|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-1426 |
0e+00 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 1933.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 17 TGRESFARPSnaeTVEQDEEDLRWAAIGRLPsqrqgTHNAiLRRSQTQTQTSGYADGNVVQT--IDVKKLDRADREMLVR 94
Cdd:PLN03140 29 GGSQSRRRTS---SVDEDEEALKWAAIEKLP-----TYSR-LRTSIMKSFVENDVYGNQLLHkeVDVTKLDGNDRQKFID 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 95 QALATSDQDNFKLLSAIKERLDRVGMEVPKIEVRFENLNIEADVQAGTRALPTLVNVSRDFFERCLSSLRIIKPRKHKLN 174
Cdd:PLN03140 100 MVFKVAEEDNEKFLKKFRNRIDRVGIKLPTVEVRFEHLTVEADCYIGSRALPTLPNAARNIAESALGMLGINLAKKTKLT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSLKKTGNITYNGENLNKFHVKRTSAYISQTDNHIAELTVRET 254
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKVSGEITYNGYRLNEFVPRKTSAYISQNDVHVGVMTVKET 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 255 LDFAARCQGASEGFaGYMKDLTRLEKERGIRPSSEIDAFMKAASVKGEKHSVSTDYVLKVLGLDVCSDTMVGNDMMRGVS 334
Cdd:PLN03140 260 LDFSARCQGVGTRY-DLLSELARREKDAGIFPEAEVDLFMKATAMEGVKSSLITDYTLKILGLDICKDTIVGDEMIRGIS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 335 GGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMALLQPAPETFDLFDDLILLSEGYMVY 414
Cdd:PLN03140 339 GGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFDLFDDIILLSEGQIVY 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 415 QGPREDVIAFFESLGFRLPPRKGVADFLQEVTSKKDQAQYWADPSKPYQFIPVSDIAAAFRNSKYGHAADSKLAAPFDKK 494
Cdd:PLN03140 419 QGPRDHILEFFESCGFKCPERKGTADFLQEVTSKKDQEQYWADRNKPYRYISVSEFAERFKSFHVGMQLENELSVPFDKS 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 495 SADPSALCRTKFAISGWENLKVCFVRELLLIKRHKFLYTFRTCQVGFVGLVTATVFLKTRLHPTSEQFGNEYLSCLFFGL 574
Cdd:PLN03140 499 QSHKAALVFSKYSVPKMELLKACWDKEWLLMKRNAFVYVFKTVQIIIVAAIASTVFLRTEMHTRNEEDGALYIGALLFSM 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 575 VHMMFNGFSELPLMISRLPVFYKQRDNSFHPAWSWSIASWLLRVPYSVLEAVVWSGVVYFTVGLAPSAGRFFRYMLLLFS 654
Cdd:PLN03140 579 IINMFNGFAELALMIQRLPVFYKQRDLLFHPPWTFTLPTFLLGIPISIIESVVWVVITYYSIGFAPEASRFFKQLLLVFL 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 655 VHQMALGLFRMMASLARDMVIANTFGSAAILIVFLLGGFVIPKADIKPWWVWGFWVSPLSYGQRAIAVNEFTATRWMT-P 733
Cdd:PLN03140 659 IQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEWAYWVSPLSYGFNALAVNEMFAPRWMNkM 738
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 734 SAISDTTIGLNLLKLRSFPTNDYWYWIGIAVLIGYAILFNNVVTLALAYLNPLRKARAVVLDDPNEE----------TAL 803
Cdd:PLN03140 739 ASDNSTRLGTAVLNIFDVFTDKNWYWIGVGALLGFTILFNVLFTLALTYLNPLGKKQAIISEETAEEmegeedsiprSLS 818
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 804 VADANQV---------------------------ISEKKGMILPFKPLTMTFHNVNYYVDMPKEMRSQGVPETRLQLLSN 856
Cdd:PLN03140 819 SADGNNTrevaiqrmsnpeglsknrdssleaangVAPKRGMVLPFTPLAMSFDDVNYFVDMPAEMKEQGVTEDRLQLLRE 898
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 857 VSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGGYTEGDIRISGHPKEQQTFARISGYVEQNDIHSPQVTVEESLWFSA 936
Cdd:PLN03140 899 VTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRESLIYSA 978
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 937 SLRLPKEITKEQKKEFVEQVMRLVELDTLRYALVGLPGTTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIV 1016
Cdd:PLN03140 979 FLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIV 1058
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1017 MRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYGGKLGTHSQVLVDYFQGINGVPPISSGYNPATWMLEV 1096
Cdd:PLN03140 1059 MRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYSGPLGRNSHKIIEYFEAIPGVPKIKEKYNPATWMLEV 1138
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1097 TTPALEEKYNMEFADLYKKSDQFREVEANIKQLSVPPEGSEPISFTSRYSQNQLSQFLLCLWKQNLVYWRSPEYNLVRLV 1176
Cdd:PLN03140 1139 SSLAAEVKLGIDFAEHYKSSSLYQRNKALVKELSTPPPGASDLYFATQYSQSTWGQFKSCLWKQWWTYWRSPDYNLVRFF 1218
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1177 FTTIAAFILGTVFWDIGSKRTSSQDLITVMGALYSACLFLGVSNASSVQPIVSIERTVFYREKAAGMYAPIPYAAAQGLV 1256
Cdd:PLN03140 1219 FTLAAALMVGTIFWKVGTKRSNANDLTMVIGAMYAAVLFVGINNCSTVQPMVAVERTVFYRERAAGMYSALPYAIAQVVC 1298
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1257 EIPYILTQTILYGVITYFTIGFERTFSKFVLYLVFMFLTFTYFTFYGMMAVGLTPNQHLAAVISSAFYSLWNLLSGFLVQ 1336
Cdd:PLN03140 1299 EIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMMTVSLTPNQQVAAIFAAAFYGLFNLFSGFFIP 1378
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1337 KPLIPVWWIWFYYICPVAWTLQGVILSQLGDVESMINEP--LFHGTVKEFIEYYFGYKPNMIGVSAAVLVGFCALFFSAF 1414
Cdd:PLN03140 1379 RPKIPKWWVWYYWICPVAWTVYGLIVSQYGDVEDTIKVPggAPDPTIKWYIQDHYGYDPDFMGPVAAVLVGFTVFFAFIF 1458
|
1450
....*....|..
gi 330253231 1415 ALSVKYLNFQRR 1426
Cdd:PLN03140 1459 AFCIRTLNFQTR 1470
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
103-1394 |
0e+00 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 1202.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 103 DNFKLLSAIKERLDRVGMEVP--KIEVRFENLNIEAdVQAGTRALPTLVNVSRDFFERclsSLRIIKPRKH--KLNILKD 178
Cdd:TIGR00956 4 NAKAWVKNFRKLIDSDPIYYKpyKLGVAYKNLSAYG-VAADSDYQPTFPNALLKILTR---GFRKLKKFRDtkTFDILKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 179 ISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSLK-KTGNITYNGENLNKF--HVKRTSAYISQTDNHIAELTVRETL 255
Cdd:TIGR00956 80 MDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIgVEGVITYDGITPEEIkkHYRGDVVYNAETDVHFPHLTVGETL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 256 DFAARCQGASEGFAGymkdLTRLEKERGIRpsseidafmkaasvkgekhsvstDYVLKVLGLDVCSDTMVGNDMMRGVSG 335
Cdd:TIGR00956 160 DFAARCKTPQNRPDG----VSREEYAKHIA-----------------------DVYMATYGLSHTRNTKVGNDFVRGVSG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 336 GQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMALLQPAPETFDLFDDLILLSEGYMVYQ 415
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYF 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 416 GPREDVIAFFESLGFRLPPRKGVADFLQEVTSKKdQAQYWADPSKPYqFIPVSDIAAAFRNSKYGHAADSKLAAPFDKKS 495
Cdd:TIGR00956 293 GPADKAKQYFEKMGFKCPDRQTTADFLTSLTSPA-ERQIKPGYEKKV-PRTPQEFETYWRNSPEYAQLMKEIDEYLDRCS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 496 ADPS---------------ALCRTKFAISGWENLKVCFVRELLLIKRHKFLYTFRTCQVGFVGLVTATVFLKTrlhPTSE 560
Cdd:TIGR00956 371 ESDTkeayreshvakqskrTRPSSPYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNL---PKNT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 561 QFGNEYLSCLFFGLVHMMFNGFSELPLMISRLPVFYKQRDNSFHPAWSWSIASWLLRVPYSVLEAVVWSGVVYFTVGLAP 640
Cdd:TIGR00956 448 SDFYSRGGALFFAILFNAFSSLLEIASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRR 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 641 SAGRFFRYMLLLFSVHQMALGLFRMMASLARDMVIANTFGSAAILIVFLLGGFVIPKADIKPWWVWGFWVSPLSYGQRAI 720
Cdd:TIGR00956 528 TAGRFFFYLLILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESL 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 721 AVNEFTATRW----MTPSAISDTTIGLN---LLKLRSFPTNDY----------------WYWIGIAVLIGYAILFNNVVT 777
Cdd:TIGR00956 608 MVNEFHGRRFecsqYVPSGGGYDNLGVTnkvCTVVGAEPGQDYvdgddylklsfqyynsHKWRNFGIIIGFTVFFFFVYI 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 778 LALAYLNPLRKARAVVL----DDPNEETALVADANQVISEKKGMILPFKPLTMTFHNVNYYVDMPKE-------MRS--- 843
Cdd:TIGR00956 688 LLTEFNKGAKQKGEILVfrrgSLKRAKKAGETSASNKNDIEAGEVLGSTDLTDESDDVNDEKDMEKEsgedifhWRNlty 767
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 844 -QGVPETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGGYTEGDIRISGHPKEQQTFARISGYVEQNDIH 922
Cdd:TIGR00956 768 eVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLH 847
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 923 SPQVTVEESLWFSASLRLPKEITKEQKKEFVEQVMRLVELDTLRYALVGLPGtTGLSTEQRKRLTIAVELVANP-SIIFM 1001
Cdd:TIGR00956 848 LPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPG-EGLNVEQRKRLTIGVELVAKPkLLLFL 926
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1002 DEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYGGKLGTHSQVLVDYFQgINGVP 1081
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGGQTVYFGDLGENSHTIINYFE-KHGAP 1005
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1082 PISSGYNPATWMLEVTTPALEEKYNMEFADLYKKSDQFREVEANIKQLSVPPEGSEPISFT---SRYSQNQLSQFLLCLW 1158
Cdd:TIGR00956 1006 KCPEDANPAEWMLEVIGAAPGAHANQDYHEVWRNSSEYQAVKNELDRLEAELSKAEDDNDPdalSKYAASLWYQFKLVLW 1085
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1159 KQNLVYWRSPEYNLVRLVFTTIAAFILGTVFWDIGskrTSSQDLITVMGALYSACLFLGVSNASSVQPIVSIERTVFYRE 1238
Cdd:TIGR00956 1086 RTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVG---TSLQGLQNQMFAVFMATVLFNPLIQQYLPPFVAQRDLYEVRE 1162
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1239 KAAGMYAPIPYAAAQGLVEIPYILTQTILYGVITYFTIGFERTFSK-------FVLYLVFMFLTFTYFTFYGMMAVGLTP 1311
Cdd:TIGR00956 1163 RPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFYWNASKtgqvherGVLFWLLSTMFFLYFSTLGQMVISFNP 1242
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1312 NQHLAAVISSAFYSLWNLLSGFLVQKPLIPVWWIWFYYICPVAWTLQGVILSQLGDVESMINEPLFHG-----------T 1380
Cdd:TIGR00956 1243 NADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLADVPVTCKVKELLTfnppsgqtcgeY 1322
|
1370
....*....|....
gi 330253231 1381 VKEFIEYYFGYKPN 1394
Cdd:TIGR00956 1323 MKPYLENAGGYLLN 1336
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
850-1369 |
1.65e-102 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 340.87 E-value: 1.65e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 850 RLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGGYT-EGDIRISGHPKEQQTFARISGYVEQNDIHSPQVTV 928
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKgSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 929 EESLWFSASLRLPKEITKEQKKEFVEQVMRLVELDTLRYALVGLPGTT-GLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1007
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRVkGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1008 LDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKrGGQVIYggkLGTHSQvLVDYFQgiNGVPPISSGY 1087
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMA-EGRVAY---LGSPDQ-AVPFFS--DLGHPCPENY 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1088 NPATWMLEV--TTPALEEKYNMEFA---DLYKKSDQFREVEANIKQLSVP----PEGSEPISFTsRYSQNQLSQFLLCLW 1158
Cdd:TIGR00955 270 NPADFYVQVlaVIPGSENESRERIEkicDSFAVSDIGRDMLVNTNLWSGKagglVKDSENMEGI-GYNASWWTQFYALLK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1159 KQNLVYWRSPEYNLVRLVFTTIAAFILGTVFWDIGSKRTSSQDlitVMGALYSACLFLGVSNASSVQPIVSIERTVFYRE 1238
Cdd:TIGR00955 349 RSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQN---INGALFLFLTNMTFQNVFPVINVFTAELPVFLRE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1239 KAAGMYAPIPYAAAQGLVEIPYILTQTILYGVITYFTIGFERTFSKFVLYLVFMFLTFTYFTFYGMMAVGLTPNQHLAAV 1318
Cdd:TIGR00955 426 TRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALT 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 330253231 1319 ISSAFYSLWNLLSGFLVQKPLIPVWWIWFYYICPVAWTLQGVILSQLGDVE 1369
Cdd:TIGR00955 506 VGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVD 556
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
823-1061 |
1.79e-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: 1.79e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 823 PLTMTFHNVNYYVDMPKEmrsqgvpetRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGGYTEGDIRISGH 902
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGG---------KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 903 PKEQqTFARISGYVEQNDIHSPQVTVEESLWFSASLRlpkeitkeqkkefveqvmrlveldtlryalvglpgttGLSTEQ 982
Cdd:cd03232 72 PLDK-NFQRSTGYVEQQDVHSPNLTVREALRFSALLR-------------------------------------GLSVEQ 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330253231 983 RKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYGG 1061
Cdd:cd03232 114 RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRGGKTVYFG 192
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
823-1061 |
1.26e-79 |
|
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: 260.56 E-value: 1.26e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 823 PLTMTFHNVNYYVDmpkemrsQGVPETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGGYTEGDIRISGH 902
Cdd:cd03213 1 GVTLSFRNLTVTVK-------SSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 903 PKEQQTFARISGYVEQNDIHSPQVTVEESLWFSASLRlpkeitkeqkkefveqvmrlveldtlryalvglpgttGLSTEQ 982
Cdd:cd03213 74 PLDKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------------GLSGGE 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330253231 983 RKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYGG 1061
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQ-GRVIYFG 194
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
155-416 |
2.65e-73 |
|
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: 242.55 E-value: 2.65e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 155 FFERCLSslRIIKPRKHKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSLKKTGNITYNGENLNKFHVK- 233
Cdd:cd03233 4 LSWRNIS--FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYKEFAEKy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 234 -RTSAYISQTDNHIAELTVRETLDFAARCQgasegfagymkdltrlekergirpsseidafmkaasvkgekhsvstdyvl 312
Cdd:cd03233 82 pGEIIYVSEEDVHFPTLTVRETLDFALRCK-------------------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 313 kvlgldvcsdtmvGNDMMRGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMALLQ 392
Cdd:cd03233 112 -------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQ 178
|
250 260
....*....|....*....|....
gi 330253231 393 PAPETFDLFDDLILLSEGYMVYQG 416
Cdd:cd03233 179 ASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
167-772 |
3.32e-70 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 248.42 E-value: 3.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 167 KPRKHklnILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSLKKTGNITYNGENLNKFHVKRTSAYISQTDNHI 246
Cdd:TIGR00955 35 RPRKH---LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 247 AELTVRETLDFAARCQgasegfagyMKDLTrlekergirpsseidafmkaaSVKGEKHSVstDYVLKVLGLDVCSDTMVG 326
Cdd:TIGR00955 112 PTLTVREHLMFQAHLR---------MPRRV---------------------TKKEKRERV--DEVLQALGLRKCANTRIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 327 N-DMMRGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRnfvHLMDA--TVLMALLQPAPETFDLFDD 403
Cdd:TIGR00955 160 VpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLK---GLAQKgkTIICTIHQPSSELFELFDK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 404 LILLSEGYMVYQGPREDVIAFFESLGFRLPPRKGVADFLQEV--TSKKDQAQYWADPSKPYQFIPVSDIAaafRNSKYGH 481
Cdd:TIGR00955 237 IILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVlaVIPGSENESRERIEKICDSFAVSDIG---RDMLVNT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 482 AADSKLAAPFDKKSADPSalcRTKFAISGWENLKVCFVRELLLIKRHKFLYTFRTCQVGFVGLVTATVFLKTRLHPTSEQ 561
Cdd:TIGR00955 314 NLWSGKAGGLVKDSENME---GIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 562 fgnEYLSCLFFGLVHMMF-NGFSELPLMISRLPVFYKQRDNSFHPAWSWSIASWLLRVPYSVLEAVVWSGVVYFTVGLAP 640
Cdd:TIGR00955 391 ---NINGALFLFLTNMTFqNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 641 SAGRFFRYMLLLFSVHQMALGLFRMMASLARDMVIANTFGSAAILIVFLLGGFVIPKADIKPWWVWGFWVSPLSYGQRAI 720
Cdd:TIGR00955 468 GATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGL 547
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 330253231 721 AVNEFTATRWMTPSAISDTTI----GLNLLKLRSFPTNDYW--YWIGIAVLIGYAILF 772
Cdd:TIGR00955 548 LINQWSDVDNIECTSANTTGPcpssGEVILETLSFRNADLYldLIGLVILIFFFRLLA 605
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
851-1061 |
7.44e-59 |
|
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: 202.12 E-value: 7.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 851 LQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGGY-TEGDIRISGHPKEQQTFARISGYVEQNDIHSPQVTVE 929
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGtTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 930 ESLWFSASLRLPKEITKEQKKEFVEQV-MRLVELDTLRYALVglpgtTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1008
Cdd:cd03234 100 ETLTYTAILRLPRKSSDAIRKKRVEDVlLRDLALTRIGGNLV-----KGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 330253231 1009 DARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGqVIYGG 1061
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGE-IVYSG 226
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
1156-1361 |
2.08e-55 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 191.72 E-value: 2.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1156 CLWKQNLVYWRSPEYNLVRLVFTTIAAFILGTVFWDIGSkrtsSQDLITVMGALYSACLFLGVSNASSVQPIVSIERTVF 1235
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGN----QQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1236 YREKAAGMYAPIPYAAAQGLVEIPYILTQTILYGVITYFTIGFERTFSKFVLYLVFMFLTFTYFTFYGMMAVGLTPNQHL 1315
Cdd:pfam01061 77 YRELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFED 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 330253231 1316 AAVISSAFYSLWNLLSGFLVQKPLIPVWWIWFYYICPVAWTLQGVI 1361
Cdd:pfam01061 157 ASQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALR 202
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
823-1425 |
7.24e-54 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 200.88 E-value: 7.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 823 PLTMTFHNVNYYVDMPKeMRSQGVPETRL-----------------QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLA 885
Cdd:PLN03211 37 PITLKFMDVCYRVKFEN-MKNKGSNIKRIlghkpkisdetrqiqerTILNGVTGMASPGEILAVLGPSGSGKSTLLNALA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 886 GRKTGGYTEGDIRISGHPKEQQTFARIsGYVEQNDIHSPQVTVEESLWFSASLRLPKEITKEQKKEFVEQVMRLVELDTL 965
Cdd:PLN03211 116 GRIQGNNFTGTILANNRKPTKQILKRT-GFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKC 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 966 RYALVGLPGTTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAF 1045
Cdd:PLN03211 195 ENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1046 DELLLMKRgGQVIYGGKLgthSQVLVdYFQGINGVPPISsgYNPATWMLEVTT-----------------PALEEKYNME 1108
Cdd:PLN03211 275 DSVLVLSE-GRCLFFGKG---SDAMA-YFESVGFSPSFP--MNPADFLLDLANgvcqtdgvserekpnvkQSLVASYNTL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1109 FADLYK---KSDQFREVEANIKQLSVPPE--GSEPISFTSRYSQnqlsqflLCLWKQNLVYWRSPE-YNLVRlVFTTIAA 1182
Cdd:PLN03211 348 LAPKVKaaiEMSHFPQANARFVGSASTKEhrSSDRISISTWFNQ-------FSILLQRSLKERKHEsFNTLR-VFQVIAA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1183 FILGTVFWdigsKRTSSQDLITVMGALYSACLFLGVSNASSVQPIVSIERTVFYREKAAGMYAPIPYAAAQGLVEIPYIL 1262
Cdd:PLN03211 420 ALLAGLMW----WHSDFRDVQDRLGLLFFISIFWGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMEL 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1263 TQTILYGVITYFTIGFERTFSKFVLYLVFMFLTFTYFTFYGMMAVGLTPNQHLAAVISSAFYSLWNLLSGFLVQKplIPV 1342
Cdd:PLN03211 496 ILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYVHK--LPS 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1343 WWIWFYYICPVAWTLQGVILSQLGD---VESMINEPLFHGTVK---EFIEyyfgykPNMIG-VSAAVLVGFCALFFSAFA 1415
Cdd:PLN03211 574 CMAWIKYISTTFYSYRLLINVQYGEgkrISSLLGCSLPHGSDRascKFVE------EDVAGqISPATSVSVLIFMFVGYR 647
|
650
....*....|
gi 330253231 1416 LsVKYLNFQR 1425
Cdd:PLN03211 648 L-LAYLALRR 656
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
167-416 |
3.81e-49 |
|
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: 173.12 E-value: 3.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 167 KPRKHKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLdKSLKKTGNITYNGENLNKFHVKRTSAYISQTDNHI 246
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRR-TGLGVSGEVLINGRPLDKRSFRKIIGYVPQDDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 247 AELTVRETLDFAARCqgasegfagymkdltrlekergirpsseidafmkaasvkgekhsvstdyvlkvlgldvcsdtmvg 326
Cdd:cd03213 95 PTLTVRETLMFAAKL----------------------------------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 327 ndmmRGVSGGQRKRVTTG-EMTVGPRkTLFMDEISTGLDSSTTFQIVKCIRNFVHlMDATVLMALLQPAPETFDLFDDLI 405
Cdd:cd03213 110 ----RGLSGGERKRVSIAlELVSNPS-LLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPSSEIFELFDKLL 183
|
250
....*....|.
gi 330253231 406 LLSEGYMVYQG 416
Cdd:cd03213 184 LLSQGRVIYFG 194
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
517-723 |
3.04e-46 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 165.14 E-value: 3.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 517 CFVRELLLIKRHKFLYTFRTCQVGFVGLVTATVFLKTRlhptSEQFGNEYLSCLFFGLVHMMFNGFSEL-PLMISRLPVF 595
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG----NQQGGLNRPGLLFFSILFNAFSALSGIsPVFEKERGVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 596 YKQRDNSFHPAWSWSIASWLLRVPYSVLEAVVWSGVVYFTVGLAPSAGRFFRYMLLLFSVHQMALGLFRMMASLARDMVI 675
Cdd:pfam01061 77 YRELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFED 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 330253231 676 ANTFGSAAILIVFLLGGFVIPKADIKPWWVWGFWVSPLSYGQRAIAVN 723
Cdd:pfam01061 157 ASQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
167-416 |
9.14e-45 |
|
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: 161.67 E-value: 9.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 167 KPRKHKLnILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSLKKTGNITYNGENLNKFHVKRTSAYISQTDNHI 246
Cdd:cd03234 15 NWNKYAR-ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 247 AELTVRETLDFAARCQgasegfagymkdLTRLEKERGIRPSSEidafmkaasvkgekhsvstdyvlkVLGLDVCSDTMVG 326
Cdd:cd03234 94 PGLTVRETLTYTAILR------------LPRKSSDAIRKKRVE------------------------DVLLRDLALTRIG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 327 NDMMRGVSGGQRKRVTTG-EMTVGPrKTLFMDEISTGLDSSTTFQIVKCIRNFVHlMDATVLMALLQPAPETFDLFDDLI 405
Cdd:cd03234 138 GNLVKGISGGERRRVSIAvQLLWDP-KVLILDEPTSGLDSFTALNLVSTLSQLAR-RNRIVILTIHQPRSDLFRLFDRIL 215
|
250
....*....|.
gi 330253231 406 LLSEGYMVYQG 416
Cdd:cd03234 216 LLSSGEIVYSG 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
175-718 |
6.33e-44 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 171.22 E-value: 6.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlKKTGNITYNGENLNKFHVKRTsAYISQTDNHIAELTVRET 254
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGN-NFTGTILANNRKPTKQILKRT-GFVTQDDILYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 255 LDFAArcqgasegfagymkdLTRLEKergirpsseidafmkaASVKGEKHSVStDYVLKVLGLDVCSDTMVGNDMMRGVS 334
Cdd:PLN03211 161 LVFCS---------------LLRLPK----------------SLTKQEKILVA-ESVISELGLTKCENTIIGNSFIRGIS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 335 GGQRKRVTTG-EMTVGPrKTLFMDEISTGLDSSTTFQIVKCIRNFVHlMDATVLMALLQPAPETFDLFDDLILLSEGYMV 413
Cdd:PLN03211 209 GGERKRVSIAhEMLINP-SLLILDEPTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 414 YQGPREDVIAFFESLGFRLPPRKGVADFLQEVTSKKDQAQYWADPSKP---------YQFIPVSDIAAAFRNSKYGHAAD 484
Cdd:PLN03211 287 FFGKGSDAMAYFESVGFSPSFPMNPADFLLDLANGVCQTDGVSEREKPnvkqslvasYNTLLAPKVKAAIEMSHFPQANA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 485 SKLAAPFDKKSADPSALCrtkfaISGWENLKVCFVRELLLIKRHKFLYTFRTCQVGFVGLVTATVFLKTRLHPTSEQFGN 564
Cdd:PLN03211 367 RFVGSASTKEHRSSDRIS-----ISTWFNQFSILLQRSLKERKHESFNTLRVFQVIAAALLAGLMWWHSDFRDVQDRLGL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 565 EYLSCLFFGLvhmmFNGFSELPLMISRLPVFYKQRDNSFHPAWSWSIASWLLRVPYSVLEAVVWSGVVYFTVGLAPSAGR 644
Cdd:PLN03211 442 LFFISIFWGV----FPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGA 517
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330253231 645 FFRYMLLLFSVHQMALGLFRMMASLARDMVIANTFGSAAILIVFLLGGFVIPKadIKPWWVWGFWVSPLSYGQR 718
Cdd:PLN03211 518 FLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYVHK--LPSCMAWIKYISTTFYSYR 589
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
851-1060 |
2.09e-38 |
|
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: 142.79 E-value: 2.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 851 LQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRkTGGY--TEGDIRISGHP--KEQQTFARISGYVEQNDIHSPQV 926
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR-TEGNvsVEGDIHYNGIPykEFAEKYPGEIIYVSEEDVHFPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 927 TVEESLWFSASLrlpkeitkeQKKEFVEqvmrlveldtlryalvglpgttGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1006
Cdd:cd03233 99 TVRETLDFALRC---------KGNEFVR----------------------GISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 1007 GLDARAAAIVMRTVRNTVD-TGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYG 1060
Cdd:cd03233 148 GLDSSTALEILKCIRTMADvLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
854-1054 |
6.84e-36 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 136.73 E-value: 6.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG--RKTggytEGDIRISGHP---KEQQTFARIsGYVEQNDIHSPQVTV 928
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGllRPT----SGEVRVLGEDvarDPAEVRRRI-GYVPQEPALYPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 929 EESLWFSASLRlpkEITKEQKKEFVEQVMRLVELDTLRYALVGlpgttGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1008
Cdd:COG1131 91 RENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVG-----TLSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 330253231 1009 DARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRG 1054
Cdd:COG1131 163 DPEARRELWELLRELAAEGKTVLLSTHYLE-EAERLCDRVAIIDKG 207
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
852-1060 |
1.05e-32 |
|
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: 127.67 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHPKEQQTFARIS--GYVEQNDIHSPQVTVE 929
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLK--PDSGSILIDGEDVRKEPREARRqiGVLPDERGLYDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 930 ESLWFSASLRlpkEITKEQKKEFVEQVMRLVELDTLRYALVGlpgttGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1009
Cdd:COG4555 93 ENIRYFAELY---GLFDEELKKRIEELIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 330253231 1010 ARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRGGQVIYG 1060
Cdd:COG4555 165 VMARRLLREILRALKKEGKTVLFSSHIMQ-EVEALCDRVVILHKGKVVAQG 214
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
166-416 |
8.70e-31 |
|
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: 120.43 E-value: 8.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 166 IKPRKHKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSLkKTGNITYNGENLNKfHVKRTSAYISQTDNH 245
Cdd:cd03232 13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGV-ITGEILINGRPLDK-NFQRSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 246 IAELTVRETLDFAARCqgasegfagymkdltrlekergirpsseidafmkaasvkgekhsvstdyvlkvlgldvcsdtmv 325
Cdd:cd03232 91 SPNLTVREALRFSALL---------------------------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 326 gndmmRGVSGGQRKRVTTG-EMTVGPrKTLFMDEISTGLDSSTTFQIVKCIRNfvhLMDA--TVLMALLQPAPETFDLFD 402
Cdd:cd03232 107 -----RGLSVEQRKRLTIGvELAAKP-SILFLDEPTSGLDSQAAYNIVRFLKK---LADSgqAILCTIHQPSASIFEKFD 177
|
250
....*....|....*
gi 330253231 403 DLILLSE-GYMVYQG 416
Cdd:cd03232 178 RLLLLKRgGKTVYFG 192
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
850-1061 |
1.04e-30 |
|
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: 120.76 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 850 RLQLLSNVSGVFSPGVlTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHP--KEQQTFARISGYVEQNDIHSPQVT 927
Cdd:cd03264 12 KKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPP--SSGTIRIDGQDvlKQPQKLRRRIGYLPQEFGVYPNFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 928 VEESLWFSASLrlpKEITKEQKKEFVEQVMRLVELDTLRYALVGlpgttGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1007
Cdd:cd03264 89 VREFLDYIAWL---KGIPSKEVKARVDEVLELVNLGDRAKKKIG-----SLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 330253231 1008 LDArAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKrGGQVIYGG 1061
Cdd:cd03264 161 LDP-EERIRFRNLLSELGEDRIVILSTHIVE-DVESLCNQVAVLN-KGKLVFEG 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
852-1054 |
2.06e-29 |
|
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: 117.18 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKtgGYTEGDIRISGHPKEQQT---FARISGYVEQNdihsPQV-- 926
Cdd:cd03225 15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL--GPTSGEVLVDGKDLTKLSlkeLRRKVGLVFQN----PDDqf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 927 ---TVEESLWFSA-SLRLPKEITKEQkkefVEQVMRLVELDTLRYALvglPGTtgLSTEQRKRLTIAVELVANPSIIFMD 1002
Cdd:cd03225 89 fgpTVEEEVAFGLeNLGLPEEEIEER----VEEALELVGLEGLRDRS---PFT--LSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 330253231 1003 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRG 1054
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDG 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
854-1054 |
2.94e-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: 2.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHPKEQQTfARIsGYVEQN---DIHSPqVTVEE 930
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP--PTSGTVRLFGKPPRRAR-RRI-GYVPQRaevDWDFP-ITVRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 931 ----SLWfsASLRLPKEITKEQKKEfVEQVMRLVELDTLRYALVGLpgttgLSTEQRKRLTIAVELVANPSIIFMDEPTS 1006
Cdd:COG1121 97 vvlmGRY--GRRGLFRRPSRADREA-VDEALERVGLEDLADRPIGE-----LSGGQQQRVLLARALAQDPDLLLLDEPFA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 330253231 1007 GLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLMKRG 1054
Cdd:COG1121 169 GVDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRG 215
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
852-1054 |
5.13e-29 |
|
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: 114.26 E-value: 5.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHPKEQ---QTFARISGYVEQndihspqvtv 928
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK--PTSGEILIDGKDIAKlplEELRRRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 929 eeslwfsaslrlpkeitkeqkkefveqvmrlveldtlryalvglpgttgLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1008
Cdd:cd00267 81 -------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 330253231 1009 DARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRG 1054
Cdd:cd00267 112 DPASRERLLELLRELAEEGRTVIIVTHDPE-LAELAADRVIVLKDG 156
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
854-1061 |
5.65e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 116.09 E-value: 5.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPKEQQTfARIsGYVEQN---DIHSPqVTVEE 930
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKP--TSGSIRVFGKPLEKER-KRI-GYVPQRrsiDRDFP-ISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 931 ----SLWfsASLRLPKEITKEQKKEfVEQVMRLVELDTLRYALVGLpgttgLSTEQRKRLTIAVELVANPSIIFMDEPTS 1006
Cdd:cd03235 90 vvlmGLY--GHKGLFRRLSKADKAK-VDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 1007 GLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLMKRGgqVIYGG 1061
Cdd:cd03235 162 GVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLNRT--VVASG 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
863-1061 |
9.44e-29 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 115.68 E-value: 9.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 863 PGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHPKEQQTFA--RISGYVEQNDIHSPQVTVEESLWFSASLR- 939
Cdd:cd03263 27 KGEIFGLLGHNGAGKTTTLKMLTGELR--PTSGTAYINGYSIRTDRKAarQSLGYCPQFDALFDELTVREHLRFYARLKg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 940 LPKEITKEQkkefVEQVMRLVELDTLRYALVGlpgttGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRT 1019
Cdd:cd03263 105 LPKSEIKEE----VELLLRVLGLTDKANKRAR-----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 330253231 1020 VrNTVDTGRTVVCTIHqpSIDIFEAF-DELLLMKRgGQVIYGG 1061
Cdd:cd03263 176 I-LEVRKGRSIILTTH--SMDEAEALcDRIAIMSD-GKLRCIG 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
852-1073 |
3.10e-28 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 114.35 E-value: 3.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPKEQQTFARIS---GYVEQN-D--IHSPq 925
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKP--TSGEVLVDGKDITKKNLRELRrkvGLVFQNpDdqLFAP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 926 vTVEESLWFS-ASLRLPKEITKEQkkefVEQVMRLVELDTLR----YALVGlpgttGlsteQRKRLTIAVELVANPSIIF 1000
Cdd:COG1122 92 -TVEEDVAFGpENLGLPREEIRER----VEEALELVGLEHLAdrppHELSG-----G----QKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330253231 1001 MDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRgGQVIYGgklGTHSQVLVDY 1073
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLD-LVAELADRVIVLDD-GRIVAD---GTPREVFSDY 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
852-1060 |
1.21e-27 |
|
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: 113.21 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHP------KEqqtFARISGYVEQNDIHSPQ 925
Cdd:COG1120 15 PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK--PSSGEVLLDGRDlaslsrRE---LARRIAYVPQEPPAPFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 926 VTVEE----------SLWFSASlrlpkeitkEQKKEFVEQVMRLVELDTLRYALVglpgtTGLSTEQRKRLTIAVELVAN 995
Cdd:COG1120 90 LTVRElvalgryphlGLFGRPS---------AEDREAVEEALERTGLEHLADRPV-----DELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330253231 996 PSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSIdifeAF---DELLLMKRGGQVIYG 1060
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRlARERGRTVVMVLHDLNL----AAryaDRLVLLKDGRIVAQG 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
853-1037 |
3.48e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 110.65 E-value: 3.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHPKEQQ--TFARISGYVEQNDIHSPQVTVEE 930
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLP--PSAGEVLWNGEPIRDAreDYRRRLAYLGHADGLKPELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 931 SLWFSASLRlPKEITKEQkkefVEQVMRLVELDTLRYALVGLpgttgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1010
Cdd:COG4133 95 NLRFWAALY-GLRADREA----IDEALEAVGLAGLADLPVRQ-----LSAGQKRRVALARLLLSPAPLWLLDEPFTALDA 164
|
170 180
....*....|....*....|....*..
