmfQSYALF-----------PHMTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 932 VYS-AWLRLPKEVDKNKrkifIEEVMELVELTPLRQALvglPGEsgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1010
Cdd:PRK11607 113 AFGlKQDKLPKAEIASR----VNEMLGLVHMQEFAKRK---PHQ--LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1011 AAAIVMRTVRNTVD-TGRTVVCTIHqpsiDIFEAFD---ELFLLKRGG-------EEIYVGPLGHESTHLI---NYFESI 1076
Cdd:PRK11607 184 LRDRMQLEVVDILErVGVTCVMVTH----DQEEAMTmagRIAIMNRGKfvqigepEEIYEHPTTRYSAEFIgsvNVFEGV 259
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
122-409 |
5.30e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 53.30 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 122 RFDHLKVEAEVHVGGRALPTFVNFISNFADKFLNtlhlVPNRKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALA 201
Cdd:PRK13536 13 RLELSPIERKHQGISEAKASIPGSMSTVAIDLAG----VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 202 GKLDQElkqTGRVTYNGhgmnEFVPQRTA---AYIG---QNDVHIGEMTVRETFAYAARFQGvgsrydmlteLARREKEA 275
Cdd:PRK13536 89 GMTSPD---AGKITVLG----VPVPARARlarARIGvvpQFDNLDLEFTVRENLLVFGRYFG----------MSTREIEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 276 NIKPdpdidifmkamstagektnvmtdyILKILGLEVCADTMVGDdmlrgISGGQKKRVTTGEMLVGPSRALFMDEISTG 355
Cdd:PRK13536 152 VIPS------------------------LLEFARLESKADARVSD-----LSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 257669152 356 LDSSTTYQIVNSLRNYvhIFNGTALISLLQPAPETFNLFDDIILIAEGEIIYEG 409
Cdd:PRK13536 203 LDPHARHLIWERLRSL--LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
850-1053 |
5.34e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.85 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 850 LVLLKGVNGAFrPGV--------------LTALMGVSGAGKTTLMDVLAG--RKTGG---YIDGNITISGyPKNQQTfAR 910
Cdd:PRK10762 4 LLQLKGIDKAF-PGVkalsgaalnvypgrVMALVGENGAGKSTMMKVLTGiyTRDAGsilYLGKEVTFNG-PKSSQE-AG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 911 ISgyceqtDIHS-----PHVTVYESL-----VYSAWLRLpkevdkNKRKIFIEEVMELVELTpLRQALVGLPGEsgLSTE 980
Cdd:PRK10762 81 IG------IIHQelnliPQLTIAENIflgreFVNRFGRI------DWKKMYAEADKLLARLN-LRFSSDKLVGE--LSIG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257669152 981 QRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELFLLKRG 1053
Cdd:PRK10762 146 EQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLK-EIFEICDDVTVFRDG 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
852-1035 |
7.32e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 52.28 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGAFRPGVLTALMGVSGAGKTTLMDVL--AGRKTGGYI-------------DGNITISGYPKNQQTFARISGYCE 916
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCInfLEKPSEGSIvvngqtinlvrdkDGQLKVADKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 917 QTDIHSpHVTVYESLVYSAW--LRLPKEVDKNKRKIFIEEVmelveltplrqalvGLPGES------GLSTEQRKRLTIA 988
Cdd:PRK10619 100 HFNLWS-HMTVLENVMEAPIqvLGLSKQEARERAVKYLAKV--------------GIDERAqgkypvHLSGGQQQRVSIA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 257669152 989 VELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1035
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
168-417 |
7.62e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 53.03 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkldQELKQTGRVTYNGHGMNEFVP-QRTAAYIGQNDVHIGEMTVR 246
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAG---FETPDSGRIMLDGQDITHVPAeNRHVNTVFQSYALFPHMTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 247 ETFAYAARFQGVGSRydmltELARREKEAnikpdpdidifmkamstagektnvmtdyiLKILGLEVCADTMVGDdmlrgI 326
Cdd:PRK09452 105 ENVAFGLRMQKTPAA-----EITPRVMEA-----------------------------LRMVQLEEFAQRKPHQ-----L 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 327 SGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNyVHIFNGTALISLLQPAPETFNLFDDIILIAEGEI- 405
Cdd:PRK09452 146 SGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKA-LQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIe 224
|
250 260
....*....|....*....|
gi 257669152 406 -------IYEGPRD-HVVEF 417
Cdd:PRK09452 225 qdgtpreIYEEPKNlFVARF 244
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
853-1021 |
1.18e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.01 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIDGNITISGYPknqQTFARISGyCEQTD---IHS-----PH 924
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEE---LQASNIRD-TERAGiaiIHQelalvKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 925 VTVYESLVysawlrLPKEVDKNKRKIFIEEVMELVELtpLRQALVGLP-----GESGLSTEQrkRLTIAVELVANPSIIF 999
Cdd:PRK13549 97 LSVLENIF------LGNEITPGGIMDYDAMYLRAQKL--LAQLKLDINpatpvGNLGLGQQQ--LVEIAKALNKQARLLI 166
|
170 180
....*....|....*....|..
gi 257669152 1000 MDEPTSGLDARAAAIVMRTVRN 1021
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRD 188
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
851-1007 |
1.37e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.75 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiDGNITISGYPKNQQTFARISGY----CEQTDIHSPHVT 926
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD--SGTLEIGGNPCARLTPAKAHQLgiylVPQEPLLFPNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 927 VYESLVYsawlRLPKEVDKNKRkiFIEEVMEL-VELTPLRQAlvglpgeSGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1005
Cdd:PRK15439 103 VKENILF----GLPKRQASMQK--MKQLLAALgCQLDLDSSA-------GSLEVADRQIVEILRGLMRDSRILILDEPTA 169
|
..
gi 257669152 1006 GL 1007
Cdd:PRK15439 170 SL 171
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
164-416 |
1.47e-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: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 164 KKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDqelKQTGRVTYNG---HGMNEFVPQRTAAYIGQnDVHI 240
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD---PQKGQILIDGidiRDISRKSLRSMIGVVLQ-DTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 241 GEMTVRETFAYAarfqgvgsrydmlTELARREKEanikpdpdidifMKAMSTAGektnvMTDYILKilgLEVCADTMVGD 320
Cdd:cd03254 89 FSGTIMENIRLG-------------RPNATDEEV------------IEAAKEAG-----AHDFIMK---LPNGYDTVLGE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 321 dmlRG--ISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNyvhIFNG-TALI-----SLLQPApetfn 392
Cdd:cd03254 136 ---NGgnLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEK---LMKGrTSIIiahrlSTIKNA----- 204
|
250 260
....*....|....*....|....
gi 257669152 393 lfDDIILIAEGEIIYEGPRDHVVE 416
Cdd:cd03254 205 --DKILVLDDGKIIEEGTHDELLA 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
853-1043 |
1.75e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 51.17 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiDGNITISGYPKNQQTF----ARISGYCEQTDIHSPHVT 926
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGllLPE----AGTITVGGMVLSEETVwdvrRQVGMVFQNPDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 927 VYESLVYSAwlrlpkEVDKNKRKIFIEEVMELVELTPLRQALVGLPgeSGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1006
Cdd:PRK13635 99 VQDDVAFGL------ENIGVPREEMVERVDQALRQVGMEDFLNREP--HRLSGGQKQRVAIAGVLALQPDIIILDEATSM 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 257669152 1007 LDARAAAIVMRTVRNTVDTGR-TVVCTIHqpsiDIFEA 1043
Cdd:PRK13635 171 LDPRGRREVLETVRQLKEQKGiTVLSITH----DLDEA 204
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
824-1010 |
1.91e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 52.52 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 824 SITFDNVVYSVDmpqemieqgtqEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLagrkTGGY--IDGNITISGY 901
Cdd:PRK11160 338 SLTLNNVSFTYP-----------DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL----TRAWdpQQGEILLNGQ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 902 PknqqtfarISGYCEQTDIHSphVTVYESLVY--SAWLR------LPKEVDKNkrkifIEEVMELVELTPLRQALVGLP- 972
Cdd:PRK11160 403 P--------IADYSEAALRQA--ISVVSQRVHlfSATLRdnlllaAPNASDEA-----LIEVLQQVGLEKLLEDDKGLNa 467
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 257669152 973 --GESG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1010
Cdd:PRK11160 468 wlGEGGrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAE 509
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
866-1008 |
1.93e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.80 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 866 TALMGVSGAGKTTLMDVLAG--RKTGGYI--------DGNITISgYPKNQQtfaRIsGYCEQTDIHSPHVTVYESLVYSA 935
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGltRPQKGRIvlngrvlfDAEKGIC-LPPEKR---RI-GYVFQDARLFPHYKVRGNLRYGM 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257669152 936 wlrlpkevdKNKRKIFIEEVMELVELTPLrqaLVGLPgeSGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1008
Cdd:PRK11144 102 ---------AKSMVAQFDKIVALLGIEPL---LDRYP--GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
153-409 |
1.95e-06 |
|
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: 50.79 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 153 FLNTLHLVPNRKKK-FTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLdqeLKQTGRVTYNGhgmneFVP----- 226
Cdd:cd03267 19 LIGSLKSLFKRKYReVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLL---QPTSGEVRVAG-----LVPwkrrk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 227 ---QRTAAYIGQNDVHIGEMTVRETFAYAARFQGV-----GSRYDMLTELarrekeanikpdpdidifmkamstagektn 298
Cdd:cd03267 91 kflRRIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLpparfKKRLDELSEL------------------------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 299 vmtdyilkiLGLEVCADTMVgddmlRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHIFNGT 378
Cdd:cd03267 141 ---------LDLEELLDTPV-----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTT 206
|
250 260 270
....*....|....*....|....*....|....*...
