|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
78-1480 |
0e+00 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 1705.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 78 EDDELKRKWAAIERLPTADRLRLSLLSSTRGGGSSGDVSEGggggaasselEVVDVRWLGAAERRAVVQRLVADVKHDHV 157
Cdd:PLN03140 41 DEDEEALKWAAIEKLPTYSRLRTSIMKSFVENDVYGNQLLH----------KEVDVTKLDGNDRQKFIDMVFKVAEEDNE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 158 RMLRKQRERMERVGVRPATVEVRWRDVCVEAECQVVSgKPLPTLWNAALSRFSLLAAKLGFS-HHQSKVQILENVSGIIK 236
Cdd:PLN03140 111 KFLKKFRNRIDRVGIKLPTVEVRFEHLTVEADCYIGS-RALPTLPNAARNIAESALGMLGINlAKKTKLTILKDASGIIK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 237 PSRITLLLGPPGCGKTTLLKALAGRLNKSLKETGEIEYNGVKLDEFVPAKTSAYVSQYDLHVADMTVRETLDFSARFQGV 316
Cdd:PLN03140 190 PSRMTLLLGPPSSGKTTLLLALAGKLDPSLKVSGEITYNGYRLNEFVPRKTSAYISQNDVHVGVMTVKETLDFSARCQGV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 317 GSRAEIMKAVIKREKEAGITPDPDIDAYMKAISMEGLQRSMQTDYIMKIMGLDKCADVKVGNAMRRGISGGEMKRLTTGE 396
Cdd:PLN03140 270 GTRYDLLSELARREKDAGIFPEAEVDLFMKATAMEGVKSSLITDYTLKILGLDICKDTIVGDEMIRGISGGQKKRVTTGE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 397 MIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILVSLLQPAPETYDLFDDIIIMGEGKVVYHGPKNLIMTFF 476
Cdd:PLN03140 350 MIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFDLFDDIILLSEGQIVYQGPRDHILEFF 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 477 ESCGFKCPERKGPADFLQEVLSKKDQQQYWSRSEQWYNFITVDQFCDKFKASQVGQSLAEDLSKLYEKSKANKNALSCSI 556
Cdd:PLN03140 430 ESCGFKCPERKGTADFLQEVTSKKDQEQYWADRNKPYRYISVSEFAERFKSFHVGMQLENELSVPFDKSQSHKAALVFSK 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 557 YSLSKWHLLKACFDRELLLMKRNAFLHITKAVQLGLLAIITGTVFFRTHKNF-DIVSANYYMGSLFYALILLMVNGIPEL 635
Cdd:PLN03140 510 YSVPKMELLKACWDKEWLLMKRNAFVYVFKTVQIIIVAAIASTVFLRTEMHTrNEEDGALYIGALLFSMIINMFNGFAEL 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 636 VMSISRLPVFYKHRDHYLYPGWAYAIPAFILKIPASLVAALSWTSISYYLIGYTPEAPRYFRQLLVLFLVHTGALSLYRC 715
Cdd:PLN03140 590 ALMIQRLPVFYKQRDLLFHPPWTFTLPTFLLGIPISIIESVVWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRL 669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 716 VGSYCQTIAVGPIAATMSLLVILLFGGFLIPRPSMPNWLKWGFWLSPLSYAEIGLTGNEFLAPRWL-KITISGVT-IGRR 793
Cdd:PLN03140 670 IASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEWAYWVSPLSYGFNALAVNEMFAPRWMnKMASDNSTrLGTA 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 794 ILIDRGLDFSVYFYWISVAALIGFILLYNIGFAIGLTIKQSPGASQAIISNDKIRICHGRDQEKSKDIKIGT-------- 865
Cdd:PLN03140 750 VLNIFDVFTDKNWYWIGVGALLGFTILFNVLFTLALTYLNPLGKKQAIISEETAEEMEGEEDSIPRSLSSADgnntreva 829
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 866 ---------------------------RRMALPFTPLTISFQDVNYYVDTPPEMRKKGYMGRKLQLLRNITGAFQPGILS 918
Cdd:PLN03140 830 iqrmsnpeglsknrdssleaangvapkRGMVLPFTPLAMSFDDVNYFVDMPAEMKEQGVTEDRLQLLREVTGAFRPGVLT 909
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 919 ALMGVTGAGKTTLLDVLAGRKTGGVIEGDIRIGGYPKVQQTFSRISGYCEQNDVHSPQITVGESVAYSAWLRLPAEIDTK 998
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKE 989
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 999 TRKEFVDEVLEIIELDEIRDALVGTPGVNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAETG 1078
Cdd:PLN03140 990 EKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTG 1069
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1079 RTVVCTIHQPSIEIFEAFDELMLIKRGGELIYAGPLGQHSCKVIQYFQSIPGVPKIKDNYNPSTWMLEVTSTSMEAQLGV 1158
Cdd:PLN03140 1070 RTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYSGPLGRNSHKIIEYFEAIPGVPKIKEKYNPATWMLEVSSLAAEVKLGI 1149
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1159 DFAQIYTGSSIRKDKDELIKGFSMPPPGTSDLHFPTRFPQKFLEQFKACLWKQFLSHWRTPSYNLVRIVFMAFSSIIFGV 1238
Cdd:PLN03140 1150 DFAEHYKSSSLYQRNKALVKELSTPPPGASDLYFATQYSQSTWGQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVGT 1229
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1239 LYWQQGNIRhiNDQQGLFTILGCMYGITIFTGINNSQSAMPFVAVERSVMYRERFAGMYSPWAYSFAQVAMEIPYVLMLA 1318
Cdd:PLN03140 1230 IFWKVGTKR--SNANDLTMVIGAMYAAVLFVGINNCSTVQPMVAVERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQT 1307
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1319 LLFMLIAYPTIGYAWTAAKFCWFFYTMFCTLLYFVYFGMLIVSITPNLQVASIYASSFYMTQHLLSGFVMPPSQIPKWWI 1398
Cdd:PLN03140 1308 TYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMMTVSLTPNQQVAAIFAAAFYGLFNLFSGFFIPRPKIPKWWV 1387
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1399 WLYYISPMSWTLNLLFTTQFG-FEDNSNILVFGETKPIAAFVRDYFGFHRELLPLSAIILAAYPVLFAILYGYSISRFNF 1477
Cdd:PLN03140 1388 WYYWICPVAWTVYGLIVSQYGdVEDTIKVPGGAPDPTIKWYIQDHYGYDPDFMGPVAAVLVGFTVFFAFIFAFCIRTLNF 1467
|
...
gi 1002313595 1478 QKR 1480
Cdd:PLN03140 1468 QTR 1470
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
160-1419 |
0e+00 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 1111.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 160 LRKQRERMERVGV--RPATVEVRWRDVCVEAecqVVSGKP-LPTLWNAALSRFSLLAAKLGFSHHQSKVQILENVSGIIK 236
Cdd:TIGR00956 9 VKNFRKLIDSDPIyyKPYKLGVAYKNLSAYG---VAADSDyQPTFPNALLKILTRGFRKLKKFRDTKTFDILKPMDGLIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 237 PSRITLLLGPPGCGKTTLLKALAGRLNKSLKE-TGEIEYNGVKLDEFVPAKT--SAYVSQYDLHVADMTVRETLDFSARF 313
Cdd:TIGR00956 86 PGELTVVLGRPGSGCSTLLKTIASNTDGFHIGvEGVITYDGITPEEIKKHYRgdVVYNAETDVHFPHLTVGETLDFAARC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 314 QGVGSRAEimkavikrekeaGITPDpdidAYMKAIsmeglqrsmqTDYIMKIMGLDKCADVKVGNAMRRGISGGEMKRLT 393
Cdd:TIGR00956 166 KTPQNRPD------------GVSRE----EYAKHI----------ADVYMATYGLSHTRNTKVGNDFVRGVSGGERKRVS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 394 TGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILVSLLQPAPETYDLFDDIIIMGEGKVVYHGPKNLIM 473
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 474 TFFESCGFKCPERKGPADFLQEVLSKKdQQQYWSRSEQwYNFITVDQFCDKFKASQVGQSLAEDLSKLYEK--------- 544
Cdd:TIGR00956 300 QYFEKMGFKCPDRQTTADFLTSLTSPA-ERQIKPGYEK-KVPRTPQEFETYWRNSPEYAQLMKEIDEYLDRcsesdtkea 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 545 ------SKANKNALSCSIYSLSKWHLLKACFDRELLLMKRNAFLHITKAVQLGLLAIITGTVFFRTHKNFDivSANYYMG 618
Cdd:TIGR00956 378 yreshvAKQSKRTRPSSPYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTS--DFYSRGG 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 619 SLFYALILLMVNGIPELVMSISRLPVFYKHRDHYLYPGWAYAIPAFILKIPASLVAALSWTSISYYLIGYTPEAPRYFRQ 698
Cdd:TIGR00956 456 ALFFAILFNAFSSLLEIASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFY 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 699 LLVLFLVHTGALSLYRCVGSYCQTIAVGPIAATMSLLVILLFGGFLIPRPSMPNWLKWGFWLSPLSYAEIGLTGNEFLAP 778
Cdd:TIGR00956 536 LLILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHGR 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 779 RWL------------------KI-TISGVTIGR-RILIDRGL----DFSVYFYWISVAALIGFILLYNIGFAIGLTIKQS 834
Cdd:TIGR00956 616 RFEcsqyvpsgggydnlgvtnKVcTVVGAEPGQdYVDGDDYLklsfQYYNSHKWRNFGIIIGFTVFFFFVYILLTEFNKG 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 835 PGASQAIIS---NDKIRICHGRDQEKSKDIKIgTRRMALPFTPLTISFQDVNYYVDTPPE-------MR----KKGYMGR 900
Cdd:TIGR00956 696 AKQKGEILVfrrGSLKRAKKAGETSASNKNDI-EAGEVLGSTDLTDESDDVNDEKDMEKEsgedifhWRnltyEVKIKKE 774
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 901 KLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGVIEGDIRIGGYPKVQQTFSRISGYCEQNDVHSPQITVG 980
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVR 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 981 ESVAYSAWLRLPAEIDTKTRKEFVDEVLEIIELDEIRDALVGTPGVnGLSREQRKRLTIAVELVSNP-SIVFMDEPTSGL 1059
Cdd:TIGR00956 855 ESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGE-GLNVEQRKRLTIGVELVAKPkLLLFLDEPTSGL 933
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1060 DARAAAIAMRAVKNVAETGRTVVCTIHQPSIEIFEAFDELMLIKRGGELIYAGPLGQHSCKVIQYFQsIPGVPKIKDNYN 1139
Cdd:TIGR00956 934 DSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGGQTVYFGDLGENSHTIINYFE-KHGAPKCPEDAN 1012
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1140 PSTWMLEVTSTSMEAQLGVDFAQIYTGSSIRKDKDELIKGFSMPPPGTSDLHFPT---RFPQKFLEQFKACLWKQFLSHW 1216
Cdd:TIGR00956 1013 PAEWMLEVIGAAPGAHANQDYHEVWRNSSEYQAVKNELDRLEAELSKAEDDNDPDalsKYAASLWYQFKLVLWRTFQQYW 1092
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1217 RTPSYNLVRIVFMAFSSIIFGVLYWQQGnirhiNDQQGLFTILGCMYGITIFTGINNSQSAMPFVAVERSVMYRERFAGM 1296
Cdd:TIGR00956 1093 RTPDYLYSKFFLTIFAALFIGFTFFKVG-----TSLQGLQNQMFAVFMATVLFNPLIQQYLPPFVAQRDLYEVRERPSRT 1167
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1297 YSPWAYSFAQVAMEIPYVLMLALLFMLIAYPTIGYAWTAAK---------FCWFFYTMFctLLYFVYFGMLIVSITPNLQ 1367
Cdd:TIGR00956 1168 FSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFYWNASKtgqvhergvLFWLLSTMF--FLYFSTLGQMVISFNPNAD 1245
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|..
gi 1002313595 1368 VASIYASSFYMTQHLLSGFVMPPSQIPKWWIWLYYISPMSWTLNLLFTTQFG 1419
Cdd:TIGR00956 1246 NAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLA 1297
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
903-1467 |
3.36e-92 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 311.98 E-value: 3.36e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 903 QLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGV-IEGDIRIGGYPKVQQTFSRISGYCEQNDVHSPQITVGE 981
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 982 SVAYSAWLRLPAEIDTKTRKEFVDEVLEIIELDEIRDALVGTPG-VNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:TIGR00955 119 HLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1061 ARAAAIAMRAVKNVAETGRTVVCTIHQPSIEIFEAFDELMLIKrGGELIYAGPlGQHSCKVIQYFqsipGVPkIKDNYNP 1140
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMA-EGRVAYLGS-PDQAVPFFSDL----GHP-CPENYNP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1141 STWMLEVTST--SMEAQLGVDFAQI---YTGSSIRKDKDELIKGFSMPPPG---TSDLHFPTRFPQKFLEQFKACLWKQF 1212
Cdd:TIGR00955 272 ADFYVQVLAVipGSENESRERIEKIcdsFAVSDIGRDMLVNTNLWSGKAGGlvkDSENMEGIGYNASWWTQFYALLKRSW 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1213 LSHWRTPSYNLVRIVFMAFSSIIFGVLYWQQGnirhiNDQQGLFTILGCMYGITIFTGINNSQSAMPFVAVERSVMYRER 1292
Cdd:TIGR00955 352 LSVLRDPLLLKVRLIQTMMTAILIGLIYLGQG-----LTQKGVQNINGALFLFLTNMTFQNVFPVINVFTAELPVFLRET 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1293 FAGMYSPWAYSFAQVAMEIPYVLMLALLFMLIAYPTIGYAWTAAKFCWFFYTMFCTLLYFVYFGMLIVSITPNLQVASIY 1372
Cdd:TIGR00955 427 RSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTV 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1373 ASSFYMTQHLLSGFVMPPSQIPKWWIWLYYISPMSWTLNLLFTTQFGFEDNSNILVFGETKPIAAF---VRDYFGFHREL 1449
Cdd:TIGR00955 507 GPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVDNIECTSANTTGPCPSSgevILETLSFRNAD 586
|
570
....*....|....*...