gi 330253231 1011 RAAAIVMRTVRNTVDTGRTVVCTIHQP 1037
Cdd:COG4133 165 AGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
854-1006 |
6.33e-27 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 107.73 E-value: 6.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHP---KEQQTFARISGYVEQNDIHSPQVTVEE 930
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS--PTEGTILLDGQDltdDERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330253231 931 SLWFSASLRLPKEITKEQKkefVEQVMRLVELDTLRYALVGLPGTTgLSTEQRKRLTIAVELVANPSIIFMDEPTS 1006
Cdd:pfam00005 79 NLRLGLLLKGLSKREKDAR---AEEALEKLGLGDLADRPVGERPGT-LSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PDR_assoc |
pfam08370 |
Plant PDR ABC transporter associated; This domain is found on the C-terminus of ABC-2 type ... |
730-793 |
1.17e-26 |
|
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: 104.12 E-value: 1.17e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 730 WMTPSA-ISDTTIGLNLLKLRSFPTNDYWYWIGIAVLIGYAILFNNVVTLALAYLNPLRKARAVV 793
Cdd:pfam08370 1 WMKPTAsNGNTTLGVAVLKSRGLFTEAYWYWIGVGALLGFTILFNILFTLALTYLNPLGKSQAII 65
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
848-1054 |
2.12e-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: 105.65 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 848 ETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHPKEQQTFARIS-------GYVEQNd 920
Cdd:cd03255 14 GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR--PTSGEVRVDGTDISKLSEKELAafrrrhiGFVFQS- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 921 iHS--PQVTVEESLwfsaslRLPKEITKEQKKEFVEQVMRLVELdtlryalVGL-------PGTtgLSTEQRKRLTIAVE 991
Cdd:cd03255 91 -FNllPDLTALENV------ELPLLLAGVPKKERRERAEELLER-------VGLgdrlnhyPSE--LSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330253231 992 LVANPSIIFMDEPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHQPsiDIFEAFDELLLMKRG 1054
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDP--ELAEYADRIIELRDG 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
759-1070 |
4.90e-25 |
|
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: 111.78 E-value: 4.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 759 WIGIAVLIGYAiLFNNVVTLALA--YLNPLRKARAVVLddpneetALVADANQVISEKKGMILPfKPLTMTFHNVNYyvd 836
Cdd:COG4987 274 LLALLVLAALA-LFEALAPLPAAaqHLGRVRAAARRLN-------ELLDAPPAVTEPAEPAPAP-GGPSLELEDVSF--- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 837 mpkemrsqGVPETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG-RKtggYTEGDIRISGHPKEQ---QTFARI 912
Cdd:COG4987 342 --------RYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRfLD---PQSGSITLGGVDLRDldeDDLRRR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 913 SGYVEQnDIHspqvtveesLwFSAS----LRLPK-EITKEQkkefVEQVMRLVELDTLryaLVGLP-------GTTG--L 978
Cdd:COG4987 411 IAVVPQ-RPH---------L-FDTTlrenLRLARpDATDEE----LWAALERVGLGDW---LAALPdgldtwlGEGGrrL 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 979 STEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDtGRTVVCTIHQPSidIFEAFDELLLMKRGGQVi 1058
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLA--GLERMDRILVLEDGRIV- 548
|
330
....*....|..
gi 330253231 1059 yggKLGTHSQVL 1070
Cdd:COG4987 549 ---EQGTHEELL 557
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
853-1070 |
9.21e-25 |
|
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: 111.85 E-value: 9.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGrktgGY--TEGDIRISGHPKEQ---QTFARISGYVEQNDihspqvt 927
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG----LYepTSGRILIDGIDLRQidpASLRRQIGVVLQDV------- 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 928 veesLWFSASLR------LPkEITKEQkkefVEQVMRLVELDT------LRYALVGLPGTTGLSTEQRKRLTIAVELVAN 995
Cdd:COG2274 559 ----FLFSGTIRenitlgDP-DATDEE----IIEAARLAGLHDfiealpMGYDTVVGEGGSNLSGGQRQRLAIARALLRN 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 996 PSIIFMDEPTSGLDARAAAIVMRTVRnTVDTGRTVVCTIHQPSidIFEAFDELLLMKRgGQVIYggkLGTHSQVL 1070
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLR-RLLKGRTVIIIAHRLS--TIRLADRIIVLDK-GRIVE---DGTHEELL 697
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
854-1054 |
9.96e-24 |
|
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: 99.39 E-value: 9.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHP--KEQQTFARISGYVEQNDIHSPQVTVEES 931
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK--PDSGEIKVLGKDikKEPEEVKRRIGYLPEEPSLYENLTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 932 LWFSaslrlpkeitkeqkkefveqvmrlveldtlryalvglpgtTGlsteQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1011
Cdd:cd03230 94 LKLS----------------------------------------GG----MKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 330253231 1012 AAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRG 1054
Cdd:cd03230 130 SRREFWELLRELKKEGKTILLSSHILE-EAERLCDRVAILNNG 171
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
762-1070 |
1.53e-23 |
|
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: 106.77 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 762 IAVLIGYAILFNNV------VTLALA--YLNPLR--------KARAV--------VLDDPNEEtalVADANQVISEKKgm 817
Cdd:COG4988 259 VAVYIGFRLLGGSLtlfaalFVLLLApeFFLPLRdlgsfyhaRANGIaaaekifaLLDAPEPA---APAGTAPLPAAG-- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 818 ilpfkPLTMTFHNVNY-YVDmpkemrsqgvpetRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGD 896
Cdd:COG4988 334 -----PPSIELEDVSFsYPG-------------GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP--YSGS 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 897 IRISGHP----KEQQTFARISgYVEQNdihspqvtveeSLWFSASLR----LPK-EITKEQkkefVEQVMRLVELDTLry 967
Cdd:COG4988 394 ILINGVDlsdlDPASWRRQIA-WVPQN-----------PYLFAGTIRenlrLGRpDASDEE----LEAALEAAGLDEF-- 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 968 aLVGLP---------GTTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNtVDTGRTVVCTIHQPS 1038
Cdd:COG4988 456 -VAALPdgldtplgeGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR-LAKGRTVILITHRLA 533
|
330 340 350
....*....|....*....|....*....|..
gi 330253231 1039 IDifEAFDELLLMkRGGQVIyggKLGTHSQVL 1070
Cdd:COG4988 534 LL--AQADRILVL-DDGRIV---EQGTHEELL 559
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
853-1057 |
3.33e-23 |
|
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: 98.87 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGrkTGGYTEGDIRISGHPKEQQTFARISGYVEQN-DIHSPQVTVEES 931
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG--LIKESSGSILLNGKPIKAKERRKSIGYVMQDvDYQLFTDSVREE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 932 LWFSAslrlpKEITKEQKKefVEQVMRLVELDTLRYALvglPGTtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1011
Cdd:cd03226 93 LLLGL-----KELDAGNEQ--AETVLKDLDLYALKERH---PLS--LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 330253231 1012 AAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLMKRGGQV 1057
Cdd:cd03226 161 NMERVGELIRELAAQGKAVIVITHDYEF-LAKVCDRVLLLANGAIV 205
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
852-1054 |
3.59e-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: 99.13 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGH-----PKEQqtfaRISGYVEQNDIHSPQV 926
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERP--DSGEILIDGRdvtgvPPER----RNIGMVFQDYALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 927 TVEESLWFSasLRLpKEITKEQKKEFVEQVMRLVELDTLRYALVglpgtTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1006
Cdd:cd03259 88 TVAENIAFG--LKL-RGVPKAEIRARVRELLELVGLEGLLNRYP-----HELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 330253231 1007 GLDARAAAIVMRTVRNT-VDTGRTVVCTIHqpsiDIFEAF---DELLLMKRG 1054
Cdd:cd03259 160 ALDAKLREELREELKELqRELGITTIYVTH----DQEEALalaDRIAVMNEG 207
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
175-423 |
1.31e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 98.21 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFH--VKRTSAYISQTDNHIAELTVR 252
Cdd:COG1131 15 ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT---SGEVRVLGEDVARDPaeVRRRIGYVPQEPALYPDLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 253 ETLDFAARCQGASEGFAgymkdltrleKERgirpsseidafmkaasvkgekhsvsTDYVLKVLGLDVCSDTMVGNdmmrg 332
Cdd:COG1131 92 ENLRFFARLYGLPRKEA----------RER-------------------------IDELLELFGLTDAADRKVGT----- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 333 VSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHlMDATVLMA--LLqpaPETFDLFDDLILLSEG 410
Cdd:COG1131 132 LSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSthYL---EEAERLCDRVAIIDKG 207
|
250
....*....|...
gi 330253231 411 YMVYQGPREDVIA 423
Cdd:COG1131 208 RIVADGTPDELKA 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
852-1060 |
2.85e-22 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 95.58 E-value: 2.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG-RKTGGyteGDIRISGHpkeqqtfarisgyveqnDIHSPQvtvee 930
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGlLKPSS---GEILLDGK-----------------DLASLS----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 931 slwfsaslrlPKEITKeqKKEFVEQVMRLVELDTLRYALVglpgtTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1010
Cdd:cd03214 68 ----------PKELAR--KIAYVPQALELLGLAHLADRPF-----NELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 330253231 1011 RAAAIVMRTVRNTVD-TGRTVVCTIHQPSIdIFEAFDELLLMKRGGQVIYG 1060
Cdd:cd03214 131 AHQIELLELLRRLAReRGKTVVMVLHDLNL-AARYADRVILLKDGRIVAQG 180
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
826-1054 |
9.51e-22 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 93.60 E-value: 9.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 826 MTFHNVNY-YvdmpkemrsqgvPETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHPK 904
Cdd:cd03228 1 IEFKNVSFsY------------PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD--PTSGEILIDGVDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 905 EQ---QTFARISGYVEQNdihsPQVtveeslwFSASLRlpkeitkeqkkefveqvmrlvelDTLryalvglpgttgLSTE 981
Cdd:cd03228 67 RDldlESLRKNIAYVPQD----PFL-------FSGTIR-----------------------ENI------------LSGG 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330253231 982 QRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNtVDTGRTVVCTIHQPSidIFEAFDELLLMKRG 1054
Cdd:cd03228 101 QRQRIAIARALLRDPPILILDEATSALDPETEALILEALRA-LAKGKTVIVIAHRLS--TIRDADRIIVLDDG 170
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
762-1039 |
2.17e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 100.05 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 762 IAVLIGYAILFNNV------VTLALA---YLnPLRK------ARAVVLDDPNEETALVADANQVISEKKGmILPFKPLTM 826
Cdd:TIGR02857 245 VAVYIGFRLLAGDLdlatglFVLLLApefYL-PLRQlgaqyhARADGVAAAEALFAVLDAAPRPLAGKAP-VTAAPASSL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 827 TFHNVnyyvdmpkEMRSQGvpetRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGrkTGGYTEGDIRISGHP--- 903
Cdd:TIGR02857 323 EFSGV--------SVAYPG----RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG--FVDPTEGSIAVNGVPlad 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 904 -KEQQTFARIsGYVEQNDiHSPQVTVEESLWFSaslrlpkeiTKEQKKEFVEQVMRLVELDTLRYAL-VGL-----PGTT 976
Cdd:TIGR02857 389 aDADSWRDQI-AWVPQHP-FLFAGTIAENIRLA---------RPDASDAEIREALERAGLDEFVAALpQGLdtpigEGGA 457
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330253231 977 GLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNtVDTGRTVVCTIHQPSI 1039
Cdd:TIGR02857 458 GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA-LAQGRTVLLVTHRLAL 519
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
854-1062 |
2.59e-21 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 94.56 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGH------PKEQQTFARISGYVEQNDIHSPQVT 927
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP--TSGSVLIDGTdinklkGKALRQLRRQIGMIFQQFNLIERLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 928 VEESL---------WFSASLRLPKEITKEQKKEFVEQVmrlvELDTLRYALVGLpgttgLSTEQRKRLTIAVELVANPSI 998
Cdd:cd03256 95 VLENVlsgrlgrrsTWRSLFGLFPKEEKQRALAALERV----GLLDKAYQRADQ-----LSGGQQQRVAIARALMQQPKL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 999 IFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSIdIFEAFDELLLMKRgGQVIYGGK 1062
Cdd:cd03256 166 ILADEPVASLDPASSRQVMDLLKRiNREEGITVIVSLHQVDL-AREYADRIVGLKD-GRIVFDGP 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
849-1031 |
2.61e-21 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 99.59 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 849 TRLQLLSNVSgvFS--PGVLTALVGSSGAGKTTLMDVLAG--RKTggytEGDIRISGHP------KEQQTFARISGYVEQ 918
Cdd:COG1123 276 GGVRAVDDVS--LTlrRGETLGLVGESGSGKSTLARLLLGllRPT----SGSILFDGKDltklsrRSLRELRRRVQMVFQ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 919 NDIHS--PQVTVEESLWFSasLRLPKEITKEQKKEFVEQVMRLVELDT---LRYalvglPGTtgLSTEQRKRLTIAVELV 993
Cdd:COG1123 350 DPYSSlnPRMTVGDIIAEP--LRLHGLLSRAERRERVAELLERVGLPPdlaDRY-----PHE--LSGGQRQRVAIARALA 420
|
170 180 190
....*....|....*....|....*....|....*....
gi 330253231 994 ANPSIIFMDEPTSGLDARAAAIVMRTVRNTVD-TGRTVV 1031
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQReLGLTYL 459
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
852-1054 |
2.63e-21 |
|
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: 92.64 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHP-----KEQQTFARISGYVEQNDIHSPQV 926
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEP--DSGSILIDGEDltdleDELPPLRRRIGMVFQDFALFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 927 TVEESLWFsaslrlpkeitkeqkkefveqvmrlveldtlryalvglpgttGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1006
Cdd:cd03229 92 TVLENIAL------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 330253231 1007 GLDARAAAIVMRTVRNTVDT-GRTVVCTIHqpsiDIFEAF---DELLLMKRG 1054
Cdd:cd03229 130 ALDPITRREVRALLKSLQAQlGITVVLVTH----DLDEAArlaDRVVVLRDG 177
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
845-1058 |
5.64e-21 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 92.92 E-value: 5.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 845 GVPETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHPKEQQTFARisGYVEQNDIHSP 924
Cdd:cd03293 11 GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLER--PTSGEVLVDGEPVTGPGPDR--GYVFQQDALLP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 925 QVTVEEslwfsaSLRLPKEITKEQKKEFVEQVMRLVEldtlryaLVGLPGTTG-----LSTEQRKRLTIAVELVANPSII 999
Cdd:cd03293 87 WLTVLD------NVALGLELQGVPKAEARERAEELLE-------LVGLSGFENayphqLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330253231 1000 FMDEPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHqpsiDIFEAF---DELLLM-KRGGQVI 1058
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWrETGKTVLLVTH----DIDEAVflaDRVVVLsARPGRIV 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
845-1054 |
6.82e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 92.80 E-value: 6.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 845 GVPETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHP------KEQQTF--ARIsGYV 916
Cdd:COG1136 15 GTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDR--PTSGEVLIDGQDisslseRELARLrrRHI-GFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 917 EQnDIH-SPQVTVEEslwfsaSLRLPKEITKEQKKEFVEQVMRLVEldtlryaLVGL-------PGTtgLSTEQRKRLTI 988
Cdd:COG1136 92 FQ-FFNlLPELTALE------NVALPLLLAGVSRKERRERARELLE-------RVGLgdrldhrPSQ--LSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330253231 989 AVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHQPsiDIFEAFDELLLMKRG 1054
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDP--ELAARADRVIRLRDG 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
852-1062 |
1.50e-20 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 92.45 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLA--------------GRKTGGYTEGDIRisghpkeqqtfARIsGYVe 917
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgdlpptygndvrlfGERRGGEDVWELR-----------KRI-GLV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 918 QNDIHSpQVTVEESLW------FSASLRLPKEITKEQKKEfVEQVMRLVELDTLRYALVGlpgttGLSTEQRKRLTIAVE 991
Cdd:COG1119 84 SPALQL-RFPRDETVLdvvlsgFFDSIGLYREPTDEQRER-ARELLELLGLAHLADRPFG-----TLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 992 LVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTvvcTI----HQPSiDIFEAFDELLLMKRGGQVIYGGK 1062
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAP---TLvlvtHHVE-EIPPGITHVLLLKDGRVVAAGPK 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
847-1102 |
2.34e-20 |
|
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: 96.51 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 847 PETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGR-KTGGYTEGDIRISGHPKEQQTFARIS---GYVEQNDIH 922
Cdd:COG1123 15 PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlPHGGRISGEVLLDGRDLLELSEALRGrriGMVFQDPMT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 923 S--PqVTVEESLWFSASLRLpkeITKEQKKEFVEQVMRLVELDTL--RYalvglpgTTGLSTEQRKRLTIAVELVANPSI 998
Cdd:COG1123 95 QlnP-VTVGDQIAEALENLG---LSRAEARARVLELLEAVGLERRldRY-------PHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 999 IFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSiDIFEAFDELLLMKRGGQVIYggklGTHSQVLVDYfQGI 1077
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRElQRERGTTVLLITHDLG-VVAEIADRVVVMDDGRIVED----GPPEEILAAP-QAL 237
|
250 260
....*....|....*....|....*
gi 330253231 1078 NGVPPISSGYNPATWMLEVTTPALE 1102
Cdd:COG1123 238 AAVPRLGAARGRAAPAAAAAEPLLE 262
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
854-1031 |
4.81e-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: 90.96 E-value: 4.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLagrkTGGY--TEGDIR-----ISGHPKEQ-------------QTFARIS 913
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLI----SGFLrpTSGSVLfdgedITGLPPHEiarlgigrtfqipRLFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 914 gyVEQNDIHSPQVTVEESLWFSASLRLPKEITKEqkkefVEQVMRLVELDTLRYALVGLpgttgLSTEQRKRLTIAVELV 993
Cdd:cd03219 92 --VLENVMVAAQARTGSGLLLARARREEREARER-----AEELLERVGLADLADRPAGE-----LSYGQQRRLEIARALA 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 330253231 994 ANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVV 1031
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVL 197
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
854-1039 |
5.55e-20 |
|
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: 90.16 E-value: 5.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHP----KEQQT--FARISGYVEQNDIHSPQVT 927
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELP--TSGTIRVNGQDvsdlRGRAIpyLRRKIGVVFQDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 928 VEESLWFsaslrlPKEITKEQKKEFVEQVMRLVELDTLRYALVGLPgtTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1007
Cdd:cd03292 95 VYENVAF------ALEVTGVPPREIRKRVPAALELVGLSHKHRALP--AELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190
....*....|....*....|....*....|..
gi 330253231 1008 LDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1039
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTTVVVATHAKEL 198
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
850-1060 |
1.52e-19 |
|
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: 88.49 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 850 RLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPKEQQTFARIsGYVEQNDIHSPQVTVE 929
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILP--DSGEVLFDGKPLDIAARNRI-GYLPEERGLYPKMKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 930 ESLWFSASLR-LPKEITKEQKKEFVEQVmrlvELDTLRYALVglpgtTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1008
Cdd:cd03269 89 DQLVYLAQLKgLKKEEARRRIDEWLERL----ELSEYANKRV-----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 330253231 1009 DARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAF-DELLLMKRGGQVIYG 1060
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQ--MELVEELcDRVLLLNKGRAVLYG 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
176-358 |
1.62e-19 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 86.55 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKF---HVKRTSAYISQTDNHIAELTVR 252
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT---EGTILLDGQDLTDDerkSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 253 ETLDFAARCQGasegfagymkdLTRLEKERgirpssEIDAFMKAasvkgekhsvstdyvlkvLGLDVCSDTMVGNdMMRG 332
Cdd:pfam00005 78 ENLRLGLLLKG-----------LSKREKDA------RAEEALEK------------------LGLGDLADRPVGE-RPGT 121
|
170 180
....*....|....*....|....*.
gi 330253231 333 VSGGQRKRVTTGEMTVGPRKTLFMDE 358
Cdd:pfam00005 122 LSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
850-1058 |
2.00e-19 |
|
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: 88.72 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 850 RLQLLSNVSgvFS--PGVLTALVGSSGAGKTTLMDVLAG--RKTGG--YTEGDIRISGHPKEQQTFARISGYVEQNDIHS 923
Cdd:cd03257 17 SVKALDDVS--FSikKGETLGLVGESGSGKSTLARAILGllKPTSGsiIFDGKDLLKLSRRLRKIRRKEIQMVFQDPMSS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 924 --PQVTVEESLWFSASLRLpKEITKEQKKEFVEQVMRLVELDTLRYALvgLPGTtgLSTEQRKRLTIAVELVANPSIIFM 1001
Cdd:cd03257 95 lnPRMTIGEQIAEPLRIHG-KLSKKEARKEAVLLLLVGVGLPEEVLNR--YPHE--LSGGQRQRVAIARALALNPKLLIA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 330253231 1002 DEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSIDIFEAfDELLLMKrGGQVI 1058
Cdd:cd03257 170 DEPTSALDVSVQAQILDLLKKlQEELGLTLLFITHDLGVVAKIA-DRVAVMY-AGKIV 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
854-1071 |
2.07e-19 |
|
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: 88.82 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLagrkTGGY--TEGDIRISGHPKEQQTFARIS---GYVEQndihspqvtv 928
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLL----MRFYdpQKGQILIDGIDIRDISRKSLRsmiGVVLQ---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 929 eESLWFSAS----LRLPKEITKEqkkEFVEQVMRLVELDTL-------RYALVGlPGTTGLSTEQRKRLTIAVELVANPS 997
Cdd:cd03254 85 -DTFLFSGTimenIRLGRPNATD---EEVIEAAKEAGAHDFimklpngYDTVLG-ENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330253231 998 IIFMDEPTSGLDARAAAIVMRTVRNTVDtGRTVVCTIHQPSIdIFEAfDELLLMKRgGQVIyggKLGTHSQVLV 1071
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLST-IKNA-DKILVLDD-GKII---EEGTHDELLA 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
853-1060 |
3.66e-19 |
|
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: 88.51 E-value: 3.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLagRKTGGYTEGDIRISGHPKEQQT---FARISGYVEQNDIHSPQVTVE 929
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI--NRLIEPTSGEIFIDGEDIREQDpveLRRKIGYVIQQIGLFPHMTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 930 ESLWFSASLrlpKEITKEQKKEFVEQVMRLVELDTL----RYalvglPGTtgLSTEQRKRLTIAVELVANPSIIFMDEPT 1005
Cdd:cd03295 94 ENIALVPKL---LKWPKEKIRERADELLALVGLDPAefadRY-----PHE--LSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330253231 1006 SGLDAraaaiVMRT------VRNTVDTGRTVVCTIHqpsiDIFEAF---DELLLMKRGGQVIYG 1060
Cdd:cd03295 164 GALDP-----ITRDqlqeefKRLQQELGKTIVFVTH----DIDEAFrlaDRIAIMKNGEIVQVG 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
175-423 |
4.88e-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: 87.99 E-value: 4.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNK--FHVKRTSAYISQTDNHIAELTVR 252
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD---SGSILIDGEDVRKepREARRQIGVLPDERGLYDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 253 ETLDFAARCQGasegfagyMKDLTRLEKergirpsseidafmkaasvkgekhsvsTDYVLKVLGLDVCSDTMVGndmmrG 332
Cdd:COG4555 93 ENIRYFAELYG--------LFDEELKKR---------------------------IEELIELLGLEEFLDRRVG-----E 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 333 VSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLmDATVLMA--LLQpapETFDLFDDLILLSEG 410
Cdd:COG4555 133 LSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSshIMQ---EVEALCDRVVILHKG 208
|
250
....*....|...
gi 330253231 411 YMVYQGPREDVIA 423
Cdd:COG4555 209 KVVAQGSLDELRE 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
856-1054 |
1.02e-18 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 86.65 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 856 NVSGVFSPGVLTALVGSSGAGKTTLMDVLAG--RKTGGytegDIRISGHP--KEQQTFARISGYVEQNDIHSPQVTVEES 931
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTllKPTSG----RATVAGHDvvREPREVRRRIGIVFQDLSVDDELTGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 932 L-WFSASLRLPKEITKEQkkefVEQVMRLVELDTLRYALVGlpgttGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1010
Cdd:cd03265 94 LyIHARLYGVPGAERRER----IDELLDFVGLLEAADRLVK-----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 330253231 1011 RAAAIVMRTVRNTVDT-GRTVVCTIHqpsiDIFEA---FDELLLMKRG 1054
Cdd:cd03265 165 QTRAHVWEYIEKLKEEfGMTILLTTH----YMEEAeqlCDRVAIIDHG 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
852-1060 |
1.52e-18 |
|
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: 86.40 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGH------PKEQQTFARISGYVEQ-----ND 920
Cdd:cd03261 14 TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRP--DSGEVLIDGEdisglsEAELYRLRRRMGMLFQsgalfDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 921 IhspqvTVEESLWFSasLRlpkEITKEQKKEFVEQVMrlveldtLRYALVGLPGT-----TGLSTEQRKRLTIAVELVAN 995
Cdd:cd03261 92 L-----TVFENVAFP--LR---EHTRLSEEEIREIVL-------EKLEAVGLRGAedlypAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330253231 996 PSIIFMDEPTSGLDARAAAIVMRTVRNTVDT-GRTVVCTIHQPSiDIFEAFDELLLMKRGGQVIYG 1060
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLD-TAFAIADRIAVLYDGKIVAEG 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
175-410 |
1.76e-18 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 85.60 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLdksLKKTGNITYNGENLNKFHVK---RTSAYISQ-TDNHIAELT 250
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL---GPTSGEVLVDGKDLTKLSLKelrRKVGLVFQnPDDQFFGPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 251 VRETLDFAARCQGASEgfagymkdltrlekergirpsSEIDAfmkaasvkgekhsvSTDYVLKVLGLDVCSDTMVGNdmm 330
Cdd:cd03225 93 VEEEVAFGLENLGLPE---------------------EEIEE--------------RVEEALELVGLEGLRDRSPFT--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 331 rgVSGGQRKRVT-TGEMTVGPrKTLFMDEISTGLDSSTTFQIVKCIRNFvHLMDATVLMA-----LLqpapetFDLFDDL 404
Cdd:cd03225 135 --LSGGQKQRVAiAGVLAMDP-DILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVthdldLL------LELADRV 204
|
....*.
gi 330253231 405 ILLSEG 410
Cdd:cd03225 205 IVLEDG 210
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
854-1035 |
2.24e-18 |
|
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: 84.78 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG--RKTGGYTEGDIRISGHPKEQQTFARIS-GYVEQN---DIHSPqvT 927
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGllRPQSGAVLIDGEPLDYSRKGLLERRQRvGLVFQDpddQLFAA--D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 928 VEESLWFSA-SLRLPKEitkeQKKEFVEQVMRLVELDTLRYALvglpgTTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1006
Cdd:TIGR01166 86 VDQDVAFGPlNLGLSEA----EVERRVREALTAVGASGLRERP-----THCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180
....*....|....*....|....*....
gi 330253231 1007 GLDARAAAIVMRTVRNTVDTGRTVVCTIH 1035
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
864-1054 |
4.82e-18 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 86.68 E-value: 4.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 864 GVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHP--KEQQTFARISGYVEQNDIHSPQVTVEESLWFSASLR-L 940
Cdd:TIGR01188 19 GEVFGFLGPNGAGKTTTIRMLTTLLRP--TSGTARVAGYDvvREPRKVRRSIGIVPQYASVDEDLTGRENLEMMGRLYgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 941 PKEITKEQKKEfveqVMRLVELDTLRYALVGlpgttGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1020
Cdd:TIGR01188 97 PKDEAEERAEE----LLELFELGEAADRPVG-----TYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYI 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 330253231 1021 RNTVDTGRTVVCTIHqpsiDIFEA---FDELLLMKRG 1054
Cdd:TIGR01188 168 RALKEEGVTILLTTH----YMEEAdklCDRIAIIDHG 200
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
175-375 |
5.70e-18 |
|
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: 84.48 E-value: 5.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENL--NKFHVKRTSAYISQTDNHIAELTVR 252
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPT---SGTAYINGYSIrtDRKAARQSLGYCPQFDALFDELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 253 ETLDFAARCQGasegfagymkdltrlekergiRPSSEIDAfmkaasvkgekhsvSTDYVLKVLGLDVCSDTMVGNdmmrg 332
Cdd:cd03263 94 EHLRFYARLKG---------------------LPKSEIKE--------------EVELLLRVLGLTDKANKRART----- 133
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 330253231 333 VSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCI 375
Cdd:cd03263 134 LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLI 176
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
854-1060 |
7.38e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.93 E-value: 7.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSgvFS--PGVLTALVGSSGAGKTTLM----DVLAgrktggYTEGDIRISGHPKEQQTFARIsGYV-EQNDIHsPQV 926
Cdd:COG4152 17 VDDVS--FTvpKGEIFGLLGPNGAGKTTTIriilGILA------PDSGEVLWDGEPLDPEDRRRI-GYLpEERGLY-PKM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 927 TVEESLWFSASLR-LPKEITKEQKKEFVEqvmRLvELDTLRYALVGlpgttGLS-TEQRKrLTIAVELVANPSIIFMDEP 1004
Cdd:COG4152 87 KVGEQLVYLARLKgLSKAEAKRRADEWLE---RL-GLGDRANKKVE-----ELSkGNQQK-VQLIAALLHDPELLILDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 330253231 1005 TSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAF-DELLLMKRGGQVIYG 1060
Cdd:COG4152 157 FSGLDPVNVELLKDVIRELAAKGTTVIFSSHQ--MELVEELcDRIVIINKGRKVLSG 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
863-1061 |
1.14e-17 |
|
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: 83.11 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 863 PGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHP---KEQQTF----ARISGYVEQNDIHSPQVTVEESLWFS 935
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEK--PDGGTIVLNGTVlfdSRKKINlppqQRKIGLVFQQYALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 936 ASLRLPKEItkeqkKEFVEQVMRLVELDTLRYAlvglpGTTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1015
Cdd:cd03297 100 LKRKRNRED-----RISVDELLDLLGLDHLLNR-----YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 330253231 1016 VMRTVRNTV-DTGRTVVCTIHQPSidifEAF---DELLLMkRGGQVIYGG 1061
Cdd:cd03297 170 LLPELKQIKkNLNIPVIFVTHDLS----EAEylaDRIVVM-EDGRLQYIG 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
847-1061 |
1.15e-17 |
|
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: 83.57 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 847 PETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG--RKTGGYTEGD-IRISGHPKEQQtfARIsGYVEQNDIHS 923
Cdd:cd03266 14 VKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGllEPDAGFATVDgFDVVKEPAEAR--RRL-GFVSDSTGLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 924 PQVTVEESLWFSASLRLPKEITKEQKKEFVEQVMRLVELDTLRyalvglpgTTGLSTEQRKRLTIAVELVANPSIIFMDE 1003
Cdd:cd03266 91 DRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRR--------VGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 330253231 1004 PTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRgGQVIYGG 1061
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLRALGKCILFSTHIMQ-EVERLCDRVVVLHR-GRVVYEG 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
762-1070 |
1.30e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 88.30 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 762 IAVLIGYAILFNNVVTLALAYLNPLRKARAV------VLDDPNEETAlvADANQVISEKKGMIlpfkpltmTFHNVNY-Y 834
Cdd:COG1132 280 LVAFILYLLRLFGPLRQLANVLNQLQRALASaerifeLLDEPPEIPD--PPGAVPLPPVRGEI--------EFENVSFsY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 835 vdmpkemrsqgvPETRlQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRktggY--TEGDIRISGHP-KE--QQTF 909
Cdd:COG1132 350 ------------PGDR-PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF----YdpTSGRILIDGVDiRDltLESL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 910 ARISGYVEQndihspqvtveESLWFSASLR------LPkEITKEQkkefVEQVMRLVE-----------LDTLryalVGL 972
Cdd:COG1132 413 RRQIGVVPQ-----------DTFLFSGTIRenirygRP-DATDEE----VEEAAKAAQahefiealpdgYDTV----VGE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 973 PGTTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNtVDTGRTVVcTI-HQPS-IdifEAFDELLL 1050
Cdd:COG1132 473 RGVN-LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALER-LMKGRTTI-VIaHRLStI---RNADRILV 546
|
330 340
....*....|....*....|
gi 330253231 1051 MKrGGQVIyggKLGTHSQVL 1070
Cdd:COG1132 547 LD-DGRIV---EQGTHEELL 562
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
175-364 |
1.36e-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: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKF--HVKRTSAYISQTDNHIAELTVR 252
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPS---AGEVLWNGEPIRDAreDYRRRLAYLGHADGLKPELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 253 ETLDFAARCQGASegfagymkdltrlekergiRPSSEIDAfmkaasvkgekhsvstdyVLKVLGLDVCSDTMVGNdmmrg 332
Cdd:COG4133 94 ENLRFWAALYGLR-------------------ADREAIDE------------------ALEAVGLAGLADLPVRQ----- 131
|
170 180 190
....*....|....*....|....*....|..