gi 257669152 379 ALIsllqpapeTFNLFDDI-------ILIAEGEIIYEG 409
Cdd:cd03267 207 VLL--------TSHYMKDIealarrvLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
825-1010 |
1.95e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 51.17 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 825 ITFDNVVYSVDMpqemieqGTQEDRLVLlKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYID-GNITISGY 901
Cdd:PRK13634 3 ITFQKVEHRYQY-------KTPFERRAL-YDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGllQPTSGTVTiGERVITAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 902 PKNQQ--TFARISGYCEQTdihsPHVTVYESLVYSAWLRLPKE--VDKNKRKIFIEEVMELVELTPlrQALVGLPGEsgL 977
Cdd:PRK13634 75 KKNKKlkPLRKKVGIVFQF----PEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIELVGLPE--ELLARSPFE--L 146
|
170 180 190
....*....|....*....|....*....|...
gi 257669152 978 STEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1010
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
852-1034 |
2.26e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.80 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIDGNITISGYPKNQQTFARIS------GYceQTDIHSPHV 925
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGESILDLEPEERAhlgiflAF--QYPIEIPGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 926 TVYE--SLVYSAwlrlpKEVDKNKRKI----FIEEVMELVELTPLRQALVGLPGESGLSTEQRKRLTIAVELVANPSIIF 999
Cdd:CHL00131 100 SNADflRLAYNS-----KRKFQGLPELdpleFLEIINEKLKLVGMDPSFLSRNVNEGFSGGEKKRNEILQMALLDSELAI 174
|
170 180 190
....*....|....*....|....*....|....*
gi 257669152 1000 MDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1034
Cdd:CHL00131 175 LDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
169-419 |
2.47e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 49.83 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 169 ILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQELKQtGRVTYNGHgmnefvpqrtaayigqndvHIGEMTVret 248
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTE-GEILFKGE-------------------DITDLPP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 249 fayaarfqgvgsrydmlTELARRekeanikpdpdiDIFMkamstagektnvMTDYILKILGLEVcadtmvgDDMLR---- 324
Cdd:cd03217 72 -----------------EERARL------------GIFL------------AFQYPPEIPGVKN-------ADFLRyvne 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 325 GISGGQKKRVTTGEMLV-GPSRALFmDEISTGLDSSTTYQIVNSLRNYVHIFNGTALISLLQpapetfNLFDDII----- 398
Cdd:cd03217 104 GFSGGEKKRNEILQLLLlEPDLAIL-DEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQ------RLLDYIKpdrvh 176
|
250 260
....*....|....*....|.
gi 257669152 399 LIAEGEIIYEGPRDHVVEFFE 419
Cdd:cd03217 177 VLYDGRIVKSGDKELALEIEK 197
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
851-1053 |
3.03e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.60 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGY------IDGNITISGYPKNQ---QTFARISGYCEQTDIH 921
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarVTGDVTLNGEPLAAidaPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 922 SPHVTVYESLVYSAW--LRLPKEVDKNKRKIfIEEVMELVELTPL-RQALVGLPGESgLSTEQRKR----LTIAVELVAN 994
Cdd:PRK13547 95 AFAFSAREIVLLGRYphARRAGALTHRDGEI-AWQALALAGATALvGRDVTTLSGGE-LARVQFARvlaqLWPPHDAAQP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 995 PSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTI-HQPSIDIFEAfDELFLLKRG 1053
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIvHDPNLAARHA-DRIAMLADG 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
169-364 |
3.04e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.47 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 169 ILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDqelKQTGRVTYNGHGMNEfvPQRTAAYIGQNDVHIGEMTVRET 248
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVP---YQHGSITLDGKPVEG--PGAERGVVFQNEGLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 249 FAYAARFQGVGsrydmltelaRREKEAnikpdpdidifmkamsTAGEktnvmtdyILKILGLEvcadtMVGDDMLRGISG 328
Cdd:PRK11248 91 VAFGLQLAGVE----------KMQRLE----------------IAHQ--------MLKKVGLE-----GAEKRYIWQLSG 131
|
170 180 190
....*....|....*....|....*....|....*.
gi 257669152 329 GQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQI 364
Cdd:PRK11248 132 GQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
853-1038 |
3.24e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.86 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLmdvlagrktggyidgnitisgypknqqtfarisgyceqtdihsphvtVYESLV 932
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL-----------------------------------------------VNEGLY 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 933 YSAWLRLPKEVDKNKRK--IFIEEVMELVEL----TPLRQALvglpgeSGLSTEQRKRLTIAVELVANP--SIIFMDEPT 1004
Cdd:cd03238 44 ASGKARLISFLPKFSRNklIFIDQLQFLIDVglgyLTLGQKL------STLSGGELQRVKLASELFSEPpgTLFILDEPS 117
|
170 180 190
....*....|....*....|....*....|....
gi 257669152 1005 SGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1038
Cdd:cd03238 118 TGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDV 151
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
168-414 |
3.63e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 50.01 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQelkQTGRVTYNGHGMNEFVPQ---RTAAYIGQNDVHIGEMT 244
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP---QSGTVFLGDKPISMLSSRqlaRRLALLPQHHLTPEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 245 VRETFAYAarfqgvgsRYDMLTELARREKEanikpdpDIDIFMKAMstagEKTNVMTdyilkilglevCADTMVGDdmlr 324
Cdd:PRK11231 93 VRELVAYG--------RSPWLSLWGRLSAE-------DNARVNQAM----EQTRINH-----------LADRRLTD---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 325 gISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHifNGTALISLLQPAPETFNLFDDIILIAEGE 404
Cdd:PRK11231 139 -LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNT--QGKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
250
....*....|
gi 257669152 405 IIYEGPRDHV 414
Cdd:PRK11231 216 VMAQGTPEEV 225
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
168-368 |
3.76e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 49.71 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDqelKQTGRVTYNGHGMNEFVPQR---TAAYIGQNDVHIGEmT 244
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIS---PTSGTLLFEGEDISTLKPEIyrqQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 245 VRET--FAYAARfqgvgsrydmltelarrekeaNIKPDPdiDIFMKAMSTAGEKTNVMTDYIlkilglevcadtmvgddm 322
Cdd:PRK10247 97 VYDNliFPWQIR---------------------NQQPDP--AIFLDDLERFALPDTILTKNI------------------ 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 257669152 323 lRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTyQIVNSL 368
Cdd:PRK10247 136 -AELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK-HNVNEI 179
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
848-1048 |
3.85e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 50.04 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 848 DRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggyIDGNITISGYPK--NQQTFAR---ISGYCEQTDIHS 922
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE---LESEVRVEGRVEffNQNIYERrvnLNRLRRQVSMVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 923 PH-----VTVYESLVYS----AWlrLPK-EVDKnkrkiFIEEVMELVEL-----TPLRQALVGLPGesglstEQRKRLTI 987
Cdd:PRK14258 95 PKpnlfpMSVYDNVAYGvkivGW--RPKlEIDD-----IVESALKDADLwdeikHKIHKSALDLSG------GQQQRLCI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257669152 988 AVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQ-PSIDIFEAFDELF 1048
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSlRLRSELTMVIVSHNlHQVSRLSDFTAFF 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
161-351 |
5.38e-06 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 49.70 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 161 PNRKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkLDQElkQTGRVTYNGHGMNEFVPQRtaAYIGQNDV-- 238
Cdd:COG1116 18 PTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAG-LEKP--TSGEVLVDGKPVTGPGPDR--GVVFQEPAll 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 239 -HigeMTVRETFAYAARFQGVGSRydmltelARREKeanikpdpdidifmkamstagektnvmTDYILKILGLEVCADTM 317
Cdd:COG1116 93 pW---LTVLDNVALGLELRGVPKA-------ERRER---------------------------ARELLELVGLAGFEDAY 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 257669152 318 VGDdmlrgISGGQKKRV----TtgemLVGPSRALFMDE 351
Cdd:COG1116 136 PHQ-----LSGGMRQRVaiarA----LANDPEVLLMDE 164
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
168-357 |
5.99e-06 |
|
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: 48.51 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQElkqTGRVTYNGHGMNE--FVPQRTAAYIGQNDVHIGEMTV 245
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPD---SGEVRWNGTPLAEqrDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 246 RETFAYAARFQGvGSRYDMLTELARrekeanikpdpdidifmkamstagektnvmtdyilkiLGLEVCADTMVGDdmlrg 325
Cdd:TIGR01189 91 LENLHFWAAIHG-GAQRTIEDALAA-------------------------------------VGLTGFEDLPAAQ----- 127
|
170 180 190
....*....|....*....|....*....|..