gi 1002313595 1450 LPLSAIILAAYPVLFAIL 1467
Cdd:TIGR00955 587 LYLDLIGLVILIFFFRLL 604
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
874-1112 |
2.13e-89 |
|
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: 287.99 E-value: 2.13e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 874 PLTISFQDVNYYVDTPpemrkkgymGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGVIEGDIRIGGY 953
Cdd:cd03232 1 GSVLTWKNLNYTVPVK---------GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 954 PKVqQTFSRISGYCEQNDVHSPQITVGESVAYSAWLRlpaeidtktrkefvdevleiieldeirdalvgtpgvnGLSREQ 1033
Cdd:cd03232 72 PLD-KNFQRSTGYVEQQDVHSPNLTVREALRFSALLR-------------------------------------GLSVEQ 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002313595 1034 RKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSIEIFEAFDELMLIKRGGELIYAG 1112
Cdd:cd03232 114 RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRGGKTVYFG 192
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
226-832 |
1.56e-76 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 266.91 E-value: 1.56e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 226 QILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSLKETGEIEYNGVKLDEFVPAKTSAYVSQYDLHVADMTVRE 305
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 306 TLDFSARFQgvgsraeiMKA-VIKREKEAGItpdpdidaymkaismeglqrsmqtDYIMKIMGLDKCADVKVGNAMR-RG 383
Cdd:TIGR00955 119 HLMFQAHLR--------MPRrVTKKEKRERV------------------------DEVLQALGLRKCANTRIGVPGRvKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 384 ISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHiSEYTILVSLLQPAPETYDLFDDIIIMGEGKV 463
Cdd:TIGR00955 167 LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQ-KGKTIICTIHQPSSELFELFDKIILMAEGRV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 464 VYHGPKNLIMTFFESCGFKCPERKGPADFLQEVLSKKDQQQYWSRSeqwynfiTVDQFCDKFKASQVGQS------LAED 537
Cdd:TIGR00955 246 AYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLAVIPGSENESRE-------RIEKICDSFAVSDIGRDmlvntnLWSG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 538 LSKLYEKSKANKNAlscSIYSLSKWHLLKACFDRELLLMKRNAFLHITKAVQLGLLAIITGTVFFRTHKNFDIVSANyyM 617
Cdd:TIGR00955 319 KAGGLVKDSENMEG---IGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNI--N 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 618 GSLFyaliLLMVNGIPELVMSI-----SRLPVFYKHRDHYLYPGWAYAIPAFILKIPASLVAALSWTSISYYLIGYTPEA 692
Cdd:TIGR00955 394 GALF----LFLTNMTFQNVFPVinvftAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 693 PRYFRQLLVLFLVHTGALSLYRCVGSYCQTIAVGPIAATMSLLVILLFGGFLIPRPSMPNWLKWGFWLSPLSYAEIGLTG 772
Cdd:TIGR00955 470 THFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLI 549
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002313595 773 NEFLAPRWLKITISGVTI-----GRRILidRGLDFSVYFYWISVAALIGFILLYNIGFAIGLTIK 832
Cdd:TIGR00955 550 NQWSDVDNIECTSANTTGpcpssGEVIL--ETLSFRNADLYLDLIGLVILIFFFRLLAYFALRIR 612
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
874-1112 |
3.87e-68 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 227.82 E-value: 3.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 874 PLTISFQDVNYYVdtppemrKKGYMGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGVIEGDIRIGGY 953
Cdd:cd03213 1 GVTLSFRNLTVTV-------KSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 954 PKVQQTFSRISGYCEQNDVHSPQITVGESVAYSAWLRlpaeidtktrkefvdevleiieldeirdalvgtpgvnGLSREQ 1033
Cdd:cd03213 74 PLDKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------------GLSGGE 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002313595 1034 RKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSIEIFEAFDELMLIKRgGELIYAG 1112
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQ-GRVIYFG 194
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
218-467 |
1.96e-66 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 223.29 E-value: 1.96e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 218 FSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSLKETGEIEYNGVKLDEF--VPAKTSAYVSQYD 295
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYKEFaeKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 296 LHVADMTVRETLDFSARFQGvgsraeimkavikrekeagitpdpdidaymkaismeglqrsmqtdyimkimgldkcadvk 375
Cdd:cd03233 93 VHFPTLTVRETLDFALRCKG------------------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 376 vgNAMRRGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILVSLLQPAPETYDLFDDI 455
Cdd:cd03233 113 --NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDKV 190
|
250
....*....|..
gi 1002313595 456 IIMGEGKVVYHG 467
Cdd:cd03233 191 LVLYEGRQIYYG 202
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
1207-1413 |
8.19e-58 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 198.65 E-value: 8.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1207 CLWKQFLSHWRTPSYNLVRIVFMAFSSIIFGVLYWQQGNirhindQQGLFTILGCMYGITIFTGINNSQSAMPFVAVERS 1286
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGN------QQGGLNRPGLLFFSILFNAFSALSGISPVFEKERG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1287 VMYRERFAGMYSPWAYSFAQVAMEIPYVLMLALLFMLIAYPTIGYAWTAAKFCWFFYTMFCTLLYFVYFGMLIVSITPNL 1366
Cdd:pfam01061 75 VLYRELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002313595 1367 QVASIYASSFYMTQHLLSGFVMPPSQIPKWWIWLYYISPMSWTLNLL 1413
Cdd:pfam01061 155 EDASQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEAL 201
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
874-1419 |
6.18e-51 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 192.40 E-value: 6.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 874 PLTISFQDVNYYVDTPpEMRKKGYMGRKL-----------------QLLRNITGAFQPGILSALMGVTGAGKTTLLDVLA 936
Cdd:PLN03211 37 PITLKFMDVCYRVKFE-NMKNKGSNIKRIlghkpkisdetrqiqerTILNGVTGMASPGEILAVLGPSGSGKSTLLNALA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 937 GRKTGGVIEGDIRIGGYPKVQQTFSRIsGYCEQNDVHSPQITVGESVAYSAWLRLPAEIDTKTRKEFVDEVLEIIELDEI 1016
Cdd:PLN03211 116 GRIQGNNFTGTILANNRKPTKQILKRT-GFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKC 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1017 RDALVGTPGVNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSIEIFEAF 1096
Cdd:PLN03211 195 ENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1097 DELMLIKRgGELIYAGPLGQhsckVIQYFQSIPGVPKIKdnYNPSTWMLEVTS---------------------TSMEAQ 1155
Cdd:PLN03211 275 DSVLVLSE-GRCLFFGKGSD----AMAYFESVGFSPSFP--MNPADFLLDLANgvcqtdgvserekpnvkqslvASYNTL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1156 LGVDFAQIYTGSSIRKDKDELIKGFSMPPPGTSDlhfpTRFPQKFLEQFkACLWKQFLSHWRTPSYNLVRIVFMAFSSII 1235
Cdd:PLN03211 348 LAPKVKAAIEMSHFPQANARFVGSASTKEHRSSD----RISISTWFNQF-SILLQRSLKERKHESFNTLRVFQVIAAALL 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1236 FGVLYWQQgNIRHINDQqglftiLGCMYGITIFTGINNSQSAMPFVAVERSVMYRERFAGMYSPWAYSFAQVAMEIPYVL 1315
Cdd:PLN03211 423 AGLMWWHS-DFRDVQDR------LGLLFFISIFWGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMEL 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1316 MLALLFMLIAYptigyaWTAA---KFCWFFYTMFCTLLYFVY---FGMLIVSITPNLQVASIYASSFYMTQHLLSGFVMp 1389
Cdd:PLN03211 496 ILPTIFLTVTY------WMAGlkpELGAFLLTLLVLLGYVLVsqgLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYV- 568
|
570 580 590
....*....|....*....|....*....|
gi 1002313595 1390 pSQIPKWWIWLYYISPMSWTLNLLFTTQFG 1419
Cdd:PLN03211 569 -HKLPSCMAWIKYISTTFYSYRLLINVQYG 597
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
899-1112 |
4.50e-50 |
|
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: 177.08 E-value: 4.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 899 GRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGR-KTGGVIEGDIRIGGYPKVQQTFSRISGYCEQNDVHSPQI 977
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvEGGGTTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 978 TVGESVAYSAWLRLPAEIDTKTRKEFVDEVLeiieLDEIRDALVGTPGVNGLSREQRKRLTIAVELVSNPSIVFMDEPTS 1057
Cdd:cd03234 97 TVRETLTYTAILRLPRKSSDAIRKKRVEDVL----LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002313595 1058 GLDARAAAIAMRAVKNVAETGRTVVCTIHQPSIEIFEAFDELMLIKRgGELIYAG 1112
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSS-GEIVYSG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
222-467 |
1.74e-48 |
|
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: 171.19 E-value: 1.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 222 QSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLnKSLKETGEIEYNGVKLDEFVPAKTSAYVSQYDLHVADM 301
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRR-TGLGVSGEVLINGRPLDKRSFRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 302 TVRETLDFSARFqgvgsraeimkavikrekeagitpdpdidaymkaismeglqrsmqtdyimkimgldkcadvkvgnamr 381
Cdd:cd03213 98 TVRETLMFAAKL-------------------------------------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 382 RGISGGEMKRLTTG-EMIVGPcKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEyTILVSLLQPAPETYDLFDDIIIMGE 460
Cdd:cd03213 110 RGLSGGERKRVSIAlELVSNP-SLLFLDEPTSGLDSSSALQVMSLLRRLADTGR-TIICSIHQPSSEIFELFDKLLLLSQ 187
|
....*..
gi 1002313595 461 GKVVYHG 467
Cdd:cd03213 188 GRVIYFG 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
227-756 |
2.49e-43 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 169.29 E-value: 2.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 227 ILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlKETGEIEYNGVKLDEFVpAKTSAYVSQYDLHVADMTVRET 306
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGN-NFTGTILANNRKPTKQI-LKRTGFVTQDDILYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 307 LDFSARFQgvgsraeIMKAVIKREKeagitpdpdidaymkaismeglqrSMQTDYIMKIMGLDKCADVKVGNAMRRGISG 386
Cdd:PLN03211 161 LVFCSLLR-------LPKSLTKQEK------------------------ILVAESVISELGLTKCENTIIGNSFIRGISG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 387 GEMKRLTTG-EMIVGPcKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEyTILVSLLQPAPETYDLFDDIIIMGEGKVVY 465
Cdd:PLN03211 210 GERKRVSIAhEMLINP-SLLILDEPTSGLDATAAYRLVLTLGSLAQKGK-TIVTSMHQPSSRVYQMFDSVLVLSEGRCLF 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 466 HGPKNLIMTFFESCGFKCPERKGPADFLQEV---------LSKKDQQQYWSRSEQWYNFITVDQFCDKFKASQVGQSLAE 536
Cdd:PLN03211 288 FGKGSDAMAYFESVGFSPSFPMNPADFLLDLangvcqtdgVSEREKPNVKQSLVASYNTLLAPKVKAAIEMSHFPQANAR 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 537 DLSKlyEKSKANKnalSCSIYSLSKWHLLKACFDRELLLMKRNAFLHITKAVQLGLLAIITGTVFFrtHKNFDIVSANyy 616
Cdd:PLN03211 368 FVGS--ASTKEHR---SSDRISISTWFNQFSILLQRSLKERKHESFNTLRVFQVIAAALLAGLMWW--HSDFRDVQDR-- 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 617 MGSLFYALILLmvnGIPELVMSISRLP----VFYKHRDHYLYPGWAYAIPAFILKIPASLVAALSWTSISYYLIGYTPEA 692
Cdd:PLN03211 439 LGLLFFISIFW---GVFPSFNSVFVFPqeraIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPEL 515
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002313595 693 PRYFRQLLVLFLVHTGALSLYRCVGSYCQTIAVGPIAATMSLLVILLFGGFLIPR-PSMPNWLKW 756
Cdd:PLN03211 516 GAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYVHKlPSCMAWIKY 580
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
223-467 |
3.51e-43 |
|
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: 157.43 E-value: 3.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 223 SKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSLKETGEIEYNGVKLDEFVPAKTSAYVSQYDLHVADMT 302
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 303 VRETLDFSARFQGvgsraeimkAVIKREKeagitpdpdidaymkaismeglQRSMQTDyimkIMGLDKCADVKVGNAMRR 382
Cdd:cd03234 98 VRETLTYTAILRL---------PRKSSDA----------------------IRKKRVE----DVLLRDLALTRIGGNLVK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 383 GISGGEMKRLTTG-EMIVGPcKVLLMDEISTGLDSSTTFQIVSCLQQLAHiSEYTILVSLLQPAPETYDLFDDIIIMGEG 461
Cdd:cd03234 143 GISGGERRRVSIAvQLLWDP-KVLILDEPTSGLDSFTALNLVSTLSQLAR-RNRIVILTIHQPRSDLFRLFDRILLLSSG 220
|
....*.
gi 1002313595 462 KVVYHG 467
Cdd:cd03234 221 EIVYSG 226
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
568-773 |
4.11e-41 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 150.50 E-value: 4.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 568 CFDRELLLMKRNAFLHITKAVQLGLLAIITGTVFFRTHknfDIVSANYYMGSLFYALILLMVNGIPELVMS-ISRLPVFY 646
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG---NQQGGLNRPGLLFFSILFNAFSALSGISPVfEKERGVLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 647 KHRDHYLYPGWAYAIPAFILKIPASLVAALSWTSISYYLIGYTPEAPRYFRQLLVLFLVHTGALSLYRCVGSYCQTIAVG 726
Cdd:pfam01061 78 RELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002313595 727 PIAATMSLLVILLFGGFLIPRPSMPNWLKWGFWLSPLSYAEIGLTGN 773
Cdd:pfam01061 158 SQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
892-1112 |
4.62e-35 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 133.16 E-value: 4.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 892 MRKKGYMGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGV-IEGDIRIGGYP--KVQQTFSRISGYCE 968
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsVEGDIHYNGIPykEFAEKYPGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 969 QNDVHSPQITVGESVAYSAWLRlpaeidtktrkefvdevleiieldeirdalvGTPGVNGLSREQRKRLTIAVELVSNPS 1048
Cdd:cd03233 90 EEDVHFPTLTVRETLDFALRCK-------------------------------GNEFVRGISGGERKRVSIAEALVSRAS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002313595 1049 IVFMDEPTSGLDARAAAIAMRAVKNVA-ETGRTVVCTIHQPSIEIFEAFDELMLIkRGGELIYAG 1112
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTMAdVLKTTTFVSLYQASDEIYDLFDKVLVL-YEGRQIYYG 202
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
905-1114 |
3.95e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 128.64 E-value: 3.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGYPKVQQ---TFSRIsGYCEQNDVHSPQITV 979
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGllRPT----SGEVRVLGEDVARDpaeVRRRI-GYVPQEPALYPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 980 GESVAYSAWLRlpaEIDTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGL 1059
Cdd:COG1131 91 RENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVGT-----LSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002313595 1060 DARAAAIAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMLIKRgGELIYAGPL 1114
Cdd:COG1131 163 DPEARRELWELLRELAAEGKTVLLSTHYLE-EAERLCDRVAIIDK-GRIVADGTP 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
901-1118 |
5.60e-30 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 119.96 E-value: 5.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 901 KLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGviEGDIRIGGYPKVQQTF---SRIsGYCEQNDVHSPQI 977
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD--SGSILIDGEDVRKEPRearRQI-GVLPDERGLYDRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 978 TVGESVAYSAWLRlpaEIDTKTRKEFVDEVLEIIELDEIRDALVGtpgvnGLSREQRKRLTIAVELVSNPSIVFMDEPTS 1057
Cdd:COG4555 90 TVRENIRYFAELY---GLFDEELKKRIEELIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002313595 1058 GLDARAAAIAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMLIKRgGELIYAGPLGQHS 1118
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGKTVLFSSHIMQ-EVEALCDRVVILHK-GKVVAQGSLDELR 220
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
222-467 |
2.73e-29 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 116.19 E-value: 2.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 222 QSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSLKeTGEIEYNGVKLDEFVPaKTSAYVSQYDLHVADM 301
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVI-TGEILINGRPLDKNFQ-RSTGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 302 TVRETLDFSARFqgvgsraeimkavikrekeagitpdpdidaymkaismeglqrsmqtdyimkimgldkcadvkvgnamr 381
Cdd:cd03232 95 TVREALRFSALL-------------------------------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 382 RGISGGEMKRLTTG-EMIVGPcKVLLMDEISTGLDSSTTFQIVSCLQQLAHiSEYTILVSLLQPAPETYDLFDDIIIMGE 460
Cdd:cd03232 107 RGLSVEQRKRLTIGvELAAKP-SILFLDEPTSGLDSQAAYNIVRFLKKLAD-SGQAILCTIHQPSASIFEKFDRLLLLKR 184
|
....*...
gi 1002313595 461 -GKVVYHG 467
Cdd:cd03232 185 gGKTVYFG 192
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
900-1112 |
2.20e-28 |
|
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: 114.21 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 900 RKLQLLRNITGAFQPGILsALMGVTGAGKTTLLDVLAGRKTGGviEGDIRIGGYP--KVQQTFSRISGYCEQNDVHSPQI 977
Cdd:cd03264 11 GKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPS--SGTIRIDGQDvlKQPQKLRRRIGYLPQEFGVYPNF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 978 TVGESVAYSAWLRlpaEIDTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTS 1057
Cdd:cd03264 88 TVREFLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIGS-----LSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002313595 1058 GLDARAAAIAMRAVKNVAETgRTVVCTIHQpsIEIFEAFDELMLIKRGGELIYAG 1112
Cdd:cd03264 160 GLDPEERIRFRNLLSELGED-RIVILSTHI--VEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
905-1112 |
2.89e-27 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 111.09 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGYPkVQQTFSRIsGYCEQN---DVHSPqITV 979
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGllKPT----SGSIRVFGKP-LEKERKRI-GYVPQRrsiDRDFP-ISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 980 GESVAYSAWLRL-PAEIDTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSG 1058
Cdd:cd03235 88 RDVVLMGLYGHKgLFRRLSKADKAKVDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002313595 1059 LDARAAAIAMRAVKNVAETGRTVVCTIHQPSIeIFEAFDELMLIKRggELIYAG 1112
Cdd:cd03235 163 VDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLNR--TVVASG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
224-477 |
1.10e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.15 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 224 KVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKL-DEFVPAKTS-AYVSQYDLHVADM 301
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT---SGEVRVLGEDVaRDPAEVRRRiGYVPQEPALYPDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 302 TVRETLDFSARFQGVgSRAEIMKAVikrekeagitpdpdidaymkaismeglqrsmqtDYIMKIMGLDKCADVKVGNamr 381
Cdd:COG1131 89 TVRENLRFFARLYGL-PRKEARERI---------------------------------DELLELFGLTDAADRKVGT--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 382 rgISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHiSEYTILVS--LLqpaPETYDLFDDIIIMG 459
Cdd:COG1131 132 --LSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSthYL---EEAERLCDRVAIID 205
|
250
....*....|....*....