gi 330253231 333 VSGGQRKRVTTGEMTVGPRKTLFMDEISTGLD 364
Cdd:COG4133 132 LSAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
175-422 |
1.42e-17 |
|
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: 83.94 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFHVK---RTSAYISQTDNHIAELTV 251
Cdd:COG1120 16 VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS---SGEVLLDGRDLASLSRRelaRRIAYVPQEPPAPFGLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 252 RETLDFaarcqgaseGFAGYMKDLTRLEKErgirpssEIDAFMKAasvkgekhsvstdyvLKVLGLDVCSDTMVGNdmmr 331
Cdd:COG1120 93 RELVAL---------GRYPHLGLFGRPSAE-------DREAVEEA---------------LERTGLEHLADRPVDE---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 332 gVSGGQRKRVttgeM-----TVGPRkTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMALlqpapetFDL------ 400
Cdd:COG1120 138 -LSGGERQRV----LiaralAQEPP-LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVL-------HDLnlaary 204
|
250 260
....*....|....*....|..
gi 330253231 401 FDDLILLSEGYMVYQGPREDVI 422
Cdd:COG1120 205 ADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
850-1054 |
1.57e-17 |
|
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: 83.54 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 850 RLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISG------HPKEQQTfarisGYVEQNDIHS 923
Cdd:cd03296 14 DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERP--DSGTILFGGedatdvPVQERNV-----GFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 924 PQVTVEESLWFSASLRLPKE-ITKEQKKEFVEQVMRLVELDTL--RYAlvglpgtTGLSTEQRKRLTIAVELVANPSIIF 1000
Cdd:cd03296 87 RHMTVFDNVAFGLRVKPRSErPPEAEIRAKVHELLKLVQLDWLadRYP-------AQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 1001 MDEPTSGLDARAAAIVMRTVRNTVD-TGRTVVCTIHQPSiDIFEAFDELLLMKRG 1054
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDeLHVTTVFVTHDQE-EALEVADRVVVMNKG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
845-1058 |
1.65e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.99 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 845 GVPETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPKEQQTFARisGYVEQNDihsp 924
Cdd:COG1116 18 PTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKP--TSGEVLVDGKPVTGPGPDR--GVVFQEP---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 925 qvtveeSL--WFSAS--LRLPKEITKEQKKEFVEQVMRLVELdtlryalVGL-------PGTtgLSTEQRKRLTIAVELV 993
Cdd:COG1116 90 ------ALlpWLTVLdnVALGLELRGVPKAERRERARELLEL-------VGLagfedayPHQ--LSGGMRQRVAIARALA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 994 ANPSIIFMDEPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHqpsiDIFEAF---DELLLM-KRGGQVI 1058
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERLQDELLRLWqETGKTVLFVTH----DVDEAVflaDRVVVLsARPGRIV 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
847-1056 |
1.69e-17 |
|
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: 81.49 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 847 PETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPKEQQ---TFARISGYVEQNDIhs 923
Cdd:cd03246 11 PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRP--TSGRVRLDGADISQWdpnELGDHVGYLPQDDE-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 924 pqvtveeslWFSASLRlpkeitkeqkkefvEQVmrlveldtlryalvglpgttgLSTEQRKRLTIAVELVANPSIIFMDE 1003
Cdd:cd03246 87 ---------LFSGSIA--------------ENI---------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 330253231 1004 PTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSidIFEAFDELLLMKRGGQ 1056
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDGRV 173
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
854-1031 |
2.51e-17 |
|
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: 83.55 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLagrkTGGY--TEGDIRISGHP----KEQQ--------TFarisgyveQN 919
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLI----TGFYrpTSGRILFDGRDitglPPHRiarlgiarTF--------QN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 920 dihsPQV----TVEESL-----------WFSASLRLPKEITKEQK-KEFVEQVMRLVELDTLRYALVGlpgttGLSTEQR 983
Cdd:COG0411 88 ----PRLfpelTVLENVlvaaharlgrgLLAALLRLPRARREEREaRERAEELLERVGLADRADEPAG-----NLSYGQQ 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 330253231 984 KRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVV 1031
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRlRDERGITIL 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
852-1070 |
4.27e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.90 E-value: 4.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPKEQ---QTFARISGYVEQndiHSPQV-- 926
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSP--DSGEVRLNGRPLADwspAELARRRAVLPQ---HSSLSfp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 927 -TVEESLWFSaslRLPKEITKEQKKEFVEQVMRLVELDTLRYALVglpgtTGLSTEQRKRLTIAVELV------ANPSII 999
Cdd:PRK13548 91 fTVEEVVAMG---RAPHGLSRAEDDALVAAALAQVDLAHLAGRDY-----PQLSGGEQQRVQLARVLAqlwepdGPPRWL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 1000 FMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHqpsiDIFEAF---DELLLMKRGGQViyggKLGTHSQVL 1070
Cdd:PRK13548 163 LLDEPTSALDLAHQHHVLRLARQlAHERGLAVIVVLH----DLNLAAryaDRIVLLHQGRLV----ADGTPAEVL 229
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
175-422 |
5.00e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 82.06 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKfhVKRTSAYISQTDNHIAE--LTVR 252
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPT---SGTVRLFGKPPRR--ARRRIGYVPQRAEVDWDfpITVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 253 ETLdfAARCQGASegfaGYMKDLTRLEKERgirpsseIDAfmkaasvkgekhsvstdyVLKVLGLDVCSDTMVGNdmmrg 332
Cdd:COG1121 96 DVV--LMGRYGRR----GLFRRPSRADREA-------VDE------------------ALERVGLEDLADRPIGE----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 333 VSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHlMDATVLMAL--LQPAPEtfdLFDDLILLSEG 410
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVThdLGAVRE---YFDRVLLLNRG 215
|
250
....*....|..
gi 330253231 411 yMVYQGPREDVI 422
Cdd:COG1121 216 -LVAHGPPEEVL 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
853-1044 |
6.58e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.69 E-value: 6.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG--RKTggytEGDIRISGHPKEQQTFARISGYVEQNDIHSPQVTVEE 930
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGllPPA----AGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 931 SLWFSASLRlpkeitkEQKKEFVEQVMRLVELDtlryALVGLPGTTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1010
Cdd:PRK13539 93 NLEFWAAFL-------GGEELDIAAALEAVGLA----PLAHLPFGY-LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180 190
....*....|....*....|....*....|....
gi 330253231 1011 RAAAIVMRTVRNTVDTGRTVVCTIHQPsIDIFEA 1044
Cdd:PRK13539 161 AAVALFAELIRAHLAQGGIVIAATHIP-LGLPGA 193
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
852-1036 |
6.82e-17 |
|
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: 80.72 E-value: 6.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG--RKTGGYTEGDIRISGHPKEqqTFARISGYVEQNDIHsPQVTVE 929
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGliKPDSGEITFDGKSYQKNIE--ALRRIGALIEAPGFY-PNLTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 930 ESLWFSASL-RLPKEItkeqkkefVEQVMRLVELDTLRYALVGlpgttGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1008
Cdd:cd03268 91 ENLRLLARLlGIRKKR--------IDEVLDVVGLKDSAKKKVK-----GFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180
....*....|....*....|....*...
gi 330253231 1009 DARAAAIVMRTVRNTVDTGRTVVCTIHQ 1036
Cdd:cd03268 158 DPDGIKELRELILSLRDQGITVLISSHL 185
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
175-428 |
1.29e-16 |
|
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: 84.95 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSLKKTGNITYNGENLNKFHVK---RTSAYISQ-TDNHIAELT 250
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEAlrgRRIGMVFQdPMTQLNPVT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 251 VRETLDFAARCQGAsegfagymkdltrlekergirPSSEIDAFMKAAsvkgekhsvstdyvLKVLGLDVCSDTMVGNdmm 330
Cdd:COG1123 101 VGDQIAEALENLGL---------------------SRAEARARVLEL--------------LEAVGLERRLDRYPHQ--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 331 rgVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMALLQPApETFDLFDDLILLSEG 410
Cdd:COG1123 143 --LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLG-VVAEIADRVVVMDDG 219
|
250
....*....|....*...
gi 330253231 411 YMVYQGPREDVIAFFESL 428
Cdd:COG1123 220 RIVEDGPPEEILAAPQAL 237
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
854-1061 |
1.76e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 80.45 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGH-PKEQQT--FARISGYVEQndihspqvtvEE 930
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQP--TSGEVRVAGLvPWKRRKkfLRRIGVVFGQ----------KT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 931 SLWFS----ASLRLPKEITKEQKKEFVEQVMRLVELDTLRyALVGLPgTTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1006
Cdd:cd03267 105 QLWWDlpviDSFYLLAAIYDLPPARFKKRLDELSELLDLE-ELLDTP-VRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 330253231 1007 GLDARAAAIVMRTVRNTV-DTGRTVVCTIHQPSiDIfEAFDELLLMKRGGQVIYGG 1061
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNrERGTTVLLTSHYMK-DI-EALARRVLVIDKGRLLYDG 236
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
172-389 |
3.82e-16 |
|
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: 79.07 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 172 KLNILKDISGIIKPGRMTLLLGPPGSGKSTlLLALAGKLDKSLKktGNITYNGENLNKFHVKRTSA-------YISQTDN 244
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKST-LLNILGGLDRPTS--GEVRVDGTDISKLSEKELAAfrrrhigFVFQSFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 245 HIAELTVRETLDFAARCQGasegfagymkdltrlekergiRPSSEIDAfmKAASvkgekhsvstdyVLKVLGLDVCSDTM 324
Cdd:cd03255 93 LLPDLTALENVELPLLLAG---------------------VPKKERRE--RAEE------------LLERVGLGDRLNHY 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330253231 325 VGNdmmrgVSGGQRKRVTTGEMTVGPRKTLFMDEiSTG-LDSSTTFQIVKCIRNFVHLMDATVLMA 389
Cdd:cd03255 138 PSE-----LSGGQQQRVAIARALANDPKIILADE-PTGnLDSETGKEVMELLRELNKEAGTTIVVV 197
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
854-1037 |
4.40e-16 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 83.18 E-value: 4.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG---RKTGGYTEGDIRISGHPkeQQTFARISGYVEQnDIHSPQVTVEE 930
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGlldPLQGEVTLDGVPVSSLD--QDEVRRRVSVCAQ-DAHLFDTTVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 931 SLWFSAslrlpKEITKEQKKEFVEQVmRLVE-LDTLRYALVGLPGTTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSG 1007
Cdd:TIGR02868 428 NLRLAR-----PDATDEELWAALERV-GLADwLRALPDGLDTVLGEGGarLSGGERQRLALARALLADAPILLLDEPTEH 501
|
170 180 190
....*....|....*....|....*....|
gi 330253231 1008 LDARAAAIVMRTVRNtVDTGRTVVCTIHQP 1037
Cdd:TIGR02868 502 LDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
852-1016 |
4.45e-16 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 79.15 E-value: 4.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG---RKTGGYTEGDIRISGHPKEQQTFARIS-----GYVEQndihS 923
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndLIPGAPDEGEVLLDGKDIYDLDVDVLElrrrvGMVFQ----K 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 924 PQV---TVEESLwfSASLRLPKEITKEQKKEFVEQVMRLVELDtlRYALVGLPGTtGLSTEQRKRLTIAVELVANPSIIF 1000
Cdd:cd03260 90 PNPfpgSIYDNV--AYGLRLHGIKLKEELDERVEEALRKAALW--DEVKDRLHAL-GLSGGQQQRLCLARALANEPEVLL 164
|
170
....*....|....*.
gi 330253231 1001 MDEPTSGLDARAAAIV 1016
Cdd:cd03260 165 LDEPTSALDPISTAKI 180
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
848-1070 |
5.10e-16 |
|
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: 79.20 E-value: 5.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 848 ETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLM-------DVlagrktggyTEGDIRISGHP-KE--QQTFARISGYVe 917
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILrllfrfyDV---------SSGSILIDGQDiREvtLDSLRRAIGVV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 918 qndihsPQVTV--EESLWF-------SASlrlPKEITKEQKKEFV-EQVMRLVE-LDTlryaLVGLPGTTgLSTEQRKRL 986
Cdd:cd03253 81 ------PQDTVlfNDTIGYnirygrpDAT---DEEVIEAAKAAQIhDKIMRFPDgYDT----IVGERGLK-LSGGEKQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 987 TIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRnTVDTGRTVVCTIHQPSiDIFEAfDELLLMKrGGQVIyggKLGTH 1066
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALR-DVSKGRTTIVIAHRLS-TIVNA-DKIIVLK-DGRIV---ERGTH 219
|
....
gi 330253231 1067 SQVL 1070
Cdd:cd03253 220 EELL 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
854-1054 |
1.11e-15 |
|
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: 77.30 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGH------PKEqqtfaRISGYVEQNDIHSPQVT 927
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEE--PTSGRIYIGGRdvtdlpPKD-----RDIAMVFQNYALYPHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 928 VEESLWFSASLR-LPKEITKEQkkefVEQVMRLVELDTL--RYalvglpgTTGLSTEQRKRLTIAVELVANPSIIFMDEP 1004
Cdd:cd03301 89 VYDNIAFGLKLRkVPKDEIDER----VREVAELLQIEHLldRK-------PKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 1005 TSGLDARaAAIVMRT--VRNTVDTGRTVVCTIHqpsiDIFEAF---DELLLMKRG 1054
Cdd:cd03301 158 LSNLDAK-LRVQMRAelKRLQQRLGTTTIYVTH----DQVEAMtmaDRIAVMNDG 207
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
854-1031 |
1.12e-15 |
|
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: 78.10 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG--RKTggytEGDIRISGH------PKEQQTFARISGYVEQN-----D 920
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGllRPD----SGEILVDGQditglsEKELYELRRRIGMLFQGgalfdS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 921 IhspqvTVEESLWFSasLRLPKEITKEQKKEFVEqvMRLveldtlryALVGLPGTTG-----LSTEQRKRLTIAVELVAN 995
Cdd:COG1127 97 L-----TVFENVAFP--LREHTDLSEAEIRELVL--EKL--------ELVGLPGAADkmpseLSGGMRKRVALARALALD 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 330253231 996 PSIIFMDEPTSGLDARAAAIVMRTVRNTVDT-GRTVV 1031
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSV 196
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
847-1057 |
1.14e-15 |
|
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: 77.63 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 847 PETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRktggY--TEGDIRISGHPKEQ---QTFARISGYVEQndi 921
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL----YkpTSGSVLLDGTDIRQldpADLRRNIGYVPQ--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 922 hspqvtveESLWFSASLRlpKEITkeQKKEFV--EQVMRLVELDTLRYALVGLP---------GTTGLSTEQRKRLTIAV 990
Cdd:cd03245 86 --------DVTLFYGTLR--DNIT--LGAPLAddERILRAAELAGVTDFVNKHPngldlqigeRGRGLSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330253231 991 ELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVdTGRTVVCTIHQPSIDifEAFDELLLMKRGGQV 1057
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLL--DLVDRIIVMDSGRIV 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
853-1070 |
1.28e-15 |
|
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: 77.91 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHP---KEQQTFARISGYVEQndihspqvtve 929
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVP--ENGRVLVDGHDlalADPAWLRRQVGVVLQ----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 930 ESLWFSASLRLPKEITKE-QKKEFVEQVMRLV-------ELDTLRYALVGLPGTtGLSTEQRKRLTIAVELVANPSIIFM 1001
Cdd:cd03252 84 ENVLFNRSIRDNIALADPgMSMERVIEAAKLAgahdfisELPEGYDTIVGEQGA-GLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330253231 1002 DEPTSGLDARAAAIVMRTVRNTVDtGRTVVCTIHQPSIdIFEAfDELLLMKRGGQViyggKLGTHSQVL 1070
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLST-VKNA-DRIIVMEKGRIV----EQGSHDELL 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
175-428 |
1.67e-15 |
|
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: 77.37 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkldksLKK--TGNITYNGENLNKFHVKRtsayISQT--------DN 244
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNG-----LLKptSGEVLVDGKDITKKNLRE----LRRKvglvfqnpDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 245 HIAELTVRETLDFAARCQGASEgfagymkdltrlekergirpsSEIDAfmkaasvkgekhsvSTDYVLKVLGLDVCSDtm 324
Cdd:COG1122 87 QLFAPTVEEDVAFGPENLGLPR---------------------EEIRE--------------RVEEALELVGLEHLAD-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 325 vgndmmRGV---SGGQRKRVT-TGEMTVGPrKTLFMDEISTGLDSSTTFQIVKCIRNFvHLMDATVLMAllqpapeTFDL 400
Cdd:COG1122 130 ------RPPhelSGGQKQRVAiAGVLAMEP-EVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIV-------THDL 194
|
250 260 270
....*....|....*....|....*....|....
gi 330253231 401 ------FDDLILLSEGYMVYQGPREDVIAFFESL 428
Cdd:COG1122 195 dlvaelADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
852-1054 |
2.52e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 79.04 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISG-------HPKEQQTfarisGYVEQNDIHSP 924
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETP--DSGRIVLNGrdlftnlPPRERRV-----GFVFQHYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 925 QVTVEESLWFSASLRLPkeiTKEQKKEFVEQVMRLVELDTL--RYalvglPGTtgLSTEQRKRLTIAVELVANPSIIFMD 1002
Cdd:COG1118 89 HMTVAENIAFGLRVRPP---SKAEIRARVEELLELVQLEGLadRY-----PSQ--LSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 330253231 1003 EPTSGLDARAAAIVMRTVRNTVD-TGRTVVCTIHqpsiDIFEAF---DELLLMKRG 1054
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLHDeLGGTTVFVTH----DQEEALelaDRVVVMNQG 210
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
852-1061 |
2.56e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 77.75 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGGYT-EGDIRISGHPKEQQ-TFAR-------ISGYVEQNDIH 922
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSaGSHIELLGRTVQREgRLARdirksraNTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 923 SPQVTVEESLWFSASLRLP------KEITKEQKKEFVEQVMRlVELDTLRYALVglpgtTGLSTEQRKRLTIAVELVANP 996
Cdd:PRK09984 98 VNRLSVLENVLIGALGSTPfwrtcfSWFTREQKQRALQALTR-VGMVHFAHQRV-----STLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330253231 997 SIIFMDEPTSGLDARAAAIVMRTVRNTVDT-GRTVVCTIHQpsIDIFEAFDELLLMKRGGQVIYGG 1061
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQ--VDYALRYCERIVALRQGHVFYDG 235
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
854-1070 |
2.67e-15 |
|
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: 76.89 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAgrKTGGYTEGDIRISGHPKEQQTFA---RISGYVEQnDIHSPQVTVEE 930
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIP--RFYDVDSGRILIDGHDVRDYTLAslrRQIGLVSQ-DVFLFNDTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 931 SLWFSASlrlpkEITKEQKKEFVEQ------VMRLVE-LDTLryalVGLPGTTgLSTEQRKRLTIAVELVANPSIIFMDE 1003
Cdd:cd03251 95 NIAYGRP-----GATREEVEEAARAanahefIMELPEgYDTV----IGERGVK-LSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330253231 1004 PTSGLDARAAAIVMRTVRNTVDtGRTVVCTIHQPSIdIFEAfDELLLMKRGGQViyggKLGTHSQVL 1070
Cdd:cd03251 165 ATSALDTESERLVQAALERLMK-NRTTFVIAHRLST-IENA-DRIVVLEDGKIV----ERGTHEELL 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
853-1012 |
2.98e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.49 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHpkeqqtfARIsGYVEQNDIHSPQVTVEESL 932
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELE--PDSGEVSIPKG-------LRI-GYLPQEPPLDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 933 W--FSASLRLPKEITK-EQKKEFVEQVM--------RLVELD------TLRYALVGLpgttGLSTE------------QR 983
Cdd:COG0488 83 LdgDAELRALEAELEElEAKLAEPDEDLerlaelqeEFEALGgweaeaRAEEILSGL----GFPEEdldrpvselsggWR 158
|
170 180
....*....|....*....|....*....
gi 330253231 984 KRLTIAVELVANPSIIFMDEPTSGLDARA 1012
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
853-1081 |
3.30e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.52 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLaGRKTGGyTEGDIRISGHPKEQ---QTFARISGYVEQNDIHSPQVTVE 929
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPP-SEGEILLDAQPLESwssKAFARKVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 930 ESL------WFSASLRLPKEitkeqKKEFVEQVMRLVELDTLRYALVglpgtTGLSTEQRKRLTIAVELVANPSIIFMDE 1003
Cdd:PRK10575 104 ELVaigrypWHGALGRFGAA-----DREKVEEAISLVGLKPLAHRLV-----DSLSGGERQRAWIAMLVAQDSRCLLLDE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1004 PTSGLDARAAAIVMRTV-RNTVDTGRTVVCTIHqpSIDIFEAFDELLLMKRGGQVIyggKLGTHSQVL-VDYFQGINGVP 1081
Cdd:PRK10575 174 PTSALDIAHQVDVLALVhRLSQERGLTVIAVLH--DINMAARYCDYLVALRGGEMI---AQGTPAELMrGETLEQIYGIP 248
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
854-1063 |
4.13e-15 |
|
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: 76.22 E-value: 4.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIR-----ISGHPKEQQTFarisGYVEQNDIHSPQVTV 928
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKP--DSGKILlngkdITNLPPEKRDI----SYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 929 EESLWFSASLRlpkeitKEQKKEFVEQVMRLVELDTLRYALVGLPGTtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1008
Cdd:cd03299 89 YKNIAYGLKKR------KVDKKEIERKVLEIAEMLGIDHLLNRKPET--LSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 1009 DARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMkRGGQVIYGGKL 1063
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIM-LNGKLIQVGKP 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
854-1060 |
4.64e-15 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 76.08 E-value: 4.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISG------HPKEQQTFARISGYVEQ--NDIHSPq 925
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLER--PTSGSVLVDGtdltllSGKELRKARRRIGMIFQhfNLLSSR- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 926 vTVEEslwfsaSLRLPKEITKEQKKEFVEQVMRLVEldtlryaLVGL-------PGTtgLSTEQRKRLTIAVELVANPSI 998
Cdd:cd03258 98 -TVFE------NVALPLEIAGVPKAEIEERVLELLE-------LVGLedkadayPAQ--LSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330253231 999 IFMDEPTSGLDARAAAIVMRTVRNT-VDTGRTVVCTIHQPSIdIFEAFDELLLMKRGGQVIYG 1060
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEV-VKRICDRVAVMEKGEVVEEG 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
854-1072 |
4.70e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 76.89 E-value: 4.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPKEQQTFARIS------------GYVEQN-- 919
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAP--DAGEVHYRMRDGQLRDLYALSeaerrrllrtewGFVHQHpr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 920 DIHSPQVT----VEESLwFSASLRLPKEItkeqkKEFVEQVMRLVELDTLRyaLVGLPGTtgLSTEQRKRLTIAVELVAN 995
Cdd:PRK11701 100 DGLRMQVSaggnIGERL-MAVGARHYGDI-----RATAGDWLERVEIDAAR--IDDLPTT--FSGGMQQRLQIARNLVTH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 996 PSIIFMDEPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHqpsiDIFEA---FDELLLMKRgGQVIyggKLGTHSQVLV 1071
Cdd:PRK11701 170 PRLVFMDEPTGGLDVSVQARLLDLLRGLVrELGLAVVIVTH----DLAVArllAHRLLVMKQ-GRVV---ESGLTDQVLD 241
|
.
gi 330253231 1072 D 1072
Cdd:PRK11701 242 D 242
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
863-1035 |
5.97e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.54 E-value: 5.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 863 PGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHP-KEQQTFARIS-GYVEQNDIHSPQVTVEESLW-FSASLR 939
Cdd:PRK13537 32 RGECFGLLGPNGAGKTTTLRMLLGLTHP--DAGSISLCGEPvPSRARHARQRvGVVPQFDNLDPDFTVRENLLvFGRYFG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 940 LPKEitkeQKKEFVEQVMRLVELDTLRYALVGlpgttGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRT 1019
Cdd:PRK13537 110 LSAA----AARALVPPLLEFAKLENKADAKVG-----ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWER 180
|
170
....*....|....*.
gi 330253231 1020 VRNTVDTGRTVVCTIH 1035
Cdd:PRK13537 181 LRSLLARGKTILLTTH 196
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
854-1054 |
7.86e-15 |
|
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: 73.62 E-value: 7.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGrkTGGYTEGDIRISGHPKEqqtfarisgyveqndIHSPQvtveeslw 933
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSG--LYKPDSGEILVDGKEVS---------------FASPR-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 934 fsASLRLPkeItkeqkkEFVEQvmrlveldtlryalvglpgttgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA 1013
Cdd:cd03216 71 --DARRAG--I------AMVYQ----------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEV 118
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 330253231 1014 AIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRG 1054
Cdd:cd03216 119 ERLFKVIRRLRAQGVAVIFISHRLD-EVFEIADRVTVLRDG 158
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
862-1038 |
1.00e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.56 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 862 SPGVLTALVGSSGAGKTTL---MDVLAGRKTGGYTEGDIRISG--HPKEQQTFARI----SGYVEQNDIHSPQVTVEESL 932
Cdd:PRK11264 27 KPGEVVAIIGPSGSGKTTLlrcINLLEQPEAGTIRVGDITIDTarSLSQQKGLIRQlrqhVGFVFQNFNLFPHRTVLENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 933 wfsasLRLPKEITKEQKKEFVEQVMRLVeldtlryALVGLPGTTG-----LSTEQRKRLTIAVELVANPSIIFMDEPTSG 1007
Cdd:PRK11264 107 -----IEGPVIVKGEPKEEATARARELL-------AKVGLAGKETsyprrLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190
....*....|....*....|....*....|.
gi 330253231 1008 LDARAAAIVMRTVRNTVDTGRTVVCTIHQPS 1038
Cdd:PRK11264 175 LDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
853-1037 |
1.06e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 74.32 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISG--HPKEQQTFARISGYVEQNDIHSPQVTVEE 930
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP--DSGEVRWNGtpLAEQRDEPHENILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 931 SLWFSASLRLPKEITkeqkkefVEQVMRLVELDTLRYALVGLpgttgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1010
Cdd:TIGR01189 93 NLHFWAAIHGGAQRT-------IEDALAAVGLTGFEDLPAAQ-----LSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*..
gi 330253231 1011 RAAAIVMRTVRNTVDTGRTVVCTIHQP 1037
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
175-423 |
1.50e-14 |
|
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: 78.65 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKF---HVKRTSAYISQtDNHIAELTV 251
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ---SGSITLGGVDLRDLdedDLRRRIAVVPQ-RPHLFDTTL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 252 RETLDFAArcQGASegfagymkdltrlekergirpsseiDAFMKAAsvkgekhsvstdyvLKVLGLD--VCS-----DTM 324
Cdd:COG4987 426 RENLRLAR--PDAT-------------------------DEELWAA--------------LERVGLGdwLAAlpdglDTW 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 325 VGnDMMRGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNfvHLMDATVLMALLQPAPetFDLFDDL 404
Cdd:COG4987 465 LG-EGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE--ALAGRTVLLITHRLAG--LERMDRI 539
|
250
....*....|....*....
gi 330253231 405 ILLSEGYMVYQGPREDVIA 423
Cdd:COG4987 540 LVLEDGRIVEQGTHEELLA 558
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
174-399 |
1.59e-14 |
|
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: 74.11 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 174 NILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFHvKRTsAYISQTD--NHIAELTV 251
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPT---SGSIRVFGKPLEKER-KRI-GYVPQRRsiDRDFPISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 252 RETLdfaarcqgaSEGFAGYMKDLTRLEKErgirpsseidafmkaasvkgEKHSVstDYVLKVLGLDVCSDTMVGNdmmr 331
Cdd:cd03235 88 RDVV---------LMGLYGHKGLFRRLSKA--------------------DKAKV--DEALERVGLSELADRQIGE---- 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 332 gVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNfVHLMDATVLMAL--LQPAPETFD 399
Cdd:cd03235 133 -LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRE-LRREGMTILVVThdLGLVLEYFD 200
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
852-1043 |
2.33e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.16 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG---RKTGGYTEGDIRISGHPKEQQTFARIsGYVEQNDIHSPQVTV 928
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGivpRDAGNIIIDDEDISLLPLHARARRGI-GYLPQEASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 929 EESLWfsASLRLPKEITKEQKKEFVEQVMRLVELDTLRYALvglpgTTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1008
Cdd:PRK10895 96 YDNLM--AVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 330253231 1009 DARAAAIVMRTVRNTVDTGRTVVCTIH--QPSIDIFE 1043
Cdd:PRK10895 169 DPISVIDIKRIIEHLRDSGLGVLITDHnvRETLAVCE 205
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
854-1058 |
2.59e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 74.35 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHPKEQQTFARisGYVEQNDIHSPQVTVEESLW 933
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVP--YQHGSITLDGKPVEGPGAER--GVVFQNEGLLPWRNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 934 FSASLRlpkEITKEQKKEFVEQVMrlveldtlryALVGLPGTTG-----LSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1008
Cdd:PRK11248 93 FGLQLA---GVEKMQRLEIAHQML----------KKVGLEGAEKryiwqLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 330253231 1009 DA--RAAaivMRTVRNTV--DTGRTVVCTIHqpsiDIFEAF---DELLLMKRG-GQVI 1058
Cdd:PRK11248 160 DAftREQ---MQTLLLKLwqETGKQVLLITH----DIEEAVfmaTELVLLSPGpGRVV 210
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
174-423 |
3.11e-14 |
|
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: 77.95 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 174 NILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFHVK--RTS-AYISQtDNHIAELT 250
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT---SGRILIDGIDLRQIDPAslRRQiGVVLQ-DVFLFSGT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 251 VRETLDFAarcqgasegfagymkdltrlekergiRPSSEIDAFMKAAsvkgeKHSVSTDYVLK-VLGLdvcsDTMVGnDM 329
Cdd:COG2274 565 IRENITLG--------------------------DPDATDEEIIEAA-----RLAGLHDFIEAlPMGY----DTVVG-EG 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 330 MRGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHlmDATVLMAllqpA--PETFDLFDDLILL 407
Cdd:COG2274 609 GSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIII----AhrLSTIRLADRIIVL 682
|
250
....*....|....*.
gi 330253231 408 SEGYMVYQGPREDVIA 423
Cdd:COG2274 683 DKGRIVEDGTHEELLA 698
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
853-1061 |
4.06e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.89 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAgR----KTGGYTEGDIRISGHPKEQqtFARISGYVEQndIH-SPQ-V 926
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RlltpQSGTVFLGDKPISMLSSRQ--LARRLALLPQ--HHlTPEgI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 927 TVEE------SLWFSASLRLpkeitKEQKKEFVEQVMRLVELDTLRYALVglpgtTGLSTEQRKRLTIAVELVANPSIIF 1000
Cdd:PRK11231 92 TVRElvaygrSPWLSLWGRL-----SAEDNARVNQAMEQTRINHLADRRL-----TDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330253231 1001 MDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpsiDIFEA---FDELLLMKrGGQVIYGG 1061
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLH----DLNQAsryCDHLVVLA-NGHVMAQG 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
854-1011 |
4.88e-14 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 73.04 E-value: 4.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPKEQ-QTFARISGYVEQNDIHSPQVTVEESL 932
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETP--TSGEILLDGKDITNlPPHKRPVNTVFQNYALFPHLTVFENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 933 WFSASLR-LPKEITKEQkkefVEQVMRLVELDTLRYALVglpgtTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1011
Cdd:cd03300 94 AFGLRLKkLPKAEIKER----VAEALDLVQLEGYANRKP-----SQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
174-423 |
4.95e-14 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 76.72 E-value: 4.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 174 NILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKF---HVKRTSAYISQtDNHIAELT 250
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY---SGSILINGVDLSDLdpaSWRRQIAWVPQ-NPYLFAGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 251 VRETLDFAARcqGASEgfagymkdltrlekergirpsSEIDAFMKAASVKGekhsvstdyVLKVL--GLdvcsDTMVGND 328
Cdd:COG4988 427 IRENLRLGRP--DASD---------------------EELEAALEAAGLDE---------FVAALpdGL----DTPLGEG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 329 mMRGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHlmDATVLMALLQPApeTFDLFDDLILLS 408
Cdd:COG4988 471 -GRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLA--LLAQADRILVLD 545
|
250
....*....|....*
gi 330253231 409 EGYMVYQGPREDVIA 423
Cdd:COG4988 546 DGRIVEQGTHEELLA 560
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
842-1009 |
5.21e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.89 E-value: 5.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 842 RSQGVPETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGGytEGDIRISGHP-----KEQ--QTFARISG 914
Cdd:PRK10584 14 KSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGS--SGEVSLVGQPlhqmdEEAraKLRAKHVG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 915 YVEQNDIHSPQVTVEESLWFSASLRlpkeitKEQKKEFVEQVMRLVELDTLRYALVGLPGTtgLSTEQRKRLTIAVELVA 994
Cdd:PRK10584 92 FVFQSFMLIPTLNALENVELPALLR------GESSRQSRNGAKALLEQLGLGKRLDHLPAQ--LSGGEQQRVALARAFNG 163
|
170
....*....|....*
gi 330253231 995 NPSIIFMDEPTSGLD 1009
Cdd:PRK10584 164 RPDVLFADEPTGNLD 178
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
853-1013 |
6.60e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 72.93 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPKEQQTFA-------RISGYVEQNDIHSPQ 925
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTP--TSGDVIFNGQPMSKLSSAakaelrnQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 926 VTVEESLwfsaslRLPKEITKEQKKEFVEQVMRLVeldtlryALVGLPG-----TTGLSTEQRKRLTIAVELVANPSIIF 1000
Cdd:PRK11629 102 FTALENV------AMPLLIGKKKPAEINSRALEML-------AAVGLEHranhrPSELSGGERQRVAIARALVNNPRLVL 168
|
170
....*....|...