gi 257669152 326 ISGGQKKRVTTGEMLVGPSRALFMDEISTGLD 357
Cdd:TIGR01189 128 LSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
825-1054 |
6.53e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 50.73 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 825 ITFDNVVYSVDMPQemieQGtqedrlvlLKGVNGAFRPGVLTALMGVSGAGKTTLMDVL-------AGRKTggyIDGN-- 895
Cdd:PRK13657 335 VEFDDVSFSYDNSR----QG--------VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRIL---IDGTdi 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 896 --ITISGYPKNQQT-------FAR-ISgycEQTDIHSPHVTVYEslvysawLRLPKEvdknkrkifIEEVMELVELTPLR 965
Cdd:PRK13657 400 rtVTRASLRRNIAVvfqdaglFNRsIE---DNIRVGRPDATDEE-------MRAAAE---------RAQAHDFIERKPDG 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 966 -QALVGLPGESgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS------- 1037
Cdd:PRK13657 461 yDTVVGERGRQ-LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAAL-DELMKGRTTFIIAHRLStvrnadr 538
|
250 260
....*....|....*....|....*
gi 257669152 1038 IDIFEA--------FDElfLLKRGG 1054
Cdd:PRK13657 539 ILVFDNgrvvesgsFDE--LVARGG 561
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
861-1008 |
8.00e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 48.81 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 861 RPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiDGNITISGYPKNQQTFAR--ISGYCEQTDIHsPHVTVYE--SLVYSAW 936
Cdd:PRK10771 23 ERGERVAILGPSGAGKSTLLNLIAGFLTPA--SGSLTLNGQDHTTTPPSRrpVSMLFQENNLF-SHLTVAQniGLGLNPG 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257669152 937 LRLPKEvdknkRKIFIEEVMELVELTPLrqaLVGLPGEsgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1008
Cdd:PRK10771 100 LKLNAA-----QREKLHAIARQMGIEDL---LARLPGQ--LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
851-1008 |
9.81e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.09 E-value: 9.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTT----LMDVLAGRktggyidGNITISGYPKNQQTFARISGYCEQT-----DIH 921
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-------GEIWFDGQPLHNLNRRQLLPVRHRIqvvfqDPN 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 922 S---PHVTVYEslVYSAWLRL-PKEVDKNKRKIFIEEVMELVELTP-LRQALvglPGEsgLSTEQRKRLTIAVELVANPS 996
Cdd:PRK15134 373 SslnPRLNVLQ--IIEEGLRVhQPTLSAAQREQQVIAVMEEVGLDPeTRHRY---PAE--FSGGQRQRIAIARALILKPS 445
|
170
....*....|..
gi 257669152 997 IIFMDEPTSGLD 1008
Cdd:PRK15134 446 LIILDEPTSSLD 457
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
168-223 |
9.98e-06 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 48.58 E-value: 9.98e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkLDQelKQTGRVTYNGH---GMNE 223
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG-LDR--PTSGTVRLAGQdlfALDE 81
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
853-1053 |
1.05e-05 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 48.30 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGrktggyID----GNITISGypknqqtfaRISGYCE-QTDIHsPHVTV 927
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAG------IYppdsGTVTVRG---------RVSSLLGlGGGFN-PELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 928 YESLVYSAWL--RLPKEVDKnkrkiFIEEVMELVEL-----TPLRQalvglpgesgLSTEQRKRLTIAVELVANPSIIFM 1000
Cdd:cd03220 102 RENIYLNGRLlgLSRKEIDE-----KIDEIIEFSELgdfidLPVKT----------YSSGMKARLAFAIATALEPDILLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 257669152 1001 DEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELFLLKRG 1053
Cdd:cd03220 167 DEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEKG 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
168-369 |
1.07e-05 |
|
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: 47.87 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDqelKQTGRVTYNGHGMNEFVP--QRTAAYIGQNDVHIGEMTV 245
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP---PLAGRVLLNGGPLDFQRDsiARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 246 RETFAYAARFqgvGSRYDMLTELARrekeanikpdpdidifmkamstagektnvmtdyilkiLGLevcadTMVGDDMLRG 325
Cdd:cd03231 91 LENLRFWHAD---HSDEQVEEALAR-------------------------------------VGL-----NGFEDRPVAQ 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 257669152 326 ISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLR 369
Cdd:cd03231 126 LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
161-447 |
1.12e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 49.03 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 161 PNRKKkfTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQELKQTGRVTYNGHGMNEFVPQRTAAYIG---QN- 236
Cdd:PRK13640 16 PDSKK--PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIREKVGivfQNp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 237 DVHIGEMTVRETFAYAARFQGVgSRYDMLTelarrekeanikpdpdidIFMKAMSTAGektnvMTDYIlkilglevcadt 316
Cdd:PRK13640 94 DNQFVGATVGDDVAFGLENRAV-PRPEMIK------------------IVRDVLADVG-----MLDYI------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 317 mvgDDMLRGISGGQKKRVT-TGEMLVGPsRALFMDEISTGLDSSTTYQIVNSLRNyVHIFNGTALISLLQPAPETfNLFD 395
Cdd:PRK13640 138 ---DSEPANLSGGQKQRVAiAGILAVEP-KIIILDESTSMLDPAGKEQILKLIRK-LKKKNNLTVISITHDIDEA-NMAD 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257669152 396 DIILIAEGEIIYEG-PRD--HVVEFFETMGFKCPPRKGVADFL--------QEVTSKKDQMQY 447
Cdd:PRK13640 212 QVLVLDDGKLLAQGsPVEifSKVEMLKEIGLDIPFVYKLKNKLkekgisvpQEINTEEKLVQY 274
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
982-1032 |
1.12e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.35 E-value: 1.12e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 257669152 982 RKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCT 1032
Cdd:NF000106 150 RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLT 200
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
167-334 |
1.20e-05 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 49.33 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 167 FTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAG--KLDQelkqtGRVTYNGHGMNEFVP-QRTAAYIGQNDV---Hi 240
Cdd:COG3842 18 VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfeTPDS-----GRILLDGRDVTGLPPeKRNVGMVFQDYAlfpH- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 241 geMTVRETFAYAARFQGVGSRydmltELARREKEAnikpdpdidifmkamstagektnvmtdyiLKILGLEVCADTMVGD 320
Cdd:COG3842 92 --LTVAENVAFGLRMRGVPKA-----EIRARVAEL-----------------------------LELVGLEGLADRYPHQ 135
|
170
....*....|....