gi 1002313595 460 EGKVVYHG-PKNLIMTFFE 477
Cdd:COG1131 206 KGRIVADGtPDELKARLLE 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
897-1105 |
2.40e-26 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 108.32 E-value: 2.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 897 YMGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKtgGVIEGDIRIGGYPKVQQT---FSRISGYCEQNdvh 973
Cdd:cd03225 9 YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL--GPTSGEVLVDGKDLTKLSlkeLRRKVGLVFQN--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 974 sP--QI---TVGESVAYSawLRL----PAEIDTKtrkefVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELV 1044
Cdd:cd03225 84 -PddQFfgpTVEEEVAFG--LENlglpEEEIEER-----VEEALELVGLEGLRDRSPFT-----LSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002313595 1045 SNPSIVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMLIKRG 1105
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDG 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
905-1113 |
1.24e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 107.48 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTggVIEGDIRIGGYPkVQQTFSRIsGYCEQN---DVHSPqITVGE 981
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP--PTSGTVRLFGKP-PRRARRRI-GYVPQRaevDWDFP-ITVRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 982 SVA-----YSAWLRLPaeidTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPT 1056
Cdd:COG1121 97 VVLmgrygRRGLFRRP----SRADREAVDEALERVGLEDLADRPIGE-----LSGGQQQRVLLARALAQDPDLLLLDEPF 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002313595 1057 SGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMLIKRGgeLIYAGP 1113
Cdd:COG1121 168 AGVDAATEEALYELLRELRREGKTILVVTHDLG-AVREYFDRVLLLNRG--LVAHGP 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
219-472 |
1.53e-25 |
|
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: 106.87 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 219 SHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDE----------FVPAKTS 288
Cdd:COG4555 8 SKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD---SGSILIDGEDVRKeprearrqigVLPDERG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 289 AYvsqydlhvADMTVRETLDFSARFQGVgSRAEIMKAVikrekeagitpdpdidaymkaismeglqrsmqtDYIMKIMGL 368
Cdd:COG4555 85 LY--------DRLTVRENIRYFAELYGL-FDEELKKRI---------------------------------EELIELLGL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 369 DKCADVKVGnamrrGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHiSEYTILVS--LLQpap 446
Cdd:COG4555 123 EEFLDRRVG-----ELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKK-EGKTVLFSshIMQ--- 193
|
250 260
....*....|....*....|....*.
gi 1002313595 447 ETYDLFDDIIIMGEGKVVYHGPKNLI 472
Cdd:COG4555 194 EVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
905-1112 |
3.25e-24 |
|
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: 102.58 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGviegDIRIGGYPKVQQTFS--RISGYCEQNDVHSPQITVG 980
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGelRPTSG----TAYINGYSIRTDRKAarQSLGYCPQFDALFDELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 981 ESVAYSAWLR-LPaeidTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGL 1059
Cdd:cd03263 94 EHLRFYARLKgLP----KSEIKEEVELLLRVLGLTDKANKRART-----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002313595 1060 DARAAAIAMRAVKNVAEtGRTVVCTIHqpSIEifEAfDEL---MLIKRGGELIYAG 1112
Cdd:cd03263 165 DPASRRAIWDLILEVRK-GRSIILTTH--SMD--EA-EALcdrIAIMSDGKLRCIG 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
216-462 |
3.48e-24 |
|
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: 102.16 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 216 LGFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVP---AKTSAYVS 292
Cdd:cd03225 5 LSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPT---SGEVLVDGKDLTKLSLkelRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 293 QY-DLHVADMTVRETLDFSARFQGVgSRAEIMKAVikrekeagitpdpdiDAYMKAISMEGLQ-RSMQTdyimkimgldk 370
Cdd:cd03225 82 QNpDDQFFGPTVEEEVAFGLENLGL-PEEEIEERV---------------EEALELVGLEGLRdRSPFT----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 371 cadvkvgnamrrgISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLaHISEYTILVSllqpapeTYD 450
Cdd:cd03225 135 -------------LSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIV-------THD 193
|
250
....*....|....*...
gi 1002313595 451 L------FDDIIIMGEGK 462
Cdd:cd03225 194 LdlllelADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
877-1113 |
4.07e-23 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 99.71 E-value: 4.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 877 ISFQDVNYYvdtppemrkkgYMGRKlQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGYP 954
Cdd:COG1122 1 IELENLSFS-----------YPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGllKPT----SGEVLVDGKD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 955 KVQQTFSRIS---GYCEQNdvhsP--QI---TVGESVAYSawLR---LP-AEIDTKtrkefVDEVLEIIELDEIRDALVG 1022
Cdd:COG1122 65 ITKKNLRELRrkvGLVFQN----PddQLfapTVEEDVAFG--PEnlgLPrEEIRER-----VEEALELVGLEHLADRPPH 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1023 TpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMLI 1102
Cdd:COG1122 134 E-----LSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLD-LVAELADRVIVL 207
|
250
....*....|.
gi 1002313595 1103 KRgGELIYAGP 1113
Cdd:COG1122 208 DD-GRIVADGT 217
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
905-1057 |
4.40e-23 |
|
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: 96.95 E-value: 4.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGgvIEGDIRIGGYPKVQQT---FSRISGYCEQNDVHSPQITVGE 981
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP--TEGTILLDGQDLTDDErksLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002313595 982 SVAYSAWLRlpaEIDTKTRKEFVDEVLEIIELDEIRDALVGTPGvNGLSREQRKRLTIAVELVSNPSIVFMDEPTS 1057
Cdd:pfam00005 79 NLRLGLLLK---GLSKREKDARAEEALEKLGLGDLADRPVGERP-GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
896-1113 |
2.75e-22 |
|
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: 97.81 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 896 GYMGRklQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIE-GDIRIGGYPkvQQTFSRISGYCEQNDV 972
Cdd:COG1120 10 GYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGllKPSSGEVLlDGRDLASLS--RRELARRIAYVPQEPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 973 HSPQITVGESVA-----YSAWLRLPAEIDtktrKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNP 1047
Cdd:COG1120 86 APFGLTVRELVAlgrypHLGLFGRPSAED----REAVEEALERTGLEHLADRPVDE-----LSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1048 SIVFMDEPTSGLDARAAAIAMRAVKN-VAETGRTVVCTIHQPSIeifeAF---DELMLIKrGGELIYAGP 1113
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRlARERGRTVVMVLHDLNL----AAryaDRLVLLK-DGRIVAQGP 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
895-1105 |
5.79e-21 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 91.15 E-value: 5.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 895 KGYMGRKLqlLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTggVIEGDIRIGGypkvqqtfsrisgyceQNDVHS 974
Cdd:cd00267 7 FRYGGRTA--LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK--PTSGEILIDG----------------KDIAKL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 975 PQITVGESVAYsawlrlpaeidtktrkefvdevleiieldeirdalvgtpgVNGLSREQRKRLTIAVELVSNPSIVFMDE 1054
Cdd:cd00267 67 PLEELRRRIGY----------------------------------------VPQLSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002313595 1055 PTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMLIKRG 1105
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPE-LAELAADRVIVLKDG 156
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
220-467 |
7.09e-21 |
|
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: 92.95 E-value: 7.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 220 HHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNG--VKLDEFVPAKTSAYVSQYDLH 297
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPT---SGTAYINGysIRTDRKAARQSLGYCPQFDAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 298 VADMTVRETLDFSARFQGVgSRAEIMKAVikrekeagitpdpdidaymkaismeglqrsmqtDYIMKIMGLDKCADVKVG 377
Cdd:cd03263 87 FDELTVREHLRFYARLKGL-PKSEIKEEV---------------------------------ELLLRVLGLTDKANKRAR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 378 NamrrgISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLahISEYTILVSllqpapeTYD------L 451
Cdd:cd03263 133 T-----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILT-------THSmdeaeaL 198
|
250
....*....|....*.
gi 1002313595 452 FDDIIIMGEGKVVYHG 467
Cdd:cd03263 199 CDRIAIMSDGKLRCIG 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
904-1088 |
1.00e-20 |
|
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: 91.77 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 904 LLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGYPKVQQ--TFSRISGYCEQNDVHSPQITV 979
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGllPPS----AGEVLWNGEPIRDAreDYRRRLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 980 GESVAYsaWLRLPAEIDTKTRkefVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGL 1059
Cdd:COG4133 93 RENLRF--WAALYGLRADREA---IDEALEAVGLAGLADLPVRQ-----LSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180
....*....|....*....|....*....
gi 1002313595 1060 DARAAAIAMRAVKNVAETGRTVVCTIHQP 1088
Cdd:COG4133 163 DAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
228-409 |
1.17e-20 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 90.01 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 228 LENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNkslKETGEIEYNGVKLDEFVPAKTS---AYVSQYDLHVADMTVR 304
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS---PTEGTILLDGQDLTDDERKSLRkeiGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 305 ETLDFSARFQGVGSRAeimkavikrekeagitpdpdidaymkaismeglqRSMQTDYIMKIMGLDKCADVKVGNAMrRGI 384
Cdd:pfam00005 78 ENLRLGLLLKGLSKRE----------------------------------KDARAEEALEKLGLGDLADRPVGERP-GTL 122
|
170 180
....*....|....*....|....*
gi 1002313595 385 SGGEMKRLTTGEMIVGPCKVLLMDE 409
Cdd:pfam00005 123 SGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
899-1105 |
1.51e-20 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 91.55 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 899 GRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGYPKVQQTFSRISGYCEQNDVHspQ 976
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGliKES----SGSILLNGKPIKAKERRKSIGYVMQDVDY--Q 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 977 ITvGESVAysAWLRLPAEiDTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPT 1056
Cdd:cd03226 84 LF-TDSVR--EELLLGLK-ELDAGNEQAETVLKDLDLYALKERHPLS-----LSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1002313595 1057 SGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSIeIFEAFDELMLIKRG 1105
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQGKAVIVITHDYEF-LAKVCDRVLLLANG 202
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
216-467 |
5.07e-20 |
|
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: 90.29 E-value: 5.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 216 LGFSHHQskvqILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVpaKTSAYVSQYd 295
Cdd:cd03235 7 VSYGGHP----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPT---SGSIRVFGKPLEKER--KRIGYVPQR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 296 lHVAD----MTVRETldfsarfqgVGSRAEIMKAVIKREKEAGitpdpdidaymKAISMEGLQRsmqtdyimkiMGLDKC 371
Cdd:cd03235 77 -RSIDrdfpISVRDV---------VLMGLYGHKGLFRRLSKAD-----------KAKVDEALER----------VGLSEL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 372 ADVKVGNAmrrgiSGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLaHISEYTILVSL--LQPAPety 449
Cdd:cd03235 126 ADRQIGEL-----SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVThdLGLVL--- 196
|
250
....*....|....*...
gi 1002313595 450 DLFDDIIIMGeGKVVYHG 467
Cdd:cd03235 197 EYFDRVLLLN-RTVVASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
211-474 |
5.20e-20 |
|
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: 91.26 E-value: 5.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 211 LLAAK-LGFSHHqsKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVP---AK 286
Cdd:COG1120 1 MLEAEnLSVGYG--GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS---SGEVLLDGRDLASLSRrelAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 287 TSAYVSQYDLHVADMTVRET-----LDFSARFQGVGsraeimkaviKREKEAgitpdpdIDAYMKAISMEGL-QRSMQTd 360
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRELvalgrYPHLGLFGRPS----------AEDREA-------VEEALERTGLEHLaDRPVDE- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 361 yimkimgldkcadvkvgnamrrgISGGEMKRLttgeMI-----VGPcKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEY 435
Cdd:COG1120 138 -----------------------LSGGERQRV----LIaralaQEP-PLLLLDEPTSHLDLAHQLEVLELLRRLARERGR 189
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1002313595 436 TILVSLlqpapetYDL------FDDIIIMGEGKVVYHGPKNLIMT 474
Cdd:COG1120 190 TVVMVL-------HDLnlaaryADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
227-415 |
5.40e-20 |
|
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: 89.85 E-value: 5.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 227 ILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVPA--KTSAYVSQYDLHVADMTVR 304
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPS---AGEVLWNGEPIRDAREDyrRRLAYLGHADGLKPELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 305 ETLDFSARFQGV-GSRAEIMKAvikrekeagitpdpdidaymkaismeglqrsmqtdyiMKIMGLDKCADVKVGNamrrg 383
Cdd:COG4133 94 ENLRFWAALYGLrADREAIDEA-------------------------------------LEAVGLAGLADLPVRQ----- 131
|
170 180 190
....*....|....*....|....*....|..
gi 1002313595 384 ISGGEMKRLTTGEMIVGPCKVLLMDEISTGLD 415
Cdd:COG4133 132 LSAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
903-1105 |
1.36e-19 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 88.73 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 903 QLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIE-GDIRIGGYPKVQqtfsRISGYCEQNDVHSPQITV 979
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGleRPDSGEILiDGRDVTGVPPER----RNIGMVFQDYALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 980 GESVAYSawLRLpAEIDTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGL 1059
Cdd:cd03259 90 AENIAFG--LKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHE-----LSGGQQQRVALARALAREPSLLLLDEPLSAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002313595 1060 DARAAAIAMRAVKNV-AETGRTVVCTIHQPSiEIFEAFDELMLIKRG 1105
Cdd:cd03259 162 DAKLREELREELKELqRELGITTIYVTHDQE-EALALADRIAVMNEG 207
|
|
| PDR_assoc |
pfam08370 |
Plant PDR ABC transporter associated; This domain is found on the C-terminus of ABC-2 type ... |
780-842 |
2.35e-19 |
|
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: 83.31 E-value: 2.35e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002313595 780 WLKIT--ISGVTIGRRILIDRGLDFSVYFYWISVAALIGFILLYNIGFAIGLTIKQSPGASQAII 842
Cdd:pfam08370 1 WMKPTasNGNTTLGVAVLKSRGLFTEAYWYWIGVGALLGFTILFNILFTLALTYLNPLGKSQAII 65
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
877-1060 |
3.19e-18 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 85.31 E-value: 3.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 877 ISFQDVNYYVDtppemrkkgymgrKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGV-IEGDIRIGGY 953
Cdd:cd03260 1 IELRDLNVYYG-------------DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlnDLIPGApDEGEVLLDGK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 954 PKVQQTFSRIS-----GYCEQndvhSP---QITVGESVAYSAWLRLpaEIDTKTRKEFVDEVLEIIEL-DEIRDALVGTp 1024
Cdd:cd03260 68 DIYDLDVDVLElrrrvGMVFQ----KPnpfPGSIYDNVAYGLRLHG--IKLKEELDERVEEALRKAALwDEVKDRLHAL- 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 1002313595 1025 gvnGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:cd03260 141 ---GLSGGQQQRLCLARALANEPEVLLLDEPTSALD 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
905-1112 |
5.50e-18 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 84.34 E-value: 5.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGviegDIRIGGYPKVQQT--FSRISGYCEQNDVHSPQITVG 980
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTllKPTSG----RATVAGHDVVREPreVRRRIGIVFQDLSVDDELTGW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 981 ESVAYSAWLR-LPAEIdtktRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGL 1059
Cdd:cd03265 92 ENLYIHARLYgVPGAE----RRERIDELLDFVGLLEAADRLVKT-----YSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002313595 1060 DARAAAIAMRAVKN-VAETGRTVVCTIHQpsIEIFEAF-DELMLIKRgGELIYAG 1112
Cdd:cd03265 163 DPQTRAHVWEYIEKlKEEFGMTILLTTHY--MEEAEQLcDRVAIIDH-GRIIAEG 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
899-1105 |
5.64e-18 |
|
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: 84.46 E-value: 5.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 899 GRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTggVIEGDIRIGGypkvqQTFSRIS------------GY 966
Cdd:cd03255 14 GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR--PTSGEVRVDG-----TDISKLSekelaafrrrhiGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 967 CEQNdvHS--PQITVGESVAysawlrLPAEIDT---KTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAV 1041
Cdd:cd03255 87 VFQS--FNllPDLTALENVE------LPLLLAGvpkKERRERAEELLERVGLGDRLNHYPSE-----LSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002313595 1042 ELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVA-ETGRTVVCTIHQPSIEifEAFDELMLIKRG 1105
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPELA--EYADRIIELRDG 216
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
216-468 |
7.63e-18 |
|
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: 84.31 E-value: 7.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 216 LGFSHHQSKvQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrLNKSlkETGEIEYNGVKLDEFVP---AKTSAYVS 292
Cdd:COG1122 6 LSFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNG-LLKP--TSGEVLVDGKDITKKNLrelRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 293 QY-DLHVADMTVRETLDFSARFQGVgSRAEIMKAVikrekeagitpdpdidaymkaismeglqrsmqtDYIMKIMGLDKC 371
Cdd:COG1122 82 QNpDDQLFAPTVEEDVAFGPENLGL-PREEIRERV---------------------------------EEALELVGLEHL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 372 ADVKVGNamrrgISGGEMKRLT-TGEMIVGPcKVLLMDEISTGLDSSTTFQIVSCLQQLaHISEYTILVS-----LLqpa 445
Cdd:COG1122 128 ADRPPHE-----LSGGQKQRVAiAGVLAMEP-EVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVthdldLV--- 197
|
250 260
....*....|....*....|...