gi 330253231 1001 MDEPTSGLDARAA 1013
Cdd:PRK11629 169 ADEPTGNLDARNA 181
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
850-1031 |
7.46e-14 |
|
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: 72.47 E-value: 7.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 850 RLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG--RKTGgyteGDIR-----ISGHPKEQQTFARIsGYVEQNDIH 922
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGllPPRS----GSIRfdgrdITGLPPHERARAGI-GYVPEGRRI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 923 SPQVTVEESLWFSASLRlpkeiTKEQKKEFVEQVMRLV-ELDTLRYALVGLpgttgLSTEQRKRLTIAVELVANPSIIFM 1001
Cdd:cd03224 87 FPELTVEENLLLGAYAR-----RRAKRKARLERVYELFpRLKERRKQLAGT-----LSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190
....*....|....*....|....*....|
gi 330253231 1002 DEPTSGLDARAAAIVMRTVRNTVDTGRTVV 1031
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEGVTIL 186
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
854-1031 |
7.92e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.83 E-value: 7.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISG------HPKEqqtfARISG----YVEQNDIhs 923
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQ--PDSGEILLDGepvrfrSPRD----AQAAGiaiiHQELNLV-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 924 PQVTVEESLWfsaslrLPKEIT-------KEQKKEfVEQVMRLVELDTLRYALVGlpgttGLSTEQRKRLTIAVELVANP 996
Cdd:COG1129 92 PNLSVAENIF------LGREPRrgglidwRAMRRR-ARELLARLGLDIDPDTPVG-----DLSVAQQQLVEIARALSRDA 159
|
170 180 190
....*....|....*....|....*....|....*
gi 330253231 997 SIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVV 1031
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAII 194
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
854-1019 |
1.16e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 73.95 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISG------HPKEqqtfaRISGYVEQNDIHSPQVT 927
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLED--PTSGEILIGGrdvtdlPPKD-----RNIAMVFQSYALYPHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 928 VEESLWFSasLRLPKeITKEQKKEFVEQVMRLVELDTL--RYalvglPGTtgLSTEQRKRLTIAVELVANPSIIFMDEPT 1005
Cdd:COG3839 92 VYENIAFP--LKLRK-VPKAEIDRRVREAAELLGLEDLldRK-----PKQ--LSGGQRQRVALGRALVREPKVFLLDEPL 161
|
170
....*....|....*.
gi 330253231 1006 SGLDA--RAAaivMRT 1019
Cdd:COG3839 162 SNLDAklRVE---MRA 174
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
868-1075 |
1.78e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.14 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 868 ALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHPkeqqtFARISGYVEQNDIHSPQ---VTVEESlwFSASLRLPKEI 944
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMGYYP--LTEGEIRLDGRP-----LSSLSHSVLRQGVAMVQqdpVVLADT--FLANVTLGRDI 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 945 TKEQkkefVEQVMRLVELDTLR-------YALVGLPGTTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVM 1017
Cdd:PRK10790 442 SEEQ----VWQALETVQLAELArslpdglYTPLGEQGNN-LSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQ 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 330253231 1018 RTVRnTVDTGRTVVCTIHQPSIdIFEAfDELLLMKRGGQViyggKLGTHSQVLVD---YFQ 1075
Cdd:PRK10790 517 QALA-AVREHTTLVVIAHRLST-IVEA-DTILVLHRGQAV----EQGTHQQLLAAqgrYWQ 570
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
852-1070 |
2.28e-13 |
|
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: 71.42 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAgRKtggY--TEGDIRISGHPKEQ---QTFARISGYVEQNdihsPQV 926
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLE-RF---YdpTSGEILLDGVDIRDlnlRWLRSQIGLVSQE----PVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 927 ---TVEESLWFSASLRLPKEITKEQKK----EFVeqvMRLVE-LDTLryalVGlPGTTGLSTEQRKRLTIAVELVANPSI 998
Cdd:cd03249 89 fdgTIAENIRYGKPDATDEEVEEAAKKanihDFI---MSLPDgYDTL----VG-ERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 330253231 999 IFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSIdIFEAfDELLLMKrGGQVIyggKLGTHSQVL 1070
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEAL-DRAMKGRTTIVIAHRLST-IRNA-DLIAVLQ-NGQVV---EQGTHDELM 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
853-1055 |
2.31e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.72 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPKEQQTFARISGYVEQndihSPQvtvEESL 932
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTP--TAGTVLVAGDDVEALSARAASRRVAS----VPQ---DTSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 933 WFSASLRLPKEITK-----------EQKKEFVEQVMRLVELDtlryALVGLPGTTgLSTEQRKRLTIAVELVANPSIIFM 1001
Cdd:PRK09536 89 SFEFDVRQVVEMGRtphrsrfdtwtETDRAAVERAMERTGVA----QFADRPVTS-LSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 1002 DEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpSIDIFEAF-DELLLMKRGG 1055
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDDGKTAVAAIH--DLDLAARYcDELVLLADGR 216
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
175-410 |
2.39e-13 |
|
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: 69.20 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFH---VKRTSAYISQtdnhiaeltv 251
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT---SGEILIDGKDIAKLPleeLRRRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 252 retldfaarcqgasegfagymkdltrlekergirpsseidafmkaasvkgekhsvstdyvlkvlgldvcsdtmvgndmmr 331
Cdd:cd00267 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330253231 332 gVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFvHLMDATVLMALLQPaPETFDLFDDLILLSEG 410
Cdd:cd00267 81 -LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDP-ELAELAADRVIVLKDG 156
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
854-1039 |
2.54e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 70.85 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG--RKtggyTEGDIRISGH-----PKEQQTFAR--IsGYVEQNdiHS- 923
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeeRP----TSGQVLVNGQdlsrlKRREIPYLRrrI-GVVFQD--FRl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 924 -PQVTVEEslwfsaSLRLPKEITKEQKKEF---VEQVMRLVELDTLRYAlvgLPGTtgLSTEQRKRLTIAVELVANPSII 999
Cdd:COG2884 91 lPDRTVYE------NVALPLRVTGKSRKEIrrrVREVLDLVGLSDKAKA---LPHE--LSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 330253231 1000 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1039
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLEL 199
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
853-1037 |
2.56e-13 |
|
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: 70.21 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG--RKTggytEGDIRISGHPKEQQ--TFARISGYVEQNDIHSPQVTV 928
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGlsPPL----AGRVLLNGGPLDFQrdSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 929 EESLWFSASLrlpkeitkeQKKEFVEQVMRLVELDTLRYALVGlpgttGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1008
Cdd:cd03231 91 LENLRFWHAD---------HSDEQVEEALARVGLNGFEDRPVA-----QLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|....*....
gi 330253231 1009 DARAAAIVMRTVRNTVDTGRTVVCTIHQP 1037
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
852-1062 |
2.67e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 71.69 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISG---HPKEQQTFARISGYVEQN-DIHSPQVT 927
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLP--QRGRVKVMGrevNAENEKWVRSKVGLVFQDpDDQVFSST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 928 VEESLWFSAslrLPKEITKEQKKEFVEQVMRLVELDTLRYAlvglpGTTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1007
Cdd:PRK13647 97 VWDDVAFGP---VNMGLDKDEVERRVEEALKAVRMWDFRDK-----PPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 330253231 1008 LDARAAAIVMRTVRNTVDTGRTVVCTIHqpSIDI-FEAFDELLLMKRGGQVIYGGK 1062
Cdd:PRK13647 169 LDPRGQETLMEILDRLHNQGKTVIVATH--DVDLaAEWADQVIVLKEGRVLAEGDK 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
852-1061 |
3.06e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 71.65 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHP-----KEQQTFARISGYVEQN---DIHS 923
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKP--TSGEVLIKGEPikydkKSLLEVRKTVGIVFQNpddQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 924 PqvTVEESLWFSA-SLRLPKEITKEQKKEFVEQVmrlveldtlryalvGLPGTTG-----LSTEQRKRLTIAVELVANPS 997
Cdd:PRK13639 94 P--TVEEDVAFGPlNLGLSKEEVEKRVKEALKAV--------------GMEGFENkpphhLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330253231 998 IIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAFDELLLMKRGGQVIYGG 1061
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD--VDLVPVYADKVYVMSDGKIIKEG 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
854-1057 |
3.88e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.79 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGhpkEQQTFARISGYVEQND--IH-----SPQV 926
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQP--DAGSILIDG---QEMRFASTTAALAAGVaiIYqelhlVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 927 TVEESLWFSaslRLPKE---ITKEQKKEFV-EQVMRL-VELD---TLRYalvglpgttgLSTEQRKRLTIAVELVANPSI 998
Cdd:PRK11288 95 TVAENLYLG---QLPHKggiVNRRLLNYEArEQLEHLgVDIDpdtPLKY----------LSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 330253231 999 IFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRGGQV 1057
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRME-EIFALCDAITVFKDGRYV 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
174-421 |
3.91e-13 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 70.67 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 174 NILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFH------VKRTSAYISQTDNHIA 247
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT---SGSVLIDGTDINKLKgkalrqLRRQIGMIFQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 248 ELTVRETLDFaarcqgaseGFAGYM-------KDLTRLEKERGIrpsseidafmkaasvkgekhsvstdYVLKVLGLDVC 320
Cdd:cd03256 92 RLSVLENVLS---------GRLGRRstwrslfGLFPKEEKQRAL-------------------------AALERVGLLDK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 321 SDTMVGNdmmrgVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMALLQPapetfDL 400
Cdd:cd03256 138 AYQRADQ-----LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQV-----DL 207
|
250 260
....*....|....*....|....*
gi 330253231 401 ----FDDLILLSEGYMVYQGPREDV 421
Cdd:cd03256 208 areyADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
851-1054 |
4.81e-13 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 69.87 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 851 LQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGH--PKEQQTFARIS---GYVEQNDIHSPQ 925
Cdd:cd03262 13 FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEE--PDSGTIIIDGLklTDDKKNINELRqkvGMVFQQFNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 926 VTVEESLWFSaslrlPKEITKEQKKEFVEQVMRLVEldtlryaLVGL-------PGTtgLSTEQRKRLTIAVELVANPSI 998
Cdd:cd03262 91 LTVLENITLA-----PIKVKGMSKAEAEERALELLE-------KVGLadkadayPAQ--LSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 330253231 999 IFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSidiF--EAFDELLLMKRG 1054
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMG---FarEVADRVIFMDDG 211
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
855-1072 |
4.98e-13 |
|
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: 70.63 E-value: 4.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 855 SNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKT--GGYTEGDIRiSGHPKE--------QQTFARIS-GYVEQNDIHS 923
Cdd:TIGR02323 20 RDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLApdHGTATYIMR-SGAELElyqlseaeRRRLMRTEwGFVHQNPRDG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 924 PQVTVEESLWFSASLRLPKEITKEQKKEFVEQVMRLVELDTLRyaLVGLPGTtgLSTEQRKRLTIAVELVANPSIIFMDE 1003
Cdd:TIGR02323 99 LRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDPTR--IDDLPRA--FSGGMQQRLQIARNLVTRPRLVFMDE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1004 PTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHQPSIDIFEAfDELLLMKRgGQVIyggKLGTHSQVLVD 1072
Cdd:TIGR02323 175 PTGGLDVSVQARLLDLLRGLVrDLGLAVIIVTHDLGVARLLA-QRLLVMQQ-GRVV---ESGLTDQVLDD 239
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
175-410 |
5.15e-13 |
|
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: 68.56 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKF---HVKRTSAYISQtDNHIAELTV 251
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT---SGEILIDGVDLRDLdleSLRKNIAYVPQ-DPFLFSGTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 252 RETLdfaarcqgasegfagymkdltrlekergirpsseidafmkaasvkgekhsvstdyvlkvlgldvcsdtmvgndmmr 331
Cdd:cd03228 93 RENI---------------------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 332 gVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFvhLMDATVLMAllqpA--PETFDLFDDLILLSE 409
Cdd:cd03228 97 -LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRAL--AKGKTVIVI----AhrLSTIRDADRIIVLDD 169
|
.
gi 330253231 410 G 410
Cdd:cd03228 170 G 170
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
863-1054 |
6.59e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 71.67 E-value: 6.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 863 PGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGhpkeqQTFARIS------GYVEQNDIHSPQVTVEESLWFSa 936
Cdd:COG3842 30 PGEFVALLGPSGCGKTTLLRMIAGFET--PDSGRILLDG-----RDVTGLPpekrnvGMVFQDYALFPHLTVAENVAFG- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 937 sLRLpKEITKEQKKEFVEQVMRLVELDTL--RYalvglPGTtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA 1014
Cdd:COG3842 102 -LRM-RGVPKAEIRARVAELLELVGLEGLadRY-----PHQ--LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLRE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 330253231 1015 IVMRTVRNTV-DTGRTVVCTIHQPSidifEAF---DELLLMKRG 1054
Cdd:COG3842 173 EMREELRRLQrELGITFIYVTHDQE----EALalaDRIAVMNDG 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
175-416 |
9.71e-13 |
|
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: 67.85 E-value: 9.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDKSLKktGNITYNGENLNKFHVK---RTSAYISQtdnhIAELTv 251
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAG-LLKPSS--GEILLDGKDLASLSPKelaRKIAYVPQ----ALELL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 252 rETLDFAARcqgasegfagymkDLTRLekergirpsseidafmkaasvkgekhsvstdyvlkvlgldvcsdtmvgndmmr 331
Cdd:cd03214 86 -GLAHLADR-------------PFNEL----------------------------------------------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 332 gvSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMAL--LQPApetFDLFDDLILLSE 409
Cdd:cd03214 99 --SGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLhdLNLA---ARYADRVILLKD 173
|
....*..
gi 330253231 410 GYMVYQG 416
Cdd:cd03214 174 GRIVAQG 180
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
852-1062 |
1.19e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 69.33 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKtgGY--TEGDIRISGH------PKEQqtfAR--IsGYVEQNDI 921
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHP--KYevTSGSILLDGEdilelsPDER---ARagI-FLAFQYPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 922 HSPQVTVEESLWFSASLRLPKEITKEQKKEFVEQVMRLVELDT--L-RYALVGLPGttGlsteQRKRLTIAVELVANPSI 998
Cdd:COG0396 88 EIPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEdfLdRYVNEGFSG--G----EKKRNEILQMLLLEPKL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330253231 999 IFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI-DIFEAfDELLLMKrGGQVIY-GGK 1062
Cdd:COG0396 162 AILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRIlDYIKP-DFVHVLV-DGRIVKsGGK 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
852-1064 |
1.68e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 69.65 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPKE---------QQTFARISGYVEQNDIH 922
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRP--QKGAVLWQGKPLDyskrgllalRQQVATVFQDPEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 923 SpqvTVEESLWFS-ASLRLPK-EITKEqkkefVEQVMRLVELDTLRYALVGLpgttgLSTEQRKRLTIAVELVANPSIIF 1000
Cdd:PRK13638 93 T---DIDSDIAFSlRNLGVPEaEITRR-----VDEALTLVDAQHFRHQPIQC-----LSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 1001 MDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpSID-IFEAFDELLLMKRgGQVIYGGKLG 1064
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSH--DIDlIYEISDAVYVLRQ-GQILTHGAPG 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
848-1072 |
2.07e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.88 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 848 ETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGGYteGDIRISG-HPKEQQTFARISGYVEQNDIHS--- 923
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKY--GTIQVGDiYIGDKKNNHELITNPYSKKIKNfke 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 924 -----------PQV-----TVEESLWFS-ASLRLPKEITKEQKKEFVEQvMRLVE--LDTLRYalvglpgttGLSTEQRK 984
Cdd:PRK13631 114 lrrrvsmvfqfPEYqlfkdTIEKDIMFGpVALGVKKSEAKKLAKFYLNK-MGLDDsyLERSPF---------GLSGGQKR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 985 RLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRGGQViyggKLG 1064
Cdd:PRK13631 184 RVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME-HVLEVADEVIVMDKGKIL----KTG 258
|
....*...
gi 330253231 1065 THSQVLVD 1072
Cdd:PRK13631 259 TPYEIFTD 266
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
850-1011 |
2.54e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 70.11 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 850 RLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISG------HPKEQQTfarisGYVEQNDIHS 923
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEH--QTSGHIRFHGtdvsrlHARDRKV-----GFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 924 PQVTVEESLWFSASLrLP--KEITKEQKKEFVEQVMRLVELDTL--RYAlvglpgtTGLSTEQRKRLTIAVELVANPSII 999
Cdd:PRK10851 87 RHMTVFDNIAFGLTV-LPrrERPNAAAIKAKVTQLLEMVQLAHLadRYP-------AQLSGGQKQRVALARALAVEPQIL 158
|
170
....*....|..
gi 330253231 1000 FMDEPTSGLDAR 1011
Cdd:PRK10851 159 LLDEPFGALDAQ 170
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
175-423 |
2.72e-12 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 68.08 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkldksLKK--TGNITYNGENLNKFHVKRTSAYISQT---------- 242
Cdd:COG1127 20 VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIG-----LLRpdSGEILVDGQDITGLSEKELYELRRRIgmlfqggalf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 243 DNhiaeLTVRETLDFaarcqgasegfagYMKDLTRLekergirPSSEIDafmkaasvkgekhsvstDYVLKVLGldvcsd 322
Cdd:COG1127 95 DS----LTVFENVAF-------------PLREHTDL-------SEAEIR-----------------ELVLEKLE------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 323 tMVG----NDMM-RGVSGGQRKRvttgemtVG--------PrKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMA 389
Cdd:COG1127 128 -LVGlpgaADKMpSELSGGMRKR-------VAlaralaldP-EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVV 198
|
250 260 270
....*....|....*....|....*....|....*..
gi 330253231 390 ---LlqpaPETFDLFDDLILLSEGYMVYQGPREDVIA 423
Cdd:COG1127 199 thdL----DSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
162-388 |
3.19e-12 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 67.15 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 162 SLRIIKPRKHKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDKslKKTGNITYNGENLNKFHV----KRTsA 237
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALAD-LDP--PTSGEIYLDGKPLSAMPPpewrRQV-A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 238 YISQtDNHIAELTVRETLDFAARcqgasegFAGYMKDLTRLEKergirpsseidafmkaasvkgekhsvstdyVLKVLGL 317
Cdd:COG4619 78 YVPQ-EPALWGGTVRDNLPFPFQ-------LRERKFDRERALE------------------------------LLERLGL 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 318 DvcsdtmvgNDMM----RGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLM 388
Cdd:COG4619 120 P--------PDILdkpvERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLW 186
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
175-257 |
3.20e-12 |
|
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: 66.27 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFH--VKRTSAYISQTDNHIAELTVR 252
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD---SGEIKVLGKDIKKEPeeVKRRIGYLPEEPSLYENLTVR 91
|
....*
gi 330253231 253 ETLDF 257
Cdd:cd03230 92 ENLKL 96
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
847-1054 |
3.55e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 68.50 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 847 PETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHPKEQQTFARIS---GYVEQN-DIH 922
Cdd:PRK13635 16 PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLL--PEAGTITVGGMVLSEETVWDVRrqvGMVFQNpDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 923 SPQVTVEESLWFSASLRlpkEITKEQKKEFVEQVMRLVELDTLryaLVGLPGTtgLSTEQRKRLTIAVELVANPSIIFMD 1002
Cdd:PRK13635 94 FVGATVQDDVAFGLENI---GVPREEMVERVDQALRQVGMEDF---LNREPHR--LSGGQKQRVAIAGVLALQPDIIILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 1003 EPTSGLDARAAAIVMRTVRNTVDTGR-TVVCTIHqpsiDIFEAF--DELLLMKRG 1054
Cdd:PRK13635 166 EATSMLDPRGRREVLETVRQLKEQKGiTVLSITH----DLDEAAqaDRVIVMNKG 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
853-1035 |
4.19e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.09 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGGytEGDIRISGHPKEQQtfARIS----GYVEQNDIHSPQVTV 928
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD--AGKITVLGVPVPAR--ARLArariGVVPQFDNLDLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 929 EESL-----WFSASLRlpkeitkeQKKEFVEQVMRLVELDTLRYALVGLpgttgLSTEQRKRLTIAVELVANPSIIFMDE 1003
Cdd:PRK13536 132 RENLlvfgrYFGMSTR--------EIEAVIPSLLEFARLESKADARVSD-----LSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190
....*....|....*....|....*....|..
gi 330253231 1004 PTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1035
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
852-1054 |
7.65e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.87 E-value: 7.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYtEGDIRISGHP---KEQQTFARISGYVEQNDiHSPQVTV 928
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP--Y-QGSLKINGIElreLDPESWRKHLSWVGQNP-QLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 929 EESLWFSASLRLPKEIT----KEQKKEFVEQVMRlvELDTlryaLVGlPGTTGLSTEQRKRLTIAVELVANPSIIFMDEP 1004
Cdd:PRK11174 440 RDNVLLGNPDASDEQLQqaleNAWVSEFLPLLPQ--GLDT----PIG-DQAAGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 330253231 1005 TSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQpsIDIFEAFDELLLMKRG 1054
Cdd:PRK11174 513 TASLDAHSEQLVMQAL-NAASRRQTTLMVTHQ--LEDLAQWDQIWVMQDG 559
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
168-364 |
9.11e-12 |
|
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: 66.06 E-value: 9.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 168 PRKHKLNilkDISGIIKPGrMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFHVK--RTSAYISQTDNH 245
Cdd:cd03264 11 GKKRALD---GVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPS---SGTIRIDGQDVLKQPQKlrRRIGYLPQEFGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 246 IAELTVRETLDFAARCQGASEgfagymkdltrlekergirpsseidafmkaasvKGEKHSVstDYVLKVLGLdvcsdTMV 325
Cdd:cd03264 84 YPNFTVREFLDYIAWLKGIPS---------------------------------KEVKARV--DEVLELVNL-----GDR 123
|
170 180 190
....*....|....*....|....*....|....*....
gi 330253231 326 GNDMMRGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLD 364
Cdd:cd03264 124 AKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
863-1054 |
9.63e-12 |
|
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: 70.43 E-value: 9.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 863 PGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGhpkeQQTFARIS------GYVEQNDIHSPQVTVEESLWFSA 936
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTT--VTSGDATVAG----KSILTNISdvhqnmGYCPQFDAIDDLLTGREHLYLYA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 937 SLR-LPKEITKEQKKEFVEQVMRLVELDTLryalvglPGTtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1015
Cdd:TIGR01257 2038 RLRgVPAEEIEKVANWSIQSLGLSLYADRL-------AGT--YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 330253231 1016 VMRTVRNTVDTGRTVVCTIHqpSIDIFEAF-DELLLMKRG 1054
Cdd:TIGR01257 2109 LWNTIVSIIREGRAVVLTSH--SMEECEALcTRLAIMVKG 2146
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
868-1060 |
9.64e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.14 E-value: 9.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 868 ALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPKEQQTFARIS---GYVEQN---DIHSPqvTVEESLWFS-ASLRL 940
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGILKP--TSGSVLIRGEPITKENIREVRkfvGLVFQNpddQIFSP--TVEQDIAFGpINLGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 941 PKEITKEQkkefVEQVMRLVELDTLRYALvglpgTTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1020
Cdd:PRK13652 110 DEETVAHR----VSSALHMLGLEELRDRV-----PHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 330253231 1021 RNTVDT-GRTVVCTIHQPSIdIFEAFDELLLMKRGGQVIYG 1060
Cdd:PRK13652 181 NDLPETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYG 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
852-1035 |
9.96e-12 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 66.41 E-value: 9.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG--RKTGGYTE-GDIRISGHPKEQQtfARIS-GYVEQNDIHSPQVT 927
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGlvKPDSGKILlDGQDITKLPMHKR--ARLGiGYLPQEASIFRKLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 928 VEESLwfSASLRLPKEITKEQKKEfVEQVMRLVELDTLRYALVGlpgttGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1007
Cdd:cd03218 92 VEENI--LAVLEIRGLSKKEREEK-LEELLEEFHITHLRKSKAS-----SLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180
....*....|....*....|....*...
gi 330253231 1008 LDARAAAIVMRTVRNTVDTGRTVVCTIH 1035
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDRGIGVLITDH 191
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
172-423 |
1.59e-11 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 65.53 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 172 KLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKF--H--VKRTSAYISQTDNHIA 247
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR---SGSIRFDGRDITGLppHerARAGIGYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 248 ELTVRETLDFAARCQGASEGFAGY--MKDL-TRLeKERgirpsseidafmkaasvkgekhsvstdyvlkvlgldvcSDTM 324
Cdd:cd03224 89 ELTVEENLLLGAYARRRAKRKARLerVYELfPRL-KER--------------------------------------RKQL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 325 VGNdmmrgVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNfVHLMDATVLMAlLQPAPETFDLFDDL 404
Cdd:cd03224 130 AGT-----LSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRE-LRDEGVTILLV-EQNARFALEIADRA 202
|
250
....*....|....*....
gi 330253231 405 ILLSEGYMVYQGPREDVIA 423
Cdd:cd03224 203 YVLERGRVVLEGTAAELLA 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
821-1058 |
1.79e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.36 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 821 FKPLTMTFHNVnyyVDMPKE----MRSQGVPETRLQ--LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGGYTE 894
Cdd:COG2401 10 LMRVTKVYSSV---LDLSERvaivLEAFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 895 GDIRisghpkeqqtfarisgyVEQNDIhSPQVTVEESlwfsaslrLPKEITKEQKKEFVEQVmRLVELDTLR--YAlvgl 972
Cdd:COG2401 87 GCVD-----------------VPDNQF-GREASLIDA--------IGRKGDFKDAVELLNAV-GLSDAVLWLrrFK---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 973 pgttGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVD-TGRTVVCTIHQPsiDIFEA-FDELLL 1050
Cdd:COG2401 136 ----ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARrAGITLVVATHHY--DVIDDlQPDLLI 209
|
....*...
gi 330253231 1051 MKRGGQVI 1058
Cdd:COG2401 210 FVGYGGVP 217
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
864-1035 |
1.81e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.44 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 864 GVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHPKEQQTFARISGYVEQN---DIHSPqVTVEESLWFS----- 935
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVR--LASGKISILGQPTRQALQKNLVAYVPQSeevDWSFP-VLVEDVVMMGryghm 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 936 ASLRLPKEitkeQKKEFVEQVMRLVELDTLRYALVGlpgttGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1015
Cdd:PRK15056 110 GWLRRAKK----RDRQIVTAALARVDMVEFRHRQIG-----ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEAR 180
|
170 180
....*....|....*....|
gi 330253231 1016 VMRTVRNTVDTGRTVVCTIH 1035
Cdd:PRK15056 181 IISLLRELRDEGKTMLVSTH 200
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
175-421 |
2.00e-11 |
|
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: 65.28 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAG--KLDKSLKKTGNITYNGENLNK-----FHVKRTSAYISQTDNHIA 247
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlnDLIPGAPDEGEVLLDGKDIYDldvdvLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 248 eLTVRETLDFAARCqgasegfagymkdltrlekeRGIRPSSEIDAFMKAAsvkgekhsvstdyvLKVLGLDvcsDTMVGN 327
Cdd:cd03260 95 -GSIYDNVAYGLRL--------------------HGIKLKEELDERVEEA--------------LRKAALW---DEVKDR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 328 DMMRGVSGGQRKRVTTGE-MTVGPRkTLFMDEISTGLDSSTTFQIVKCIRNFVHlmDATVLMA---LLQPApetfDLFDD 403
Cdd:cd03260 137 LHALGLSGGQQQRLCLARaLANEPE-VLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVthnMQQAA----RVADR 209
|
250
....*....|....*...
gi 330253231 404 LILLSEGYMVYQGPREDV 421
Cdd:cd03260 210 TAFLLNGRLVEFGPTEQI 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
854-1061 |
2.03e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 66.41 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHP-----KEQQTFARISGYVEQNDIHSP-QVT 927
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP--SSGRILFDGKPidysrKGLMKLRESVGMVFQDPDNQLfSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 928 VEESLWFSA-SLRLPKEITKEQkkefVEQVMRLVELDTLRYAlvglpGTTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1006
Cdd:PRK13636 100 VYQDVSFGAvNLKLPEDEVRKR----VDNALKRTGIEHLKDK-----PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 330253231 1007 GLDARAAAIVMRTVRNTV-DTGRTVVCTIHqpSIDIFEAF-DELLLMKRGGQVIYGG 1061
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQkELGLTIIIATH--DIDIVPLYcDNVFVMKEGRVILQGN 225
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
826-1081 |
2.07e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.30 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 826 MTFHNVNYYVDMPKEMRSQGVPETRLQLlsnvsgvfSPGVLTALVGSSGAGKTTLMDVLAG--RKTGGYTE-GDIRISGH 902
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRALFDIDLEV--------KKGSYTALIGHTGSGKSTLLQHLNGllQPTEGKVTvGDIVVSST 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 903 PKEQQT--FARISGYVEQndihSPQVTVEESLWFSASLRLPKE--ITKEQKKEFVEQVMRLVELDTLRYAlvglPGTTGL 978
Cdd:PRK13643 74 SKQKEIkpVRKKVGVVFQ----FPESQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEKLEMVGLADEFWE----KSPFEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 979 STEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRGGQVi 1058
Cdd:PRK13643 146 SGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMD-DVADYADYVYLLEKGHII- 223
|
250 260
....*....|....*....|....*.
gi 330253231 1059 yggKLGTHSQVL--VDYFQGIN-GVP 1081
Cdd:PRK13643 224 ---SCGTPSDVFqeVDFLKAHElGVP 246
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
852-1054 |
2.48e-11 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 65.18 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLagRKTGGYTEGDIRISGHPkeqqtfarISGYvEQNDIHSPQVTV-EE 930
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALL--ENFYQPQGGQVLLDGKP--------ISQY-EHKYLHSKVSLVgQE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 931 SLWFSASLR------LP----KEITKEQKKEFVEQVMRLVELDTlrYALVGLPGTTgLSTEQRKRLTIAVELVANPSIIF 1000
Cdd:cd03248 97 PVLFARSLQdniaygLQscsfECVKEAAQKAHAHSFISELASGY--DTEVGEKGSQ-LSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 330253231 1001 MDEPTSGLDARAAAIVMRTVRNTvDTGRTVVCTIHQpsIDIFEAFDELLLMKRG 1054
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYDW-PERRTVLVIAHR--LSTVERADQILVLDGG 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
176-389 |
2.60e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 64.74 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkldKSLKKTGNITYNGENLNKFHVKRTSAY------ISQTDNHIAEL 249
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYK---EELPTSGTIRVNGQDVSDLRGRAIPYLrrkigvVFQDFRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 250 TVRETLDFAARCQGAsegfagymkdltrlekergirPSSEIDAFMKAAsvkgekhsvstdyvLKVLGLDVCSDTMVGndm 329
Cdd:cd03292 94 NVYENVAFALEVTGV---------------------PPREIRKRVPAA--------------LELVGLSHKHRALPA--- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 330 mrGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKcIRNFVHLMDATVLMA 389
Cdd:cd03292 136 --ELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMN-LLKKINKAGTTVVVA 192
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
175-269 |
2.65e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.51 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFHVKRTSAYISQTDNHIAELTVRET 254
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPA---AGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAEN 93
|
90
....*....|....*
gi 330253231 255 LDFAARCQGASEGFA 269
Cdd:PRK13539 94 LEFWAAFLGGEELDI 108
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
176-425 |
2.91e-11 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 65.05 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDKSlkKTGNITYNGENLNKFHVK-RTSAYISQtdnHIA---ELTV 251
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG-LERP--DSGTILFGGEDATDVPVQeRNVGFVFQ---HYAlfrHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 252 RETLDFAARcqgasegfagymkdltrlEKERGIRPSseidafmkAASVKGEKHSVstdyvLKVLGLDvcsdtMVGNDMMR 331
Cdd:cd03296 92 FDNVAFGLR------------------VKPRSERPP--------EAEIRAKVHEL-----LKLVQLD-----WLADRYPA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 332 GVSGGQRKRVTTGE-MTVGPrKTLFMDEISTGLDSsttfQIVKCIRNFV-HLMD----ATVLMALLQpaPETFDLFDDLI 405
Cdd:cd03296 136 QLSGGQRQRVALARaLAVEP-KVLLLDEPFGALDA----KVRKELRRWLrRLHDelhvTTVFVTHDQ--EEALEVADRVV 208
|
250 260
....*....|....*....|....*...
gi 330253231 406 LLSEGYM--------VYQGPREDVIAFF 425
Cdd:cd03296 209 VMNKGRIeqvgtpdeVYDHPASPFVYSF 236
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
852-1016 |
3.30e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 65.44 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLM-------DVLAGRKTggytEGDIRISGHpkeqqtfarisgyveqnDIHSP 924
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPGARV----EGEILLDGE-----------------DIYDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 925 QVTVEEslwfsasLR------------LPKEI--------------TKEQKKEFVEQVMRLVEL-----DTLRyalvgLP 973
Cdd:COG1117 84 DVDVVE-------LRrrvgmvfqkpnpFPKSIydnvayglrlhgikSKSELDEIVEESLRKAALwdevkDRLK-----KS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 330253231 974 GTtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIV 1016
Cdd:COG1117 152 AL-GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKI 193
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
849-1062 |
3.44e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.88 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 849 TRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIR-ISGHPKEQQTFARISGYVEQNDIHSPQV- 926
Cdd:PRK13651 18 TELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLP--DTGTIEwIFKDEKNKKKTKEKEKVLEKLVIQKTRFk 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 927 --------------------------TVEESLWFSA-SLRLPKEITKEQKKEFVEqvmrlveldtlryaLVGLP------ 973
Cdd:PRK13651 96 kikkikeirrrvgvvfqfaeyqlfeqTIEKDIIFGPvSMGVSKEEAKKRAAKYIE--------------LVGLDesylqr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 974 GTTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpSIDIFEAFDELLLMKR 1053
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH--DLDNVLEWTKRTIFFK 239
|
....*....
gi 330253231 1054 GGQVIYGGK 1062
Cdd:PRK13651 240 DGKIIKDGD 248
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
839-1009 |
3.93e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.09 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 839 KEMRSQGVPETR--LQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHP------KEQQTFA 910
Cdd:PRK10419 11 HHYAHGGLSGKHqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESP--SQGNVSWRGEPlaklnrAQRKAFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 911 RISGYVEQNDIHS--PQVTVEESLwfSASLRLPKEITKEQKKEFVEQVMRLVELDTlrYALVGLPGTtgLSTEQRKRLTI 988
Cdd:PRK10419 89 RDIQMVFQDSISAvnPRKTVREII--REPLRHLLSLDKAERLARASEMLRAVDLDD--SVLDKRPPQ--LSGGQLQRVCL 162
|
170 180
....*....|....*....|.
gi 330253231 989 AVELVANPSIIFMDEPTSGLD 1009
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLD 183
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
169-422 |
4.16e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.23 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 169 RKHKLnILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSLKK-----TGNITYNGENLNKFHVKRtsayisqtd 243
Cdd:PRK13547 11 RRHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPrgarvTGDVTLNGEPLAAIDAPR--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 244 nhIAELTvretldfAARCQGASEGFAGYMKDLTRLekerGIRPSseidafmkaASVKGEKHSVSTDYVLKVLGLdVCSDT 323
Cdd:PRK13547 81 --LARLR-------AVLPQAAQPAFAFSAREIVLL----GRYPH---------ARRAGALTHRDGEIAWQALAL-AGATA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 324 MVGNDMMRgVSGGQRKRVT----------TGEMTVGPRkTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMALLQP 393
Cdd:PRK13547 138 LVGRDVTT-LSGGELARVQfarvlaqlwpPHDAAQPPR-YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDP 215
|
250 260 270
....*....|....*....|....*....|...