gi 257669152 321 dmlrgISGGQKKRV 334
Cdd:COG3842 136 -----LSGGQQQRV 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
851-1019 |
1.42e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 49.29 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 851 VLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGR--KTGGYID-G-NITISGYPKNQQTFarisgyceqtdihSPHVT 926
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGElePDSGTVKlGeTVKIGYFDQHQEEL-------------DPDKT 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 927 VYEslvysaWLRlpkEVDKNKRKIFIeevmelveltplRQAL--VGLPGE------SGLSTEQRKRLTIAVELVANPSII 998
Cdd:COG0488 396 VLD------ELR---DGAPGGTEQEV------------RGYLgrFLFSGDdafkpvGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180
....*....|....*....|.
gi 257669152 999 FMDEPTSGLDaraaaIVMRTV 1019
Cdd:COG0488 455 LLDEPTNHLD-----IETLEA 470
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
252-421 |
1.44e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 48.46 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 252 AARFQGVGSRYDMLTELARREKEANIKPDPDIDIFMkamstagekTNVMTDYILKILGLEVCAD----------TMVGDD 321
Cdd:PRK13638 57 AVLWQGKPLDYSKRGLLALRQQVATVFQDPEQQIFY---------TDIDSDIAFSLRNLGVPEAeitrrvdealTLVDAQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 322 MLRG-----ISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYV----HIFNGTALISLLqpapetFN 392
Cdd:PRK13638 128 HFRHqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVaqgnHVIISSHDIDLI------YE 201
|
170 180
....*....|....*....|....*....
gi 257669152 393 LFDDIILIAEGEIIYEGPRDHVVEFFETM 421
Cdd:PRK13638 202 ISDAVYVLRQGQILTHGAPGEVFACTEAM 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
160-381 |
1.46e-05 |
|
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: 49.55 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 160 VPNRKKkftILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkLDQElkqtgrvtYNGHGMneFVPQRTAAYIGQNDVH 239
Cdd:TIGR03719 14 VPPKKE---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKD--------FNGEAR--PQPGIKVGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 240 IGEMTVRETFayaarFQGVGSRYDMLTELarreKEANIK---PDPDIDIFMKAMSTAGEKTNVMTDYILKiLGLEVCADT 316
Cdd:TIGR03719 80 DPTKTVRENV-----EEGVAEIKDALDRF----NEISAKyaePDADFDKLAAEQAELQEIIDAADAWDLD-SQLEIAMDA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257669152 317 M---VGDDMLRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTtyqiVNSLRNYVHIFNGTALI 381
Cdd:TIGR03719 150 LrcpPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEYPGTVVA 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
823-1053 |
1.57e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 48.21 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 823 HSITFDNVVYSVdmpqemieqgtQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIDGNITISGYP 902
Cdd:PRK13648 6 SIIVFKNVSFQY-----------QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEK--VKSGEIFYNNQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 903 KNQQTFARISgycEQTDI--HSPHVTVYESLV-YSAWLRLPKEV---DKNKRKIfiEEVMELVELTPLRQAlvglpGESG 976
Cdd:PRK13648 73 ITDDNFEKLR---KHIGIvfQNPDNQFVGSIVkYDVAFGLENHAvpyDEMHRRV--SEALKQVDMLERADY-----EPNA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 977 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNT-VDTGRTVVCTIHqpsiDIFEAF--DELFLLKRG 1053
Cdd:PRK13648 143 LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITH----DLSEAMeaDHVIVMNKG 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
825-1060 |
1.71e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 48.06 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 825 ITFDNVVYSVDmpqemieqgtqEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiDGNITISGYP 902
Cdd:PRK13632 8 IKVENVSFSYP-----------NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGllKPQ----SGEIKIDGIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 903 KNQQTFARIS---GYCEQT-DIHSPHVTVYESLVYSawlrLP-KEVDKNKRKIFIEEVMELVELTPLrqalvgLPGES-G 976
Cdd:PRK13632 73 ISKENLKEIRkkiGIIFQNpDNQFIGATVEDDIAFG----LEnKKVPPKKMKDIIDDLAKKVGMEDY------LDKEPqN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 977 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIV---MRTVRNTVDtgRTVVCTIHqpsiDIFEAF--DELFLLK 1051
Cdd:PRK13632 143 LSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIkkiMVDLRKTRK--KTLISITH----DMDEAIlaDKVIVFS 216
|
....*....
gi 257669152 1052 rGGEEIYVG 1060
Cdd:PRK13632 217 -EGKLIAQG 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
825-1053 |
1.72e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 49.25 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 825 ITFDNVVYSVdmpqemieQGTQEdrlVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLagrkTGGY-ID-GNITISGYP 902
Cdd:PRK11176 342 IEFRNVTFTY--------PGKEV---PALRNINFKIPAGKTVALVGRSGSGKSTIANLL----TRFYdIDeGEILLDGHD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 903 KNQQTFARISGYCE--QTDIHSPHVTVYESLVYSAWLRLPKEVdknkrkifIEE------VMELVEltPLRQALVGLPGE 974
Cdd:PRK11176 407 LRDYTLASLRNQVAlvSQNVHLFNDTIANNIAYARTEQYSREQ--------IEEaarmayAMDFIN--KMDNGLDTVIGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 975 SG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAaivmRTVRNTVDT---GRTVVCTIHQPSidIFEAFDELFL 1049
Cdd:PRK11176 477 NGvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESE----RAIQAALDElqkNRTSLVIAHRLS--TIEKADEILV 550
|
....
gi 257669152 1050 LKRG 1053
Cdd:PRK11176 551 VEDG 554
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
853-1030 |
2.60e-05 |
|
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: 46.27 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIDGNITISGypknqqtfarisgycEQTDIHSPHVTVYESLV 932
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP--PASGEITLDG---------------KPVTRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 933 YsawlrLPKevDKNKRKIFIEevMELVELTPLRQALVGlpgesGlstEQRKrLTIAVELVANPSIIFMDEPTSGLDARAA 1012
Cdd:cd03215 79 Y-----VPE--DRKREGLVLD--LSVAENIALSSLLSG-----G---NQQK-VVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170
....*....|....*...
gi 257669152 1013 AIVMRTVRNTVDTGRTVV 1030
Cdd:cd03215 141 AEIYRLIRELADAGKAVL 158
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
853-1057 |
2.78e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 48.28 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIDGNITISGYPKNQQTFaRISGYCEQTDIHS-----PHVTV 927
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNI-RDTERAGIVIIHQeltlvPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 928 YESLVYSAWLRLP-KEVDKNKRKIFIEEVMELVELTPLRQALVglPGESGLSTEQrkRLTIAVELVANPSIIFMDEPTSG 1006
Cdd:TIGR02633 96 AENIFLGNEITLPgGRMAYNAMYLRAKNLLRELQLDADNVTRP--VGDYGGGQQQ--LVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 257669152 1007 LDARAAAIVMRTVRNTvdTGRTVVCTIHQPSIDIFEAFDELFLLKRGGEEI 1057
Cdd:TIGR02633 172 LTEKETEILLDIIRDL--KAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
853-1011 |
2.96e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 47.74 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDGnITISGYPKNQQTFARISGYCEQTdihsPHVTVY 928
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGllKPTSGkiIIDG-VDITDKKVKLSDIRKKVGLVFQY----PEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 929 ESLVYSAWLRLPKEVDKNKRKIF--IEEVMELVeltplrqalvGLPGES-------GLSTEQRKRLTIAVELVANPSIIF 999
Cdd:PRK13637 98 EETIEKDIAFGPINLGLSEEEIEnrVKRAMNIV----------GLDYEDykdkspfELSGGQKRRVAIAGVVAMEPKILI 167
|
170
....*....|..
gi 257669152 1000 MDEPTSGLDARA 1011
Cdd:PRK13637 168 LDEPTAGLDPKG 179
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
170-409 |
3.16e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.48 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 170 LNDVSGIVKPGRMALLLGPPSSGKTTL--LLALAGKLDQelkqtGRVTYNGHGMNEFVP---QRTAAYIGQNdVHIGEMT 244
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIanLLTRFYDIDE-----GEILLDGHDLRDYTLaslRNQVALVSQN-VHLFNDT 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 245 VRETFAYAArfQGVGSRYDMltelarrEKEANikpdpdidifmkaMSTAgektnvmTDYILKilgLEVCADTMVGDD--M 322
Cdd:PRK11176 433 IANNIAYAR--TEQYSREQI-------EEAAR-------------MAYA-------MDFINK---MDNGLDTVIGENgvL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 323 LrgiSGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHifNGTALI-----SLLQPApetfnlfDDI 397
Cdd:PRK11176 481 L---SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLViahrlSTIEKA-------DEI 548
|
250
....*....|..