gi 1002313595 446 petYDLFDDIIIMGEGKVVYHGP 468
Cdd:COG1122 198 ---AELADRVIVLDDGRIVADGT 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
900-1112 |
1.42e-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: 83.19 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 900 RKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIEgdirIGGYPKVQQTF---SRIsGYCEQNDVHS 974
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGllEPDAGFAT----VDGFDVVKEPAearRRL-GFVSDSTGLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 975 PQITVGESVAYSAWLRLPAEIDTKTRKEFVDEVLEIIELDEIRdalvgtpgVNGLSREQRKRLTIAVELVSNPSIVFMDE 1054
Cdd:cd03266 91 DRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRR--------VGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002313595 1055 PTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMLIKRgGELIYAG 1112
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLRALGKCILFSTHIMQ-EVERLCDRVVVLHR-GRVVYEG 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
896-1112 |
3.36e-17 |
|
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: 80.94 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 896 GYMGRklQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG-RKtggVIEGDIRIGGYPkvqqtfsrisgyceqndvhs 974
Cdd:cd03214 8 GYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGlLK---PSSGEILLDGKD-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 975 pqitvgesvaysawlrlpaeIDTKTRKE------FVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPS 1048
Cdd:cd03214 63 --------------------LASLSPKElarkiaYVPQALELLGLAHLADRPFNE-----LSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002313595 1049 IVFMDEPTSGLDARAAAIAMRAVKNVA-ETGRTVVCTIHQPSIeIFEAFDELMLIKrGGELIYAG 1112
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNL-AARYADRVILLK-DGRIVAQG 180
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
217-472 |
4.49e-17 |
|
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: 81.84 E-value: 4.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 217 GFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAgRLNKSLKE---TGEIEYNGV---KLDEFVPA--KTS 288
Cdd:cd03260 5 DLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLN-RLNDLIPGapdEGEVLLDGKdiyDLDVDVLElrRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 289 AYVSQYdLHVADMTVRETLDFSARFQGVGSRAEimkavikrekeagitpdpdidayMKAISMEGLQRsmqtdyimkiMGL 368
Cdd:cd03260 84 GMVFQK-PNPFPGSIYDNVAYGLRLHGIKLKEE-----------------------LDERVEEALRK----------AAL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 369 DkcADVKvGNAMRRGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHisEYTILV---SLLQPA 445
Cdd:cd03260 130 W--DEVK-DRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIvthNMQQAA 204
|
250 260
....*....|....*....|....*..
gi 1002313595 446 petyDLFDDIIIMGEGKVVYHGPKNLI 472
Cdd:cd03260 205 ----RVADRTAFLLNGRLVEFGPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
216-468 |
9.77e-17 |
|
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: 85.34 E-value: 9.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 216 LGFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSLKETGEIEYNG---VKLDEFVPAKTSAYVS 292
Cdd:COG1123 10 LSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGrdlLELSEALRGRRIGMVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 293 QYDLHVADM-TVRETLDFSARFQGVgSRAEIMKAVIKREKEAGitpdpdIDAYMKAISMEglqrsmqtdyimkimgldkc 371
Cdd:COG1123 90 QDPMTQLNPvTVGDQIAEALENLGL-SRAEARARVLELLEAVG------LERRLDRYPHQ-------------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 372 advkvgnamrrgISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILVSLLQPApETYDL 451
Cdd:COG1123 143 ------------LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLG-VVAEI 209
|
250
....*....|....*..
gi 1002313595 452 FDDIIIMGEGKVVYHGP 468
Cdd:COG1123 210 ADRVVVMDDGRIVEDGP 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
905-1105 |
1.04e-16 |
|
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: 79.36 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGYPKVQQT--FSRISGYCEQNDVHSPQITVg 980
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGllKPD----SGEIKVLGKDIKKEPeeVKRRIGYLPEEPSLYENLTV- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 981 esvaysawlrlpaeidtktrKEFVDevleiieldeirdalvgtpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:cd03230 91 --------------------RENLK-----------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1002313595 1061 ARAAAIAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMLIKRG 1105
Cdd:cd03230 128 PESRREFWELLRELKKEGKTILLSSHILE-EAERLCDRVAILNNG 171
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
905-1086 |
1.15e-16 |
|
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: 79.77 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIEGDIRIGGYPKVQQTFSRIS-GYCEQN---DVHSPqiT 978
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGllRPQSGAVLIDGEPLDYSRKGLLERRQRvGLVFQDpddQLFAA--D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 979 VGESVAYSAwLRLPAEIDTKTRKefVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSG 1058
Cdd:TIGR01166 86 VDQDVAFGP-LNLGLSEAEVERR--VREALTAVGASGLRERPTHC-----LSGGEKKRVAIAGAVAMRPDVLLLDEPTAG 157
|
170 180
....*....|....*....|....*...
gi 1002313595 1059 LDARAAAIAMRAVKNVAETGRTVVCTIH 1086
Cdd:TIGR01166 158 LDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
218-467 |
2.40e-16 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 79.86 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 218 FSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrLNKslKETGEIEYNGVKLDEFVPA------KTSAYV 291
Cdd:cd03257 11 FPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILG-LLK--PTSGSIIFDGKDLLKLSRRlrkirrKEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 292 SQYDLHVAD--MTVRETLDFSARFQGVGSRAEIMKAVIkREKEAGITPDPDidaymkaismeglqrsmqtdyimkimgld 369
Cdd:cd03257 88 FQDPMSSLNprMTIGEQIAEPLRIHGKLSKKEARKEAV-LLLLVGVGLPEE----------------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 370 kcadvkVGNAMRRGISGGEMKRLttgeMI-----VGPcKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTIL-----V 439
Cdd:cd03257 138 ------VLNRYPHELSGGQRQRV----AIaralaLNP-KLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLfithdL 206
|
250 260
....*....|....*....|....*...
gi 1002313595 440 SLLQpapetyDLFDDIIIMGEGKVVYHG 467
Cdd:cd03257 207 GVVA------KIADRVAVMYAGKIVEEG 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
905-1082 |
3.25e-16 |
|
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: 79.79 E-value: 3.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVI--EGDiRIGGYPKVQ-------QTFSRISGYceqndvh 973
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGflRPTSGSVlfDGE-DITGLPPHEiarlgigRTFQIPRLF------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 974 sPQITVGESVA--------YSAWLRLPAEIDTKTRKEfVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVS 1045
Cdd:cd03219 88 -PELTVLENVMvaaqartgSGLLLARARREEREARER-AEELLERVGLADLADRPAGE-----LSYGQQRRLEIARALAT 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1002313595 1046 NPSIVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVV 1082
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVL 197
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
894-1112 |
3.85e-16 |
|
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: 78.80 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 894 KKGYMGRklQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIEgdIRIGGYPKVQQTFSRISGYCEQND 971
Cdd:cd03268 7 TKTYGKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGliKPDSGEIT--FDGKSYQKNIEALRRIGALIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 972 VHsPQITVGESVAYSAWLRLpaeidtkTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVF 1051
Cdd:cd03268 83 FY-PNLTARENLRLLARLLG-------IRKKRIDEVLDVVGLKDSAKKKVKG-----FSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002313595 1052 MDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMLIkRGGELIYAG 1112
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLS-EIQKVADRIGII-NKGKLIEEG 208
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
187-464 |
5.19e-16 |
|
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: 83.27 E-value: 5.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 187 EAECQVVSGKPLPtlwnaALSRFSLLAAKLGFSHHQSKvQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSl 266
Cdd:COG4988 318 PEPAAPAGTAPLP-----AAGPPSIELEDVSFSYPGGR-PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 267 keTGEIEYNGVKLDEFVPA---KTSAYVSQyDLHVADMTVRETLDFSARfqgVGSRAEIMKAVikreKEAGItpdpdida 343
Cdd:COG4988 391 --SGSILINGVDLSDLDPAswrRQIAWVPQ-NPYLFAGTIRENLRLGRP---DASDEELEAAL----EAAGL-------- 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 344 ymkaismeglqrsmqTDYIMKI-MGLdkcaDVKVG-NAmrRGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQ 421
Cdd:COG4988 453 ---------------DEFVAALpDGL----DTPLGeGG--RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAE 511
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1002313595 422 IVSCLQQLAHisEYTILVSLLQPApeTYDLFDDIIIMGEGKVV 464
Cdd:COG4988 512 ILQALRRLAK--GRTVILITHRLA--LLAQADRILVLDDGRIV 550
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
914-1112 |
6.87e-16 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 78.11 E-value: 6.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 914 PGILSALMGVTGAGKTTLLDVLAG--RKTGGVIE------GDIRIGGYPKVQQtfsRISGYCEQNDVHSPQITVGESVAY 985
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGleKPDGGTIVlngtvlFDSRKKINLPPQQ---RKIGLVFQQYALFPHLNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 986 SAWLRLPAEidtktRKEFVDEVLEIIELDEIRDAlvgtpGVNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAA 1065
Cdd:cd03297 99 GLKRKRNRE-----DRISVDELLDLLGLDHLLNR-----YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1002313595 1066 IAMRAVKNV-AETGRTVVCTIHQPSiEIFEAFDELMLIkRGGELIYAG 1112
Cdd:cd03297 169 QLLPELKQIkKNLNIPVIFVTHDLS-EAEYLADRIVVM-EDGRLQYIG 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
903-1105 |
7.07e-16 |
|
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: 77.23 E-value: 7.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 903 QLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIE-GDIRIGGYPKVQQTFSRISGYCEQNDVHSPQITV 979
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGleEPDSGSILiDGEDLTDLEDELPPLRRRIGMVFQDFALFPHLTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 980 GESVAYsawlrlpaeidtktrkefvdevleiieldeirdalvgtpgvnGLSREQRKRLTIAVELVSNPSIVFMDEPTSGL 1059
Cdd:cd03229 94 LENIAL------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002313595 1060 DARAAAIAMRAVKNV-AETGRTVVCTIHQPSiEIFEAFDELMLIKRG 1105
Cdd:cd03229 132 DPITRREVRALLKSLqAQLGITVVLVTHDLD-EAARLADRVVVLRDG 177
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
217-467 |
7.60e-16 |
|
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: 77.94 E-value: 7.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 217 GFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVPAKTS-AYVSQ-Y 294
Cdd:cd03259 5 GLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD---SGEILIDGRDVTGVPPERRNiGMVFQdY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 295 DL--HvadMTVRETLDFSARFQGVgSRAEImkavIKREKEagitpdpdidaymkaismeglqrsmqtdyIMKIMGLDKCA 372
Cdd:cd03259 82 ALfpH---LTVAENIAFGLKLRGV-PKAEI----RARVRE-----------------------------LLELVGLEGLL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 373 DVKVgnamrRGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYT-ILVSLLQpaPETYDL 451
Cdd:cd03259 125 NRYP-----HELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITtIYVTHDQ--EEALAL 197
|
250
....*....|....*.
gi 1002313595 452 FDDIIIMGEGKVVYHG 467
Cdd:cd03259 198 ADRIAVMNEGRIVQVG 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
216-462 |
1.32e-15 |
|
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: 76.27 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 216 LGFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNkslKETGEIEYNGVKLDEFVPA---KTSAYVS 292
Cdd:cd03228 6 VSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD---PTSGEILIDGVDLRDLDLEslrKNIAYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 293 QyDLHVADMTVRETLdfsarfqgvgsraeimkavikrekeagitpdpdidaymkaismeglqrsmqtdyimkimgldkca 372
Cdd:cd03228 83 Q-DPFLFSGTIRENI----------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 373 dvkvgnamrrgISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHisEYT-ILVSllqPAPETYDL 451
Cdd:cd03228 97 -----------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTvIVIA---HRLSTIRD 160
|
250
....*....|.
gi 1002313595 452 FDDIIIMGEGK 462
Cdd:cd03228 161 ADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
216-469 |
1.37e-15 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 82.19 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 216 LGFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrLNKSlkETGEIEYNGVKLDEFVPA---KTSAYVS 292
Cdd:COG2274 479 VSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG-LYEP--TSGRILIDGIDLRQIDPAslrRQIGVVL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 293 QyDLHVADMTVRETLDFSArfqgvgsraeimkavikrekeagitPDPDIDAYMKAISMEGLqrsmqTDYIMKI-MGLDKc 371
Cdd:COG2274 556 Q-DVFLFSGTIRENITLGD-------------------------PDATDEEIIEAARLAGL-----HDFIEALpMGYDT- 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 372 advKVGNaMRRGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHisEYTILVSllqpA--PETY 449
Cdd:COG2274 604 ---VVGE-GGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIII----AhrLSTI 673
|
250 260
....*....|....*....|
gi 1002313595 450 DLFDDIIIMGEGKVVYHGPK 469
Cdd:COG2274 674 RLADRIIVLDKGRIVEDGTH 693
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
218-467 |
1.48e-15 |
|
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: 77.41 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 218 FSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDE----------FVPAKT 287
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD---AGFATVDGFDVVKepaearrrlgFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 288 SAYvsqydlhvADMTVRETLDFSARFQGVgSRAEIMKAVikrekeagitpdpdidaymkaismeglqrsmqtDYIMKIMG 367
Cdd:cd03266 88 GLY--------DRLTARENLEYFAGLYGL-KGDELTARL---------------------------------EELADRLG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 368 LDKCADVKVGnamrrGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLD---SSTTFQIVSCLQQLAHiseyTILVS--LL 442
Cdd:cd03266 126 MEELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDvmaTRALREFIRQLRALGK----CILFSthIM 196
|
250 260
....*....|....*....|....*
gi 1002313595 443 QpapETYDLFDDIIIMGEGKVVYHG 467
Cdd:cd03266 197 Q---EVERLCDRVVVLHRGRVVYEG 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
894-1060 |
2.48e-15 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 80.72 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 894 KKGYMGRK---LQLLRNITGAFQPG-ILsALMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGYP------KVQQTFS 961
Cdd:COG1123 267 SKRYPVRGkggVRAVDDVSLTLRRGeTL-GLVGESGSGKSTLARLLLGllRPT----SGSILFDGKDltklsrRSLRELR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 962 RISGYCEQNDVHS--PQITVGESVAYsaWLRLPAEIDTKTRKEFVDEVLEIIELD-EIRDALVGTpgvngLSREQRKRLT 1038
Cdd:COG1123 342 RRVQMVFQDPYSSlnPRMTVGDIIAE--PLRLHGLLSRAERRERVAELLERVGLPpDLADRYPHE-----LSGGQRQRVA 414
|
170 180
....*....|....*....|..