gi 330253231 394 apetfDL----FDDLILLSEGYMVYQGPREDVI 422
Cdd:PRK13547 216 -----NLaarhADRIAMLADGAIVAHGAPADVL 243
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
824-1057 |
5.37e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 65.19 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 824 LTMTFHNVNYyvdmpkeMRSQGVPeTRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG---RKTGGYTEGDIRIS 900
Cdd:PRK13646 1 MTIRFDNVSY-------TYQKGTP-YEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAllkPTTGTVTVDDITIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 901 GHPKEQ--QTFARISGYVEQndIHSPQV---TVEESLWFSaslrlPKE--ITKEQKKEFVEQVmrLVELDTLRYALVGLP 973
Cdd:PRK13646 73 HKTKDKyiRPVRKRIGMVFQ--FPESQLfedTVEREIIFG-----PKNfkMNLDEVKNYAHRL--LMDLGFSRDVMSQSP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 974 GTtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSiDIFEAFDELLLMK 1052
Cdd:PRK13646 144 FQ--MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlQTDENKTIILVSHDMN-EVARYADEVIVMK 220
|
....*
gi 330253231 1053 RGGQV 1057
Cdd:PRK13646 221 EGSIV 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
822-1075 |
5.66e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.16 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 822 KPLTMTFHNVNYyvdmpkemrsqGVPETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLagrkTGGY--TEGDIRI 899
Cdd:PRK11160 335 DQVSLTLNNVSF-----------TYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL----TRAWdpQQGEILL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 900 SGHP----KEQQTFARISgYVEQNdIHSpqvtveeslwFSASLR----LPK-EITKEQKKEFVEQVmrlvELDTLRYALV 970
Cdd:PRK11160 400 NGQPiadySEAALRQAIS-VVSQR-VHL----------FSATLRdnllLAApNASDEALIEVLQQV----GLEKLLEDDK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 971 GLPGTTG-----LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRnTVDTGRTVVCTIHQpsIDIFEAF 1045
Cdd:PRK11160 464 GLNAWLGeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLA-EHAQNKTVLMITHR--LTGLEQF 540
|
250 260 270
....*....|....*....|....*....|...
gi 330253231 1046 DELLLMKrGGQVIyggKLGTHSQVLVD---YFQ 1075
Cdd:PRK11160 541 DRICVMD-NGQII---EQGTHQELLAQqgrYYQ 569
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
164-389 |
6.01e-11 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 63.91 E-value: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 164 RIIKPRKHKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDKSlkKTGNITYNGENLNKFHVKRTSA------ 237
Cdd:COG1136 12 KSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG-LDRP--TSGEVLIDGQDISSLSERELARlrrrhi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 238 -YISQTDNHIAELTVRETLDFAARCQGASegfagymkdltrlEKERGIRPsseidafmkaasvkgekhsvstDYVLKVLG 316
Cdd:COG1136 89 gFVFQFFNLLPELTALENVALPLLLAGVS-------------RKERRERA----------------------RELLERVG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330253231 317 LDVCSDTMVGNdmmrgVSGGQRKRVTTGEMTVGPRKTLFMDEIsTG-LDSSTTFQIVKCIRNFVHLMDATVLMA 389
Cdd:COG1136 134 LGDRLDHRPSQ-----LSGGQQQRVAIARALVNRPKLILADEP-TGnLDSKTGEEVLELLRELNRELGTTIVMV 201
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
176-416 |
6.95e-11 |
|
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: 63.54 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNG--ENLNKFHVKRTSAYISQTDNHIAELTVRE 253
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD---AGFATVDGfdVVKEPAEARRRLGFVSDSTGLYDRLTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 254 TLDFAARCQGasegfagymkdltrlekergirpsseidafmkaasVKGEKHSVSTDYVLKVLGLDVCSDTMVGndmmrGV 333
Cdd:cd03266 98 NLEYFAGLYG-----------------------------------LKGDELTARLEELADRLGMEELLDRRVG-----GF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 334 SGGQRKRVTTGEMTVGPRKTLFMDEISTGLD---SSTTFQIV-------KCIRNFVHLMDatvlmallqpapETFDLFDD 403
Cdd:cd03266 138 STGMRQKVAIARALVHDPPVLLLDEPTTGLDvmaTRALREFIrqlralgKCILFSTHIMQ------------EVERLCDR 205
|
250
....*....|...
gi 330253231 404 LILLSEGYMVYQG 416
Cdd:cd03266 206 VVVLHRGRVVYEG 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
870-1018 |
8.62e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.44 E-value: 8.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 870 VGSSGAGKTTLMDVLAGRKTggYTEGDIRISGH------PKEqqtfaRISGYVEQNDIHSPQVTVEESLWFSasLRLPKe 943
Cdd:PRK11000 35 VGPSGCGKSTLLRMIAGLED--ITSGDLFIGEKrmndvpPAE-----RGVGMVFQSYALYPHLSVAENMSFG--LKLAG- 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 944 ITKEQKKEFVEQVMRLVELDTLryaLVGLPgtTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDArAAAIVMR 1018
Cdd:PRK11000 105 AKKEEINQRVNQVAEVLQLAHL---LDRKP--KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA-ALRVQMR 173
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
862-1015 |
9.21e-11 |
|
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: 65.12 E-value: 9.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 862 SPGVlTALVGSSGAGKTTLMDVLAG--RKTGGYtegdIRISGH-----------PKEQQtfaRIsGYVEQNDIHSPQVTV 928
Cdd:COG4148 24 GRGV-TALFGPSGSGKTTLLRAIAGleRPDSGR----IRLGGEvlqdsargiflPPHRR---RI-GYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 929 EESLWFSASlRLPKEITKEQkkefVEQVMRLVELDTL--RYalvglPGTtgLSTEQRKRLTIAVELVANPSIIFMDEPTS 1006
Cdd:COG4148 95 RGNLLYGRK-RAPRAERRIS----FDEVVELLGIGHLldRR-----PAT--LSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170
....*....|
gi 330253231 1007 GLD-ARAAAI 1015
Cdd:COG4148 163 ALDlARKAEI 172
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
176-389 |
1.04e-10 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 66.16 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKF---HVKRTSAYISQTDnHIAELTVR 252
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT---EGSIAVNGVPLADAdadSWRDQIAWVPQHP-FLFAGTIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 253 ETLDFAARcqGASEgfagymkdltrlekergirpsseidafmkaASVKGEKHSVSTDYVLKVLGLDVcsDTMVGNDmMRG 332
Cdd:TIGR02857 414 ENIRLARP--DASD------------------------------AEIREALERAGLDEFVAALPQGL--DTPIGEG-GAG 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 330253231 333 VSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFvhLMDATVLMA 389
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLV 513
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
868-1010 |
1.15e-10 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 64.69 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 868 ALVGSSGAGKTTL----MDVLagrKTGGYTEGDIRISGH------PKEQQTF--ARISgYVEQNDIHS--PQVTVEESLw 933
Cdd:COG0444 35 GLVGESGSGKSTLaraiLGLL---PPPGITSGEILFDGEdllklsEKELRKIrgREIQ-MIFQDPMTSlnPVMTVGDQI- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 934 fSASLRLPKEITKEQKKEfveqvmRLVELdtLRyaLVGLPGTTG--------LSTEQRKRLTIAVELVANPSIIFMDEPT 1005
Cdd:COG0444 110 -AEPLRIHGGLSKAEARE------RAIEL--LE--RVGLPDPERrldrypheLSGGMRQRVMIARALALEPKLLIADEPT 178
|
....*
gi 330253231 1006 SGLDA 1010
Cdd:COG0444 179 TALDV 183
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
847-1062 |
1.20e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.86 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 847 PETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG-RKTggyTEGDIRISGHPKEQQTFARIS---GYVEQN-DI 921
Cdd:PRK13632 18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGlLKP---QSGEIKIDGITISKENLKEIRkkiGIIFQNpDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 922 HSPQVTVEESLWFSASlrlPKEITKEQKKEFVEQVMRLVELDTLryaLVGLPgtTGLSTEQRKRLTIAVELVANPSIIFM 1001
Cdd:PRK13632 95 QFIGATVEDDIAFGLE---NKKVPPKKMKDIIDDLAKKVGMEDY---LDKEP--QNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330253231 1002 DEPTSGLDARAAAIV---MRTVRNTVDtgRTVVCTIHqpsiDIFEAF--DELLLMKrGGQVIYGGK 1062
Cdd:PRK13632 167 DESTSMLDPKGKREIkkiMVDLRKTRK--KTLISITH----DMDEAIlaDKVIVFS-EGKLIAQGK 225
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
854-1054 |
1.41e-10 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 62.90 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLmdVLAGRKTGGYTEGDIRISGH-----------------PKEQQTFariSGYV 916
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSL--LLALFRLVELSSGSILIDGVdiskiglhdlrsrisiiPQDPVLF---SGTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 917 EQN----DIHSpqvtvEESLWfsaslrlpkEITKE-QKKEFVEQVMRLVELDTLRyalvglpGTTGLSTEQRKRLTIAVE 991
Cdd:cd03244 95 RSNldpfGEYS-----DEELW---------QALERvGLKEFVESLPGGLDTVVEE-------GGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330253231 992 LVANPSIIFMDEPTSGLDARAAAIVMRTVRnTVDTGRTVVCTIHQpsIDIFEAFDELLLMKRG 1054
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIR-EAFKDCTVLTIAHR--LDTIIDSDRILVLDKG 213
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
827-1054 |
2.23e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 64.98 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 827 TFHNVNYYVDMpkemRSQGVpetrlqllSNVSGVFSPGVLTALVGSSGAGKTTLMDVLagRKTGGYTEGDIRISGhpkeq 906
Cdd:PRK13657 336 EFDDVSFSYDN----SRQGV--------EDVSFEAKPGQTVAIVGPTGAGKSTLINLL--QRVFDPQSGRILIDG----- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 907 qtfARISGYVEQNDIHSPQVTVEESLWFSAS----LRLPKE-ITKEQKKEFVE--QVMRLVELDTLRY-ALVGLPGTTgL 978
Cdd:PRK13657 397 ---TDIRTVTRASLRRNIAVVFQDAGLFNRSiednIRVGRPdATDEEMRAAAEraQAHDFIERKPDGYdTVVGERGRQ-L 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330253231 979 STEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSIdIFEAfDELLLMKRG 1054
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAAL-DELMKGRTTFIIAHRLST-VRNA-DRILVFDNG 545
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
168-423 |
2.92e-10 |
|
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: 64.54 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 168 PRKHKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDKSlkKTGNITYNGENLNKFHVKRTSA------YISQ 241
Cdd:COG1123 273 RGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG-LLRP--TSGSILFDGKDLTKLSRRSLRElrrrvqMVFQ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 242 TDNH--IAELTVRETLDFAARCqgasegfagymkdltrlekeRGIRPSSEIDAfmKAASvkgekhsvstdyVLKVLGLDv 319
Cdd:COG1123 350 DPYSslNPRMTVGDIIAEPLRL--------------------HGLLSRAERRE--RVAE------------LLERVGLP- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 320 csdtmvgNDMMR----GVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMAllqpap 395
Cdd:COG1123 395 -------PDLADryphELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFI------ 461
|
250 260 270
....*....|....*....|....*....|....
gi 330253231 396 eTFDL------FDDLILLSEGYMVYQGPREDVIA 423
Cdd:COG1123 462 -SHDLavvryiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
851-1072 |
3.66e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 64.74 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 851 LQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRktggY--TEGDIRISGHPKEQqtfarisgyVEQNDIHSPQVTV 928
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL----YqpTGGQVLLDGVPLVQ---------YDHHYLHRQVALV 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 929 -EESLWFSASLRlpKEITKEQKKEFVEQVMRLVELDTLRYALVGLP-------GTTG--LSTEQRKRLTIAVELVANPSI 998
Cdd:TIGR00958 561 gQEPVLFSGSVR--ENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPngydtevGEKGsqLSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 999 IFMDEPTSGLDARaaaiVMRTVRNTVDT-GRTVVCTIHQPSidIFEAFDELLLMKRGGQViyggKLGTHSQVLVD 1072
Cdd:TIGR00958 639 LILDEATSALDAE----CEQLLQESRSRaSRTVLLIAHRLS--TVERADQILVLKKGSVV----EMGTHKQLMED 703
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
176-277 |
3.69e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.17 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkktGNITYNGENLNKFHVK---RTSAYISQTDNHIAELTVR 252
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ----GEILLNGRPLSDWSAAelaRHRAYLSQQQSPPFAMPVF 87
|
90 100
....*....|....*....|....*
gi 330253231 253 ETLDFAARCQGASEGFAGYMKDLTR 277
Cdd:COG4138 88 QYLALHQPAGASSEAVEQLLAQLAE 112
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
854-1060 |
3.88e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 62.31 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISG----HPKEQQTFARISGYVEQNdihsPQV--- 926
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRP--QKGKVLVSGidtgDFSKLQGIRKLVGIVFQN----PETqfv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 927 --TVEESLWFSA-SLRLPK-EITKEqkkefVEQVMRLVELDTLRYALvglPGTtgLSTEQRKRLTIAVELVANPSIIFMD 1002
Cdd:PRK13644 92 grTVEEDLAFGPeNLCLPPiEIRKR-----VDRALAEIGLEKYRHRS---PKT--LSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 330253231 1003 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpSIDIFEAFDELLLMKRGGQVIYG 1060
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGKTIVYITH--NLEELHDADRIIVMDRGKIVLEG 217
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
847-1009 |
4.09e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 63.06 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 847 PETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGH-----PKEQQTFARIS-GYVEQND 920
Cdd:PRK11308 24 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETP--TGGELYYQGQdllkaDPEAQKLLRQKiQIVFQNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 921 IHS--PQVTVEESLwfSASLRLPKEITKEQKKEFVEQVMRLVELDT---LRYALVglpgttgLSTEQRKRLTIAVELVAN 995
Cdd:PRK11308 102 YGSlnPRKKVGQIL--EEPLLINTSLSAAERREKALAMMAKVGLRPehyDRYPHM-------FSGGQRQRIAIARALMLD 172
|
170
....*....|....
gi 330253231 996 PSIIFMDEPTSGLD 1009
Cdd:PRK11308 173 PDVVVADEPVSALD 186
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
854-1054 |
4.31e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.08 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHPKEQQTFARIS---GYVEQNdihsPQVT-VE 929
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEK--VKSGEIFYNNQAITDDNFEKLRkhiGIVFQN----PDNQfVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 930 ESLWFSASLRLPKE-ITKEQKKEFVEQVmrLVELDTLRYAlvgLPGTTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1008
Cdd:PRK13648 99 SIVKYDVAFGLENHaVPYDEMHRRVSEA--LKQVDMLERA---DYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 330253231 1009 DARAAAIVMRTVRNT-VDTGRTVVCTIHqpsiDIFEAF--DELLLMKRG 1054
Cdd:PRK13648 174 DPDARQNLLDLVRKVkSEHNITIISITH----DLSEAMeaDHVIVMNKG 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
824-1054 |
4.85e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 62.15 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 824 LTMTFHNVNYYVDMPKEMRSQGvpetrlqlLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHP 903
Cdd:PRK13641 1 MSIKFENVDYIYSPGTPMEKKG--------LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKP--SSGTITIAGYH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 904 KEQQT-------FARISGYVEQndihSPQV-----TVEESLWFSaslrlPKE--ITKEQKKEFVEQVMRLVELDTLryal 969
Cdd:PRK13641 71 ITPETgnknlkkLRKKVSLVFQ----FPEAqlfenTVLKDVEFG-----PKNfgFSEDEAKEKALKWLKKVGLSED---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 970 VGLPGTTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELL 1049
Cdd:PRK13641 138 LISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMD-DVAEYADDVL 216
|
....*
gi 330253231 1050 LMKRG 1054
Cdd:PRK13641 217 VLEHG 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
830-1057 |
5.61e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 830 NVNYYVDMPKEMRSQGVpetrLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGH--PKEQQ 907
Cdd:PRK09700 1 MATPYISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP--TKGTITINNInyNKLDH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 908 TFARISG----YVEQNDIHspQVTVEESLWFSaslRLP-KEIT-------KEQKKEFVEQVMRL---VELDTlryaLVGl 972
Cdd:PRK09700 75 KLAAQLGigiiYQELSVID--ELTVLENLYIG---RHLtKKVCgvniidwREMRVRAAMMLLRVglkVDLDE----KVA- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 973 pgttGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA---IVMRTVRNtvdTGRTVVCTIHQPSiDIFEAFDELL 1049
Cdd:PRK09700 145 ----NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDylfLIMNQLRK---EGTAIVYISHKLA-EIRRICDRYT 216
|
....*...
gi 330253231 1050 LMKRGGQV 1057
Cdd:PRK09700 217 VMKDGSSV 224
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
799-1070 |
5.81e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.58 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 799 EETALVADANQVISEKKGMilpfkpLTMTFHNVNYyvdmpkemrsqgvPETRLQLLSNVSGVFSPGVLTALVGSSGAGKT 878
Cdd:PRK10789 295 AEAPVVKDGSEPVPEGRGE------LDVNIRQFTY-------------PQTDHPALENVNFTLKPGQMLGICGPTGSGKS 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 879 TLMDVLagRKTGGYTEGDIRISGHPKEQqtfarisgyVEQNDIHSPQVTVEES-LWFSAS------LRLPkEITKEQkke 951
Cdd:PRK10789 356 TLLSLI--QRHFDVSEGDIRFHDIPLTK---------LQLDSWRSRLAVVSQTpFLFSDTvanniaLGRP-DATQQE--- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 952 fVEQVMRL--VELDTLRyalvgLP-------GTTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1020
Cdd:PRK10789 421 -IEHVARLasVHDDILR-----LPqgydtevGERGvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNL 494
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 330253231 1021 RNTVDtGRTVVCTIHQPSIdIFEAfDELLLMKRGGQViyggKLGTHSQVL 1070
Cdd:PRK10789 495 RQWGE-GRTVIISAHRLSA-LTEA-SEILVMQHGHIA----QRGNHDQLA 537
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
174-422 |
6.08e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.57 E-value: 6.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 174 NILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAgKLDKSlkKTGNITYNGENLNKFHVKRTSAYISQTDNH--IAE-LT 250
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RLLTP--QSGTVFLGDKPISMLSSRQLARRLALLPQHhlTPEgIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 251 VRETLDFaarcqgaseGFAGYMKDLTRLEKErgirpsseidafmkaasvkgEKHSVstDYVLKVLGLDVCSDTMVGNdmm 330
Cdd:PRK11231 93 VRELVAY---------GRSPWLSLWGRLSAE--------------------DNARV--NQAMEQTRINHLADRRLTD--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 331 rgVSGGQRKRVTTGeMTVGPRKTLFM-DEISTGLDssttfqivkcIRNFVHLMDatvLMALLQPAPETF-----DL---- 400
Cdd:PRK11231 139 --LSGGQRQRAFLA-MVLAQDTPVVLlDEPTTYLD----------INHQVELMR---LMRELNTQGKTVvtvlhDLnqas 202
|
250 260
....*....|....*....|....
gi 330253231 401 --FDDLILLSEGYMVYQGPREDVI 422
Cdd:PRK11231 203 ryCDHLVVLANGHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
176-450 |
7.72e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 61.79 E-value: 7.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNK-----FHVKRTSAYISQT-DNHIAEL 249
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPS---SGRILFDGKPIDYsrkglMKLRESVGMVFQDpDNQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 250 TVRETLDFAARcqgasegfagymkDLTRLEKERGIRpsseIDAFMKAASVKGEKHSVStdyvlkvlgldvcsdtmvgndm 329
Cdd:PRK13636 99 SVYQDVSFGAV-------------NLKLPEDEVRKR----VDNALKRTGIEHLKDKPT---------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 330 mRGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMAllqpapeTFDL------FDD 403
Cdd:PRK13636 140 -HCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIA-------THDIdivplyCDN 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 330253231 404 LILLSEGYMVYQGPREDVIA---FFESLGFRLpPRKGvadFLQEVTSKKD 450
Cdd:PRK13636 212 VFVMKEGRVILQGNPKEVFAekeMLRKVNLRL-PRIG---HLMEILKEKD 257
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
175-410 |
9.06e-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: 59.79 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGenlnkfhvkrTSAYISQTdnhiAEL---TV 251
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKL---SGSVSVPG----------SIAYVSQE----PWIqngTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 252 RETLDFAArcqgasegfagymkdltRLEKERgirpsseidafmkaasvkgekhsvsTDYVLKVLGLDVCSDTMVGNDMM- 330
Cdd:cd03250 83 RENILFGK-----------------PFDEER-------------------------YEKVIKACALEPDLEILPDGDLTe 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 331 ---RGV--SGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIV-KCIRNfvHLMD-ATVLMA-----LLQPApetf 398
Cdd:cd03250 121 igeKGInlSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILG--LLLNnKTRILVthqlqLLPHA---- 194
|
250
....*....|..
gi 330253231 399 dlfDDLILLSEG 410
Cdd:cd03250 195 ---DQIVVLDNG 203
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
854-1063 |
9.59e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.64 E-value: 9.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSgvFS--PGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGH-P-KEQQTFARISGYV----EQndihspq 925
Cdd:COG4586 38 VDDIS--FTiePGEIVGFIGPNGAGKSTTIKMLTGILVP--TSGEVRVLGYvPfKRRKEFARRIGVVfgqrSQ------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 926 vtveesLWF----SASLRLPKEITKEQKKEFVEQVMRLVELDTLRyALVGLPgTTGLSTEQRKRLTIAVELVANPSIIFM 1001
Cdd:COG4586 107 ------LWWdlpaIDSFRLLKAIYRIPDAEYKKRLDELVELLDLG-ELLDTP-VRQLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330253231 1002 DEPTSGLDaraaAIVMRTVRNTV-----DTGRTVVCTIHQPSiDIfEAFDELLLMKRGGQVIYGGKL 1063
Cdd:COG4586 179 DEPTIGLD----VVSKEAIREFLkeynrERGTTILLTSHDMD-DI-EALCDRVIVIDHGRIIYDGSL 239
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
175-372 |
9.65e-10 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 62.76 E-value: 9.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFHVKRTSAYISQT--DNHIAELTVR 252
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL---QGEVTLDGVPVSSLDQDEVRRRVSVCaqDAHLFDTTVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 253 ETLDFAarCQGASEgfAGYMKDLTRLEKERGIRPSSEidafmkaasvkgekhsvstdyvlkvlGLdvcsDTMVGNDMMRg 332
Cdd:TIGR02868 427 ENLRLA--RPDATD--EELWAALERVGLADWLRALPD--------------------------GL----DTVLGEGGAR- 471
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 330253231 333 VSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIV 372
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELL 511
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
852-1060 |
9.99e-10 |
|
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: 60.12 E-value: 9.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLmdVLAGRKTGGYTEGDIRISGhpkeqqtfarisgyveQNDIHSPQVTVEES 931
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTL--ILALFRFLEAEEGKIEIDG----------------IDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 932 L--------WFSASLRLPKEITKEQKKEFVEQVMRLVEldtlryalvglpGTTGLSTEQRKRLTIAVELVANPSIIFMDE 1003
Cdd:cd03369 84 LtiipqdptLFSGTIRSNLDPFDEYSDEEIYGALRVSE------------GGLNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 330253231 1004 PTSGLDARAAAIVMRTVRNTVdTGRTVVCTIH--QPSIDifeaFDELLLMKRGGQVIYG 1060
Cdd:cd03369 152 ATASIDYATDALIQKTIREEF-TNSTILTIAHrlRTIID----YDKILVMDAGEVKEYD 205
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
854-1058 |
1.06e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLagrkTGGYTE--GDIRISGH------PKEQQTfARIS-GYVEQNDIhsP 924
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVL----TGIYTRdaGSILYLGKevtfngPKSSQE-AGIGiIHQELNLI--P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 925 QVTVEESLWfsaslrLPKEITKE----QKKEFVEQVMRLVELDTLRYALVGLPGTtgLSTEQRKRLTIAVELVANPSIIF 1000
Cdd:PRK10762 93 QLTIAENIF------LGREFVNRfgriDWKKMYAEADKLLARLNLRFSSDKLVGE--LSIGEQQMVEIAKVLSFESKVII 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 330253231 1001 MDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMkRGGQVI 1058
Cdd:PRK10762 165 MDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLK-EIFEICDDVTVF-RDGQFI 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
175-227 |
1.48e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 60.17 E-value: 1.48e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENL 227
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD---SGEVRLNGRPL 66
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
175-423 |
1.54e-09 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 59.82 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDKSLKktGNITYNGENLNK------FHVKRTSAYISQ-----TD 243
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVG-LLRPDS--GEVLIDGEDISGlseaelYRLRRRMGMLFQsgalfDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 244 nhiaeLTVRETLDFAARcqgasegfagymkdltrlekERGIRPSSEIDafmkaasvkgekhsvstDYVLKVLGldvcsdt 323
Cdd:cd03261 92 -----LTVFENVAFPLR--------------------EHTRLSEEEIR-----------------EIVLEKLE------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 324 MVG----NDMMRG-VSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMALLQpAPETF 398
Cdd:cd03261 123 AVGlrgaEDLYPAeLSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHD-LDTAF 201
|
250 260
....*....|....*....|....*
gi 330253231 399 DLFDDLILLSEGYMVYQGPREDVIA 423
Cdd:cd03261 202 AIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
183-423 |
1.67e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 59.77 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 183 IKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFHV-KRTSAYISQTDNHIAELTVRETLDFaarc 261
Cdd:COG3840 22 IAAGERVAILGPSGAGKSTLLNLIAGFLPPD---SGRILWNGQDLTALPPaERPVSMLFQENNLFPHLTVAQNIGL---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 262 qgasegfagymkdltrlekerGIRPSSEIDAfmkaasvkGEKHSVSTdyVLKVLGLDVCSDTMVGNdmmrgVSGGQRKRV 341
Cdd:COG3840 95 ---------------------GLRPGLKLTA--------EQRAQVEQ--ALERVGLAGLLDRLPGQ-----LSGGQRQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 342 TTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMALLQPApETFDLFDDLILLSEGYMVYQGPREDV 421
Cdd:COG3840 139 ALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPE-DAARIADRVLLVADGRIAADGPTAAL 217
|
..
gi 330253231 422 IA 423
Cdd:COG3840 218 LD 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
826-1061 |
1.72e-09 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 58.48 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 826 MTFHNVNYyvdmpkemrsqGVPETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPke 905
Cdd:cd03247 1 LSINNVSF-----------SYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKP--QQGEITLDGVP-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 906 qqtfarISGYVEQndihspqvtveeslwfsaslrLPKEITkeqkkeFVEQVMRLVElDTLRYALvGLPgttgLSTEQRKR 985
Cdd:cd03247 66 ------VSDLEKA---------------------LSSLIS------VLNQRPYLFD-TTLRNNL-GRR----FSGGERQR 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330253231 986 LTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNtVDTGRTVV-CTIHQPSIdifEAFDELLLMKRgGQVIYGG 1061
Cdd:cd03247 107 LALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFE-VLKDKTLIwITHHLTGI---EHMDKILFLEN-GKIIMQG 178
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
176-423 |
1.79e-09 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 59.76 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLN--KFHvKRTSAYIS---QTDNHIAELT 250
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT---SGSVLFDGEDITglPPH-EIARLGIGrtfQIPRLFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 251 VRETLDFAARCQGASEGFAGymkdltrlekergiRPSSEIDAFMKAAsvkgekhsvstDYVLKVLGLDVCSDTMVGNdmm 330
Cdd:cd03219 92 VLENVMVAAQARTGSGLLLA--------------RARREEREARERA-----------EELLERVGLADLADRPAGE--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 331 rgVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNfVHLMDATVL-----MALLqpapetFDLFDDLI 405
Cdd:cd03219 144 --LSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRE-LRERGITVLlvehdMDVV------MSLADRVT 214
|
250
....*....|....*...
gi 330253231 406 LLSEGYMVYQGPREDVIA 423
Cdd:cd03219 215 VLDQGRVIAEGTPDEVRN 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
854-1038 |
1.86e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.17 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTL------MDVLAGRKTggyTEGDIRISGH----PKEQQTFARIS-GYVEQNDIH 922
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLlrsinrMNDLNPEVT---ITGSIVYNGHniysPRTDTVDLRKEiGMVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 923 SPQVTVEESLWfsaSLRLPKEITKEQKKEFVEQVMRLVEL-----DTLRYALVGLPGTtglsteQRKRLTIAVELVANPS 997
Cdd:PRK14239 98 FPMSIYENVVY---GLRLKGIKDKQVLDEAVEKSLKGASIwdevkDRLHDSALGLSGG------QQQRVCIARVLATSPK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 330253231 998 IIFMDEPTSGLDARAAAIVMRTVRNTVD--TGRTVVCTIHQPS 1038
Cdd:PRK14239 169 IILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRSMQQAS 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
176-416 |
2.07e-09 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 59.14 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFH---VKRTSAYISQtDNHIAELTVR 252
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT---SGSVLLDGTDIRQLDpadLRRNIGYVPQ-DVTLFYGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 253 ETLDFAArcqgasegfagymkdltrlekergirPSSEIDAFMKAASVKGekhsvSTDYVLK-VLGLdvcsDTMVGnDMMR 331
Cdd:cd03245 96 DNITLGA--------------------------PLADDERILRAAELAG-----VTDFVNKhPNGL----DLQIG-ERGR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 332 GVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFvhLMDATVLMALLQPApeTFDLFDDLILLSEGY 411
Cdd:cd03245 140 GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL--LGDKTLIIITHRPS--LLDLVDRIIVMDSGR 215
|
....*
gi 330253231 412 MVYQG 416
Cdd:cd03245 216 IVADG 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
863-1009 |
2.21e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 59.60 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 863 PGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPKEQQTFAR--ISGYVEQNDIHsPQVTVEE--SLWFSASL 938
Cdd:PRK10771 24 RGERVAILGPSGAGKSTLLNLIAGFLTP--ASGSLTLNGQDHTTTPPSRrpVSMLFQENNLF-SHLTVAQniGLGLNPGL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 330253231 939 RLpkeiTKEQKKEfVEQVMRLVELDTLryaLVGLPGTtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1009
Cdd:PRK10771 101 KL----NAAQREK-LHAIARQMGIEDL---LARLPGQ--LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
844-1054 |
2.63e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 58.63 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 844 QGVPETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG--RKtggyTEGDIRISGhpkeqqtfaRISgYVEQndi 921
Cdd:cd03250 11 DSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGelEK----LSGSVSVPG---------SIA-YVSQ--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 922 hSPqvtveeslW-FSASLRlpKEIT--KEQKKEFVEQVMRLVELD-----------TlryaLVGLPGTTgLSTEQRKRLT 987
Cdd:cd03250 74 -EP--------WiQNGTIR--ENILfgKPFDEERYEKVIKACALEpdleilpdgdlT----EIGEKGIN-LSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330253231 988 IAVELVANPSIIFMDEPTSGLDAR-AAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAFDELLLMKRG 1054
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHvGRHIFENCILGLLLNNKTRILVTHQ--LQLLPHADQIVVLDNG 203
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
854-1009 |
2.82e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTT----LMDVLAgrktggyTEGDIRISGHPKEQQT------FARISGYVEQ--NDI 921
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-------SQGEIWFDGQPLHNLNrrqllpVRHRIQVVFQdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 922 HSPQVTVEESLwfSASLRL-PKEITKEQKKEFVEQVMRLVELDTL---RYAlvglpgtTGLSTEQRKRLTIAVELVANPS 997
Cdd:PRK15134 375 LNPRLNVLQII--EEGLRVhQPTLSAAQREQQVIAVMEEVGLDPEtrhRYP-------AEFSGGQRQRIAIARALILKPS 445
|
170
....*....|..
gi 330253231 998 IIFMDEPTSGLD 1009
Cdd:PRK15134 446 LIILDEPTSSLD 457
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
852-1036 |
2.93e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 59.26 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGH---------PKEQQTFARISGYVEQNDIH 922
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMP--RSGTLNIAGNhfdfsktpsDKAIRELRRNVGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 923 SPQVTVEESLwfsasLRLPKEITKEQKKEFVEQVMRLveLDTLRYALVGLPGTTGLSTEQRKRLTIAVELVANPSIIFMD 1002
Cdd:PRK11124 94 WPHLTVQQNL-----IEAPCRVLGLSKDQALARAEKL--LERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190
....*....|....*....|....*....|....
gi 330253231 1003 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1036
Cdd:PRK11124 167 EPTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
852-1036 |
5.57e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 58.18 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISG----HPKEQQTFARI-SGYVEQNDIHSPQV 926
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEE--ITSGDLIVDGlkvnDPKVDERLIRQeAGMVFQQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 927 TVEESLWFSaslrlPKEITKEQKKEFVEQVMRLVeldtlryALVGLPGTTG-----LSTEQRKRLTIAVELVANPSIIFM 1001
Cdd:PRK09493 93 TALENVMFG-----PLRVRGASKEEAEKQARELL-------AKVGLAERAHhypseLSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190
....*....|....*....|....*....|....*
gi 330253231 1002 DEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1036
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
166-416 |
5.84e-09 |
|
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: 57.90 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 166 IKPRKHKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDKslKKTGNITYNGENLNKFHVKRTS------AYI 239
Cdd:cd03257 11 FPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILG-LLK--PTSGSIIFDGKDLLKLSRRLRKirrkeiQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 240 SQtdNHIAEL----TVRETLDFAARCQGASEGFAgyMKDLTRLEKERGIRPSSEidafmkaasvkgekhsvstdyvlkvl 315
Cdd:cd03257 88 FQ--DPMSSLnprmTIGEQIAEPLRIHGKLSKKE--ARKEAVLLLLVGVGLPEE-------------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 316 gldvcsdtmVGNDMMRGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMAllqpap 395
Cdd:cd03257 138 ---------VLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFI------ 202
|
250 260
....*....|....*....|....*..
gi 330253231 396 eTFDL------FDDLILLSEGYMVYQG 416
Cdd:cd03257 203 -THDLgvvakiADRVAVMYAGKIVEEG 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
863-1031 |
5.90e-09 |
|
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: 58.07 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 863 PGVLTALVGSSGAGKTTLMDVLAG--RKTGgyteGDIR-----ISGHPkeqqTFARIS---GYVEQN-DIHsPQVTVEES 931
Cdd:COG0410 28 EGEIVALLGRNGAGKTTLLKAISGllPPRS----GSIRfdgedITGLP----PHRIARlgiGYVPEGrRIF-PSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 932 LWFSASLRLPKEITKEQkkefVEQVMRLV-ELDTLRYALVGLpgttgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1010
Cdd:COG0410 99 LLLGAYARRDRAEVRAD----LERVYELFpRLKERRRQRAGT-----LSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAP 169
|
170 180
....*....|....*....|.