gi 257669152 398 ILIAEGEIIYEG 409
Cdd:PRK11176 549 LVVEDGEIVERG 560
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
852-1032 |
3.44e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.40 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGAFRPGVLTALMGVSGAGKTTLM-------DVLAG-RKTGGYIDGNITISGYpKNQQTFARISGYCEQTDIHSP 923
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmnDKVSGyRYSGDVLLGGRSIFNY-RDVLEFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 924 hVTVYESLVysAWLRLPKEVDKNK-RKIFIEEVMELVELTPLRQALVGLPGEsgLSTEQRKRLTIAVELVANPSIIFMDE 1002
Cdd:PRK14271 115 -MSIMDNVL--AGVRAHKLVPRKEfRGVAQARLTEVGLWDAVKDRLSDSPFR--LSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190
....*....|....*....|....*....|
gi 257669152 1003 PTSGLDARAAAIVMRTVRNTVDTGRTVVCT 1032
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADRLTVIIVT 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
853-1033 |
3.45e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 46.80 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 853 LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI--DGN-IT-----------ISGYPKNQQTFARIsgyce 916
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGdpRATSGRIvfDGKdITdwqtakimreaVAIVPEGRRVFSRM----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 917 qtdihsphvTVYESLVYSAWLrlpkeVDKNKRKIFIEEVMELV-ELTPLRQALVGLpgesgLSTEQRKRLTIAVELVANP 995
Cdd:PRK11614 96 ---------TVEENLAMGGFF-----AERDQFQERIKWVYELFpRLHERRIQRAGT-----MSGGEQQMLAIGRALMSQP 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 257669152 996 SIIFMDEPTSGLdaraAAIVMRTVRNTVDTGRTVVCTI 1033
Cdd:PRK11614 157 RLLLLDEPSLGL----APIIIQQIFDTIEQLREQGMTI 190
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
825-1053 |
4.71e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 46.92 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 825 ITFDNV--VYSVDMPQEmieqgtqedrlvlLKGVNGA---FRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIDGNI 896
Cdd:PRK13645 7 IILDNVsyTYAKKTPFE-------------FKALNNTsltFKKNKVTCVIGTTGSGKSTMIQLTNGliiSETGQTIVGDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 897 TIsgyPKNQQTFARISGYCEQTDI--HSPHVTVYESLVYSAWLRLPKEVDKNKRKIF--IEEVMELVELTplRQALVGLP 972
Cdd:PRK13645 74 AI---PANLKKIKEVKRLRKEIGLvfQFPEYQLFQETIEKDIAFGPVNLGENKQEAYkkVPELLKLVQLP--EDYVKRSP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 973 GEsgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRT-VRNTVDTGRTVVCTIHQPSiDIFEAFDELFLLK 1051
Cdd:PRK13645 149 FE--LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLfERLNKEYKKRIIMVTHNMD-QVLRIADEVIVMH 225
|
..
gi 257669152 1052 RG 1053
Cdd:PRK13645 226 EG 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
168-409 |
4.76e-05 |
|
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: 45.38 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDqelKQTGRVTYNGHgmnefvpqrtaayigqnDVHIGEMTVRE 247
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLK---PQQGEITLDGV-----------------PVSDLEKALSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 248 TFAYaarfqgvgsrydmltelarrekeANIKPdpdidifmkamstagektnvmtdYILkilglevcaDTMVGDDMLRGIS 327
Cdd:cd03247 76 LISV-----------------------LNQRP-----------------------YLF---------DTTLRNNLGRRFS 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 328 GGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVN----SLRNYVHIFNGTALISLLQpapetfnlFDDIILIAEG 403
Cdd:cd03247 101 GGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSlifeVLKDKTLIWITHHLTGIEH--------MDKILFLENG 172
|
....*.
gi 257669152 404 EIIYEG 409
Cdd:cd03247 173 KIIMQG 178
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
968-1034 |
5.10e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.00 E-value: 5.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257669152 968 LVGLPGES------GLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1034
Cdd:PRK13651 151 LVGLDESYlqrspfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
862-1053 |
5.95e-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: 44.67 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 862 PGVLTALMGVSGAGKTTLMDVLAGRktggyidgnitisgYPKNQQTFARISGyceqtdihsphvtvyeslvysawlrlpk 941
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARE--------------LGPPGGGVIYIDG---------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 942 evdknkrkifieevmELVELTPLRQALVGLPGESGLSTEQRKRLTIAVELV--ANPSIIFMDEPTSGLDARAAAIVMRTV 1019
Cdd:smart00382 39 ---------------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALArkLKPDVLILDEITSLLDAEQEALLLLLE 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 257669152 1020 RNTVD------TGRTVVCTIHQPSI----DIFEAFDELFLLKRG 1053
Cdd:smart00382 104 ELRLLlllkseKNLTVILTTNDEKDlgpaLLRRRFDRRIVLLLI 147
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
160-418 |
6.08e-05 |
|
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: 47.49 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 160 VPNRKKKF---TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkLDQELKQTGRVTYNGHGMNEFVPQRTAAYIGQN 236
Cdd:TIGR03269 3 VKNLTKKFdgkEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRG-MDQYEPTSGRIIYHVALCEKCGYVERPSKVGEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 237 -DVHIGEMTVREtfayaARFQGVGS--RYDMLTELA--RREKEANIKPDPDIDIFMKAMSTAGEKTNVMTDYILKILGLE 311
Cdd:TIGR03269 82 cPVCGGTLEPEE-----VDFWNLSDklRRRIRKRIAimLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 312 VCADTMVgdDMLRGISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVhIFNGTALIsLLQPAPETF 391
Cdd:TIGR03269 157 QLSHRIT--HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAV-KASGISMV-LTSHWPEVI 232
|
250 260
....*....|....*....|....*...
gi 257669152 392 -NLFDDIILIAEGEIIYEGPRDHVVEFF 418
Cdd:TIGR03269 233 eDLSDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
850-1035 |
6.19e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 45.78 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 850 LVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIDGNITISGYPKNQQTFARiSGYCEQTDIHSP---H 924
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGemQTLEGKVHWSNKNESEPSFEATRSR-NRYSVAYAAQKPwllN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 925 VTVYESLVYSAwlrlpkEVDKNKRKIFIE--EVMELVELTPL-RQALVGLPGESgLSTEQRKRLTIAVELVANPSIIFMD 1001
Cdd:cd03290 93 ATVEENITFGS------PFNKQRYKAVTDacSLQPDIDLLPFgDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 257669152 1002 EPTSGLDARAAAIVMRT--VRNTVDTGRTVVCTIHQ 1035
Cdd:cd03290 166 DPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHK 201
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
865-1008 |
6.25e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 46.31 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 865 LTALMGVSGAGKTTLM-------DVLAGRKtggyIDGNITISGypknqqtfarisgyceqTDIHSPHVTVYE-----SLV 932
Cdd:PRK14243 38 ITAFIGPSGCGKSTILrcfnrlnDLIPGFR----VEGKVTFHG-----------------KNLYAPDVDPVEvrrriGMV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 933 YSAWLRLPKEVDKN-----KRKIFIEEVMELVElTPLRQALV-----GLPGESGLSTE--QRKRLTIAVELVANPSIIFM 1000
Cdd:PRK14243 97 FQKPNPFPKSIYDNiaygaRINGYKGDMDELVE-RSLRQAALwdevkDKLKQSGLSLSggQQQRLCIARAIAVQPEVILM 175
|
....*...