gi 1002313595 1039 IAVELVSNPSIVFMDEPTSGLD 1060
Cdd:COG1123 415 IARALALEPKLLILDEPTSALD 436
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
211-468 |
3.23e-15 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 80.33 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 211 LLAAK-LGFSHHQSK---VQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVPAK 286
Cdd:COG1123 260 LLEVRnLSKRYPVRGkggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT---SGSILFDGKDLTKLSRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 287 TSA------YVSQ--YDLHVADMTVRETLDFSARFQGVGSRAEIMKAVikrekeagitpdpdidaymkaismeglqrsmq 358
Cdd:COG1123 337 LRElrrrvqMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERV-------------------------------- 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 359 tDYIMKIMGLDKcadvkvgNAMRR---GISGGEMKRLTTGEMIV-GPcKVLLMDEISTGLDSSTTFQIVSCLQQLAHISE 434
Cdd:COG1123 385 -AELLERVGLPP-------DLADRyphELSGGQRQRVAIARALAlEP-KLLILDEPTSALDVSVQAQILNLLRDLQRELG 455
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1002313595 435 YTILVSllqpapeTYDL------FDDIIIMGEGKVVYHGP 468
Cdd:COG1123 456 LTYLFI-------SHDLavvryiADRVAVMYDGRIVEDGP 488
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
216-467 |
4.21e-15 |
|
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: 74.78 E-value: 4.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 216 LGFSHHQSkvQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrLNKSLKetGEIEYNGVKLDEFVP---AKTSAYVS 292
Cdd:cd03214 5 LSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAG-LLKPSS--GEILLDGKDLASLSPkelARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 293 QydlhvadmtvretldfsarfqgvgsraeimkavikrekeagitpdpdidaymkaismeglqrsmqtdyIMKIMGLDKCA 372
Cdd:cd03214 80 Q--------------------------------------------------------------------ALELLGLAHLA 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 373 DvkvgnamrRGI---SGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILVSLlqpapetY 449
Cdd:cd03214 92 D--------RPFnelSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVL-------H 156
|
250 260
....*....|....*....|....
gi 1002313595 450 DL------FDDIIIMGEGKVVYHG 467
Cdd:cd03214 157 DLnlaaryADRVILLKDGRIVAQG 180
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
895-1113 |
5.36e-15 |
|
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: 76.07 E-value: 5.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 895 KGYMGRKlQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVI---EGDIRIGGYPKVQQTFSRIsGYCEQ 969
Cdd:cd03256 8 KTYPNGK-KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGlvEPTSGSVlidGTDINKLKGKALRQLRRQI-GMIFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 970 NDVHSPQITVGESV---------AYSAWLRLPAEIDTKTRKEFVDEVlEIIELDEIRdalvgtpgVNGLSREQRKRLTIA 1040
Cdd:cd03256 86 QFNLIERLSVLENVlsgrlgrrsTWRSLFGLFPKEEKQRALAALERV-GLLDKAYQR--------ADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002313595 1041 VELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAET-GRTVVCTIHQPsiEIFEAFDELMLIKRGGELIYAGP 1113
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQV--DLAREYADRIVGLKDGRIVFDGP 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
874-1090 |
5.94e-15 |
|
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: 79.64 E-value: 5.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 874 PLTISFQDVNY-YVDTPPemrkkgymgrklqLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGrkTGGVIEGDIRIGG 952
Cdd:TIGR02857 319 ASSLEFSGVSVaYPGRRP-------------ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG--FVDPTEGSIAVNG 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 953 YP----KVQQTFSRIsGYCEQNdvhsPQITVGeSVAYSAWLRLPAEIDTKtrkefVDEVLEIIELDEIRDAL-------V 1021
Cdd:TIGR02857 384 VPladaDADSWRDQI-AWVPQH----PFLFAG-TIAENIRLARPDASDAE-----IREALERAGLDEFVAALpqgldtpI 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002313595 1022 GTPGvNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAEtGRTVVCTIHQPSI 1090
Cdd:TIGR02857 453 GEGG-AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLAL 519
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
915-1112 |
6.98e-15 |
|
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: 77.05 E-value: 6.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 915 GILSALMGVTGAGKTTLLDVLAG--RKTGGviegDIRIGGYPKVQQ--TFSRISGYCEQndvhspQITVGEsvAYSAW-- 988
Cdd:TIGR01188 19 GEVFGFLGPNGAGKTTTIRMLTTllRPTSG----TARVAGYDVVREprKVRRSIGIVPQ------YASVDE--DLTGRen 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 989 LRLPAE---IDTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAA 1065
Cdd:TIGR01188 87 LEMMGRlygLPKDEAEERAEELLELFELGEAADRPVGT-----YSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRR 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002313595 1066 IAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMLIKRgGELIYAG 1112
Cdd:TIGR01188 162 AIWDYIRALKEEGVTILLTTHYME-EADKLCDRIAIIDH-GRIIAEG 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
877-1116 |
9.27e-15 |
|
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: 75.23 E-value: 9.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 877 ISFQDVnyyvdtppemrKKGYMGRklQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVI--EGDIRIGG 952
Cdd:cd03261 1 IELRGL-----------TKSFGGR--TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGllRPDSGEVliDGEDISGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 953 YPKVQQTFSRISGYCEQNDVHSPQITVGESVAYsaWLRLPAEIDTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSRE 1032
Cdd:cd03261 68 SEAELYRLRRRMGMLFQSGALFDSLTVFENVAF--PLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE-----LSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1033 QRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAET-GRTVVCTIHQPSiEIFEAFDELMLIKRgGELIYA 1111
Cdd:cd03261 141 MKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLD-TAFAIADRIAVLYD-GKIVAE 218
|
....*
gi 1002313595 1112 GPLGQ 1116
Cdd:cd03261 219 GTPEE 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
900-1112 |
9.37e-15 |
|
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: 75.45 E-value: 9.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 900 RKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGY-PKVQQT--FSRISGYCEQNDVHS 974
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGllQPT----SGEVRVAGLvPWKRRKkfLRRIGVVFGQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 975 PQITVGESvaysawLRLPAEI---DTKTRKEFVDEVLEIIELDEIRDalvgTPgVNGLSREQRKRLTIAVELVSNPSIVF 1051
Cdd:cd03267 108 WDLPVIDS------FYLLAAIydlPPARFKKRLDELSELLDLEELLD----TP-VRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002313595 1052 MDEPTSGLDARAAAIAMRAVKN-VAETGRTVVCTIHQPSiEIFEAFDELMLIKRgGELIYAG 1112
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEyNRERGTTVLLTSHYMK-DIEALARRVLVIDK-GRLLYDG 236
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
919-1112 |
1.22e-14 |
|
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: 75.06 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 919 ALMGVTGAGKTTLLDVLAG---RKTGGVIEGDIRIGGYPKVQQTFSrisgYCEQNDVHSPQITVGESVAYSAWLRLpaeI 995
Cdd:cd03299 29 VILGPTGSGKSVLLETIAGfikPDSGKILLNGKDITNLPPEKRDIS----YVPQNYALFPHMTVYKNIAYGLKKRK---V 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 996 DTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVA 1075
Cdd:cd03299 102 DKKEIERKVLEIAEMLGIDHLLNRKPET-----LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIR 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 1002313595 1076 ETGRTVVCTIHQPSIEIFEAFDElMLIKRGGELIYAG 1112
Cdd:cd03299 177 KEFGVTVLHVTHDFEEAWALADK-VAIMLNGKLIQVG 212
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
919-1114 |
1.26e-14 |
|
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: 75.51 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 919 ALMGVTGAGKTTLLDVLA--------------GRKTGGV-IEgDIRiggypkvqqtfSRIsGYCeQNDVHSpQITVGESV 983
Cdd:COG1119 33 AILGPNGAGKSTLLSLITgdlpptygndvrlfGERRGGEdVW-ELR-----------KRI-GLV-SPALQL-RFPRDETV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 984 ------AYSAWLRLPAEIDTKTRKEfVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTS 1057
Cdd:COG1119 98 ldvvlsGFFDSIGLYREPTDEQRER-ARELLELLGLAHLADRPFGT-----LSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002313595 1058 GLDARAAAIAMRAVKNVAETGRTvvcTI----HQPSiEIFEAFDELMLIKRgGELIYAGPL 1114
Cdd:COG1119 172 GLDLGARELLLALLDKLAAEGAP---TLvlvtHHVE-EIPPGITHVLLLKD-GRVVAAGPK 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
897-1105 |
1.45e-14 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 73.02 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 897 YMGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIegdiRIGGypkvqqtfsrisgyceqndvhs 974
Cdd:cd03246 10 YPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGllRPTSGRV----RLDG---------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 975 pqitvgesVAYSAWlrlpaeiDTKTRKEFVDEVLEIIELdeirdaLVGTPGVNGLSREQRKRLTIAVELVSNPSIVFMDE 1054
Cdd:cd03246 64 --------ADISQW-------DPNELGDHVGYLPQDDEL------FSGSIAENILSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002313595 1055 PTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPsiEIFEAFDELMLIKRG 1105
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVIAHRP--ETLASADRILVLEDG 171
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
217-462 |
1.86e-14 |
|
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: 72.28 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 217 GFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVPA---KTSAYVSQ 293
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT---SGEILIDGKDIAKLPLEelrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 294 ydlhvadmtvretldfsarfqgvgsraeimkavikrekeagitpdpdidaymkaismeglqrsmqtdyimkimgldkcad 373
Cdd:cd00267 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 374 vkvgnamrrgISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAhISEYTILVSLLQPaPETYDLFD 453
Cdd:cd00267 81 ----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELA-EEGRTVIIVTHDP-ELAELAAD 148
|
....*....
gi 1002313595 454 DIIIMGEGK 462
Cdd:cd00267 149 RVIVLKDGK 157
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
217-467 |
2.07e-14 |
|
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: 73.77 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 217 GFSHHQSKVQILENVSGIIkPSRITLLLGPPGCGKTTLLKALAGrlnksLKET--GEIEYNGVKLDEFVPA--KTSAYVS 292
Cdd:cd03264 5 NLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILAT-----LTPPssGTIRIDGQDVLKQPQKlrRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 293 QYDLHVADMTVRETLDFSARFQGVgsraeimkavikrekeagitPDPDIDAymkaismeglqrsmQTDYIMKIMGLDKCA 372
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGI--------------------PSKEVKA--------------RVDEVLELVNLGDRA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 373 DVKVGnamrrGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAhiSEYTILVSllqpapeTYDLF 452
Cdd:cd03264 125 KKKIG-----SLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELG--EDRIVILS-------THIVE 190
|
250 260
....*....|....*....|.
gi 1002313595 453 D------DIIIMGEGKVVYHG 467
Cdd:cd03264 191 DveslcnQVAVLNKGKLVFEG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
897-1116 |
2.31e-14 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 77.64 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 897 YMGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGR-KTGGVIEGDIRIGGYPKVQQTFSRIS---GYCEQNDV 972
Cdd:COG1123 14 YPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlPHGGRISGEVLLDGRDLLELSEALRGrriGMVFQDPM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 973 HS--PqITVGESVAYSAWLRLpaeIDTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIV 1050
Cdd:COG1123 94 TQlnP-VTVGDQIAEALENLG---LSRAEARARVLELLEAVGLERRLDRYPHQ-----LSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002313595 1051 FMDEPTSGLDARAAAIAMRAVKNV-AETGRTVVCTIHQPSiEIFEAFDELMLIKRgGELIYAGPLGQ 1116
Cdd:COG1123 165 IADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLG-VVAEIADRVVVMDD-GRIVEDGPPEE 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
224-468 |
2.47e-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: 73.62 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 224 KVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVPAKTS----AYVSQYDLHVA 299
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR---SGSIRFDGRDITGLPPHERAragiGYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 300 DMTVRETLDFSARFQGVGSRAEIMKAVIK---REKEagitpdpdidaymkaismeglqRSMQtdyimkimgldkcadvKV 376
Cdd:cd03224 89 ELTVEENLLLGAYARRRAKRKARLERVYElfpRLKE----------------------RRKQ----------------LA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 377 GNamrrgISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHiSEYTILVSlLQPAPETYDLFDDII 456
Cdd:cd03224 131 GT-----LSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLV-EQNARFALEIADRAY 203
|
250
....*....|..
gi 1002313595 457 IMGEGKVVYHGP 468
Cdd:cd03224 204 VLERGRVVLEGT 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
224-463 |
2.61e-14 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 73.68 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 224 KVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrLNKSLKetGEIEYNGV--------KLDEFVpAKTSAYVSQ-Y 294
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG-LDRPTS--GEVRVDGTdisklsekELAAFR-RRHIGFVFQsF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 295 DLhVADMTVRETLDFSARFQGVGSRaeimkavikrekeagitpdpdidaymkaismeglQRSMQTDYIMKIMGLDKCADV 374
Cdd:cd03255 92 NL-LPDLTALENVELPLLLAGVPKK----------------------------------ERRERAEELLERVGLGDRLNH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 375 KVGNamrrgISGGEMKRLTTGEMIVGPCKVLLMDEiSTG-LDSSTTFQIVSCLQQLAHISEYTILVSllqpapeTYD--- 450
Cdd:cd03255 137 YPSE-----LSGGQQQRVAIARALANDPKIILADE-PTGnLDSETGKEVMELLRELNKEAGTTIVVV-------THDpel 203
|
250
....*....|....*
gi 1002313595 451 --LFDDIIIMGEGKV 463
Cdd:cd03255 204 aeYADRIIELRDGKI 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
873-1060 |
2.88e-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: 77.49 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 873 TPLTISFQDVNY-YVDTPPemrkkgymgrklqLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTggVIEGDIRIG 951
Cdd:COG4988 333 GPPSIELEDVSFsYPGGRP-------------ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP--PYSGSILIN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 952 GYP----KVQQTFSRISgYCEQNdvhsPQITVGeSVAysAWLRLPAEIDTKTRkefVDEVLEIIELDEIRDAL------- 1020
Cdd:COG4988 398 GVDlsdlDPASWRRQIA-WVPQN----PYLFAG-TIR--ENLRLGRPDASDEE---LEAALEAAGLDEFVAALpdgldtp 466
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1002313595 1021 VGTPGVnGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:COG4988 467 LGEGGR-GLSGGQAQRLALARALLRDAPLLLLDEPTAHLD 505
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
905-1060 |
2.97e-14 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 73.81 E-value: 2.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTggVIEGDIRIGGYPKVQ-QTFSRISGYCEQNDVHSPQITVGESV 983
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFET--PTSGEILLDGKDITNlPPHKRPVNTVFQNYALFPHLTVFENI 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002313595 984 AYSawLRLpAEIDTKTRKEFVDEVLEIIELDEIRDALVgtpgvNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:cd03300 94 AFG--LRL-KKLPKAEIKERVAEALDLVQLEGYANRKP-----SQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
905-1108 |
3.11e-14 |
|
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: 73.21 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKT---GGVIEGDIRIGGYPKVQQTFSRIS-GYCEQNDVHSPQITVG 980
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELptsGTIRVNGQDVSDLRGRAIPYLRRKiGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 981 ESVAysawlrLPAEIDTKTRKEF---VDEVLEIIELDEIRDALVgtpgvNGLSREQRKRLTIAVELVSNPSIVFMDEPTS 1057
Cdd:cd03292 97 ENVA------FALEVTGVPPREIrkrVPAALELVGLSHKHRALP-----AELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002313595 1058 GLDARAAAIAMRAVKNVAETGRTVVCTIHQPsiEIFEAFDELMLIKRGGEL 1108
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATHAK--ELVDTTRHRVIALERGKL 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
899-1060 |
3.23e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 73.54 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 899 GRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIE-GDIRIGGYPKVQ-------------QTFSR 962
Cdd:COG1136 18 EGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGldRPTSGEVLiDGQDISSLSERElarlrrrhigfvfQFFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 963 IsgyceqndvhsPQITVGESVAYSAWLrlpAEIDTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVE 1042
Cdd:COG1136 98 L-----------PELTALENVALPLLL---AGVSRKERRERARELLERVGLGDRLDHRPSQ-----LSGGQQQRVAIARA 158
|
170
....*....|....*...