gi 330253231 1011 RAAAIVMRTVRNTVDTGRTVV 1031
Cdd:COG0410 170 LIVEEIFEIIRRLNREGVTIL 190
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
869-1062 |
6.04e-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: 60.20 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 869 LVGSSGAGKTTLMDVLAGRKTGGYTEGDIRISGH--------PKEQQTFARISGYVEQNDIHSPQVTVEESLWFSASLRL 940
Cdd:TIGR03269 315 IVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEwvdmtkpgPDGRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLEL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 941 PKEITKeqKKEFVEQVMRLVELDTLRYALVGLPGTtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDaraaAIVMRTV 1020
Cdd:TIGR03269 395 PDELAR--MKAVITLKMVGFDEEKAEEILDKYPDE--LSEGERHRVALAQVLIKEPRIVILDEPTGTMD----PITKVDV 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 330253231 1021 RNTV-----DTGRTVVCTIHqpSID-IFEAFDELLLMkRGGQVIYGGK 1062
Cdd:TIGR03269 467 THSIlkareEMEQTFIIVSH--DMDfVLDVCDRAALM-RDGKIVKIGD 511
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
842-1039 |
7.33e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 60.12 E-value: 7.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 842 RSQGVPETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLagrktgGY----TEGDIRISGH---PKEQQTFARIS- 913
Cdd:PRK10535 12 RSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL------GCldkpTSGTYRVAGQdvaTLDADALAQLRr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 914 ---GYVEQNDIHSPQVTVEESLWFSASLR-LPKeitKEQKKEFVEQVMRLVELDTLRYAlvglPGTtgLSTEQRKRLTIA 989
Cdd:PRK10535 86 ehfGFIFQRYHLLSHLTAAQNVEVPAVYAgLER---KQRLLRAQELLQRLGLEDRVEYQ----PSQ--LSGGQQQRVSIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 330253231 990 VELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1039
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQV 206
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
176-388 |
8.82e-09 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 57.38 E-value: 8.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNK--FHVKRTSAYISQTDNHIAELTVRE 253
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPT---SGRATVAGHDVVRepREVRRRIGIVFQDLSVDDELTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 254 TLDFAARCQGasegfagymkdltrlekergirpsseidafmkaasVKGEKHSVSTDYVLKVLGLDVCSDTMVGNdmmrgV 333
Cdd:cd03265 93 NLYIHARLYG-----------------------------------VPGAERRERIDELLDFVGLLEAADRLVKT-----Y 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 334 SGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLM 388
Cdd:cd03265 133 SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILL 187
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
864-1054 |
1.16e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 58.58 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 864 GVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGhpkEQQTFARIsgyvEQNDI----HS----PQVTVEESLWFS 935
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRLVAGLEKP--TEGQIFIDG---EDVTHRSI----QQRDIcmvfQSyalfPHMSLGENVGYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 936 asLRLPKeITKEQKKEFVEQVMRLVELDTL--RYalvglpgTTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARaa 1013
Cdd:PRK11432 103 --LKMLG-VPKEERKQRVKEALELVDLAGFedRY-------VDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN-- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 330253231 1014 aiVMRTVRNTV-----DTGRTVVCTIHQPSidifEAF---DELLLMKRG 1054
Cdd:PRK11432 171 --LRRSMREKIrelqqQFNITSLYVTHDQS----EAFavsDTVIVMNKG 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
175-395 |
1.55e-08 |
|
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: 56.21 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDKSLKktGNITYNGENLNK--FHVKRTSAYISQTDNHIAELTVR 252
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAG-LLRPDS--GEVRWNGTPLAEqrDEPHENILYLGHLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 253 ETLDFAARCQGAsegfagymkdltrlekergirpsseidafmkaasvkgekHSVSTDYVLKVLGLDVCSDTMVGNdmmrg 332
Cdd:TIGR01189 92 ENLHFWAAIHGG---------------------------------------AQRTIEDALAAVGLTGFEDLPAAQ----- 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330253231 333 VSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDssttfqiVKCIRNFVHLMDA------TVLMALLQPAP 395
Cdd:TIGR01189 128 LSAGQQRRLALARLWLSRRPLWILDEPTTALD-------KAGVALLAGLLRAhlarggIVLLTTHQDLG 189
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
854-1031 |
1.57e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.88 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRktggY--TEGDIRISGHPkeqqtfARIS----------GYVEQndi 921
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGL----YqpDSGEILIDGKP------VRIRsprdaialgiGMVHQ--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 922 H---SPQVTVEESLWFSASLRLPKEITKEQKKEFVEQVMRL----VELDtlryALVGlpgttGLSTEQRKRLTIAVELVA 994
Cdd:COG3845 88 HfmlVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERygldVDPD----AKVE-----DLSVGEQQRVEILKALYR 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 330253231 995 NPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVV 1031
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSII 195
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
854-1070 |
1.62e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.88 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLagrkTGGY--TEGDIRISGHPKEQQTFARIS---GYVEQNdIHSPQVTV 928
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLL----TRFYdiDEGEILLDGHDLRDYTLASLRnqvALVSQN-VHLFNDTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 929 EESLWFSASLRLPKEITKEQKK-----EFVEQVMRlvELDTLryalVGLPGTTgLSTEQRKRLTIAVELVANPSIIFMDE 1003
Cdd:PRK11176 434 ANNIAYARTEQYSREQIEEAARmayamDFINKMDN--GLDTV----IGENGVL-LSGGQRQRIAIARALLRDSPILILDE 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1004 PTSGLDARAAaivmRTVRNTVDT---GRTVVCTIHQPSidIFEAFDELLLMKRGGQVIYggklGTHSQVL 1070
Cdd:PRK11176 507 ATSALDTESE----RAIQAALDElqkNRTSLVIAHRLS--TIEKADEILVVEDGEIVER----GTHAELL 566
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
852-1062 |
1.66e-08 |
|
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: 56.00 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGGYTEGDIRISGHpkeqqtfarisgyveqnDIhsPQVTVEES 931
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGE-----------------DI--TDLPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 932 ------LWFSAslrlPKEITKEQKKEFveqvmrlveldtLRYALVGLPGttGlsteQRKRLTIAVELVANPSIIFMDEPT 1005
Cdd:cd03217 75 arlgifLAFQY----PPEIPGVKNADF------------LRYVNEGFSG--G----EKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 330253231 1006 SGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYGGK 1062
Cdd:cd03217 133 SGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYDGRIVKSGDK 189
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
854-1063 |
1.73e-08 |
|
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: 55.79 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMdvlagrKTGGYTEGDIRISGHPkeqQTFarisgyveqndihSPQVTVeeslw 933
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV------NEGLYASGKARLISFL---PKF-------------SRNKLI----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 934 fsaslrlpkeitkeqkkeFVEQVMRLVELDtLRYALVGLPGTTgLSTEQRKRLTIAVELVANP--SIIFMDEPTSGLDAR 1011
Cdd:cd03238 64 ------------------FIDQLQFLIDVG-LGYLTLGQKLST-LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQ 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 330253231 1012 AAAIVMRTVRNTVDTGRTVVCTIHQPsiDIFEAFDELLLM-KRGGQviYGGKL 1063
Cdd:cd03238 124 DINQLLEVIKGLIDLGNTVILIEHNL--DVLSSADWIIDFgPGSGK--SGGKV 172
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
175-410 |
1.94e-08 |
|
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: 56.37 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFHV-KRTSAYISQTDNHIAELTVRE 253
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD---SGEILIDGRDVTGVPPeRRNIGMVFQDYALFPHLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 254 TLDFAARCQGasegfagymkdltrlekergiRPSSEIDAFMKAAsvkgekhsvstdyvLKVLGLDVCSDTMVgndmmRGV 333
Cdd:cd03259 92 NIAFGLKLRG---------------------VPKAEIRARVREL--------------LELVGLEGLLNRYP-----HEL 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330253231 334 SGGQRKRVTTGE-MTVGPRkTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMALLQPApETFDLFDDLILLSEG 410
Cdd:cd03259 132 SGGQQQRVALARaLAREPS-LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQE-EALALADRIAVMNEG 207
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
854-1022 |
2.02e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.79 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGGYTEGDIRISGHPkeqQTFARISGyVEQND---IHS-----PQ 925
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEE---LQASNIRD-TERAGiaiIHQelalvKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 926 VTVEESLWfsaslrLPKEITKEQKKEFVEQVMRLVE-LDTLRYAL-VGLP-GTTGLSTEQRkrLTIAVELVANPSIIFMD 1002
Cdd:PRK13549 97 LSVLENIF------LGNEITPGGIMDYDAMYLRAQKlLAQLKLDInPATPvGNLGLGQQQL--VEIAKALNKQARLLILD 168
|
170 180
....*....|....*....|
gi 330253231 1003 EPTSGLDARAAAIVMRTVRN 1022
Cdd:PRK13549 169 EPTASLTESETAVLLDIIRD 188
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
851-1054 |
3.03e-08 |
|
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: 55.80 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 851 LQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPKEQQTFARISGYVEQNDIHSPQ----- 925
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQT--LEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQkpwll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 926 -VTVEESLWFSASLrlpkeiTKEQKKEFVEQVMRLVELDTLRYALVGLPGTTG--LSTEQRKRLTIAVELVANPSIIFMD 1002
Cdd:cd03290 92 nATVEENITFGSPF------NKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGinLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 330253231 1003 EPTSGLDARAAAIVMRT--VRNTVDTGRTVVCTIHQpsIDIFEAFDELLLMKRG 1054
Cdd:cd03290 166 DPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHK--LQYLPHADWIIAMKDG 217
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
850-1034 |
3.24e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.04 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 850 RLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPKEQQTFARIS----GYVEQNDIHSPQ 925
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRA--TSGRIVFDGKDITDWQTAKIMreavAIVPEGRRVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 926 VTVEESLWFSASLrlpkeITKEQKKEFVEQVM----RLVELDTLRyalvglPGTtgLSTEQRKRLTIAVELVANPSIIFM 1001
Cdd:PRK11614 95 MTVEENLAMGGFF-----AERDQFQERIKWVYelfpRLHERRIQR------AGT--MSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190
....*....|....*....|....*....|...
gi 330253231 1002 DEPTSGLdaraAAIVMRTVRNTVDTGRTVVCTI 1034
Cdd:PRK11614 162 DEPSLGL----APIIIQQIFDTIEQLREQGMTI 190
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
171-416 |
3.33e-08 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 55.76 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 171 HKLNILKDIsgiikPGRMTLLLGPPGSGKSTLLLALAG--KLDKslkktGNITYNGENL----NKFHV---KRTSAYISQ 241
Cdd:cd03297 13 FTLKIDFDL-----NEEVTGIFGASGAGKSTLLRCIAGleKPDG-----GTIVLNGTVLfdsrKKINLppqQRKIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 242 TDNHIAELTVRETLDFAARcqgasegFAGYMKDLTRLEKergirpsseidafmkaasvkgekhsvstdyVLKVLGLDVCS 321
Cdd:cd03297 83 QYALFPHLNVRENLAFGLK-------RKRNREDRISVDE------------------------------LLDLLGLDHLL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 322 DTMVGndmmrGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMALLQPApETFDLF 401
Cdd:cd03297 126 NRYPA-----QLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLS-EAEYLA 199
|
250
....*....|....*
gi 330253231 402 DDLILLSEGYMVYQG 416
Cdd:cd03297 200 DRIVVMEDGRLQYIG 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
866-1011 |
3.34e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 57.26 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 866 LTaLVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGH-----PKEQqtfaRISGYVEQNDIHSPQVTVEESLWFsaSLRL 940
Cdd:PRK09452 43 LT-LLGPSGCGKTTVLRLIAGFETP--DSGRIMLDGQdithvPAEN----RHVNTVFQSYALFPHMTVFENVAF--GLRM 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 330253231 941 PKeITKEQKKEFVEQVMRLVELDTLRYALVglpgtTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1011
Cdd:PRK09452 114 QK-TPAAEITPRVMEALRMVQLEEFAQRKP-----HQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
854-1072 |
3.38e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.57 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG--RKTGG-YTEGDIRISGHPKEQQ--TFARISGYVEQNDIHspQV-- 926
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGllQPTSGtVTIGERVITAGKKNKKlkPLRKKVGIVFQFPEH--QLfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 927 -TVEESLWFSAS-LRLPKEITKEQKKEFVEqvmrlveldtlryaLVGLPGTT------GLSTEQRKRLTIAVELVANPSI 998
Cdd:PRK13634 101 eTVEKDICFGPMnFGVSEEDAKQKAREMIE--------------LVGLPEELlarspfELSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 999 IFMDEPTSGLDARAAAIVMRTV-RNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRGGQViyggKLGTHSQVLVD 1072
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMMEMFyKLHKEKGLTTVLVTHSME-DAARYADQIVVMHKGTVF----LQGTPREIFAD 236
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
847-1054 |
3.43e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 56.73 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 847 PETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG-RKTGGYTEGDIRISGHPKEQQTFARIS---GYVEQN-DI 921
Cdd:PRK13640 16 PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPDDNPNSKITVDGITLTAKTVWDIRekvGIVFQNpDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 922 HSPQVTVEESLWFSASLRlpkEITKEQKKEFVEQVmrLVELDTLRYAlvgLPGTTGLSTEQRKRLTIAVELVANPSIIFM 1001
Cdd:PRK13640 96 QFVGATVGDDVAFGLENR---AVPRPEMIKIVRDV--LADVGMLDYI---DSEPANLSGGQKQRVAIAGILAVEPKIIIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 330253231 1002 DEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHqpsiDIFEA--FDELLLMKRG 1054
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKlKKKNNLTVISITH----DIDEAnmADQVLVLDDG 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
175-422 |
3.73e-08 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 55.86 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSLKKT----GNiTYNGENLnkFHVKRTSAYISQ--TDNHIAE 248
Cdd:COG1119 18 ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfGE-RRGGEDV--WELRKRIGLVSPalQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 249 LTVRETLdfaarcqgASEGFA--GYMKDLTRLEKERgirpsseidafmkaasvkgekhsvsTDYVLKVLGLDVCSDTmvg 326
Cdd:COG1119 95 ETVLDVV--------LSGFFDsiGLYREPTDEQRER-------------------------ARELLELLGLAHLADR--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 327 ndMMRGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMA--LLQPAPETfdlFDDL 404
Cdd:COG1119 139 --PFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVthHVEEIPPG---ITHV 213
|
250
....*....|....*...
gi 330253231 405 ILLSEGYMVYQGPREDVI 422
Cdd:COG1119 214 LLLKDGRVVAAGPKEEVL 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
160-416 |
4.10e-08 |
|
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: 55.80 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 160 LSSLRIIKPRKHKL-NILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNG----ENLNKfHVKR 234
Cdd:cd03267 20 IGSLKSLFKRKYREvEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPT---SGEVRVAGlvpwKRRKK-FLRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 235 TSAYISQTDNHIAELTVRETLDFaarcqgasegfagyMKDLTRLEKERGIRPSSEIDAFMKAAsvkgekhsvstdyvlKV 314
Cdd:cd03267 96 IGVVFGQKTQLWWDLPVIDSFYL--------------LAAIYDLPPARFKKRLDELSELLDLE---------------EL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 315 LgldvcsDTMVgndmmRGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMAllqpa 394
Cdd:cd03267 147 L------DTPV-----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLT----- 210
|
250 260
....*....|....*....|....*...
gi 330253231 395 peTFDLFD------DLILLSEGYMVYQG 416
Cdd:cd03267 211 --SHYMKDiealarRVLVIDKGRLLYDG 236
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
169-388 |
4.19e-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: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 169 RKHKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKF--HVKRTS-AYISQtDNH 245
Cdd:cd03244 13 RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELS---SGSILIDGVDISKIglHDLRSRiSIIPQ-DPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 246 IAELTVRETLDFaarcqgasegfagymkdltrlekeRGIRPSSEIDAFMKAASVKgekhsvstDYVLKVLGLDvcsDTMV 325
Cdd:cd03244 89 LFSGTIRSNLDP------------------------FGEYSDEELWQALERVGLK--------EFVESLPGGL---DTVV 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330253231 326 gNDMMRGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNfvHLMDATVLM 388
Cdd:cd03244 134 -EEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLT 193
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
175-253 |
4.59e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 55.86 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFHVK---RTSAYISQtDNHI-AELT 250
Cdd:COG4604 16 VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPD---SGEVLVDGLDVATTPSRelaKRLAILRQ-ENHInSRLT 91
|
...
gi 330253231 251 VRE 253
Cdd:COG4604 92 VRE 94
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
853-1037 |
5.00e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.81 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGrkTGGYTEGDIRISGHPKEQQ--TFARISGYV-EQNDIhSPQVTVE 929
Cdd:PRK13538 16 LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG--LARPDAGEVLWQGEPIRRQrdEYHQDLLYLgHQPGI-KTELTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 930 ESLWFSASLRlpkeitkeqkkefveqvmRLVELDTLRYAL--VGLPGT-----TGLSTEQRKRLTIAVELVANPSIIFMD 1002
Cdd:PRK13538 93 ENLRFYQRLH------------------GPGDDEALWEALaqVGLAGFedvpvRQLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180 190
....*....|....*....|....*....|....*
gi 330253231 1003 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQP 1037
Cdd:PRK13538 155 EPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
175-228 |
5.45e-08 |
|
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: 54.84 E-value: 5.45e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSLKKtGNITYNGENLN 228
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTE-GEILFKGEDIT 67
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
854-1060 |
5.49e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.32 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgytEGDIRISGHPKEQ---QTFARISGYVEQNDIHSPQVTVee 930
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG---SGSIQFAGQPLEAwsaAELARHRAYLSQQQTPPFAMPV-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 931 slWFSASLRLPKEITKEQKKEFVEQVMRLVELDTLryalvgLPGTTG-LS-TE-QRKRLTiAVELVANPSI------IFM 1001
Cdd:PRK03695 87 --FQYLTLHQPDKTRTEAVASALNEVAEALGLDDK------LGRSVNqLSgGEwQRVRLA-AVVLQVWPDInpagqlLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 330253231 1002 DEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAfDELLLMKRGGQVIYG 1060
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHA-DRVWLLKQGKLLASG 215
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
867-1009 |
6.51e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.42 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 867 TALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGH-----------PKEQQtfaRIsGYVEQNDIHSPQVTVEESLWFS 935
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGLTRP--QKGRIVLNGRvlfdaekgiclPPEKR---RI-GYVFQDARLFPHYKVRGNLRYG 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330253231 936 aslrlpkeITKEQKKEFvEQVMRLVELDTLryaLVGLPGTtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1009
Cdd:PRK11144 101 --------MAKSMVAQF-DKIVALLGIEPL---LDRYPGS--LSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
853-1033 |
8.53e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.49 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVL--AGRKTGGYT-EGDIRISGHP----KEQQTFARISGYVEQNDIHSPQ 925
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrMNDKVSGYRySGDVLLGGRSifnyRDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 926 VTVEESLwfsASLRLPKEITKEQKKEFVEQvmRLVEL---DTLRYALVGLPGTtgLSTEQRKRLTIAVELVANPSIIFMD 1002
Cdd:PRK14271 116 SIMDNVL---AGVRAHKLVPRKEFRGVAQA--RLTEVglwDAVKDRLSDSPFR--LSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190
....*....|....*....|....*....|.
gi 330253231 1003 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCT 1033
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVT 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
856-1011 |
9.43e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 56.00 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 856 NVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGhpkeqQTFARISGYVE------QNDIHSPQVTVE 929
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP--TAGQIMLDG-----VDLSHVPPYQRpinmmfQSYALFPHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 930 ESLWFSASL-RLPK-EITKEqkkefVEQVMRLVELdtLRYAlvgLPGTTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1007
Cdd:PRK11607 110 QNIAFGLKQdKLPKaEIASR-----VNEMLGLVHM--QEFA---KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
....
gi 330253231 1008 LDAR 1011
Cdd:PRK11607 180 LDKK 183
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
824-1084 |
9.75e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 55.14 E-value: 9.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 824 LTMTFHNVNYyvdmpkeMRSQGVP-ETRLqlLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGh 902
Cdd:PRK13649 1 MGINLQNVSY-------TYQAGTPfEGRA--LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVP--TQGSVRVDD- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 903 pkeqqtfARISGYVEQNDIHSPQVTVEESLWFSASLRLPKEITKEQ---------KKEFVEQVMRLveldtlRYALVGLP 973
Cdd:PRK13649 69 -------TLITSTSKNKDIKQIRKKVGLVFQFPESQLFEETVLKDVafgpqnfgvSQEEAEALARE------KLALVGIS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 974 GTT------GLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDE 1047
Cdd:PRK13649 136 ESLfeknpfELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMD-DVANYADF 214
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 330253231 1048 LLLMKRGGQViyggKLGTHSQVL--VDYFQGIN-GVPPIS 1084
Cdd:PRK13649 215 VYVLEKGKLV----LSGKPKDIFqdVDFLEEKQlGVPKIT 250
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
175-258 |
1.00e-07 |
|
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: 53.34 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDKslKKTGNITYNGENLNKFHV-----KRTSAYISQTDNHIAEL 249
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAG-LEE--PDSGSILIDGEDLTDLEDelpplRRRIGMVFQDFALFPHL 91
|
....*....
gi 330253231 250 TVRETLDFA 258
Cdd:cd03229 92 TVLENIALG 100
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
854-1058 |
1.10e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.37 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGGYTEGDIRISGHPKEQQ----TFARISGYVEQNDIHSPQVTVE 929
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASnirdTERAGIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 930 ESLWFSASLRLPKEITKEQKKEF-VEQVMRLVELDTLRyalVGLP-GTTGLSTEQrkRLTIAVELVANPSIIFMDEPTSG 1007
Cdd:TIGR02633 97 ENIFLGNEITLPGGRMAYNAMYLrAKNLLRELQLDADN---VTRPvGDYGGGQQQ--LVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 330253231 1008 LDARAAAIVMRTVRNTvdTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVI 1058
Cdd:TIGR02633 172 LTEKETEILLDIIRDL--KAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
853-1036 |
1.31e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGH--PKEQQTFARISGYVEQNDIHSPQVTVEE 930
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNP--EKGEILFERQsiKKDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 931 SLWFsaslrlpkEITKEQKKEFVEQVMRLVELDTLRYALVGLpgttgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1010
Cdd:PRK13540 94 NCLY--------DIHFSPGAVGITELCRLFSLEHLIDYPCGL-----LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180
....*....|....*....|....*.
gi 330253231 1011 RAAAIVMRTVRNTVDTGRTVVCTIHQ 1036
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
169-423 |
1.33e-07 |
|
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: 54.16 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 169 RKHKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFHVK---RTSAYISQtDNH 245
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVD---SGRILIDGHDVRDYTLAslrRQIGLVSQ-DVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 246 IAELTVRETLDFAARcqGASEgfagymkdltrlekergirpsSEIDAFMKAAsvkgEKHSVstdyvlkVLGLDVCSDTMV 325
Cdd:cd03251 87 LFNDTVAENIAYGRP--GATR---------------------EEVEEAARAA----NAHEF-------IMELPEGYDTVI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 326 GNdmmRGV--SGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRnfvHLM-DATVL-----MALLQPApet 397
Cdd:cd03251 133 GE---RGVklSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALE---RLMkNRTTFviahrLSTIENA--- 203
|
250 260
....*....|....*....|....*.
gi 330253231 398 fdlfDDLILLSEGYMVYQGPREDVIA 423
Cdd:cd03251 204 ----DRIVVLEDGKIVERGTHEELLA 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
173-265 |
1.56e-07 |
|
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: 53.63 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 173 LNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFHVKRtsAYISQTDNHIAELTVR 252
Cdd:cd03293 17 VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT---SGEVLVDGEPVTGPGPDR--GYVFQQDALLPWLTVL 91
|
90
....*....|...
gi 330253231 253 ETLDFAARCQGAS 265
Cdd:cd03293 92 DNVALGLELQGVP 104
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
171-228 |
1.66e-07 |
|
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: 53.98 E-value: 1.66e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 330253231 171 HKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDksLKKTGNITYNGENLN 228
Cdd:COG4181 23 GELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG-LD--RPTSGTVRLAGQDLF 77
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
176-442 |
1.86e-07 |
|
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: 53.88 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLALAG--KLDkslkkTGNITYNGENLNKFH-VKRTSAYISQTDNHIAELTVR 252
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGfiKPD-----SGKILLNGKDITNLPpEKRDISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 253 ETLDFAARcqgasegfagyMKDLTRLEKERGIRpssEIDAFMKaasvkgekhsvsTDYVLkvlgldvcsdtmvgNDMMRG 332
Cdd:cd03299 90 KNIAYGLK-----------KRKVDKKEIERKVL---EIAEMLG------------IDHLL--------------NRKPET 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 333 VSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMAllqpapeTFDLFDDLIL------ 406
Cdd:cd03299 130 LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHV-------THDFEEAWALadkvai 202
|
250 260 270
....*....|....*....|....*....|....*.
gi 330253231 407 LSEGYMVYQGPREDViaffeslgFRLPPRKGVADFL 442
Cdd:cd03299 203 MLNGKLIQVGKPEEV--------FKKPKNEFVAEFL 230
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
852-1014 |
1.98e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 53.76 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLaGRKTGGYTE----GDIRISGHPKEQQTFARISGYVeQNDIHSPQVT 927
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-NRLIELYPEarvsGEVYLDGQDIFKMDVIELRRRV-QMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 928 VEESLWFSASLRLPKEITKEQKKEFVEQVMRLVELDTLRYAL---VGLPGTTgLSTEQRKRLTIAVELVANPSIIFMDEP 1004
Cdd:PRK14247 95 PNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVkdrLDAPAGK-LSGGQQQRLCIARALAFQPEVLLADEP 173
|
170
....*....|
gi 330253231 1005 TSGLDARAAA 1014
Cdd:PRK14247 174 TANLDPENTA 183
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
854-1009 |
2.04e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 54.70 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFS--PGVLTAL---------------VGSSGAGKTTLMDVLAGRKTggYTEGDIRISGH------PKEQQTF- 909
Cdd:COG1135 4 LENLSKTFPtkGGPVTALddvsltiekgeifgiIGYSGAGKSTLIRCINLLER--PTSGSVLVDGVdltalsERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 910 ARIsGYVEQ--NDIHSpqVTVEESLwfsaslRLPKEITKEQKKEFVEQVMRLVELdtlryalVGLPGTTG-----LSTEQ 982
Cdd:COG1135 82 RKI-GMIFQhfNLLSS--RTVAENV------ALPLEIAGVPKAEIRKRVAELLEL-------VGLSDKADaypsqLSGGQ 145
|
170 180
....*....|....*....|....*..
gi 330253231 983 RKRLTIAVELVANPSIIFMDEPTSGLD 1009
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALD 172
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
176-371 |
2.14e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.63 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLAL--AGKLDKSLKKTGNITYNGENL-----NKFHVKRTSAYISQTDNHIAe 248
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGHNIysprtDTVDLRKEIGMVFQQPNPFP- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 249 LTVRETLDFAARCQGasegfagyMKDLTRLEK--ERGIRPSSEIDafmkaaSVKGEKHsvstdyvlkvlgldvcsdtmvg 326
Cdd:PRK14239 100 MSIYENVVYGLRLKG--------IKDKQVLDEavEKSLKGASIWD------EVKDRLH---------------------- 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 330253231 327 nDMMRGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQI 371
Cdd:PRK14239 144 -DSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKI 187
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
863-1035 |
2.64e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.93 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 863 PGVLTALVGSSGAGKTTLMDVLAGRKTGGytEGDIRISGHPKEQQTFARISGYVEQNDIHSPQVTVEESLWFSASL--RL 940
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVE--SGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLhgRR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 941 PKEITKEQkkefveqvmrlveldtlrYALVGLPG-----TTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1015
Cdd:PRK13543 114 AKQMPGSA------------------LAIVGLAGyedtlVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITL 175
|
170 180
....*....|....*....|
gi 330253231 1016 VMRTVRNTVDTGRTVVCTIH 1035
Cdd:PRK13543 176 VNRMISAHLRGGGAALVTTH 195
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
868-1038 |
3.15e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 53.31 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 868 ALVGSSGAGKTTLM---DVLAGRKTGGYTEGDIRISG--------HPKEQQtfaRISGYVEQNDIHSPQVTVEESLwfSA 936
Cdd:PRK14267 34 ALMGPSGCGKSTLLrtfNRLLELNEEARVEGEVRLFGrniyspdvDPIEVR---REVGMVFQYPNPFPHLTIYDNV--AI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 937 SLRLPKEI-TKEQKKEFVEQVMRLVEL-DTLRYALVGLPGTtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA 1014
Cdd:PRK14267 109 GVKLNGLVkSKKELDERVEWALKKAALwDEVKDRLNDYPSN--LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTA 186
|
170 180
....*....|....*....|....
gi 330253231 1015 IVMRTVRNtVDTGRTVVCTIHQPS 1038
Cdd:PRK14267 187 KIEELLFE-LKKEYTIVLVTHSPA 209
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
864-1009 |
3.44e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.45 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 864 GVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPKEQ---QTFARISGYVEQNDIHSPQVTVEEslwFSASLRL 940
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTP--AHGHVWLDGEHIQHyasKEVARRIGLLAQNATTPGDITVQE---LVARGRY 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330253231 941 PKE--ITKEQKK--EFVEQVMRLVELDTLryalvGLPGTTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1009
Cdd:PRK10253 108 PHQplFTRWRKEdeEAVTKAMQATGITHL-----ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
854-1054 |
3.98e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.47 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG---RKTGGYTEGDIRISGH---PKEQQTFARISGYVEQ-NDIHSPQV 926
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGliiSETGQTIVGDYAIPANlkkIKEVKRLRKEIGLVFQfPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 927 TVEESLWFSaslrlPKEItKEQKKEFVEQVMRLVELdtlryalVGLP------GTTGLSTEQRKRLTIAVELVANPSIIF 1000
Cdd:PRK13645 107 TIEKDIAFG-----PVNL-GENKQEAYKKVPELLKL-------VQLPedyvkrSPFELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 1001 MDEPTSGLDARAAAIVMRT-VRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRG 1054
Cdd:PRK13645 174 LDEPTGGLDPKGEEDFINLfERLNKEYKKRIIMVTHNMD-QVLRIADEVIVMHEG 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
848-1058 |
4.13e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.17 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 848 ETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHPKEQQT---FARISGYVEQN-DIHS 923
Cdd:PRK13642 17 ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE--EFEGKVKIDGELLTAENvwnLRRKIGMVFQNpDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 924 PQVTVEESLWFSASLR-LPKEitkEQKKEFVEQVMRLVELDTLRYALVGLPGTtglsteQRKRLTIAVELVANPSIIFMD 1002
Cdd:PRK13642 95 VGATVEDDVAFGMENQgIPRE---EMIKRVDEALLAVNMLDFKTREPARLSGG------QKQRVAVAGIIALRPEIIILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 330253231 1003 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpSIDIFEAFDELLLMkRGGQVI 1058
Cdd:PRK13642 166 ESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITH-DLDEAASSDRILVM-KAGEII 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
854-1054 |
4.15e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.20 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMdvlagRKTGGYTE---GDIRISGHPKEQQTFARIS---GYVEQN-DIHSPQV 926
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTV-----RLIDGLLEaesGQIIIDGDLLTEENVWDIRhkiGMVFQNpDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 927 TVEESLWFSASlrlPKEITKEQKKEFVEQVMRLVELDTLRYAlvglpGTTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1006
Cdd:PRK13650 98 TVEDDVAFGLE---NKGIPHEEMKERVNEALELVGMQDFKER-----EPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 330253231 1007 GLDARAAAIVMRTVRNTVDT-GRTVVCTIHqpSIDIFEAFDELLLMKRG 1054
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDyQMTVISITH--DLDEVALSDRVLVMKNG 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
861-1036 |
4.16e-07 |
|
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: 55.02 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 861 FSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPKEQQTFA-RIS-GYVEQNDIHSPQVTVEESLWFSASL 938
Cdd:TIGR01257 953 FYENQITAFLGHNGAGKTTTLSILTGLLPP--TSGTVLVGGKDIETNLDAvRQSlGMCPQHNILFHHLTVAEHILFYAQL 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 939 rlpKEITKEQKKEFVEQVMRLVELDTLRYAlvglpGTTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA---RAAAI 1015
Cdd:TIGR01257 1031 ---KGRSWEEAQLEMEAMLEDTGLHHKRNE-----EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPysrRSIWD 1102
|
170 180
....*....|....*....|.
gi 330253231 1016 VMRTVRntvdTGRTVVCTIHQ 1036
Cdd:TIGR01257 1103 LLLKYR----SGRTIIMSTHH 1119
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
183-416 |
6.56e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 52.32 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 183 IKPGRMTLLLGPPGSGKSTLLLALAGKL--DKS----LKKTGNITYNGENLNKfHVKRTSA---YISQTDNHIAELTVRE 253
Cdd:PRK09984 27 IHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSagshIELLGRTVQREGRLAR-DIRKSRAntgYIFQQFNLVNRLSVLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 254 TLDFAArcQGASEGFAGYMKDLTRLEKERGIRpsseidAFMKAASVKGEKHSVSTdyvlkvlgldvcsdtmvgndmmrgV 333
Cdd:PRK09984 106 NVLIGA--LGSTPFWRTCFSWFTREQKQRALQ------ALTRVGMVHFAHQRVST------------------------L 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 334 SGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNfVHLMDATVLMALLQPAPETFDLFDDLILLSEGYMV 413
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRD-INQNDGITVVVTLHQVDYALRYCERIVALRQGHVF 232
|
...
gi 330253231 414 YQG 416
Cdd:PRK09984 233 YDG 235
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
167-229 |
7.42e-07 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 52.11 E-value: 7.42e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330253231 167 KPRKHKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDKslKKTGNITYNGENLNK 229
Cdd:COG1124 12 GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAG-LER--PWSGEVTFDGRPVTR 71
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
861-1053 |
8.08e-07 |
|
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: 50.44 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 861 FSPGVLTALVGSSGAGKTTLMDVLagrktgGYTEGdirisghpkeQQTFARISGYVEQNDIHSPQVTVEeslwfsaslrl 940
Cdd:cd03227 18 FGEGSLTIITGPNGSGKSTILDAI------GLALG----------GAQSATRRRSGVKAGCIVAAVSAE----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 941 pkeitkeqkkefveqvmrlveldtLRYALVGLPGttGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1020
Cdd:cd03227 71 ------------------------LIFTRLQLSG--GEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAI 124
|
170 180 190
....*....|....*....|....*....|...