gi 257669152 1001 DEPTSGLD 1008
Cdd:PRK14243 176 DEPCSALD 183
|
|
| ABC_trans_N |
pfam14510 |
ABC-transporter N-terminal; This domain is found at the N-terminus of ABC-transporter proteins ... |
98-145 |
6.42e-05 |
|
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: 42.69 E-value: 6.42e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 257669152 98 HEKLLWKLKKRIDRVG-IDLPTIEVRFDHLKVEAeVHVGGRALPTFVNF 145
Cdd:pfam14510 33 LRKWLKNLRRLIDEDGyIKPRKLGVAFKNLTVSG-VGAGADYQPTVGNA 80
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
870-1010 |
7.18e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.43 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 870 GVSGAGKTTLMDVLAG---------RKTGGYIDgnitisgyPKNQQTFARIsGYCEQ-----TDIhsphvTVYESLVYSA 935
Cdd:NF033858 299 GSNGCGKSTTMKMLTGllpasegeaWLFGQPVD--------AGDIATRRRV-GYMSQafslyGEL-----TVRQNLELHA 364
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257669152 936 WL-RLPKEvDKNKRkifIEEVMELVELTPLRQALvglPGEsgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD--AR 1010
Cdd:NF033858 365 RLfHLPAA-EIAAR---VAEMLERFDLADVADAL---PDS--LPLGIRQRLSLAVAVIHKPELLILDEPTSGVDpvAR 433
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
852-1035 |
8.16e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.33 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 852 LLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIdgNITISGYPKNQQTFARISGYCEQTDIHSPHVTVYE 929
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGllNPEKGEI--LFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 930 SLVYsawlrlpkEVDKNKRKIFIEEVMELVELTPLRQALVGLpgesgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1009
Cdd:PRK13540 94 NCLY--------DIHFSPGAVGITELCRLFSLEHLIDYPCGL-----LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180
....*....|....*....|....*.
gi 257669152 1010 RAAAIVMRTVRNTVDTGRTVVCTIHQ 1035
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
966-1021 |
8.26e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 8.26e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 257669152 966 QALVGlPGESGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN 1021
Cdd:PTZ00265 570 ETLVG-SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINN 624
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
163-258 |
8.28e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 46.26 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 163 RKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQElkqTGRVTYNGHGMNEFVPQRtaayigqndvhIG- 241
Cdd:COG4152 10 RFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD---SGEVLWDGEPLDPEDRRR-----------IGy 75
|
90 100
....*....|....*....|....*.
gi 257669152 242 --E-------MTVRETFAYAARFQGV 258
Cdd:COG4152 76 lpEerglypkMKVGEQLVYLARLKGL 101
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
168-404 |
9.83e-05 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 44.49 E-value: 9.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkldQELKQTGRVTYNG-----HGMNEFVPQRTAAYIGQNDVHIGE 242
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAG---LEEPDSGSILIDGedltdLEDELPPLRRRIGMVFQDFALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 243 MTVREtfayaarfqgvgsrydmltelarrekeanikpdpdidifmkamstagektNVMtdyilkiLGLevcadtmvgddm 322
Cdd:cd03229 91 LTVLE--------------------------------------------------NIA-------LGL------------ 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 323 lrgiSGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNyVHIFNGTALISLLQPAPETFNLFDDIILIAE 402
Cdd:cd03229 102 ----SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKS-LQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
..
gi 257669152 403 GE 404
Cdd:cd03229 177 GK 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
964-1053 |
1.19e-04 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 44.71 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 964 LRQALVGLPGESGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVdTGRTVVCTIH--QPSIDif 1041
Cdd:cd03369 113 IYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEF-TNSTILTIAHrlRTIID-- 189
|
90
....*....|..
gi 257669152 1042 eaFDELFLLKRG 1053
Cdd:cd03369 190 --YDKILVMDAG 199
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
168-416 |
1.33e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 46.24 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALagkldqelkqtgrvtynghgmnefvpQRtaayigQNDVHIGEMTVRE 247
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLI--------------------------QR------HFDVSEGDIRFHD 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 248 TFAYAARFQGVGSRYDMLTE---LARREKEANI---KPDPDIDIFMKAMSTAgektNVMTDyilkILGLEVCADTMVGDd 321
Cdd:PRK10789 377 IPLTKLQLDSWRSRLAVVSQtpfLFSDTVANNIalgRPDATQQEIEHVARLA----SVHDD----ILRLPQGYDTEVGE- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 322 mlRGI--SGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHifNGTALI-----SLLQPApetfnlf 394
Cdd:PRK10789 448 --RGVmlSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIIsahrlSALTEA------- 516
|
250 260
....*....|....*....|..
gi 257669152 395 DDIILIAEGEIIYEGPRDHVVE 416
Cdd:PRK10789 517 SEILVMQHGHIAQRGNHDQLAQ 538
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
185-351 |
2.36e-04 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 45.09 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 185 LLGPPSSGKTTLLLALAGkLDQelKQTGRVTYNGH-----GMNEFVP--QRTAAYIGQNDV---HigeMTVRETFAYAAR 254
Cdd:COG4148 30 LFGPSGSGKTTLLRAIAG-LER--PDSGRIRLGGEvlqdsARGIFLPphRRRIGYVFQEARlfpH---LSVRGNLLYGRK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 255 FQGVGSRYDMLtelarrekeanikpdpdidifmkamstagektnvmtDYILKILGLEvcadtmvgdDML----RGISGGQ 330
Cdd:COG4148 104 RAPRAERRISF------------------------------------DEVVELLGIG---------HLLdrrpATLSGGE 138
|
170 180
....*....|....*....|..
gi 257669152 331 KKRVTTGE-MLVGPsRALFMDE 351
Cdd:COG4148 139 RQRVAIGRaLLSSP-RLLLMDE 159
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
798-1035 |
2.81e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 798 QSARSEGVV-EAGANKKRGMVLPFE------PHSITFDNVvYSVDMPQEMIEQGTQEDRLVLlKGVNgAFRpgvlTALMG 870
Cdd:PTZ00265 1192 DSKKTTAIVgETGSGKSTVMSLLMRfydlknDHHIVFKNE-HTNDMTNEQDYQGDEEQNVGM-KNVN-EFS----LTKEG 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 871 VSGAGKTTLmdvlagRKTGGYIDGNITISGYpkNQQTFARISGYCEQTDIHSpHVTVYESLVYSawlRLPKEVDKNKRKI 950
Cdd:PTZ00265 1265 GSGEDSTVF------KNSGKILLDGVDICDY--NLKDLRNLFSIVSQEPMLF-NMSIYENIKFG---KEDATREDVKRAC 1332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 951 FIEEVMELVELTPLR-QALVGLPGESgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTG-RT 1028
Cdd:PTZ00265 1333 KFAAIDEFIESLPNKyDTNVGPYGKS-LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKT 1411
|
....*..
gi 257669152 1029 VVCTIHQ 1035
Cdd:PTZ00265 1412 IITIAHR 1418
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
150-381 |
2.88e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 44.00 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 150 ADKFLNTLHL---VPNRKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkLDQelKQTGRVTYNG---HGMNE 223
Cdd:PRK10584 3 AENIVEVHHLkksVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAG-LDD--GSSGEVSLVGqplHQMDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 224 fvPQRTA------AYIGQNDVHIGEMTVRETFAYAARFQGvgsrydmltELARREKEANIKpdpdidifmkamstagekt 297
Cdd:PRK10584 80 --EARAKlrakhvGFVFQSFMLIPTLNALENVELPALLRG---------ESSRQSRNGAKA------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 298 nvmtdyILKILGLEVCADTMVGDdmlrgISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSL----RNYvh 373
Cdd:PRK10584 130 ------LLEQLGLGKRLDHLPAQ-----LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREH-- 196
|
....*...
gi 257669152 374 ifnGTALI 381
Cdd:PRK10584 197 ---GTTLI 201
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
327-414 |
3.07e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.73 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 327 SGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNYVHifNGTALISLLQPAPETFNLFDDIILIAEGEII 406
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR--DGATVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
....*...
gi 257669152 407 YEGPRDHV 414
Cdd:NF000106 224 ADGKVDEL 231
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
976-1052 |
3.28e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.73 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 976 GLSTEQRKRLTIAVEL----VANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPsiDIFEAFDELFLLK 1051
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP--ELAELADKLIHIK 154
|
.
gi 257669152 1052 R 1052
Cdd:cd03227 155 K 155
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1257-1372 |
3.46e-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: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 1257 IPYVLVQAIVYGLIVYAMIGFEWTAVKFFWYLFFMYGSFLTFTFYGMMAVAMTPNHHIASVVSSAFYGIWNLFSGFLIPR 1336
Cdd:pfam12698 211 LGDFLVGLLQLLIILLLLFGIGIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPL 290
|
90 100 110
....*....|....*....|....*....|....*.