gi 1002313595 1043 LVSNPSIVFMDEPTSGLD 1060
Cdd:COG1136 159 LVNRPKLILADEPTGNLD 176
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
877-1060 |
3.70e-14 |
|
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: 73.42 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 877 ISFQDVNYyvdtppemrkkGYMGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAgrKTGGVIEGDIRIGGYP-- 954
Cdd:cd03251 1 VEFKNVTF-----------RYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIP--RFYDVDSGRILIDGHDvr 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 955 --KVQQTFSRIsGYCEQnDVHSPQITVGESVAYSAWLRLPAEIDTKTRKEFVDEVleIIELDEIRDALVGTPGVNgLSRE 1032
Cdd:cd03251 68 dyTLASLRRQI-GLVSQ-DVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEF--IMELPEGYDTVIGERGVK-LSGG 142
|
170 180
....*....|....*....|....*...
gi 1002313595 1033 QRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:cd03251 143 QRQRIAIARALLKDPPILILDEATSALD 170
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
155-439 |
4.11e-14 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 77.02 E-value: 4.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 155 DHVRMLRKQRERMErvGVRPATVEVRwrDVCVEAECQVVSGKPlptlwnaalsrfSLLAAKLGFSHHQSKVqILENVSGI 234
Cdd:TIGR02868 295 QQLTRVRAAAERIV--EVLDAAGPVA--EGSAPAAGAVGLGKP------------TLELRDLSAGYPGAPP-VLDGVSLD 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 235 IKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGV---KLDEFVPAKTSAYVSQyDLHVADMTVRETLDFSA 311
Cdd:TIGR02868 358 LPPGERVAILGPSGSGKSTLLATLAGLLDPL---QGEVTLDGVpvsSLDQDEVRRRVSVCAQ-DAHLFDTTVRENLRLAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 312 rfqGVGSRAEIMKAVikreKEAGITPDPDidaymkaismeglqrsmqtdyimkimGLDKCADVKVGNAMRRgISGGEMKR 391
Cdd:TIGR02868 434 ---PDATDEELWAAL----ERVGLADWLR--------------------------ALPDGLDTVLGEGGAR-LSGGERQR 479
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1002313595 392 LTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLqqLAHISEYTILV 439
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVL 525
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
224-409 |
4.28e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 75.49 E-value: 4.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 224 KVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrLnkslkET---GEIEYNGVKLDEFVPAKTS-AYVSQ-YDL-- 296
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG-L-----EDptsGEILIGGRDVTDLPPKDRNiAMVFQsYALyp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 297 HvadMTVRETLDFSARFQGVgSRAEIMKAVikreKEAgitpdpdidaymkaismeglqrsmqtdyiMKIMGLDKCADVKV 376
Cdd:COG3839 89 H---MTVYENIAFPLKLRKV-PKAEIDRRV----REA-----------------------------AELLGLEDLLDRKP 131
|
170 180 190
....*....|....*....|....*....|...
gi 1002313595 377 GNamrrgISGGEMKRLTTGEMIVGPCKVLLMDE 409
Cdd:COG3839 132 KQ-----LSGGQRQRVALGRALVREPKVFLLDE 159
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
237-467 |
4.30e-14 |
|
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: 73.10 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 237 PSRITLLLGPPGCGKTTLLKALAGRLNKslkETGEIEYNGVKLDE-----FVPA---KTSAYVSQYDL--HvadMTVRET 306
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKP---DGGTIVLNGTVLFDsrkkiNLPPqqrKIGLVFQQYALfpH---LNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 307 LDFSARFqgvgsraeimkaviKREKEagitpdpdidaymkaismeglqRSMQTDYIMKIMGLDKCADVKVGnamrrGISG 386
Cdd:cd03297 96 LAFGLKR--------------KRNRE----------------------DRISVDELLDLLGLDHLLNRYPA-----QLSG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 387 GEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQL-AHISEYTILVSllQPAPETYDLFDDIIIMGEGKVVY 465
Cdd:cd03297 135 GEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIkKNLNIPVIFVT--HDLSEAEYLADRIVVMEDGRLQY 212
|
..
gi 1002313595 466 HG 467
Cdd:cd03297 213 IG 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
899-1060 |
4.50e-14 |
|
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: 72.89 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 899 GRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGYPKVQQTFSRisGYCEQNDVHSPQ 976
Cdd:cd03293 14 GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGleRPT----SGEVLVDGEPVTGPGPDR--GYVFQQDALLPW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 977 ITVGESVAYSawLRLpAEIDTKTRKEFVDEVLEIIELDEIRDALvgtPGvnGLSREQRKRLTIAVELVSNPSIVFMDEPT 1056
Cdd:cd03293 88 LTVLDNVALG--LEL-QGVPKAEARERAEELLELVGLSGFENAY---PH--QLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
....
gi 1002313595 1057 SGLD 1060
Cdd:cd03293 160 SALD 163
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
903-1110 |
5.59e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 72.31 E-value: 5.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 903 QLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGrktggVI---EGDIRIGGYPKVQQTFSRIsGYCEQNDVHSPQITV 979
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILG-----IIlpdSGEVLFDGKPLDIAARNRI-GYLPEERGLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 980 GESVAYSAWLR--LPAEIdtktrKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTS 1057
Cdd:cd03269 88 IDQLVYLAQLKglKKEEA-----RRRIDEWLERLELSEYANKRVEE-----LSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002313595 1058 GLDARAAAIAMRAVKNVAETGRTVVCTIHQpsIEIFEAF-DELMLIKRGGELIY 1110
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQ--MELVEELcDRVLLLNKGRAVLY 209
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
913-1086 |
5.86e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.46 E-value: 5.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 913 QPGILSALMGVTGAGKTTLLDVLAGRKTGGVieGDIRIGGYP---KVQQTFSRIsGYCEQNDVHSPQITVGESV-AYSAW 988
Cdd:PRK13537 31 QRGECFGLLGPNGAGKTTTLRMLLGLTHPDA--GSISLCGEPvpsRARHARQRV-GVVPQFDNLDPDFTVRENLlVFGRY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 989 LRLPAEidtkTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAM 1068
Cdd:PRK13537 108 FGLSAA----AARALVPPLLEFAKLENKADAKVGE-----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMW 178
|
170
....*....|....*...
gi 1002313595 1069 RAVKNVAETGRTVVCTIH 1086
Cdd:PRK13537 179 ERLRSLLARGKTILLTTH 196
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
809-1060 |
5.93e-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: 76.80 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 809 ISVAALIGFILLynIGFAIG-LT--IKQSPGASQAIISNDKIRICHGRDQEKSKdikiGTRRMALPFTPLTISFQDVNYy 885
Cdd:COG2274 409 LTLGQLIAFNIL--SGRFLApVAqlIGLLQRFQDAKIALERLDDILDLPPEREE----GRSKLSLPRLKGDIELENVSF- 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 886 vdtppemrkkGYMGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGYPkvQQTFSRI 963
Cdd:COG2274 482 ----------RYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGlyEPT----SGRILIDGID--LRQIDPA 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 964 S-----GYCEQNDvhspQI---TVGESVAYSAwlrlpAEIDtktrkefVDEVLEIIEL----DEIR------DALVGTPG 1025
Cdd:COG2274 546 SlrrqiGVVLQDV----FLfsgTIRENITLGD-----PDAT-------DEEIIEAARLaglhDFIEalpmgyDTVVGEGG 609
|
250 260 270
....*....|....*....|....*....|....*
gi 1002313595 1026 VNgLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:COG2274 610 SN-LSGGQRQRLAIARALLRNPRILILDEATSALD 643
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
901-1082 |
6.56e-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: 6.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 901 KLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIE-GDIRIGGYPkvqqTFSRIS---GYCEQNDVHS 974
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGllPPRSGSIRfDGRDITGLP----PHERARagiGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 975 PQITVGESVAYSAWLRLPAEidtktRKEFVDEVLEII-ELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMD 1053
Cdd:cd03224 88 PELTVEENLLLGAYARRRAK-----RKARLERVYELFpRLKERRKQLAGT-----LSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180
....*....|....*....|....*....
gi 1002313595 1054 EPTSGLDARAAAIAMRAVKNVAETGRTVV 1082
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEGVTIL 186
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
873-1105 |
7.21e-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: 76.34 E-value: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 873 TPLTISFQDVNYyvdtppemrkkGYMGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTggviEGDIRI 950
Cdd:COG4987 330 GGPSLELEDVSF-----------RYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRflDPQ----SGSITL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 951 GGYPK---VQQTFSRISGYCEQnDVHSPQITVGESvaysawLRLPAeiDTKTRKEFVdEVLEIIELDE-IR------DAL 1020
Cdd:COG4987 395 GGVDLrdlDEDDLRRRIAVVPQ-RPHLFDTTLREN------LRLAR--PDATDEELW-AALERVGLGDwLAalpdglDTW 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1021 VGTPGVNgLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAEtGRTVVCTIHQPSieIFEAFDELM 1100
Cdd:COG4987 465 LGEGGRR-LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLA--GLERMDRIL 540
|
....*
gi 1002313595 1101 LIKRG 1105
Cdd:COG4987 541 VLEDG 545
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
226-468 |
2.27e-13 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 71.55 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 226 QILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrLNKslKETGEIEYNGVKLDEFVPAKTSA------YVSQ----YD 295
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIG-LLR--PDSGEILVDGQDITGLSEKELYElrrrigMLFQggalFD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 296 lhvaDMTVRETLDFSARFQGVGSRAEIMKAVikREKeagitpdpdidaymkaismegLQRsmqtdyimkiMGLDKCADvk 375
Cdd:COG1127 96 ----SLTVFENVAFPLREHTDLSEAEIRELV--LEK---------------------LEL----------VGLPGAAD-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 376 vgnAMRRGISGGEMKRlttgemiVG--------PcKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILV------SL 441
Cdd:COG1127 137 ---KMPSELSGGMRKR-------VAlaralaldP-EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVvthdldSA 205
|
250 260
....*....|....*....|....*..
gi 1002313595 442 LQPApetydlfDDIIIMGEGKVVYHGP 468
Cdd:COG1127 206 FAIA-------DRVAVLADGKIIAEGT 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
877-1105 |
2.89e-13 |
|
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: 70.70 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 877 ISFQDVNYYvdtppemrkkgYMGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGviEGDIRIGGYPKV 956
Cdd:cd03245 3 IEFRNVSFS-----------YPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT--SGSVLLDGTDIR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 957 Q---QTFSRISGYCEQnDVHSPQITVGESVAYSAwlrlPAEIDtktrkEFVDEVLEIIELDE-IR------DALVGTPGV 1026
Cdd:cd03245 70 QldpADLRRNIGYVPQ-DVTLFYGTLRDNITLGA----PLADD-----ERILRAAELAGVTDfVNkhpnglDLQIGERGR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002313595 1027 nGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAEtGRTVVCTIHQPSieIFEAFDELMLIKRG 1105
Cdd:cd03245 140 -GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPS--LLDLVDRIIVMDSG 214
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
1264-1427 |
3.38e-13 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 69.84 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1264 GITIFTGINNSQSAMPFVaversvMYRERFAGMY--------SPWAYSFAQVAMEIPYVLMLALLFMLIAYPTIGYAWTA 1335
Cdd:COG0842 8 GLLAMSLLFTALMLTALS------IAREREQGTLerllvtpvSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1336 AKFCWFFYTMFCTLLYFVYFGMLIVSITPNLQVASIYASSFYMTQHLLSGFVMPPSQIPKWWIWLYYISPMSWTLNLLFT 1415
Cdd:COG0842 82 LSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRA 161
|
170
....*....|..
gi 1002313595 1416 TQFGFEDNSNIL 1427
Cdd:COG0842 162 LFLGGAGLADVW 173
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
215-415 |
5.91e-13 |
|
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: 69.21 E-value: 5.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 215 KLGFSHHQSKvQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrLNKSLKetGEIEYNGVKLDEFVPAKTSAYVSQ- 293
Cdd:cd03226 4 NISFSYKKGT-EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG-LIKESS--GSILLNGKPIKAKERRKSIGYVMQd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 294 YDLHVADMTVRETLDFSArfqgvgsraeimkavikrekeagitpdPDIDAYMKaismeglqrsmQTDYIMKIMGLDKCAD 373
Cdd:cd03226 80 VDYQLFTDSVREELLLGL---------------------------KELDAGNE-----------QAETVLKDLDLYALKE 121
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1002313595 374 VKvgnamRRGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLD 415
Cdd:cd03226 122 RH-----PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
899-1060 |
8.86e-13 |
|
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: 69.46 E-value: 8.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 899 GRKLQLLRNITGAFQPG-ILsALMGVTGAGKTTLLDVLAG--RKTGGVI--EGDIRIGGYPKVQQTFSRISGYCEQNDVH 973
Cdd:cd03257 15 GGSVKALDDVSFSIKKGeTL-GLVGESGSGKSTLARAILGllKPTSGSIifDGKDLLKLSRRLRKIRRKEIQMVFQDPMS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 974 S--PQITVGESVAYSAWLRLPAEiDTKTRKEFVDEVLEIIELDEIR-DALvgtPgvNGLSREQRKRLTIAVELVSNPSIV 1050
Cdd:cd03257 94 SlnPRMTIGEQIAEPLRIHGKLS-KKEARKEAVLLLLVGVGLPEEVlNRY---P--HELSGGQRQRVAIARALALNPKLL 167
|
170
....*....|
gi 1002313595 1051 FMDEPTSGLD 1060
Cdd:cd03257 168 IADEPTSALD 177
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
877-1060 |
1.09e-12 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 67.79 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 877 ISFQDVNYyvdtppemrkkGYMGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTggVIEGDIRIGGYPK- 955
Cdd:cd03228 1 IEFKNVSF-----------SYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD--PTSGEILIDGVDLr 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 956 --VQQTFSRISGYCEQNdvhsPQItvgesvaYSawlrlpaeiDTktrkefvdevleiieldeIRDalvgtpgvNGLSREQ 1033
Cdd:cd03228 68 dlDLESLRKNIAYVPQD----PFL-------FS---------GT------------------IRE--------NILSGGQ 101
|
170 180
....*....|....*....|....*..
gi 1002313595 1034 RKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:cd03228 102 RQRIAIARALLRDPPILILDEATSALD 128
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
228-430 |
2.07e-12 |
|
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: 71.55 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 228 LENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLnksLKETGEIEYNGVKLDEFVPA---KTSAYVSQYDLHVADmTVR 304
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFV---DPTEGSIAVNGVPLADADADswrDQIAWVPQHPFLFAG-TIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 305 ETLDFSarfQGVGSRAEIMKAVIKrekeAGitpdpdIDAYMKAISmEGLQRsmqtdyimkimgldkcadvKVGNAmRRGI 384
Cdd:TIGR02857 414 ENIRLA---RPDASDAEIREALER----AG------LDEFVAALP-QGLDT-------------------PIGEG-GAGL 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1002313595 385 SGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLA 430
Cdd:TIGR02857 460 SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA 505
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
905-1060 |
2.47e-12 |
|
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: 68.52 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRK---TGGVIEGDIRIGGYPkVQQtfsRISGYCEQNDVHSPQITVGE 981
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLErpdSGTILFGGEDATDVP-VQE---RNVGFVFQHYALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 982 SVAYSAWLRLPAEIDTKTR-KEFVDEVLEIIELDEIRDALvgtPgvNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:cd03296 94 NVAFGLRVKPRSERPPEAEiRAKVHELLKLVQLDWLADRY---P--AQLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
877-1105 |
3.54e-12 |
|
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: 67.64 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 877 ISFQDVNYyvdtppemrkkGYmGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTggVIEGDIRIGGYPKV 956
Cdd:cd03254 3 IEFENVNF-----------SY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD--PQKGQILIDGIDIR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 957 QQTFSRIS---GYCEQnDVHSPQITVGESVAYSawlrlpaeiDTKTRKEFVDEVLEIIELDE-IR------DALVGtPGV 1026
Cdd:cd03254 69 DISRKSLRsmiGVVLQ-DTFLFSGTIMENIRLG---------RPNATDEEVIEAAKEAGAHDfIMklpngyDTVLG-ENG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002313595 1027 NGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAEtGRTVVCTIHQPSIeIFEAfDELMLIKRG 1105
Cdd:cd03254 138 GNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLST-IKNA-DKILVLDDG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
919-1060 |
4.69e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 69.36 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 919 ALMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGypkvqQTFSRIS------GYCEQNDVHSPQITVGESVAYSawLR 990
Cdd:COG3842 35 ALLGPSGCGKTTLLRMIAGfeTPD----SGRILLDG-----RDVTGLPpekrnvGMVFQDYALFPHLTVAENVAFG--LR 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002313595 991 L----PAEIDTKtrkefVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:COG3842 104 MrgvpKAEIRAR-----VAELLELVGLEGLADRYPHQ-----LSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
228-468 |
4.76e-12 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 67.46 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 228 LENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVPAKTSAY--------VSQYdlhvA 299
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT---SGSVLFDGEDITGLPPHEIARLgigrtfqiPRLF----P 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 300 DMTVRETLDFSARFQGvgSRAEIMKAVIKREKEAgitpdpdidaymkaismegLQRSMQtdyIMKIMGLDKCADVKVGNa 379
Cdd:cd03219 89 ELTVLENVMVAAQART--GSGLLLARARREEREA-------------------RERAEE---LLERVGLADLADRPAGE- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 380 mrrgISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHiSEYTILV-----SLLqpapetYDLFDD 454
Cdd:cd03219 144 ----LSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLvehdmDVV------MSLADR 212
|
250
....*....|....