gi 330253231 1021 RNTVDTGRTVVCTIHQPsiDIFEAFDELLLMKR 1053
Cdd:cd03227 125 LEHLVKGAQVIVITHLP--ELAELADKLIHIKK 155
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
852-1036 |
8.26e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 52.28 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLM---DVLAGRKTGGY------------TEGDIRISGHPKEQQTFARISGYV 916
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLrciNFLEKPSEGSIvvngqtinlvrdKDGQLKVADKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 917 EQNDIHSPQVTVEESLWFSAS-LRLPKEITKEQKKEFVEQVmRLVELDTLRYALvglpgttGLSTEQRKRLTIAVELVAN 995
Cdd:PRK10619 99 QHFNLWSHMTVLENVMEAPIQvLGLSKQEARERAVKYLAKV-GIDERAQGKYPV-------HLSGGQQQRVSIARALAME 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 330253231 996 PSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1036
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
853-1060 |
8.51e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.14 E-value: 8.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGGYT------EGDIRISGHPKEQ---QTFARISGYVEQNDIHS 923
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAprgarvTGDVTLNGEPLAAidaPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 924 PQVTVEESLWFSaslRLPKE----ITKEQKKEFVEQVMRLVELDtlryALVGLPGTTgLSTEQRKRLTIAVEL------- 992
Cdd:PRK13547 96 FAFSAREIVLLG---RYPHArragALTHRDGEIAWQALALAGAT----ALVGRDVTT-LSGGELARVQFARVLaqlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 330253231 993 --VANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTI-HQPSIDIFEAfDELLLMKRGGQVIYG 1060
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIvHDPNLAARHA-DRIAMLADGAIVAHG 237
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
175-423 |
9.43e-07 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 9.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKF---HVKRTSAYISQtDNHIAELTV 251
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVS---SGSILIDGQDIREVtldSLRRAIGVVPQ-DTVLFNDTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 252 RETLDFAarCQGASEgfagymkdltrlekergirpsSEIDAFMKAASVKGEKHSVSTDYvlkvlgldvcsDTMVGNdmmR 331
Cdd:cd03253 92 GYNIRYG--RPDATD---------------------EEVIEAAKAAQIHDKIMRFPDGY-----------DTIVGE---R 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 332 GV--SGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIR----NFVHLMDA----TVLMAllqpapetfdlf 401
Cdd:cd03253 135 GLklSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRdvskGRTTIVIAhrlsTIVNA------------ 202
|
250 260
....*....|....*....|..
gi 330253231 402 DDLILLSEGYMVYQGPREDVIA 423
Cdd:cd03253 203 DKIIVLKDGRIVERGTHEELLA 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
170-372 |
1.21e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 51.32 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 170 KHKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFHVKRTSA-------YISQT 242
Cdd:PRK10584 20 EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGS---SGEVSLVGQPLHQMDEEARAKlrakhvgFVFQS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 243 DNHIAELTVRETLDFAARCQGASEgfagymkdltRLEKERGIRpsseidafmkaasvkgekhsvstdyVLKVLGLDVCSD 322
Cdd:PRK10584 97 FMLIPTLNALENVELPALLRGESS----------RQSRNGAKA-------------------------LLEQLGLGKRLD 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 330253231 323 TMVGNdmmrgVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIV 372
Cdd:PRK10584 142 HLPAQ-----LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIA 186
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
175-454 |
1.57e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.34 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSLKKTGNITYNGENLNKFHV----KRTSAYISQTDNHIAELT 250
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVwdirEKVGIVFQNPDNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 251 VRETLDFAarcqgasegfagymkdltrLEKeRGIrPSSEIDAFMKAasvkgekhsvstdyVLKVLGLDVCSDTMVGNdmm 330
Cdd:PRK13640 102 VGDDVAFG-------------------LEN-RAV-PRPEMIKIVRD--------------VLADVGMLDYIDSEPAN--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 331 rgVSGGQRKRVT-TGEMTVGPrKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLmALLQPAPETfDLFDDLILLSE 409
Cdd:PRK13640 144 --LSGGQKQRVAiAGILAVEP-KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVI-SITHDIDEA-NMADQVLVLDD 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 330253231 410 GYMVYQGPREDV-------------IAFFESLGFRLpPRKGVAdFLQEVTSKKDQAQY 454
Cdd:PRK13640 219 GKLLAQGSPVEIfskvemlkeigldIPFVYKLKNKL-KEKGIS-VPQEINTEEKLVQY 274
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
171-416 |
1.58e-06 |
|
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: 50.29 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 171 HKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDKslKKTGNITYNGENLNKFHVKRtsayisqtdNHIAELt 250
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILG-LIK--PDSGEITFDGKSYQKNIEAL---------RRIGAL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 251 vretLDfaarcqgaSEGFAGYM---KDLTRLEKERGIRpSSEIDAfmkaasvkgekhsvstdyVLKVLGLDVCSDTMVGn 327
Cdd:cd03268 78 ----IE--------APGFYPNLtarENLRLLARLLGIR-KKRIDE------------------VLDVVGLKDSAKKKVK- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 328 dmmrGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSsttfQIVKCIRNFVHLMDA---TVLMA--LLQpapETFDLFD 402
Cdd:cd03268 126 ----GFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP----DGIKELRELILSLRDqgiTVLISshLLS---EIQKVAD 194
|
250
....*....|....
gi 330253231 403 DLILLSEGYMVYQG 416
Cdd:cd03268 195 RIGIINKGKLIEEG 208
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
845-1067 |
1.59e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.36 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 845 GVPetrlqLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPKEQQTFARISGY----VEQND 920
Cdd:PRK15439 23 GVE-----VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPP--DSGTLEIGGNPCARLTPAKAHQLgiylVPQEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 921 IHSPQVTVEESLWFsaslRLPKEITKEQKkefVEQVMRL--VELDtlryaLVGLPGTtgLSTEQRKRLTIAVELVANPSI 998
Cdd:PRK15439 96 LLFPNLSVKENILF----GLPKRQASMQK---MKQLLAAlgCQLD-----LDSSAGS--LEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330253231 999 IFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMkRGGQVIYGGKLGTHS 1067
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLP-EIRQLADRISVM-RDGTIALSGKTADLS 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
147-423 |
1.59e-06 |
|
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: 51.04 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 147 TLVNVSRDFferclsslriiKPRKHKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDKSlkKTGNITYNGEN 226
Cdd:cd03258 3 ELKNVSKVF-----------GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LERP--TSGSVLVDGTD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 227 LNKF------HVKRTSAYISQTDNHIAELTVRETLDFAARCQGASegfagymkdltRLEKERGIRPsseidafmkaasvk 300
Cdd:cd03258 69 LTLLsgkelrKARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVP-----------KAEIEERVLE-------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 301 gekhsvstdyVLKVLGLDVCSDTMVGNdmmrgVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVH 380
Cdd:cd03258 124 ----------LLELVGLEDKADAYPAQ-----LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINR 188
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 330253231 381 LMDATVL-----MALLQpapetfDLFDDLILLSEGYMVYQGPREDVIA 423
Cdd:cd03258 189 ELGLTIVlitheMEVVK------RICDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
966-1063 |
1.98e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.66 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 966 RYALVGLPGTTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIhQPSIDIFE 1043
Cdd:NF000106 131 RFSLTEAAGRAAakYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTT-QYMEEAEQ 209
|
90 100
....*....|....*....|
gi 330253231 1044 AFDELLLMKRgGQVIYGGKL 1063
Cdd:NF000106 210 LAHELTVIDR-GRVIADGKV 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
868-1024 |
2.28e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 51.99 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 868 ALVGSSGAGKTTL----MDVLAgrktggyTEGDIRISGHP------KEQQTFARisgyveqnDIH----------SPQVT 927
Cdd:COG4172 316 GLVGESGSGKSTLglalLRLIP-------SEGEIRFDGQDldglsrRALRPLRR--------RMQvvfqdpfgslSPRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 928 VEESLwfSASLRL-PKEITKEQKKEFVEQVMRLVELD--TL-RYalvglPGTtgLSTEQRKRLTIAVELVANPSIIFMDE 1003
Cdd:COG4172 381 VGQII--AEGLRVhGPGLSAAERRARVAEALEEVGLDpaARhRY-----PHE--FSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180
....*....|....*....|.
gi 330253231 1004 PTSGLDaraaaivmRTVRNTV 1024
Cdd:COG4172 452 PTSALD--------VSVQAQI 464
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
854-1061 |
2.29e-06 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 50.22 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGhpkeqqtfaRISGYVEQNDIHSPQVTVEESLW 933
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYP--PDSGTVTVRG---------RVSSLLGLGGGFNPELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 934 FSASL--RLPKEItkEQKKEFVEQvmrLVELDTLRYALVGlpgttGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1011
Cdd:cd03220 107 LNGRLlgLSRKEI--DEKIDEIIE---FSELGDFIDLPVK-----TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 330253231 1012 AAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLMKRgGQVIYGG 1061
Cdd:cd03220 177 FQEKCQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEK-GKIRFDG 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
175-229 |
2.60e-06 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 50.05 E-value: 2.60e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNK 229
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPT---SGQVLVNGQDLSR 68
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
863-1039 |
2.76e-06 |
|
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: 50.44 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 863 PGVLTALVGSSGAGKTTLMDVLAGRKT---GGYTEGD-----IRISGHPKEQQTFARISGYvEQNDIHSPQVtVEeslwf 934
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKpnlGKFDDPPdwdeiLDEFRGSELQNYFTKLLEG-DVKVIVKPQY-VD----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 935 saslRLPKE--------ITKEQKKEFVEQVMRLVELDTLRYALVglpgtTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1006
Cdd:cd03236 98 ----LIPKAvkgkvgelLKKKDERGKLDELVDQLELRHVLDRNI-----DQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190
....*....|....*....|....*....|...
gi 330253231 1007 GLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1039
Cdd:cd03236 169 YLDIKQRLNAARLIRELAEDDNYVLVVEHDLAV 201
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
869-1018 |
2.80e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.38 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 869 LVGSSGAGKTTLMDVLAGRKTggYTEGDIRISG------HPKEqqtfaRISGYVEQNDIHSPQVTVEESLWFSASLR-LP 941
Cdd:PRK11650 35 LVGPSGCGKSTLLRMVAGLER--ITSGEIWIGGrvvnelEPAD-----RDIAMVFQNYALYPHMSVRENMAYGLKIRgMP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 942 K-EItkEQKkefVEQVMRLVELDTL-----RyalvglpgttGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA--RAA 1013
Cdd:PRK11650 108 KaEI--EER---VAEAARILELEPLldrkpR----------ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAklRVQ 172
|
....*
gi 330253231 1014 aivMR 1018
Cdd:PRK11650 173 ---MR 174
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
172-423 |
2.90e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 50.37 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 172 KLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKF---HVKRTSAYISQTDNHIAE 248
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPA---HGHVWLDGEHIQHYaskEVARRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 249 LTVRETLdfaarcqgaSEGFAGYMKDLTRLEKErgirpssEIDAFMKAASVKGEKHsVSTDYVlkvlgldvcsDTMvgnd 328
Cdd:PRK10253 96 ITVQELV---------ARGRYPHQPLFTRWRKE-------DEEAVTKAMQATGITH-LADQSV----------DTL---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 329 mmrgvSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATvLMALLQPAPETFDLFDDLILLS 408
Cdd:PRK10253 145 -----SGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYT-LAAVLHDLNQACRYASHLIALR 218
|
250
....*....|....*.
gi 330253231 409 EGYMVYQG-PREDVIA 423
Cdd:PRK10253 219 EGKIVAQGaPKEIVTA 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
854-1058 |
2.97e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG--RKtggyTEGDIRISGHPKEQQTF--ARISG--YVEQNDIHSPQVT 927
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGiyQK----DSGSILFQGKEIDFKSSkeALENGisMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 928 VEESLWFSaslRLP-KEITKEQKKEFVEQVMRLVELDTlryALVGLPGTTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1006
Cdd:PRK10982 90 VMDNMWLG---RYPtKGMFVDQDKMYRDTKAIFDELDI---DIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 330253231 1007 GLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMkRGGQVI 1058
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKLKERGCGIVYISHKME-EIFQLCDEITIL-RDGQWI 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
175-233 |
3.54e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.85 E-value: 3.54e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFHVK 233
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT---SGHIRFHGTDVSRLHAR 72
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
170-423 |
3.71e-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: 49.53 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 170 KHKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLN--KFHVKRTS-AYISQtDNHI 246
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ---KGQILIDGIDIRdiSRKSLRSMiGVVLQ-DTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 247 AELTVRETLDFAarcqgasegfagymkdltrlekergiRPSSEIDAFMKAASVKGekhsvSTDYVLKVL-GLdvcsDTMV 325
Cdd:cd03254 89 FSGTIMENIRLG--------------------------RPNATDEEVIEAAKEAG-----AHDFIMKLPnGY----DTVL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 326 GNdmmRG--VSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNfvhLMDA-TVLMALLQPApeTFDLFD 402
Cdd:cd03254 134 GE---NGgnLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEK---LMKGrTSIIIAHRLS--TIKNAD 205
|
250 260
....*....|....*....|.
gi 330253231 403 DLILLSEGYMVYQGPREDVIA 423
Cdd:cd03254 206 KILVLDDGKIIEEGTHDELLA 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
176-389 |
4.32e-06 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 48.77 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGenlnkfhvKRTSAYISQtdnHIAE-----LT 250
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPT---SGTVRRAG--------GARVAYVPQ---RSEVpdslpLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 251 VRETLD---FAARcqgasegfaGYMKDLTRLEKERgirpsseIDAFMKAASVKG-EKHSVSTdyvlkvlgldvcsdtmvg 326
Cdd:NF040873 74 VRDLVAmgrWARR---------GLWRRLTRDDRAA-------VDDALERVGLADlAGRQLGE------------------ 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330253231 327 ndmmrgVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRnFVHLMDATVLMA 389
Cdd:NF040873 120 ------LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLA-EEHARGATVVVV 175
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
854-1085 |
4.41e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 50.05 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAG---RKTGGYTEGDIRISGHPKEQQTFARISGYVEQNDIHspQV---T 927
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGllkPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQYPEY--QLfeeT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 928 VEESLWFSaslrlPKE--ITKEQKKEFVEQVMRLVELDtlrYALVGLPGTTGLSTEQRKRLTIAVELVANPSIIFMDEPT 1005
Cdd:PRK13637 101 IEKDIAFG-----PINlgLSEEEIENRVKRAMNIVGLD---YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1006 SGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIyggkLGTHSQVL--VDYFQGIN-GVPP 1082
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCEL----QGTPREVFkeVETLESIGlAVPQ 248
|
...
gi 330253231 1083 ISS 1085
Cdd:PRK13637 249 VTY 251
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
852-1045 |
4.79e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 49.65 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggyTEGDIRISGHPK--EQQTFAR---ISGYVEQNDIHSPQ- 925
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE---LESEVRVEGRVEffNQNIYERrvnLNRLRRQVSMVHPKp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 926 ----VTVEESLWFSasLRLPKEITKEQKKEFVEQVMRLVEL-DTLRYALvgLPGTTGLSTEQRKRLTIAVELVANPSIIF 1000
Cdd:PRK14258 98 nlfpMSVYDNVAYG--VKIVGWRPKLEIDDIVESALKDADLwDEIKHKI--HKSALDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 330253231 1001 MDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQ----PSIDIFEAF 1045
Cdd:PRK14258 174 MDEPCFGLDPIASMKVESLIQSlRLRSELTMVIVSHNlhqvSRLSDFTAF 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
853-1037 |
4.82e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 49.66 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLaGRKTGGYtEGDIRISGH---------PKEQQTFARISGYVEQNDIHS 923
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL-NRLIEIY-DSKIKVDGKvlyfgkdifQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 924 PQVTVEESLWFSASLRLPKEitKEQKKEFVEQVMRLVELDTLRYALVGLPGTTgLSTEQRKRLTIAVELVANPSIIFMDE 1003
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKE--KREIKKIVEECLRKVGLWKEVYDRLNSPASQ-LSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190
....*....|....*....|....*....|....
gi 330253231 1004 PTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQP 1037
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLI-TELKNEIAIVIVSHNP 212
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
175-387 |
4.88e-06 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 49.18 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAG--KLDKslkktGNITYNGENLNKFHVK-RTSAYISQTDNHIAELTV 251
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGleEPTS-----GRIYIGGRDVTDLPPKdRDIAMVFQNYALYPHMTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 252 RETLDFAARCQGasegfagymkdltrlekergiRPSSEIDAFMKAASvkgekhsvstdyvlKVLGLDVCSDTMVgndmmR 331
Cdd:cd03301 90 YDNIAFGLKLRK---------------------VPKDEIDERVREVA--------------ELLQIEHLLDRKP-----K 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 330253231 332 GVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVL 387
Cdd:cd03301 130 QLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTI 185
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
871-1011 |
5.29e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 871 GSSGAGKTTLMDVLagrkTG--GYTEGDIRISGHP---KEQQTFARIsGYVEQ-----NDIhspqvTVEESLWFSASL-R 939
Cdd:NF033858 299 GSNGCGKSTTMKML----TGllPASEGEAWLFGQPvdaGDIATRRRV-GYMSQafslyGEL-----TVRQNLELHARLfH 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330253231 940 LPKEitkeQKKEFVEQVMRlveldtlRYALVG----LPGttGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD--AR 1011
Cdd:NF033858 369 LPAA----EIAARVAEMLE-------RFDLADvadaLPD--SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDpvAR 433
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
175-416 |
5.36e-06 |
|
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: 48.46 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSLkktGNITYNGENLnkfhvkrtSAYISQTDNHIAELTVRET 254
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQ---GEITLDGVPV--------SDLEKALSSLISVLNQRPY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 255 LdFaarcqgasegfagymkdltrlekergirpsseidafmkaasvkgekhsvstdyvlkvlgldvcsDTMVGNDMMRGVS 334
Cdd:cd03247 86 L-F----------------------------------------------------------------DTTLRNNLGRRFS 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 335 GGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIrnFVHLMDATVLMAllqpapeTFDL-----FDDLILLSE 409
Cdd:cd03247 101 GGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWI-------THHLtgiehMDKILFLEN 171
|
....*..
gi 330253231 410 GYMVYQG 416
Cdd:cd03247 172 GKIIMQG 178
|
|
| ABC_trans_N |
pfam14510 |
ABC-transporter N-terminal; This domain is found at the N-terminus of ABC-transporter proteins ... |
98-151 |
5.68e-06 |
|
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: 45.77 E-value: 5.68e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 98 ATSDQDNFKLLSAIKERLDRVG-MEVPKIEVRFENLNIEAdVQAGTRALPTLVNV 151
Cdd:pfam14510 27 EDSEFDLRKWLKNLRRLIDEDGyIKPRKLGVAFKNLTVSG-VGAGADYQPTVGNA 80
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
175-341 |
6.19e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 50.45 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITY-NGENLnkfhvkrtsAYISQTDNHIAELTVRE 253
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPD---SGEVSIpKGLRI---------GYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 254 TLdfaarcqgaSEGFAGYMKDLTRLEK--ERGIRPSSEIDAFMKAASVKGEKHSVSTDY----VLKVLGLdvcsDTMVGN 327
Cdd:COG0488 81 TV---------LDGDAELRALEAELEEleAKLAEPDEDLERLAELQEEFEALGGWEAEAraeeILSGLGF----PEEDLD 147
|
170
....*....|....
gi 330253231 328 DMMRGVSGGQRKRV 341
Cdd:COG0488 148 RPVSELSGGWRRRV 161
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
853-1054 |
6.59e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 49.52 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTL-------MDVLAGRKTggyTEGdIRISGHPKeQQTFARISgyveqndihspq 925
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIV---IDG-IDISKLPL-HTLRSRLS------------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 926 VTVEESLWFSASLRLPKEITKEQKKEFVEQVMRLVELDTLRYALVG------LPGTTGLSTEQRKRLTIAVELVANPSII 999
Cdd:cd03288 99 IILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGgldavvTEGGENFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 1000 FMDEPTSGLDARAAAIVMRTVRnTVDTGRTVVCTIHQPSiDIFEAfDELLLMKRG 1054
Cdd:cd03288 179 IMDEATASIDMATENILQKVVM-TAFADRTVVTIAHRVS-TILDA-DLVLVLSRG 230
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
850-1009 |
9.03e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.02 E-value: 9.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 850 RLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGrkTGGYTEGDIRISGHPKEQQTFARISGYVE---QNDIHS--P 924
Cdd:PRK15112 25 TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAG--MIEPTSGELLIDDHPLHFGDYSYRSQRIRmifQDPSTSlnP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 925 QVTVEESLWFsaSLRLPKEITKEQKKEFVEQVMRLVEL--DTLRYalvgLPGTtgLSTEQRKRLTIAVELVANPSIIFMD 1002
Cdd:PRK15112 103 RQRISQILDF--PLRLNTDLEPEQREKQIIETLRQVGLlpDHASY----YPHM--LAPGQKQRLGLARALILRPKVIIAD 174
|
....*..
gi 330253231 1003 EPTSGLD 1009
Cdd:PRK15112 175 EALASLD 181
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
169-265 |
9.29e-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: 48.93 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 169 RKHKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDKSlkKTGNITYNGENLNKFHVKRtsAYISQTDNHIAE 248
Cdd:COG1116 20 GGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAG-LEKP--TSGEVLVDGKPVTGPGPDR--GVVFQEPALLPW 94
|
90
....*....|....*..
gi 330253231 249 LTVRETLDFAARCQGAS 265
Cdd:COG1116 95 LTVLDNVALGLELRGVP 111
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
852-1009 |
1.10e-05 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 46.67 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPKeqqtfariSGYVEQndihspqvtvees 931
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEP--DEGIVTWGSTVK--------IGYFEQ------------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330253231 932 lwfsaslrlpkeitkeqkkefveqvmrlveldtlryalvglpgttgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1009
Cdd:cd03221 71 ----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
183-423 |
1.18e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 48.42 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 183 IKPGRMTLLLGPPGSGKSTLLLALAGKLdksLKKTGNITYNGENlnkfHV-----KRTSAYISQTDNHIAELTVRETLDF 257
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLLNLIAGFL---TPASGSLTLNGQD----HTttppsRRPVSMLFQENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 258 aarcqgasegfagymkdltrlekerGIRPSSEIDAFMKAasvkgekhsvSTDYVLKVLGLDVCSDTMVGNdmmrgVSGGQ 337
Cdd:PRK10771 95 -------------------------GLNPGLKLNAAQRE----------KLHAIARQMGIEDLLARLPGQ-----LSGGQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 338 RKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMA------LLQPAPETfdlfddlILLSEGY 411
Cdd:PRK10771 135 RQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVshsledAARIAPRS-------LVVADGR 207
|
250
....*....|..
gi 330253231 412 MVYQGPREDVIA 423
Cdd:PRK10771 208 IAWDGPTDELLS 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
175-423 |
1.40e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 47.97 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLN--KFH--VKRTSAYISQTDNHIAELT 250
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD---AGNIIIDDEDISllPLHarARRGIGYLPQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 251 VRETLDFAARCQgasegfagymKDLTRLEKERgirpsseidafmKAASVKGEKHSvstdyvlkvlgldvcsdTMVGNDMM 330
Cdd:PRK10895 95 VYDNLMAVLQIR----------DDLSAEQRED------------RANELMEEFHI-----------------EHLRDSMG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 331 RGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRnfvHLMDATV-LMALLQPAPETFDLFDDLILLSE 409
Cdd:PRK10895 136 QSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIE---HLRDSGLgVLITDHNVRETLAVCERAYIVSQ 212
|
250
....*....|....
gi 330253231 410 GYMVYQGPREDVIA 423
Cdd:PRK10895 213 GHLIAHGTPTEILQ 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
175-342 |
1.55e-05 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 49.39 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNkfHVKRTS-----AYISQtDNHIAEL 249
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT---SGRILIDGVDIR--DLTLESlrrqiGVVPQ-DTFLFSG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 250 TVRETLDFAArcQGASEgfagymkdltrlekergirpsSEIDAFMKAASVkgekhsvsTDYVLKvL--GLdvcsDTMVGN 327
Cdd:COG1132 429 TIRENIRYGR--PDATD---------------------EEVEEAAKAAQA--------HEFIEA-LpdGY----DTVVGE 472
|
170
....*....|....*..
gi 330253231 328 dmmRGV--SGGQRKRVT 342
Cdd:COG1132 473 ---RGVnlSGGQRQRIA 486
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
183-389 |
1.72e-05 |
|
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: 49.63 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 183 IKPGRMTLLLGPPGSGKSTLLLALAGklDKSLKkTGNITYNGENL--NKFHVKRTSAYISQTDNHIAELTVRETLDFAAR 260
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTG--DTTVT-SGDATVAGKSIltNISDVHQNMGYCPQFDAIDDLLTGREHLYLYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 261 CQGAsegfagymkdltrlekergirPSSEIDAFmkaasvkgekhsvsTDYVLKVLGLDVCSDTMVGNdmmrgVSGGQRKR 340
Cdd:TIGR01257 2039 LRGV---------------------PAEEIEKV--------------ANWSIQSLGLSLYADRLAGT-----YSGGNKRK 2078
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 330253231 341 VTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMA 389
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTS 2127
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
185-216 |
1.83e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.21 E-value: 1.83e-05
10 20 30
....*....|....*....|....*....|..
gi 330253231 185 PGRMTLLLGPPGSGKSTLLLALAGKLDKSLKK 216
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG 32
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
175-388 |
1.86e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 48.16 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFHVKRTSAYISQ--------TdnhI 246
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPD---SGSILIDGKDVTKLPEYKRAKYIGRvfqdpmmgT---A 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 247 AELTVRETLDFAARcQGASEGFAgymkdltrlekeRGIRpSSEIDAFMKAASVKGekhsvstdyvlkvLGLDVCSDTMVG 326
Cdd:COG1101 95 PSMTIEENLALAYR-RGKRRGLR------------RGLT-KKRRELFRELLATLG-------------LGLENRLDTKVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 330253231 327 NdmmrgVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLM 388
Cdd:COG1101 148 L-----LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLM 204
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
175-387 |
2.14e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.71 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSLKKtGNITYNGENLNKFhvkrtsayisqTDNHIAELTVRET 254
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILE-GDILFKGESILDL-----------EPEERAHLGIFLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 255 LDFAARCQGASEgfagymKDLTRL-----EKERGIrpsSEIDA--FMKAASVKgekhsvstdyvLKVLGLDvcsDTMVGN 327
Cdd:CHL00131 90 FQYPIEIPGVSN------ADFLRLaynskRKFQGL---PELDPleFLEIINEK-----------LKLVGMD---PSFLSR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 328 DMMRGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVL 387
Cdd:CHL00131 147 NVNEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIL 206
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
854-1054 |
2.47e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.20 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKtggytegdirisghPKEQQTFARISGYVEqndiHSPQVTveeslW 933
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGEL--------------SHAETSSVVIRGSVA----YVPQVS-----W 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 934 -FSASLRlpKEITKEQKKEfVEQVMRLVELDTLRYALVGLPGT---------TGLSTEQRKRLTIAVELVANPSIIFMDE 1003
Cdd:PLN03232 690 iFNATVR--ENILFGSDFE-SERYWRAIDVTALQHDLDLLPGRdlteigergVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 330253231 1004 PTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAFDELLLMKRG 1054
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQ--LHFLPLMDRIILVSEG 815
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
175-365 |
2.65e-05 |
|
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: 47.15 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKST---LLLALAGKLDkslkktGNITYNGENLNKFHVKRTS---AYISQtDNHIAE 248
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTvvsLLERFYDPTS------GEILLDGVDIRDLNLRWLRsqiGLVSQ-EPVLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 249 LTVRETLDFAARcqgasegfagymkDLTRLEKERGIRpSSEIDAFmkaasvkgekhsvstdyvlkVLGLDVCSDTMVGNd 328
Cdd:cd03249 91 GTIAENIRYGKP-------------DATDEEVEEAAK-KANIHDF--------------------IMSLPDGYDTLVGE- 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 330253231 329 mmRGV--SGGQRKRVTTGEMTVGPRKTLFMDEISTGLDS 365
Cdd:cd03249 136 --RGSqlSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
176-433 |
3.45e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 47.35 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFHVKRTS-----AYISQTDNH-IAEL 249
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPT---SGKIIIDGVDITDKKVKLSDirkkvGLVFQYPEYqLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 250 TVRETLDFAARCQGASEgfagymkdltrlekergirpsSEIDAFMKAAsvkgekhsvstdyvLKVLGLDVcsDTMVGNDM 329
Cdd:PRK13637 100 TIEKDIAFGPINLGLSE---------------------EEIENRVKRA--------------MNIVGLDY--EDYKDKSP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 330 MRgVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMaLLQPAPETFDLFDDLILLSE 409
Cdd:PRK13637 143 FE-LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIIL-VSHSMEDVAKLADRIIVMNK 220
|
250 260
....*....|....*....|....*..
gi 330253231 410 GYMVYQGPREDV---IAFFESLGFRLP 433
Cdd:PRK13637 221 GKCELQGTPREVfkeVETLESIGLAVP 247
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
174-416 |
3.78e-05 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 46.50 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 174 NILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLdksLKKTGNITYNGenlnkfhvkrtsayisqtdnhiaeltvrE 253
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGII---LPDSGEVLFDG----------------------------K 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 254 TLDFAARcqgasEGFaGYmkdltrLEKERGIRPSSEI-DAFMKAASVKGEKHS---VSTDYVLKVLGLdvcsdTMVGNDM 329
Cdd:cd03269 63 PLDIAAR-----NRI-GY------LPEERGLYPKMKViDQLVYLAQLKGLKKEearRRIDEWLERLEL-----SEYANKR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 330 MRGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTfQIVKCI-----RNFVHLMDATVLMALLQpapetfDLFDDL 404
Cdd:cd03269 126 VEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNV-ELLKDVirelaRAGKTVILSTHQMELVE------ELCDRV 198
|
250
....*....|..
gi 330253231 405 ILLSEGYMVYQG 416
Cdd:cd03269 199 LLLNKGRAVLYG 210
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
176-421 |
4.45e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.86 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFHVKRTS----AYISQTDNHIAELTV 251
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT---KGTITINNINYNKLDHKLAAqlgiGIIYQELSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 252 RETLdfaarcqgasegFAGymKDLTRleKERGIrpsSEID-AFMKaasvkgekhsVSTDYVLKVLGLDVCSDTMVGNdmm 330
Cdd:PRK09700 98 LENL------------YIG--RHLTK--KVCGV---NIIDwREMR----------VRAAMMLLRVGLKVDLDEKVAN--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 331 rgVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTT---FQIVKCIRNfvhlmDATVLMALLQPAPETFDLFDDLILL 407
Cdd:PRK09700 146 --LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVdylFLIMNQLRK-----EGTAIVYISHKLAEIRRICDRYTVM 218
|
250
....*....|....
gi 330253231 408 SEGYMVYQGPREDV 421
Cdd:PRK09700 219 KDGSSVCSGMVSDV 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
175-341 |
4.65e-05 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 47.38 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFHVK-RTSAYISQtdN-----Hiae 248
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPT---SGEILIGGRDVTDLPPKdRNIAMVFQ--SyalypH--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 249 LTVRETLDFAARCQGAsegfagymkdltrlekergirPSSEIDAfmkaasvkgekhsvSTDYVLKVLGLDvcsdtmvgnD 328
Cdd:COG3839 90 MTVYENIAFPLKLRKV---------------------PKAEIDR--------------RVREAAELLGLE---------D 125
|
170
....*....|....*..
gi 330253231 329 MM----RGVSGGQRKRV 341
Cdd:COG3839 126 LLdrkpKQLSGGQRQRV 142
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
846-1054 |
4.95e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.51 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 846 VPETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGGYtEGDIRISGHPKE-----QQTFARISGYVEQND 920
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKF-EGNVFINGKPVDirnpaQAIRAGIAMVPEDRK 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 921 IHS--PQVTVEESLWFSAslrLPKEITKEQKKEFVEQ--VMRLVELDTLRYALVGLPgTTGLSTEQRKRLTIAVELVANP 996
Cdd:TIGR02633 347 RHGivPILGVGKNITLSV---LKSFCFKMRIDAAAELqiIGSAIQRLKVKTASPFLP-IGRLSGGNQQKAVLAKMLLTNP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 330253231 997 SIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVcTIHQPSIDIFEAFDELLLMKRG 1054
Cdd:TIGR02633 423 RVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAII-VVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
174-423 |
5.33e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 47.51 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 174 NILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFH---VKRTSAYISQTdNHIAELT 250
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQ---QGEILLNGQPIADYSeaaLRQAISVVSQR-VHLFSAT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 251 VRETLDFAArcqgasegfagymkdltrlekergirpSSEIDAFMKAasvkgekhsvstdyVLKVLGLDVCSDTMVGNDMM 330
Cdd:PRK11160 430 LRDNLLLAA---------------------------PNASDEALIE--------------VLQQVGLEKLLEDDKGLNAW 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 331 -----RGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNfvHLMDATVLM------ALLQpapetfd 399
Cdd:PRK11160 469 lgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE--HAQNKTVLMithrltGLEQ------- 539
|
250 260
....*....|....*....|....
gi 330253231 400 lFDDLILLSEGYMVYQGPREDVIA 423
Cdd:PRK11160 540 -FDRICVMDNGQIIEQGTHQELLA 562
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
103-208 |
5.34e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 47.49 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 103 DNFKLLSAIKERLDRVGMevpkievrFENLNIEADVQAGTRALPTLVNVSRDFFERclssLRIIKPRKHKLniLKDISGI 182
Cdd:COG4178 320 DNYQSLAEWRATVDRLAG--------FEEALEAADALPEAASRIETSEDGALALED----LTLRTPDGRPL--LEDLSLS 385
|
90 100
....*....|....*....|....*.
gi 330253231 183 IKPGRMTLLLGPPGSGKSTLLLALAG 208
Cdd:COG4178 386 LKPGERLLITGPSGSGKSTLLRAIAG 411
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
175-229 |
6.70e-05 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 45.60 E-value: 6.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDKSlkKTGNITYNGENLNK 229
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINL-LEEP--DSGTIIIDGLKLTD 66
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
175-364 |
7.20e-05 |
|
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: 45.69 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAG--KLDKslkktGNITYNGENLNKFHV-KRTSAYISQTDNHIAELTV 251
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGfeTPTS-----GEILLDGKDITNLPPhKRPVNTVFQNYALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 252 RETLDFAARCQGASEgfagymkdltrlekergirpsSEIDAFMKAAsvkgekhsvstdyvLKVLGLDvcsdtMVGNDMMR 331
Cdd:cd03300 90 FENIAFGLRLKKLPK---------------------AEIKERVAEA--------------LDLVQLE-----GYANRKPS 129
|
170 180 190
....*....|....*....|....*....|...
gi 330253231 332 GVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLD 364
Cdd:cd03300 130 QLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
179-244 |
7.58e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.08 E-value: 7.58e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 330253231 179 ISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkktGNITYNGENL-----NKFHVKRtsAYISQTDN 244
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS----GSIQFAGQPLeawsaAELARHR--AYLSQQQT 79
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
174-229 |
7.70e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 45.96 E-value: 7.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 330253231 174 NILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDKSlkKTGNITYNGENLNK 229
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGG-LDTP--TSGDVIFNGQPMSK 75
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
175-210 |
7.71e-05 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 44.36 E-value: 7.71e-05
10 20 30
....*....|....*....|....*....|....*.