gi 257669152 1337 PSMPVWWEWYYWLCPVAWTLYGLIASQFGDITEPMA 1372
Cdd:pfam12698 291 EDPPSFLQWIFSIIPFFSPIDGLLRLIYGDSLWEIA 326
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
25-214 |
3.68e-04 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 45.18 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 25 GREIFSRSSREEDDEEALRWAALEKLPTFDRLRKGILTASHAGGPINEIDIQKLGFQDTKKLLERLIKVGDDEHEKLLWK 104
Cdd:COG5635 23 TRLAIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAAALLARALSALLLVLLLLESLLLLLLLLLLLAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 105 LKKRIDRVGIDLPTIEVRFDHLKVEAEVHVGGRALPT--FVNFISNFADKFLNTLHLVPNRKKKFTILNDVSGIVKPGRM 182
Cdd:COG5635 103 ALLALLELAALLKAVLLSLSGGSDLVLLLSESDLLLAllILLLDADGLLVSLDDLYVPLNLLERIESLKRLELLEAKKKR 182
|
170 180 190
....*....|....*....|....*....|...
gi 257669152 183 ALLLGPPSSGKTTLLLALAGKL-DQELKQTGRV 214
Cdd:COG5635 183 LLILGEPGSGKTTLLRYLALELaERYLDAEDPI 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
168-409 |
4.11e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 44.67 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 168 TILNDVSGIVKPG-RMALLlGPPSSGKTTLLLALAGKLDQelkQTGRVTYnGHGMNefvpqrtAAYIGQ-NDVHIGEMTV 245
Cdd:COG0488 329 TLLDDLSLRIDRGdRIGLI-GPNGAGKSTLLKLLAGELEP---DSGTVKL-GETVK-------IGYFDQhQEELDPDKTV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 246 RETFAYAArfqgvgsryDMLTELARREkeanikpdpdidiFMKAMSTAGEKtnvmtdyilkilglevcADTMVGDdmlrg 325
Cdd:COG0488 397 LDELRDGA---------PGGTEQEVRG-------------YLGRFLFSGDD-----------------AFKPVGV----- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 326 ISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNyvhiFNGTAL-IS----LLQpapetfNLFDDIILI 400
Cdd:COG0488 433 LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD----FPGTVLlVShdryFLD------RVATRILEF 502
|
250
....*....|
gi 257669152 401 AEGEII-YEG 409
Cdd:COG0488 503 EDGGVReYPG 512
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
566-713 |
5.10e-04 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 42.88 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 566 ILMMLMFNGMSELSMTIaklpVFYKQRDLLFYpAWVYSLPPWLL---KI----PISFMEAALTTFITYYVIGFDPNVGRL 638
Cdd:COG0842 10 LAMSLLFTALMLTALSI----AREREQGTLER-LLVTPVSRLEIllgKVlaylLRGLLQALLVLLVALLFFGVPLRGLSL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257669152 639 FKQYILLVLMNQMASALFKMVAALGRNMIVANTFGAFAMLVFFALGGVVLSRDDIKKWWIWGYWISPIMYGQNAI 713
Cdd:COG0842 85 LLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEAL 159
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
164-219 |
6.13e-04 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 42.73 E-value: 6.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 257669152 164 KKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkldqELKQT-GRVTYNGH 219
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG----EERPTsGQVLVNGQ 64
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
179-256 |
8.10e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.59 E-value: 8.10e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257669152 179 PGRMALLLGPPSSGKTTLLLALAGKLDQELKQTGRVTYNGHGMNEFVPQRTAAYIGQNDVHIGEMTVRETFAYAARFQ 256
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLK 78
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
167-381 |
9.55e-04 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 43.21 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 167 FTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkLDQElkQTGRVTYNGHGMNEFVP--QRTAAYIGQNDV---Hig 241
Cdd:COG1118 15 FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAG-LETP--DSGRIVLNGRDLFTNLPprERRVGFVFQHYAlfpH-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 242 eMTVRETFAYAARfqgvgsrydmltelarrekeanIKPDPDIDIFMKAMStagektnvmtdyILKILGLEVCADtmvgdd 321
Cdd:COG1118 90 -MTVAENIAFGLR----------------------VRPPSKAEIRARVEE------------LLELVQLEGLAD------ 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257669152 322 mlR---GISGGQKKRVTTGEML-VGPsRALFMDEISTGLDSSTTYQIVNSLRNYVHIFNGTALI 381
Cdd:COG1118 129 --RypsQLSGGQRQRVALARALaVEP-EVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVF 189
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
326-409 |
1.01e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.54 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 326 ISGGQKKRV-TTGEMLVGPSRALF-MDEISTGLDSSTTYQIVNSLRNYVHifNGTALIsLLQPAPETFNLFDDIILIAE- 402
Cdd:cd03238 88 LSGGELQRVkLASELFSEPPGTLFiLDEPSTGLHQQDINQLLEVIKGLID--LGNTVI-LIEHNLDVLSSADWIIDFGPg 164
|
90
....*....|..
gi 257669152 403 -----GEIIYEG 409
Cdd:cd03238 165 sgksgGKVVFSG 176
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
177-270 |
1.22e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 41.71 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 177 VKPGRMALLLGPPSSGKTTLLLALAGKLDQElkqTGRVTYNGHGMNEfvpQRTA-----AYIG-QNDVHiGEMTVRETFA 250
Cdd:PRK13538 24 LNAGELVQIEGPNGAGKTSLLRILAGLARPD---AGEVLWQGEPIRR---QRDEyhqdlLYLGhQPGIK-TELTALENLR 96
|
90 100
....*....|....*....|
gi 257669152 251 YAARFQGVGSRYDMLTELAR 270
Cdd:PRK13538 97 FYQRLHGPGDDEALWEALAQ 116
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
858-1020 |
1.23e-03 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 42.40 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 858 GAFRPGVLTALMGVSGAGKTTLMDVLAGR--KTGGYID-GNITISgYpKNQQTFARISGyceqtdihsphvTVYEsLVYS 934
Cdd:cd03237 20 GSISESEVIGILGPNGIGKTTFIKMLAGVlkPDEGDIEiELDTVS-Y-KPQYIKADYEG------------TVRD-LLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 935 awlrlpKEVDKNKRKIFIEEVMELVELTPLRQALVglpgeSGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1014
Cdd:cd03237 85 ------ITKDFYTHPYFKTEIAKPLQIEQILDREV-----PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
....*.
gi 257669152 1015 VMRTVR 1020
Cdd:cd03237 154 ASKVIR 159
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
863-1008 |
1.59e-03 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 41.90 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 863 GVLTALMGVSGAGKTTLMDVLAGRKTGgyIDGNITISGYPKNQ---QTFARISGYCEQTDIHSPHVTVYESLVYSAWLRL 939
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTP--AHGHVWLDGEHIQHyasKEVARRIGLLAQNATTPGDITVQELVARGRYPHQ 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257669152 940 P-----KEVDKNKrkifIEEVMELVELTPLRQALVglpgeSGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1008
Cdd:PRK10253 111 PlftrwRKEDEEA----VTKAMQATGITHLADQSV-----DTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
965-1023 |
1.93e-03 |
|
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: 42.36 E-value: 1.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257669152 965 RQAL--VGLPGESG------LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDaraaaivmRTVRNTV 1023
Cdd:COG4172 406 AEALeeVGLDPAARhrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALD--------VSVQAQI 464
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
168-204 |
1.96e-03 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 40.12 E-value: 1.96e-03
10 20 30
....*....|....*....|....*....|....*..