gi 1002313595 455 IIIMGEGKVVYHGP 468
Cdd:cd03219 213 VTVLDQGRVIAEGT 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
913-1096 |
5.23e-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: 71.20 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 913 QPGILSALMGVTGAGKTTLLDVLAGRKTggVIEGDIRIGGypkvQQTFSRIS------GYCEQNDVHSPQITVGESVAYS 986
Cdd:TIGR01257 1963 RPGECFGLLGVNGAGKTTTFKMLTGDTT--VTSGDATVAG----KSILTNISdvhqnmGYCPQFDAIDDLLTGREHLYLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 987 AWLR-LPAEIDTKTrkefVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAA 1065
Cdd:TIGR01257 2037 ARLRgVPAEEIEKV----ANWSIQSLGLSLYADRLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180 190
....*....|....*....|....*....|.
gi 1002313595 1066 IAMRAVKNVAETGRTVVCTIHqpSIEIFEAF 1096
Cdd:TIGR01257 2108 MLWNTIVSIIREGRAVVLTSH--SMEECEAL 2136
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
877-1087 |
6.67e-12 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 66.84 E-value: 6.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 877 ISFQDVN-YYVDTppemrkkgymGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGY 953
Cdd:cd03258 2 IELKNVSkVFGDT----------GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGleRPT----SGSVLVDGT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 954 ------PKVQQTFSRISGYCEQ--NDVHSPqiTVGESVAYSawLRLpAEIDTKTRKEFVDEVLEIIELDEIRDALVGTpg 1025
Cdd:cd03258 68 dltllsGKELRKARRRIGMIFQhfNLLSSR--TVFENVALP--LEI-AGVPKAEIEERVLELLELVGLEDKADAYPAQ-- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002313595 1026 vngLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNV-AETGRTVVCTIHQ 1087
Cdd:cd03258 141 ---LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHE 200
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
218-467 |
8.03e-12 |
|
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: 66.46 E-value: 8.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 218 FSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLnksLKETGEIEYNGVKLDEFVPAKTSA---YVSQy 294
Cdd:cd03245 10 FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY---KPTSGSVLLDGTDIRQLDPADLRRnigYVPQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 295 DLHVADMTVRETLDFSARFqgvGSRAEIMKAVikreKEAGITP----DPDIDAYMkaISMEGlqrsmqtdyimkimgldk 370
Cdd:cd03245 86 DVTLFYGTLRDNITLGAPL---ADDERILRAA----ELAGVTDfvnkHPNGLDLQ--IGERG------------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 371 cadvkvgnamrRGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLahISEYTILV-----SLLqpa 445
Cdd:cd03245 139 -----------RGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL--LGDKTLIIithrpSLL--- 202
|
250 260
....*....|....*....|..
gi 1002313595 446 petyDLFDDIIIMGEGKVVYHG 467
Cdd:cd03245 203 ----DLVDRIIVMDSGRIVADG 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
877-1060 |
8.25e-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: 66.93 E-value: 8.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 877 ISFQDVnyyvdtppemrKKGYMGRklQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGyp 954
Cdd:COG1127 6 IEVRNL-----------TKSFGDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGllRPD----SGEILVDG-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 955 kvqQTFSRISGYcEQNDVHSpQI-------------TVGESVAYsaWLRLPAEIDTKTRKEFVDEVLEIIELDEIRDALv 1021
Cdd:COG1127 67 ---QDITGLSEK-ELYELRR-RIgmlfqggalfdslTVFENVAF--PLREHTDLSEAEIRELVLEKLELVGLPGAADKM- 138
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002313595 1022 gtPGvnGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:COG1127 139 --PS--ELSGGMRKRVALARALALDPEILLYDEPTAGLD 173
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
895-1112 |
8.44e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.84 E-value: 8.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 895 KGYMGRKLqlLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG---RKTGGVIEGDIRIGGYPkVQQTFSRISGYCEQND 971
Cdd:PRK10895 11 KAYKGRRV--VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGivpRDAGNIIIDDEDISLLP-LHARARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 972 VHSPQITVGESVAysAWLRLPAEIDTKTRKEFVDEVLEIIELDEIRDALVgtpgvNGLSREQRKRLTIAVELVSNPSIVF 1051
Cdd:PRK10895 88 SIFRRLSVYDNLM--AVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMG-----QSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002313595 1052 MDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQpsieIFEAFD--ELMLIKRGGELIYAG 1112
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHN----VRETLAvcERAYIVSQGHLIAHG 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
223-470 |
8.50e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 67.11 E-value: 8.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 223 SKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKAL--AGRLNKSLKETGEIEYNGVKL-----DEFVPAKTSAYVSQYD 295
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGHNIysprtDTVDLRKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 296 lHVADMTVRETLDFSARFQGVGSRAEIMKAVIKREKEAGItpdpdidaymkaismeglqrsmqtdyimkimgLDKCADVK 375
Cdd:PRK14239 96 -NPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASI--------------------------------WDEVKDRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 376 VGNAMrrGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHisEYTILVSL--LQPAPETYD--- 450
Cdd:PRK14239 143 HDSAL--GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTrsMQQASRISDrtg 218
|
250 260
....*....|....*....|..
gi 1002313595 451 --LFDDIIIMGEGKVVYHGPKN 470
Cdd:PRK14239 219 ffLDGDLIEYNDTKQMFMNPKH 240
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
224-310 |
1.07e-11 |
|
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: 64.73 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 224 KVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVPA--KTSAYVSQYDLHVADM 301
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD---SGEIKVLGKDIKKEPEEvkRRIGYLPEEPSLYENL 88
|
....*....
gi 1002313595 302 TVRETLDFS 310
Cdd:cd03230 89 TVRENLKLS 97
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
227-418 |
1.16e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.67 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 227 ILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLnksLKETGEIEYNGVKLDEFVPAKTSAYVSQYDLHVADMTVRET 306
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLL---PPAAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 307 LDFSARFQGvgsraeimkavikrekeagiTPDPDIDAYMKAismeglqrsmqtdyimkiMGLDKCADVKVGNamrrgISG 386
Cdd:PRK13539 94 LEFWAAFLG--------------------GEELDIAAALEA------------------VGLAPLAHLPFGY-----LSA 130
|
170 180 190
....*....|....*....|....*....|..
gi 1002313595 387 GEMKRLTTGEMIVGPCKVLLMDEISTGLDSST 418
Cdd:PRK13539 131 GQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
903-1113 |
1.17e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.95 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 903 QLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVI--EG---DIRIGGYPKVQQTFSRISGYCEQNDVHSp 975
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGllRPQKGAVlwQGkplDYSKRGLLALRQQVATVFQDPEQQIFYT- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 976 qiTVGESVAYSawLR-LPAEIDTKTRKefVDEVLEIIELDEIRDalvgTPgVNGLSREQRKRLTIAVELVSNPSIVFMDE 1054
Cdd:PRK13638 94 --DIDSDIAFS--LRnLGVPEAEITRR--VDEALTLVDAQHFRH----QP-IQCLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002313595 1055 PTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSIeIFEAFDELMLIKRGGELIYAGP 1113
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHGAP 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
904-1086 |
1.30e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.58 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 904 LLRNITGAFQPGILSALMGVTGAGKTTLLDVLAgR----KTGGVIEGDIRIGGYPKVQqtFSRISGYCEQNDVHSPQITV 979
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RlltpQSGTVFLGDKPISMLSSRQ--LARRLALLPQHHLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 980 GESVAY--SAWLRLPAEIDTKTRkEFVDEVLEIIELDEIRDALVgtpgvNGLSREQRKRLTIAVELVSNPSIVFMDEPTS 1057
Cdd:PRK11231 94 RELVAYgrSPWLSLWGRLSAEDN-ARVNQAMEQTRINHLADRRL-----TDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180
....*....|....*....|....*....
gi 1002313595 1058 GLDARAAAIAMRAVKNVAETGRTVVCTIH 1086
Cdd:PRK11231 168 YLDINHQVELMRLMRELNTQGKTVVTVLH 196
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
920-1060 |
1.57e-11 |
|
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: 65.35 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 920 LMGVTGAGKTTLLDVLAGRKTggVIEGDIRIGG------YPKvqqtfSRISGYCEQNDVHSPQITVGESVAYSAWLRL-- 991
Cdd:cd03301 31 LLGPSGCGKTTTLRMIAGLEE--PTSGRIYIGGrdvtdlPPK-----DRDIAMVFQNYALYPHMTVYDNIAFGLKLRKvp 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002313595 992 PAEIDTKtrkefVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:cd03301 104 KDEIDER-----VREVAELLQIEHLLDRKPKQ-----LSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
905-1060 |
2.11e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 67.41 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAGrktggvIE----GDIRIGG------YPK---VQQTFsrisgyceQND 971
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG------LEdptsGEILIGGrdvtdlPPKdrnIAMVF--------QSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 972 VHSPQITVGESVAYSawLRL----PAEIDTKtrkefVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNP 1047
Cdd:COG3839 85 ALYPHMTVYENIAFP--LKLrkvpKAEIDRR-----VREAAELLGLEDLLDRKPKQ-----LSGGQRQRVALGRALVREP 152
|
170
....*....|...
gi 1002313595 1048 SIVFMDEPTSGLD 1060
Cdd:COG3839 153 KVFLLDEPLSNLD 165
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
905-1113 |
2.38e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.06 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTggVIEGDIRIGGYPKVQQTFSRISGYCEQND-------VHSPQI 977
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVR--LASGKISILGQPTRQALQKNLVAYVPQSEevdwsfpVLVEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 978 TVGESVAYSAWLRLPAEIDtktrKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTS 1057
Cdd:PRK15056 101 VMMGRYGHMGWLRRAKKRD----RQIVTAALARVDMVEFRHRQIGE-----LSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002313595 1058 GLDARAAAIAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMLIKrgGELIYAGP 1113
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTHNLG-SVTEFCDYTVMVK--GTVLASGP 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
217-409 |
3.58e-11 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 64.42 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 217 GFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEfvPAKTSAYVSQYDL 296
Cdd:cd03293 9 TYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT---SGEVLVDGEPVTG--PGPDRGYVFQQDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 297 HVADMTVRETLDFSARFQGVgSRAEIMKAVikrekeagitpdpdidayMKAISMEGLQrsmqtdyimkimgldkcadvKV 376
Cdd:cd03293 84 LLPWLTVLDNVALGLELQGV-PKAEARERA------------------EELLELVGLS--------------------GF 124
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002313595 377 GNAMRRGISGGeMK------RLttgeMIVGPcKVLLMDE 409
Cdd:cd03293 125 ENAYPHQLSGG-MRqrvalaRA----LAVDP-DVLLLDE 157
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
904-1095 |
3.64e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.12 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 904 LLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIEGDIRIGGYPKVqqtFSRISgYCEQNDVHSPQITVGE 981
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGllPPAAGTIKLDGGDIDDPDV---AEACH-YLGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 982 SVAYsaWLRLPAeidtkTRKEFVDEVLEIIELDEIRDalvgTPGvNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDA 1061
Cdd:PRK13539 93 NLEF--WAAFLG-----GEELDIAAALEAVGLAPLAH----LPF-GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180 190
....*....|....*....|....*....|....
gi 1002313595 1062 RAAAIAMRAVKNVAETGRTVVCTIHQPsIEIFEA 1095
Cdd:PRK13539 161 AAVALFAELIRAHLAQGGIVIAATHIP-LGLPGA 193
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
904-1113 |
3.68e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.19 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 904 LLRNITGAFQPGILSALMGVTGAGKTTLLDVLaGRKTGGViEGDIRIGGYPKVQ---QTFSRISGYCEQNDVHSPQITVG 980
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPS-EGEILLDAQPLESwssKAFARKVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 981 ESVA------YSAWLRLPAEidtktRKEFVDEVLEIIELDEIRDALVgtpgvNGLSREQRKRLTIAVELVSNPSIVFMDE 1054
Cdd:PRK10575 104 ELVAigrypwHGALGRFGAA-----DREKVEEAISLVGLKPLAHRLV-----DSLSGGERQRAWIAMLVAQDSRCLLLDE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1055 PTSGLDARAAAIAMRAVKNVA-ETGRTVVCTIHqpSIEIFEAFDELMLIKRGGELIYAGP 1113
Cdd:PRK10575 174 PTSALDIAHQVDVLALVHRLSqERGLTVIAVLH--DINMAARYCDYLVALRGGEMIAQGT 231
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
860-1060 |
3.84e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 67.50 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 860 DIKIGTRRMALPFTPLTISFQDVNY-YVDTPPemrkkgymgrklqLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGR 938
Cdd:COG1132 323 EIPDPPGAVPLPPVRGEIEFENVSFsYPGDRP-------------VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 939 KTggVIEGDIRIGG-----YPK---------VQQTFSRISGyceqndvhspqiTVGESVAYSawlRLPAeidtkTRKEfV 1004
Cdd:COG1132 390 YD--PTSGRILIDGvdirdLTLeslrrqigvVPQDTFLFSG------------TIRENIRYG---RPDA-----TDEE-V 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002313595 1005 DEVLEIIELDE-IR------DALVGTPGVNgLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:COG1132 447 EEAAKAAQAHEfIEalpdgyDTVVGERGVN-LSGGQRQRIAIARALLKDPPILILDEATSALD 508
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
904-1088 |
4.71e-11 |
|
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: 63.53 E-value: 4.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 904 LLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGviegDIRIGGYPKVQQTFS--RISGYCEQNDVHSPQITV 979
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGllRPDSG----EVRWNGTPLAEQRDEphENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 980 GESVAYSAWLRLPAEIDtktrkefVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGL 1059
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRT-------IEDALAAVGLTGFEDLPAAQ-----LSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180
....*....|....*....|....*....
gi 1002313595 1060 DARAAAIAMRAVKNVAETGRTVVCTIHQP 1088
Cdd:TIGR01189 159 DKAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
911-1112 |
4.78e-11 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 64.05 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 911 AFQPGILSALMGVTGAGKTTLLDVLAGRKT---GGVIEGDIRIGGYPKVQQTFSRIsgyCEQNDVHsPQITVGESVAY-- 985
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETpqsGRVLINGVDVTAAPPADRPVSML---FQENNLF-AHLTVEQNVGLgl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 986 SAWLRLPAEidtktRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAA 1065
Cdd:cd03298 96 SPGLKLTAE-----DRQAIEVALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1002313595 1066 IAMRAVKNV-AETGRTVVCTIHQPSiEIFEAFDELMLIKRgGELIYAG 1112
Cdd:cd03298 166 EMLDLVLDLhAETKMTVLMVTHQPE-DAKRLAQRVVFLDN-GRIAAQG 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
224-464 |
4.92e-11 |
|
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: 63.81 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 224 KVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrLNKSLKetGEIEYNGVKLDEFVPAKTS-AYVSQ-YDLHvADM 301
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAG-LEEPTS--GRIYIGGRDVTDLPPKDRDiAMVFQnYALY-PHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 302 TVRETLDFSARFQGVgSRAEIMKAVikreKEAGitpdpdidaymkaismeglqrsmqtdyimKIMGLDKCADVKVgnamr 381
Cdd:cd03301 88 TVYDNIAFGLKLRKV-PKDEIDERV----REVA-----------------------------ELLQIEHLLDRKP----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 382 RGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYT-ILVSLLQpaPETYDLFDDIIIMGE 460
Cdd:cd03301 129 KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTtIYVTHDQ--VEAMTMADRIAVMND 206
|
....