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKL 210
Cdd:cd03221 15 LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGEL 50
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
154-444 |
7.95e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 46.64 E-value: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 154 DFFErclssLRIIKPRKHKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDKSlkKTGNITYNGENLNKFHVK 233
Cdd:PRK11432 5 NFVV-----LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAG-LEKP--TEGQIFIDGEDVTHRSIQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 234 -RTSAYISQTDNHIAELTVRETLDFAARCQGasegfagymkdltrlekergiRPSSEIDAFMKAAsvkgekhsvstdyvL 312
Cdd:PRK11432 77 qRDICMVFQSYALFPHMSLGENVGYGLKMLG---------------------VPKEERKQRVKEA--------------L 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 313 KVLGLDVCSDTMVGNdmmrgVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMaLLQ 392
Cdd:PRK11432 122 ELVDLAGFEDRYVDQ-----ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLY-VTH 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 330253231 393 PAPETFDLFDDLILLSEGYMVYQGPREDViaffeslgFRLPPRKGVADFLQE 444
Cdd:PRK11432 196 DQSEAFAVSDTVIVMNKGKIMQIGSPQEL--------YRQPASRFMASFMGD 239
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
863-1054 |
8.25e-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: 44.29 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 863 PGVLTALVGSSGAGKTTLMDVLAgRKTGGYTEGDIRISGHPKEQQTFARIsgyveqndihspqvtveeslwfsaslrlpk 942
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALA-RELGPPGGGVIYIDGEDILEEVLDQL------------------------------ 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 943 eitkeqkkefveqvmrlveldtlryaLVGLPGTTGLSTEQRKRLTIAVELV--ANPSIIFMDEPTSGLDARAAAIVMRTV 1020
Cdd:smart00382 50 --------------------------LLIIVGGKKASGSGELRLRLALALArkLKPDVLILDEITSLLDAEQEALLLLLE 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 330253231 1021 RNTVD------TGRTVVCTIHQPSI----DIFEAFDELLLMKRG 1054
Cdd:smart00382 104 ELRLLlllkseKNLTVILTTNDEKDlgpaLLRRRFDRRIVLLLI 147
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
175-228 |
8.51e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 45.80 E-value: 8.51e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLD--KSLKKTGNITYNGENLN 228
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGARVEGEILLDGEDIY 81
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
175-227 |
8.79e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.94 E-value: 8.79e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSLKKtGNITYNGENL 227
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTG-GTVEFKGKDL 67
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
1203-1411 |
1.00e-04 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 44.81 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1203 ITVMGALYSACLFLGVSnassvqpivsiertvFYREKAAGMY-----APIP---YAAAQGLVEIPYILTQTILYGVITYF 1274
Cdd:COG0842 9 LLAMSLLFTALMLTALS---------------IAREREQGTLerllvTPVSrleILLGKVLAYLLRGLLQALLVLLVALL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 1275 TIGFERTFSKFVLYLVFMFLTFTYFTFYGMMAVGLTPNQHLAAVISSAFYSLWNLLSGFLVQKPLIPVWWIWFYYICPVA 1354
Cdd:COG0842 74 FFGVPLRGLSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 330253231 1355 WTLQGVILSQLGDVEsmineplfhgtvkefieyyfgykPNMIGVSAAVLVGFCALFF 1411
Cdd:COG0842 154 YFVEALRALFLGGAG-----------------------LADVWPSLLVLLAFAVVLL 187
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
183-364 |
1.03e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 45.22 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 183 IKPGRMTLLLGPPGSGKSTLLLALAGKLDkslKKTGNITYNGENLNKFHVKRTSAYISQTDNHIAELTVRETLDFAArcq 262
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLH---VESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLC--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 263 gaseGFAGYMKDLTrlekergirPSSeidafmkaasvkgekhsvstdyVLKVLGLDVCSDTMVgndmmRGVSGGQRKRVT 342
Cdd:PRK13543 108 ----GLHGRRAKQM---------PGS----------------------ALAIVGLAGYEDTLV-----RQLSAGQKKRLA 147
|
170 180
....*....|....*....|..
gi 330253231 343 TGEMTVGPRKTLFMDEISTGLD 364
Cdd:PRK13543 148 LARLWLSPAPLWLLDEPYANLD 169
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
159-208 |
1.32e-04 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 44.07 E-value: 1.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 330253231 159 CLSSLRIIKPRKHKLniLKDISGIIKPGRMTLLLGPPGSGKSTLLLALAG 208
Cdd:cd03223 2 ELENLSLATPDGRVL--LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG 49
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
866-1009 |
1.33e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 45.54 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 866 LTALVGSSGAGKTTLM-------DVLAGRKTggytEGDIRISGHpkeqqtfarisgyveqnDIHSPQVTVEE-----SLW 933
Cdd:PRK14243 38 ITAFIGPSGCGKSTILrcfnrlnDLIPGFRV----EGKVTFHGK-----------------NLYAPDVDPVEvrrriGMV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 934 FSASLRLPKEIT------------KEQKKEFVEQVMRLVEL-----DTLRYAlvGLpgttGLSTEQRKRLTIAVELVANP 996
Cdd:PRK14243 97 FQKPNPFPKSIYdniaygaringyKGDMDELVERSLRQAALwdevkDKLKQS--GL----SLSGGQQQRLCIARAIAVQP 170
|
170
....*....|...
gi 330253231 997 SIIFMDEPTSGLD 1009
Cdd:PRK14243 171 EVILMDEPCSALD 183
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
175-423 |
1.40e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 46.24 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKF---HVKRTSAYISQTDNHIAElTV 251
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS---EGDIRFHDIPLTKLqldSWRSRLAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 252 RETLdfAARCQGASEgfagymkdltrlekergirpsSEIDAFMKAASVKGEkhsvstdyvlkVLGLDVCSDTMVGNdmmR 331
Cdd:PRK10789 406 ANNI--ALGRPDATQ---------------------QEIEHVARLASVHDD-----------ILRLPQGYDTEVGE---R 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 332 GV--SGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVH----LMDATVLMALLQPapetfdlfDDLI 405
Cdd:PRK10789 449 GVmlSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEgrtvIISAHRLSALTEA--------SEIL 520
|
250
....*....|....*...
gi 330253231 406 LLSEGYMVYQGPREDVIA 423
Cdd:PRK10789 521 VMQHGHIAQRGNHDQLAQ 538
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
183-269 |
1.44e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 44.41 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 183 IKPGRMTLLLGPPGSGKSTLLLALAGkLdkSLKKTGNITYNGENLNK----FHvkRTSAYISqtdnHIA----ELTVRET 254
Cdd:PRK13538 24 LNAGELVQIEGPNGAGKTSLLRILAG-L--ARPDAGEVLWQGEPIRRqrdeYH--QDLLYLG----HQPgiktELTALEN 94
|
90
....*....|....*
gi 330253231 255 LDFAARCQGASEGFA 269
Cdd:PRK13538 95 LRFYQRLHGPGDDEA 109
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
112-255 |
1.96e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 45.83 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 112 KERLDRVGMEVPKIEVRFENLNIEADVQAGTRALpTLVNVSRDFFERclsslriikprkhklNILKDISGIIKPGRMTLL 191
Cdd:COG0488 283 IKALEKLEREEPPRRDKTVEIRFPPPERLGKKVL-ELEGLSKSYGDK---------------TLLDDLSLRIDRGDRIGL 346
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330253231 192 LGPPGSGKSTLLLALAGKLDKSlkkTGNITYnGENLNKfhvkrtsAYISQtdnHIAEL----TVRETL 255
Cdd:COG0488 347 IGPNGAGKSTLLKLLAGELEPD---SGTVKL-GETVKI-------GYFDQ---HQEELdpdkTVLDEL 400
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
969-1022 |
2.15e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 2.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 330253231 969 LVGlPGTTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN 1022
Cdd:PTZ00265 572 LVG-SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINN 624
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
840-905 |
2.16e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 2.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 330253231 840 EMRS-----QGVpetrlQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGGYTEGDIRISGHPKE 905
Cdd:NF040905 3 EMRGitktfPGV-----KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEILFDGEVCR 68
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
175-231 |
2.26e-04 |
|
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: 43.36 E-value: 2.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFH 231
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT---SGRVRLDGADISQWD 70
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
392-435 |
2.45e-04 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 45.28 E-value: 2.45e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 330253231 392 QPAPETFDLFDDLILLSEG-YMVYQGPREDVIAFFESLGFRLPPR 435
Cdd:pfam19055 2 QPSYTLFKMFDDLILLAKGgLTVYHGPVKKVEEYFAGLGINVPER 46
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
176-266 |
2.63e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.50 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLALAG--KLdkslkKTGNITYNGENL-NKFHVKRTS---AYISQT--DNHIA 247
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarKI-----QQGRVEVLGGDMaDARHRRAVCpriAYMPQGlgKNLYP 91
|
90 100
....*....|....*....|.
gi 330253231 248 ELTVRETLDFAARC--QGASE 266
Cdd:NF033858 92 TLSVFENLDFFGRLfgQDAAE 112
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
176-228 |
2.85e-04 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 44.75 E-value: 2.85e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDKSlkKTGNITYNGENLN 228
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAG-LETP--DSGRIVLNGRDLF 67
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
868-1031 |
3.25e-04 |
|
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: 43.19 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 868 ALVGSSGAGKTTLMDVLAGRKTggYTEGDIRISGHPKEqqtfarisgyveqndIHSPQVTVEESLWFsaslrlpkeITKE 947
Cdd:cd03215 30 GIAGLVGNGQTELAEALFGLRP--PASGEITLDGKPVT---------------RRSPRDAIRAGIAY---------VPED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 948 QKKEFVEQVMRLVELDTLRYALVGlpGTtglsteQRKrLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTG 1027
Cdd:cd03215 84 RKREGLVLDLSVAENIALSSLLSG--GN------QQK-VVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAG 154
|
....
gi 330253231 1028 RTVV 1031
Cdd:cd03215 155 KAVL 158
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
926-1070 |
3.36e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 926 VTVEESLWFSASLRLPKEITKEQ-KKEFVEQVMRLVELDTLRYAL-------VGlPGTTGLSTEQRKRLTIAVELVANPS 997
Cdd:PTZ00265 1300 IVSQEPMLFNMSIYENIKFGKEDaTREDVKRACKFAAIDEFIESLpnkydtnVG-PYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330253231 998 IIFMDEPTSGLDARAAAIVMRTVRNTVDTG-RTVVCTIHQpsIDIFEAFDELLLMK---RGGQVIYGGklGTHSQVL 1070
Cdd:PTZ00265 1379 ILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHR--IASIKRSDKIVVFNnpdRTGSFVQAH--GTHEELL 1451
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
150-208 |
3.45e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 43.92 E-value: 3.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330253231 150 NVSRDF--FERCLSSLRII-----KPRKHKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAG 208
Cdd:COG1134 9 NVSKSYrlYHEPSRSLKELllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG 74
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
176-234 |
3.87e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 44.33 E-value: 3.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFHVKR 234
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD---SGEVLWDGEPLDPEDRRR 72
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
28-207 |
3.95e-04 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 45.18 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 28 AETVEQDEEDLRWAAIGRLPSQRQGTHNAILRRSQTQTQTSGYADGNVVQTIDVKKLDRADREMLVRQALATSDQDNFKL 107
Cdd:COG5635 21 LVTRLAIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAAALLARALSALLLVLLLLESLLLLLLLLLLL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 108 LSAIKERLDRVGMEVPKIEVRFENLNIEADVQAGTRALPTLVNVSRDFFER-CLSSLRIIKPRKHKLNILKDISGIIKPG 186
Cdd:COG5635 101 AEALLALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLvSLDDLYVPLNLLERIESLKRLELLEAKK 180
|
170 180
....*....|....*....|.
gi 330253231 187 RMTLLLGPPGSGKSTLLLALA 207
Cdd:COG5635 181 KRLLILGEPGSGKTTLLRYLA 201
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
853-1032 |
4.59e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.90 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggyTEGDIRISG---HPKEQQTFARISGYVEQndihspQVTVe 929
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS---TEGEIQIDGvswNSVTLQTWRKAFGVIPQ------KVFI- 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 930 eslwFSASLRLPKEITKEQKKEFVEQVMRLVEL--------DTLRYALVGlpGTTGLSTEQRKRLTIAVELVANPSIIFM 1001
Cdd:TIGR01271 1304 ----FSGTFRKNLDPYEQWSDEEIWKVAEEVGLksvieqfpDKLDFVLVD--GGYVLSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190
....*....|....*....|....*....|.
gi 330253231 1002 DEPTSGLDARAAAIVMRTVRNTVDTGRTVVC 1032
Cdd:TIGR01271 1378 DEPSAHLDPVTLQIIRKTLKQSFSNCTVILS 1408
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
853-1034 |
5.06e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 44.94 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLmdVLAGRKTGGYTEGDIRISGhpkeqQTFARISgyveQNDIHSpQVTV--EE 930
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSL--TLGLFRINESAEGEIIIDG-----LNIAKIG----LHDLRF-KITIipQD 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 931 SLWFSASLRLPKEITKEQKKEFVEQVMRLVELDTLRYAL-VGL-----PGTTGLSTEQRKRLTIAVELVANPSIIFMDEP 1004
Cdd:TIGR00957 1369 PVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALpDKLdhecaEGGENLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190
....*....|....*....|....*....|
gi 330253231 1005 TSGLDARAAAIVMRTVRNTVDTgrtvvCTI 1034
Cdd:TIGR00957 1449 TAAVDLETDNLIQSTIRTQFED-----CTV 1473
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
181-216 |
5.10e-04 |
|
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a role in recombination and recombinational repair of DNA damaged by UV radiation, X-rays, and chemical agent and is responsible for the stabilization or processing of branched DNA molecules.
Pssm-ID: 410866 [Multi-domain] Cd Length: 268 Bit Score: 43.67 E-value: 5.10e-04
10 20 30
....*....|....*....|....*....|....*.
gi 330253231 181 GIIkPGRMTLLLGPPGSGKSTLLLALAGKLDKSLKK 216
Cdd:cd01121 78 GLV-PGSVVLIGGDPGIGKSTLLLQVAARLAQRGGK 112
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
175-228 |
5.55e-04 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 43.93 E-value: 5.55e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAG--KLDkslkkTGNITYNGENLN 228
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfeTPD-----SGRILLDGRDVT 70
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
183-207 |
6.06e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.51 E-value: 6.06e-04
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
843-1070 |
6.14e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 44.55 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 843 SQGVPETrlqlLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGHPK--EQQTFArisgyveQND 920
Cdd:TIGR00957 647 ARDLPPT----LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK--VEGHVHMKGSVAyvPQQAWI-------QND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 921 ihspqvTVEESLWFSASLRLPKeitkeqKKEFVEQVMRLVELDTLRYALVGLPGTTG--LSTEQRKRLTIAVELVANPSI 998
Cdd:TIGR00957 714 ------SLRENILFGKALNEKY------YQQVLEACALLPDLEILPSGDRTEIGEKGvnLSGGQKQRVSLARAVYSNADI 781
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330253231 999 IFMDEPTSGLDARAAAIVMRTVRNT--VDTGRTVVCTIHqpSIDIFEAFDELLLMKrGGQViygGKLGTHSQVL 1070
Cdd:TIGR00957 782 YLFDDPLSAVDAHVGKHIFEHVIGPegVLKNKTRILVTH--GISYLPQVDVIIVMS-GGKI---SEMGSYQELL 849
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
605-720 |
6.87e-04 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 42.49 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 605 PAWSWSIASWLLRVPYSVLEAVVWSGVVYFTVGLAPSAGRFFRYML--LLFSVHQMALGLFrmMASLARDMVIANTFGSA 682
Cdd:COG0842 44 SRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLLLLLLvlLLFALAFSGLGLL--ISTLARSQEQASAISNL 121
|
90 100 110
....*....|....*....|....*....|....*...
gi 330253231 683 AILIVFLLGGFVIPKADIKPWWVWGFWVSPLSYGQRAI 720
Cdd:COG0842 122 VILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEAL 159
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
175-318 |
6.98e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 42.78 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGEN---LNKFHVKRTSAYISQTDNHIAElTV 251
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPT---SGTLLFEGEDistLKPEIYRQQVSYCAQTPTLFGD-TV 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 330253231 252 RETLDFAARCQGASEGFAGYMKDLTRLEkergiRPSSEIDAFMKAASvKGEKHSVS----TDYVLKVLGLD 318
Cdd:PRK10247 98 YDNLIFPWQIRNQQPDPAIFLDDLERFA-----LPDTILTKNIAELS-GGEKQRISlirnLQFMPKVLLLD 162
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
167-260 |
7.45e-04 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 42.95 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 167 KPRKHKLnilkdisgiiKPGRMTLLLGPPGSGKSTLLLALAGKLDKSLkktgnITYNGENLnkfhvkrTSAYISQTDNHI 246
Cdd:COG1223 26 NLRKFGL----------WPPRKILFYGPPGTGKTMLAEALAGELKLPL-----LTVRLDSL-------IGSYLGETARNL 83
|
90
....*....|....
gi 330253231 247 AELtvretLDFAAR 260
Cdd:COG1223 84 RKL-----FDFARR 92
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
854-1013 |
7.71e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.34 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 854 LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGrKTGGYTEGDIRISGhpkeqqTFArisgYVeqndihsPQVtveeSLW 933
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPPRSDASVVIRG------TVA----YV-------PQV----SWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 934 FSASLR------LPKEITKEQkkefveqvmRLVELDTLRYALVGLPG---------TTGLSTEQRKRLTIAVELVANPSI 998
Cdd:PLN03130 691 FNATVRdnilfgSPFDPERYE---------RAIDVTALQHDLDLLPGgdlteigerGVNISGGQKQRVSMARAVYSNSDV 761
|
170
....*....|....*
gi 330253231 999 IFMDEPTSGLDARAA 1013
Cdd:PLN03130 762 YIFDDPLSALDAHVG 776
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
175-422 |
8.43e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 42.85 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFHVK---RTSAYISQTDNHIAELTV 251
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS---EGEILLDAQPLESWSSKafaRKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 252 RETLdfaarcqgaSEGFAGYMKDLTRLEKERGIRPSSEIDafmkaasvkgekhsvstdyvlkVLGLdvcsdTMVGNDMMR 331
Cdd:PRK10575 103 RELV---------AIGRYPWHGALGRFGAADREKVEEAIS----------------------LVGL-----KPLAHRLVD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 332 GVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLmALLQPAPETFDLFDDLILLSEGY 411
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVI-AVLHDINMAARYCDYLVALRGGE 225
|
250
....*....|.
gi 330253231 412 MVYQGPREDVI 422
Cdd:PRK10575 226 MIAQGTPAELM 236
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
179-207 |
8.96e-04 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 42.97 E-value: 8.96e-04
10 20
....*....|....*....|....*....
gi 330253231 179 ISGIIKPGRMTLLLGPPGSGKSTLLLALA 207
Cdd:COG3598 6 VPGLLPEGGVTLLAGPPGTGKSFLALQLA 34
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
842-1070 |
1.15e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 43.10 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 842 RSQGVPETRLQL-LSNVSGVFSPGVLTALVGSSGAGKTTLMDVLagRKTGGYTEGDIRISGHPKEQQTFARIS------- 913
Cdd:PRK10070 31 KEQILEKTGLSLgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLL--NRLIEPTRGQVLIDGVDIAKISDAELRevrrkki 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 914 GYVEQNDIHSPQVTVEESLWFSASLrlpKEITKEQKKEFVEQVMRLVELDTLRYalvGLPGTtgLSTEQRKRLTIAVELV 993
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMEL---AGINAEERREKALDALRQVGLENYAH---SYPDE--LSGGMRQRVGLARALA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 994 ANPSIIFMDEPTSGLDAraaaiVMRT------VRNTVDTGRTVVCTIHqpsiDIFEAF---DELLLMKRGGQViyggKLG 1064
Cdd:PRK10070 181 INPDILLMDEAFSALDP-----LIRTemqdelVKLQAKHQRTIVFISH----DLDEAMrigDRIAIMQNGEVV----QVG 247
|
....*.
gi 330253231 1065 THSQVL 1070
Cdd:PRK10070 248 TPDEIL 253
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
157-210 |
1.15e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 42.25 E-value: 1.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 330253231 157 ERCLSSLRI--IKPRKHKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKL 210
Cdd:COG2401 25 ERVAIVLEAfgVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL 80
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
853-1009 |
1.17e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 43.75 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGhpkeqqtfaRISgyveqndiHSPQV------ 926
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEP--SEGKIKHSG---------RIS--------FSPQTswimpg 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 927 TVEESLWFSASLRLPKEITKEQKKEFVEQVMRLVELDTLryaLVGLPGTTgLSTEQRKRLTIAVELVANPSIIFMDEPTS 1006
Cdd:TIGR01271 502 TIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKT---VLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFT 577
|
...
gi 330253231 1007 GLD 1009
Cdd:TIGR01271 578 HLD 580
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
169-230 |
1.20e-03 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 42.73 E-value: 1.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330253231 169 RKHKLNILKDISGIIKPGRmTL-LLGPPGSGKSTLLLALAGKLDKSLKKTGNITYNGENLNKF 230
Cdd:COG0444 14 RRGVVKAVDGVSFDVRRGE-TLgLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEDLLKL 75
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
943-1061 |
1.23e-03 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 42.22 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 943 EITKEQKKEFVEQVMRLVE-LDTLR-----YALVGLPGTTgLSTEQRKRLTIAVELvANPS----IIFMDEPTSGL---D 1009
Cdd:cd03271 130 DMTVEEALEFFENIPKIARkLQTLCdvglgYIKLGQPATT-LSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLhfhD 207
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 330253231 1010 ARAAAIVMRTVrntVDTGRTVVCTIHQpsIDIFEAFDELLLM-----KRGGQVIYGG 1061
Cdd:cd03271 208 VKKLLEVLQRL---VDKGNTVVVIEHN--LDVIKCADWIIDLgpeggDGGGQVVASG 259
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
168-371 |
1.23e-03 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 42.07 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 168 PRKHKLNILKDISGIIKPGRMTLLLGPPGSGKST---LLLALAGKLDkslkktGNITYNGENLNKF---HVKRTSAYISQ 241
Cdd:cd03248 22 PTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTvvaLLENFYQPQG------GQVLLDGKPISQYehkYLHSKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 242 tdnhiaELTVretldfaarcqgasegFAGYMKD-----LTRLEKERgirpsseidafMKAASVKGEKHSVstdyvlkVLG 316
Cdd:cd03248 96 ------EPVL----------------FARSLQDniaygLQSCSFEC-----------VKEAAQKAHAHSF-------ISE 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 330253231 317 LDVCSDTMVGNdmmRG--VSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQI 371
Cdd:cd03248 136 LASGYDTEVGE---KGsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV 189
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
176-373 |
1.33e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 42.37 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLD----KSLKKTGNITYNGENLNKfhVKRTSAYISQT-DNHIAELT 250
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKptsgEVLIKGEPIKYDKKSLLE--VRKTVGIVFQNpDDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 251 VRETLDFAARCQGASEGfagymkdltrlEKERGIRPSseidafMKAASVKGEKhsvstdyvlkvlgldvcsdtmvgNDMM 330
Cdd:PRK13639 96 VEEDVAFGPLNLGLSKE-----------EVEKRVKEA------LKAVGMEGFE-----------------------NKPP 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 330253231 331 RGVSGGQRKRVT-TGEMTVGPrKTLFMDEISTGLDSSTTFQIVK 373
Cdd:PRK13639 136 HHLSGGQKKRVAiAGILAMKP-EIIVLDEPTSGLDPMGASQIMK 178
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
852-1020 |
1.33e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 43.13 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 852 QLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTggYTEGDIRIsGHPkeqqtfARIsGYVEQ-NDIHSPQVTVEE 930
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE--PDSGTVKL-GET------VKI-GYFDQhQEELDPDKTVLD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 931 SLWfsaslrlpkEITKEQKKEFV-----------EQVMRLVEldtlryalvglpgttGLSTEQRKRLTIAVELVANPSII 999
Cdd:COG0488 399 ELR---------DGAPGGTEQEVrgylgrflfsgDDAFKPVG---------------VLSGGEKARLALAKLLLSPPNVL 454
|
170 180
....*....|....*....|.
gi 330253231 1000 FMDEPTSGLDaraaaIVMRTV 1020
Cdd:COG0488 455 LLDEPTNHLD-----IETLEA 470
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
850-1021 |
1.34e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.31 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 850 RLQLLSNVSGVFSPGVLTALVGSSGAGKT----TLMDVLagRKTGGYTEGD---IR------ISGHPKEQQTFARISG-- 914
Cdd:PRK10261 28 KIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLL--EQAGGLVQCDkmlLRrrsrqvIELSEQSAAQMRHVRGad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 915 ----YVEQNDIHSPQVTVEESLwfSASLRLPKEITKE----QKKEFVEQVmRLVELDTL--RYAlvglpgtTGLSTEQRK 984
Cdd:PRK10261 106 mamiFQEPMTSLNPVFTVGEQI--AESIRLHQGASREeamvEAKRMLDQV-RIPEAQTIlsRYP-------HQLSGGMRQ 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 330253231 985 RLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVR 1021
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIK 212
|
|
| Sms |
COG1066 |
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and ... |
181-217 |
1.75e-03 |
|
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and repair];
Pssm-ID: 440685 [Multi-domain] Cd Length: 453 Bit Score: 42.73 E-value: 1.75e-03
10 20 30
....*....|....*....|....*....|....*..
gi 330253231 181 GIIkPGRMTLLLGPPGSGKSTLLLALAGKLDKSLKKT 217
Cdd:COG1066 85 GLV-PGSVVLIGGEPGIGKSTLLLQVAARLAKKGGKV 120
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
853-1009 |
1.79e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 42.15 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 853 LLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGgyTEGDIRISGhpkeqqtfaRISgyveqndiHSPQV------ 926
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEP--SEGKIKHSG---------RIS--------FSSQFswimpg 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 927 TVEESLWFSASLRLPKEITKEQKKEFVEQVMRLVELDtlrYALVGLPGTTgLSTEQRKRLTIAVELVANPSIIFMDEPTS 1006
Cdd:cd03291 113 TIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKD---NTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFG 188
|
...
gi 330253231 1007 GLD 1009
Cdd:cd03291 189 YLD 191
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
986-1039 |
2.08e-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: 41.99 E-value: 2.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 330253231 986 LTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1039
Cdd:pfam13304 248 LAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLL 301
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
164-253 |
2.31e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 42.23 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 164 RIIKPRKHklnILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDKSlkktgnitYNGEnlNKFHVKRTSAYISQTD 243
Cdd:TIGR03719 12 KVVPPKKE---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKD--------FNGE--ARPQPGIKVGYLPQEP 77
|
90
....*....|
gi 330253231 244 NHIAELTVRE 253
Cdd:TIGR03719 78 QLDPTKTVRE 87
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
185-253 |
2.40e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.30 E-value: 2.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330253231 185 PGRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNkFHVKRTS--AYIS---QTDNHIAELTVRE 253
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYTRD---AGSILYLGKEVT-FNGPKSSqeAGIGiihQELNLIPQLTIAE 98
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
858-898 |
2.42e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.84 E-value: 2.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 330253231 858 SGVFSPGVLTALVGSSGAGKTTLMDVLAGR---KTGGYTEGDIR 898
Cdd:PRK01889 189 AAWLSGGKTVALLGSSGVGKSTLVNALLGEevqKTGAVREDDSK 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
856-1009 |
2.44e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.15 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 856 NVSGVFSPGVLTALVGSSGAGKTTL---MDVLAGRKTGGYTEGDIRISGHPKEQ-QTFARISGYVEQNDIHS--PQVTVE 929
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTgraLLRLVESQGGEIIFNGQRIDTLSPGKlQALRRDIQFIFQDPYASldPRQTVG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 930 ESLWfsASLR----LPKEITKEQKKEFVEQVMRLVElDTLRYAlvglpgtTGLSTEQRKRLTIAVELVANPSIIFMDEPT 1005
Cdd:PRK10261 422 DSIM--EPLRvhglLPGKAAAARVAWLLERVGLLPE-HAWRYP-------HEFSGGQRQRICIARALALNPKVIIADEAV 491
|
....
gi 330253231 1006 SGLD 1009
Cdd:PRK10261 492 SALD 495
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
176-208 |
2.48e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 41.64 E-value: 2.48e-03
10 20 30
....*....|....*....|....*....|...
gi 330253231 176 LKDISGIIKPGRMTLLLGPPGSGKSTLLLALAG 208
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNG 53
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
175-227 |
2.48e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 41.29 E-value: 2.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLdksLKKTGNITYNGENL 227
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQI---APDHGEILFDGENI 71
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
175-202 |
2.52e-03 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 42.11 E-value: 2.52e-03
10 20
....*....|....*....|....*...
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTL 202
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTL 400
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
175-364 |
2.58e-03 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 41.86 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAG--KLDkslkkTGNITYNGENLNkfHV---KRTSAYISQTDNHIAEL 249
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGfeTPD-----SGRIMLDGQDIT--HVpaeNRHVNTVFQSYALFPHM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 250 TVRETLDFAARCQGasegfagymkdltrlekergiRPSSEIDAFMKAAsvkgekhsvstdyvLKVLGLDvcsdtMVGNDM 329
Cdd:PRK09452 102 TVFENVAFGLRMQK---------------------TPAAEITPRVMEA--------------LRMVQLE-----EFAQRK 141
|
170 180 190
....*....|....*....|....*....|....*
gi 330253231 330 MRGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLD 364
Cdd:PRK09452 142 PHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| RecA-like_BCS1 |
cd19510 |
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ... |
187-213 |
2.66e-03 |
|
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410918 [Multi-domain] Cd Length: 153 Bit Score: 40.03 E-value: 2.66e-03
10 20
....*....|....*....|....*..
gi 330253231 187 RMTLLLGPPGSGKSTLLLALAGKLDKS 213
Cdd:cd19510 24 RGYLLYGPPGTGKSSFIAALAGELDYD 50
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
164-225 |
3.29e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.64 E-value: 3.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 330253231 164 RIIKPRKHklnILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGkLDKSlkktgnitYNGE 225
Cdd:PRK11819 14 KVVPPKKQ---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKE--------FEGE 63
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
142-264 |
3.52e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.07 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 142 TRALPTLVNVSRDFFErclsslriIKPRKhklnILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSlkktgnit 221
Cdd:PTZ00243 654 ERSAKTPKMKTDDFFE--------LEPKV----LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEIS-------- 713
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 330253231 222 yNGENLnkfhVKRTSAYISQtDNHIAELTVRETLDF-----AARCQGA 264
Cdd:PTZ00243 714 -EGRVW----AERSIAYVPQ-QAWIMNATVRGNILFfdeedAARLADA 755
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
943-1061 |
3.73e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 943 EITKEQKKEFVEQVMRL-VELDT-----LRYALVGLPGTTgLSTEQRKRLTIAVEL---VANPSIIFMDEPTSGLDARAA 1013
Cdd:TIGR00630 790 DMTVEEAYEFFEAVPSIsRKLQTlcdvgLGYIRLGQPATT-LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDI 868
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 330253231 1014 AIVMRTVRNTVDTGRTVVCTIHqpSIDIFEAFDELLLM-----KRGGQVIYGG 1061
Cdd:TIGR00630 869 KKLLEVLQRLVDKGNTVVVIEH--NLDVIKTADYIIDLgpeggDGGGTVVASG 919
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
147-208 |
4.61e-03 |
|
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: 40.21 E-value: 4.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330253231 147 TLVNVSRDF--FERCLSSLRIIKPRKHKLN-----ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAG 208
Cdd:cd03220 2 ELENVSKSYptYKGGSSSLKKLGILGRKGEvgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAG 70
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
145-208 |
5.07e-03 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 40.48 E-value: 5.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330253231 145 LPTLVNVSRDFFERclsslriikprkhklNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAG 208
Cdd:PRK09544 4 LVSLENVSVSFGQR---------------RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLG 52
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
175-222 |
5.71e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 40.61 E-value: 5.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKS---LKKTGNITY 222
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSegkIKHSGRISF 102
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
186-260 |
6.21e-03 |
|
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: 39.78 E-value: 6.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330253231 186 GRMTLLLGPPGSGKSTLLLALAGKLDKSlkkTGNITYNGENLNKFH--VKRTSAYISQTDNHIAELTVRETLDFAAR 260
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPL---AGRVLLNGGPLDFQRdsIARGLLYLGHAPGIKTTLSVLENLRFWHA 99
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
861-932 |
6.57e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.40 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253231 861 FSPGvLTALVGSSGAGKTTLMD----VLAGRKTGGYTEGDIRISGHPKEQQTFARISGYVE-----QNDIHSPQVTVEES 931
Cdd:pfam13476 16 FSKG-LTLITGPNGSGKTTILDaiklALYGKTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEitfenNDGRYTYAIERSRE 94
|
.
gi 330253231 932 L 932
Cdd:pfam13476 95 L 95
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
175-222 |
7.24e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 41.05 E-value: 7.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 330253231 175 ILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKS---LKKTGNITY 222
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSegkIKHSGRISF 491
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
334-381 |
8.15e-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: 38.84 E-value: 8.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 330253231 334 SGGQRKRV-TTGEMTVGPRKTLF-MDEISTGLDSSTTFQIVKCIRNFVHL 381
Cdd:cd03238 89 SGGELQRVkLASELFSEPPGTLFiLDEPSTGLHQQDINQLLEVIKGLIDL 138
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
168-206 |
8.48e-03 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 40.48 E-value: 8.48e-03
10 20 30
....*....|....*....|....*....|....*....
gi 330253231 168 PRKHKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLAL 206
Cdd:TIGR00958 489 PNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL 527
|
|
| |