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKL 204
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGEL 50
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
844-1008 |
2.58e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 41.24 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 844 GTQEDRLVLLKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI--DGNiTISGYPKnqQTFARISGYCEQTd 919
Cdd:PRK10247 14 GYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASliSPTSGTLlfEGE-DISTLKP--EIYRQQVSYCAQT- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 920 ihsPHV---TVYESLVYSAWLRlpkeVDKNKRKIFIEEVMELveltplrqalvGLPGE------SGLSTEQRKRLTIAVE 990
Cdd:PRK10247 90 ---PTLfgdTVYDNLIFPWQIR----NQQPDPAIFLDDLERF-----------ALPDTiltkniAELSGGEKQRISLIRN 151
|
170
....*....|....*...
gi 257669152 991 LVANPSIIFMDEPTSGLD 1008
Cdd:PRK10247 152 LQFMPKVLLLDEITSALD 169
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
985-1038 |
2.58e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.61 E-value: 2.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 257669152 985 LTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1038
Cdd:pfam13304 248 LAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLL 301
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
156-405 |
2.86e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 42.12 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 156 TLHLVPNRKKKFtiLNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLdqELKQTGRVTYNGHGMNEFVPQRTaayIGQ 235
Cdd:TIGR02633 264 TCWDVINPHRKR--VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY--PGKFEGNVFINGKPVDIRNPAQA---IRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 236 NDVHIGEMTVRETFAyaaRFQGVGSRYdMLTELARREKEANIKPDPDIDIFMKAMSTAGEKTnvmTDYILKILGLevcad 315
Cdd:TIGR02633 337 GIAMVPEDRKRHGIV---PILGVGKNI-TLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKT---ASPFLPIGRL----- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 316 tmvgddmlrgiSGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQI---VNSLRNyvhifNGTALISLLQPAPETFN 392
Cdd:TIGR02633 405 -----------SGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIyklINQLAQ-----EGVAIIVVSSELAEVLG 468
|
250
....*....|...
gi 257669152 393 LFDDIILIAEGEI 405
Cdd:TIGR02633 469 LSDRVLVIGEGKL 481
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
835-1060 |
3.23e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 41.56 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 835 DMPQ---EMIEQGTQEDRLVL-------LKGVNGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIDG-NITIS 899
Cdd:PRK10070 16 EHPQrafKYIEQGLSKEQILEktglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRliEPTRGqvLIDGvDIAKI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 900 GYPKNQQTFARISGYCEQTDIHSPHVTVYESLVYSAWLrlpKEVDKNKRKifiEEVMELVELTPLRQALVGLPGEsgLST 979
Cdd:PRK10070 96 SDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMEL---AGINAEERR---EKALDALRQVGLENYAHSYPDE--LSG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 980 EQRKRLTIAVELVANPSIIFMDEPTSGLDAraaaiVMRT------VRNTVDTGRTVVCTIHqpsiDIFEAF---DELFLL 1050
Cdd:PRK10070 168 GMRQRVGLARALAINPDILLMDEAFSALDP-----LIRTemqdelVKLQAKHQRTIVFISH----DLDEAMrigDRIAIM 238
|
250
....*....|
gi 257669152 1051 KrGGEEIYVG 1060
Cdd:PRK10070 239 Q-NGEVVQVG 247
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
169-381 |
3.65e-03 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 40.57 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 169 ILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkLDQelKQTGRVTYNGHGMNEFVPQRTAayigqndvhigEMTVRET 248
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGG-LDT--PTSGDVIFNGQPMSKLSSAAKA-----------ELRNQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 249 -FAYaaRFQGVGSRYDMLTELARREKEANIKPDpdidifmKAMSTAGEktnvmtdyILKILGLEVCADTMVGDdmlrgIS 327
Cdd:PRK11629 90 gFIY--QFHHLLPDFTALENVAMPLLIGKKKPA-------EINSRALE--------MLAAVGLEHRANHRPSE-----LS 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 257669152 328 GGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNyVHIFNGTALI 381
Cdd:PRK11629 148 GGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGE-LNRLQGTAFL 200
|
|
| GntK |
COG3265 |
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ... |
868-894 |
4.02e-03 |
|
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442496 [Multi-domain] Cd Length: 164 Bit Score: 39.73 E-value: 4.02e-03
10 20
....*....|....*....|....*..
gi 257669152 868 LMGVSGAGKTTLMDVLAGRKTGGYIDG 894
Cdd:COG3265 6 VMGVSGSGKSTVGQALAERLGWPFIDG 32
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
160-271 |
4.46e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 40.69 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 160 VPNRkkkftiLNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQElkqtGRVTYNGHGMNEFVPQRTA---AYIGQN 236
Cdd:PRK03695 8 VSTR------LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS----GSIQFAGQPLEAWSAAELArhrAYLSQQ 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 257669152 237 DVHIGEMTVretFAYAARFQGVGSR----YDMLTELARR 271
Cdd:PRK03695 78 QTPPFAMPV---FQYLTLHQPDKTRteavASALNEVAEA 113
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
160-204 |
4.66e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 40.33 E-value: 4.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 257669152 160 VPNRKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKL 204
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL 80
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
546-714 |
5.33e-03 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 40.84 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 546 TEMQKKTEVDGSLYtGALFFILMMLMFNGMSELSMTIA--KLPVFYKQRDLLFYPAWVYslppWLLKIPISFMEAALTTF 623
Cdd:pfam12698 148 ESTPLFNPQSGYAY-YLVGLILMIIILIGAAIIAVSIVeeKESRIKERLLVSGVSPLQY----WLGKILGDFLVGLLQLL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 624 IT-YYVIGFDPNVGRLFKQYILLVLMNQMASALFKMVAALGRNMIVANTFGAFAMLVFFALGGVVLSRDDIKKWWIWGYW 702
Cdd:pfam12698 223 IIlLLLFGIGIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFS 302
|
170
....*....|..
gi 257669152 703 ISPIMYGQNAIL 714
Cdd:pfam12698 303 IIPFFSPIDGLL 314
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
385-428 |
5.90e-03 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 40.66 E-value: 5.90e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 257669152 385 QPAPETFNLFDDIILIAE-GEIIYEGPRDHVVEFFETMGFKCPPR 428
Cdd:pfam19055 2 QPSYTLFKMFDDLILLAKgGLTVYHGPVKKVEEYFAGLGINVPER 46
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
858-1021 |
6.53e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 858 GAFRPG-VLTALmGVSGAGKTTLMDVLAGR--KTGGYIDGNITISgYpKNQqtfaRISGyceqtdihSPHVTVYEslvys 934
Cdd:PRK13409 360 GEIYEGeVIGIV-GPNGIGKTTFAKLLAGVlkPDEGEVDPELKIS-Y-KPQ----YIKP--------DYDGTVED----- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 935 aWLRlpKEVDKNKRKIFIEEVMELVELTPLRQALVglpgeSGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1014
Cdd:PRK13409 420 -LLR--SITDDLGSSYYKSEIIKPLQLERLLDKNV-----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
....*..
gi 257669152 1015 VMRTVRN 1021
Cdd:PRK13409 492 VAKAIRR 498
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
326-426 |
6.88e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 40.03 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 326 ISGGQKKRVTTGEMLVGPSRALFMDEISTGLDSSTTYQIVNSLRNyVHIFNGTALISLLQPAPETFNLFDDIILIAEGEI 405
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKE-LHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
90 100
....*....|....*....|....
gi 257669152 406 IYEGPRDHV---VEFFETMGFKCP 426
Cdd:PRK13637 224 ELQGTPREVfkeVETLESIGLAVP 247
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
161-247 |
6.94e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 40.06 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 161 PNRKKKFTILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGKLDQElkqTGRVTYNGhgmnefvpqRTAAYIGQNDVHI 240
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT---SGRVEVNG---------RVSALLELGAGFH 100
|
....*..
gi 257669152 241 GEMTVRE 247
Cdd:COG1134 101 PELTGRE 107
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
168-228 |
8.78e-03 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 40.56 E-value: 8.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257669152 168 TILNDVSGIVKPGRMALLLGPPSSGKTTLLLALAGkldqeL--KQTGRVTYNGHG--MneFVPQR 228
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-----LwpYGSGRIARPAGArvL--FLPQR 434
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
326-416 |
8.82e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 39.59 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257669152 326 ISGGQKKRVTTGEML-VGPSRALFmDEISTGLD---SSTTYQIVNSLRNyvhifNGT-ALISLLQPAPETFNLfDDIILI 400
Cdd:PRK13632 143 LSGGQKQRVAIASVLaLNPEIIIF-DESTSMLDpkgKREIKKIMVDLRK-----TRKkTLISITHDMDEAILA-DKVIVF 215
|
90
....*....|....*.
gi 257669152 401 AEGEIIYEGPRDHVVE 416
Cdd:PRK13632 216 SEGKLIAQGKPKEILN 231
|
|
| HypB |
COG0378 |
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ... |
185-209 |
9.40e-03 |
|
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440147 [Multi-domain] Cd Length: 200 Bit Score: 38.89 E-value: 9.40e-03
10 20
....*....|....*....|....*
gi 257669152 185 LLGPPSSGKTTLLLALAGKLDQELK 209
Cdd:COG0378 18 LMGSPGSGKTTLLEKTIRALKDRLR 42
|
|
| |