gi 1002313595 461 GKVV 464
Cdd:cd03301 207 GQIQ 210
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
895-1060 |
6.21e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.07 E-value: 6.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 895 KGYMGRKLQ--LLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGgvIEGDIRIGGypkvqQTFSRIS-------- 964
Cdd:PRK11629 13 KRYQEGSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTP--TSGDVIFNG-----QPMSKLSsaakaelr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 965 ----GYCEQNDVHSPQITVGESVAysawlrLPAEIDTKTRKEFVDEVLEIIeldeirdALVGTPG-----VNGLSREQRK 1035
Cdd:PRK11629 86 nqklGFIYQFHHLLPDFTALENVA------MPLLIGKKKPAEINSRALEML-------AAVGLEHranhrPSELSGGERQ 152
|
170 180
....*....|....*....|....*
gi 1002313595 1036 RLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:PRK11629 153 RVAIARALVNNPRLVLADEPTGNLD 177
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
228-493 |
6.58e-11 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 63.89 E-value: 6.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 228 LENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKslkETGEIEYNGVKLDEFVPAKTS-AYVSQ-YDL--HvadMTV 303
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKP---DSGKILLNGKDITNLPPEKRDiSYVPQnYALfpH---MTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 304 RETLDFSARFQGVgSRAEIMKAVIKrekeagitpdpdidaymkaismeglqrsmqtdyIMKIMGLDKCADVKVGNamrrg 383
Cdd:cd03299 89 YKNIAYGLKKRKV-DKKEIERKVLE---------------------------------IAEMLGIDHLLNRKPET----- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 384 ISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILvSLLQPAPETYDLFDDIIIMGEGKV 463
Cdd:cd03299 130 LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVL-HVTHDFEEAWALADKVAIMLNGKL 208
|
250 260 270
....*....|....*....|....*....|
gi 1002313595 464 VYHGPKNLImtffescgFKCPERKGPADFL 493
Cdd:cd03299 209 IQVGKPEEV--------FKKPKNEFVAEFL 230
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
905-1113 |
7.14e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 64.09 E-value: 7.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGgviEGDIRIGG-----YPKVQQtfSRISGYCEQNDVHSPQITV 979
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG---QGEILLNGrplsdWSAAEL--ARHRAYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 980 GESVAysawLRLPAEIDTKTRKEFVDEVLEIIELDEirdaLVGTPgVNGLS--REQRKRLTiAVEL----VSNPS--IVF 1051
Cdd:COG4138 87 FQYLA----LHQPAGASSEAVEQLLAQLAEALGLED----KLSRP-LTQLSggEWQRVRLA-AVLLqvwpTINPEgqLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002313595 1052 MDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSIEIFEAfDELMLIKRgGELIYAGP 1113
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHA-DRVWLLKQ-GKLVASGE 216
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
227-474 |
7.89e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 64.26 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 227 ILENVSGIIKPSRITLLLGPPGCGKTTLLKALAgRLNKSlkETGEIEYNGVKLDEFVP---AKTSAYVSQYDLHVADMTV 303
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RLLTP--QSGTVFLGDKPISMLSSrqlARRLALLPQHHLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 304 RETLDFsarfqgvgsraeimkavikrekeaGITPdpdidaYMKAISMEGLQRSMQTDYIMKIMGLDKCADVKVGNamrrg 383
Cdd:PRK11231 94 RELVAY------------------------GRSP------WLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTD----- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 384 ISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEyTILVSLlqpapetYDL------FDDIII 457
Cdd:PRK11231 139 LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVL-------HDLnqasryCDHLVV 210
|
250
....*....|....*..
gi 1002313595 458 MGEGKVVYHGPKNLIMT 474
Cdd:PRK11231 211 LANGHVMAQGTPEEVMT 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
905-1088 |
8.51e-11 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 66.23 E-value: 8.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAG----RKtggvieGDIRIGGYP---KVQQTFSRISGYCEQnDVHSPQI 977
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGlldpLQ------GEVTLDGVPvssLDQDEVRRRVSVCAQ-DAHLFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 978 TVGESvaysawLRLPAEIDTKtrkEFVDEVLEIIELDEIRDALVG------TPGVNGLSREQRKRLTIAVELVSNPSIVF 1051
Cdd:TIGR02868 424 TVREN------LRLARPDATD---EELWAALERVGLADWLRALPDgldtvlGEGGARLSGGERQRLALARALLADAPILL 494
|
170 180 190
....*....|....*....|....*....|....*..
gi 1002313595 1052 MDEPTSGLDARAAAIAMRAVkNVAETGRTVVCTIHQP 1088
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDL-LAALSGRTVVLITHHL 530
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
226-469 |
8.89e-11 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 63.67 E-value: 8.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 226 QILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrLNKslKETGEIEYNGVKLDEFVPA------KTSAYVSQ----YD 295
Cdd:cd03261 14 TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVG-LLR--PDSGEVLIDGEDISGLSEAelyrlrRRMGMLFQsgalFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 296 lhvaDMTVRETLDFSARFQGVGSRAEImkavikrekeagitpdpdidaymKAISMEGLQRsmqtdyimkiMGLDKCADVK 375
Cdd:cd03261 91 ----SLTVFENVAFPLREHTRLSEEEI-----------------------REIVLEKLEA----------VGLRGAEDLY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 376 VGNamrrgISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSC---LQQLAHISeyTILVSllQPAPETYDLF 452
Cdd:cd03261 134 PAE-----LSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLirsLKKELGLT--SIMVT--HDLDTAFAIA 204
|
250
....*....|....*..
gi 1002313595 453 DDIIIMGEGKVVYHGPK 469
Cdd:cd03261 205 DRIAVLYDGKIVAEGTP 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
226-474 |
9.23e-11 |
|
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: 63.95 E-value: 9.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 226 QILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSLKET----GEiEYNGVKLDEFvpaKTS-AYVSQyDLH--- 297
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfGE-RRGGEDVWEL---RKRiGLVSP-ALQlrf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 298 VADMTVRETLdFSARFQGVGSRAEIMKAVIKREKEagitpdpdidaymkaismeglqrsmqtdyIMKIMGLDKCADVKVG 377
Cdd:COG1119 92 PRDETVLDVV-LSGFFDSIGLYREPTDEQRERARE-----------------------------LLELLGLAHLADRPFG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 378 NamrrgISGGEMKRLttgeMI----VGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYT-ILVS-LLQPAPETydl 451
Cdd:COG1119 142 T-----LSQGEQRRV----LIaralVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTlVLVThHVEEIPPG--- 209
|
250 260
....*....|....*....|...
gi 1002313595 452 FDDIIIMGEGKVVYHGPKNLIMT 474
Cdd:COG1119 210 ITHVLLLKDGRVVAAGPKEEVLT 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
920-1129 |
1.45e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.47 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 920 LMGVTGAGKTTLLDVLAGRKTGGviEGDIRIGGYP---KVQQTFSRIsGYCEQNDVHSPQITVGES-VAYSAWLRLpaei 995
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPD--AGKITVLGVPvpaRARLARARI-GVVPQFDNLDLEFTVRENlLVFGRYFGM---- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 996 DTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVA 1075
Cdd:PRK13536 145 STREIEAVIPSLLEFARLESKADARVSD-----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLL 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002313595 1076 ETGRTVVCTIHqpSIEIFEAF-DELMLIKRGGELIYAGPLG----QHSCKVIQYFQSIP 1129
Cdd:PRK13536 220 ARGKTILLTTH--FMEEAERLcDRLCVLEAGRKIAEGRPHAlideHIGCQVIEIYGGDP 276
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
218-464 |
1.91e-10 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 62.37 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 218 FSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVPAKTSA-------Y 290
Cdd:COG1136 14 YGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPT---SGEVLIDGQDISSLSERELARlrrrhigF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 291 VSQ-YDLhVADMTVRETLDFSARFQGVgSRAEimkavikREKEAgitpdpdidaymkaismeglqrsmqtDYIMKIMGLD 369
Cdd:COG1136 91 VFQfFNL-LPELTALENVALPLLLAGV-SRKE-------RRERA--------------------------RELLERVGLG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 370 KCADVKVGNamrrgISGGEMKRLTTGEMIVGPCKVLLMDEIsTG-LDSSTTFQIVSCLQQLAHISEYTILVSllqpapeT 448
Cdd:COG1136 136 DRLDHRPSQ-----LSGGQQQRVAIARALVNRPKLILADEP-TGnLDSKTGEEVLELLRELNRELGTTIVMV-------T 202
|
250 260
....*....|....*....|.
gi 1002313595 449 YDL-----FDDIIIMGEGKVV 464
Cdd:COG1136 203 HDPelaarADRVIRLRDGRIV 223
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
226-472 |
2.47e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 62.39 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 226 QILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRlnKSLKET-GEIEYNGVKLDEFVP---AKTSAYVS-QYDLHVAD 300
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH--PKYEVTsGSILLDGEDILELSPderARAGIFLAfQYPVEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 301 MTVRETLdfsarfqgvgsRAEIMKaviKREKEagitpdPDIDAYMKAISMEglqrsmqtdyiMKIMGLDKcadvkvgNAM 380
Cdd:COG0396 92 VSVSNFL-----------RTALNA---RRGEE------LSAREFLKLLKEK-----------MKELGLDE-------DFL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 381 RR----GISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSStTFQIVS-CLQQLAH-------ISEYTILVSLLQPapet 448
Cdd:COG0396 134 DRyvneGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDID-ALRIVAeGVNKLRSpdrgiliITHYQRILDYIKP---- 208
|
250 260
....*....|....*....|....
gi 1002313595 449 ydlfDDIIIMGEGKVVYHGPKNLI 472
Cdd:COG0396 209 ----DFVHVLVDGRIVKSGGKELA 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
914-1060 |
2.56e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.64 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 914 PGILSALMGVTGAGKTTLLDVLAGR--KTGGVIEGDIRIGGYPKV-------QQTFSRIS-GYCEQN--DVHSPQITVGE 981
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSARlaPDAGEVHYRMRDGQLRDLyalseaeRRRLLRTEwGFVHQHprDGLRMQVSAGG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 982 SVAYsawlRLPA-------EIdtktRKEFVDEvLEIIELDEIR-DALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMD 1053
Cdd:PRK11701 111 NIGE----RLMAvgarhygDI----RATAGDW-LERVEIDAARiDDLPTT-----FSGGMQQRLQIARNLVTHPRLVFMD 176
|
....*..
gi 1002313595 1054 EPTSGLD 1060
Cdd:PRK11701 177 EPTGGLD 183
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
895-1060 |
2.76e-10 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 62.80 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 895 KGYMGRK--LQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGYPkVQQTFSRIsGYCEQN 970
Cdd:COG1116 15 KRFPTGGggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGleKPT----SGEVLVDGKP-VTGPGPDR-GVVFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 971 DVHSPQITVGESVAYSawLRLpAEIDTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIV 1050
Cdd:COG1116 89 PALLPWLTVLDNVALG--LEL-RGVPKAERRERARELLELVGLAGFEDAYPHQ-----LSGGMRQRVAIARALANDPEVL 160
|
170
....*....|
gi 1002313595 1051 FMDEPTSGLD 1060
Cdd:COG1116 161 LMDEPFGALD 170
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
895-1060 |
3.04e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.70 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 895 KGYMGRKLqlLRNITGAFQPG--IlsALMGVTGAGKTTLLDVLAGRK--TGG--VIEGDIRIGgypkvqqtfsrisgYCE 968
Cdd:COG0488 6 KSFGGRPL--LDDVSLSINPGdrI--GLVGRNGAGKSTLLKILAGELepDSGevSIPKGLRIG--------------YLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 969 QNDVHSPQITVGESV--AYSAWLRLPAEIDTKTRK-EFVDEVL--------EIIELD------EIRDALVG--------- 1022
Cdd:COG0488 68 QEPPLDDDLTVLDTVldGDAELRALEAELEELEAKlAEPDEDLerlaelqeEFEALGgweaeaRAEEILSGlgfpeedld 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002313595 1023 TPgVNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:COG0488 148 RP-VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
228-476 |
3.11e-10 |
|
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: 61.97 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 228 LENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrLNKSlkETGEIEYNGVKL-DEFVPAKTSAYVSQydlHVA---DMTV 303
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG-LERP--DSGTILFGGEDAtDVPVQERNVGFVFQ---HYAlfrHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 304 RETLDFSARFQGVGSRAEimKAVIKREkeagitpdpdIDAYMKAISMEGLQRSMQTDyimkimgldkcadvkvgnamrrg 383
Cdd:cd03296 92 FDNVAFGLRVKPRSERPP--EAEIRAK----------VHELLKLVQLDWLADRYPAQ----------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 384 ISGGEMKRLTTGE-MIVGPcKVLLMDEISTGLDSSTTFQIVSCLQQLAH-ISEYTILVSLLQpaPETYDLFDDIIIMGEG 461
Cdd:cd03296 137 LSGGQRQRVALARaLAVEP-KVLLLDEPFGALDAKVRKELRRWLRRLHDeLHVTTVFVTHDQ--EEALEVADRVVVMNKG 213
|
250 260
....*....|....*....|...
gi 1002313595 462 KV--------VYHGPKNLIMTFF 476
Cdd:cd03296 214 RIeqvgtpdeVYDHPASPFVYSF 236
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
877-1111 |
3.51e-10 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 61.79 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 877 ISFQDVNYYVDTPPEMrkkgymgrklQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLagRKTGGVIEGDIRIGGYP-- 954
Cdd:cd03249 1 IEFKNVSFRYPSRPDV----------PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL--ERFYDPTSGEILLDGVDir 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 955 --KVQQTFSRIsGYCEQNdvhsPQI---TVGESVAYSAWLRLPAEIDTKTRKEFVDEVleIIELDEIRDALVGTPGVNgL 1029
Cdd:cd03249 69 dlNLRWLRSQI-GLVSQE----PVLfdgTIAENIRYGKPDATDEEVEEAAKKANIHDF--IMSLPDGYDTLVGERGSQ-L 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1030 SREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAEtGRTVVCTIHQPS-------IEIFEA------- 1095
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK-GRTTIVIAHRLStirnadlIAVLQNgqvveqg 219
|
250
....*....|....*..
gi 1002313595 1096 -FDELMliKRGGelIYA 1111
Cdd:cd03249 220 tHDELM--AQKG--VYA 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
227-409 |
3.84e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.32 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 227 ILENVSGIIKP-SRITLLlGPPGCGKTTLLKALAGRLnksLKETGEIEY-NGVKLdefvpaktsAYVSQYDLHVADMTVR 304
Cdd:COG0488 13 LLDDVSLSINPgDRIGLV-GRNGAGKSTLLKILAGEL---EPDSGEVSIpKGLRI---------GYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 305 ETLdfsarFQGVGSRAEIMKAvIKREKEAGITPDPDIDAYMKAIS----MEGLQRSMQTDYIMKIMGLDKC-ADVKVGNa 379
Cdd:COG0488 80 DTV-----LDGDAELRALEAE-LEELEAKLAEPDEDLERLAELQEefeaLGGWEAEARAEEILSGLGFPEEdLDRPVSE- 152
|
170 180 190
....*....|....*....|....*....|
gi 1002313595 380 mrrgISGGEMKRLTTGEMIVGPCKVLLMDE 409
Cdd:COG0488 153 ----LSGGWRRRVALARALLSEPDLLLLDE 178
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
868-1060 |
3.86e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 61.98 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 868 MALPFTPLT--ISFQDVN-YYVDTppemrkkgymgrklQLLRNITGAFQPGILSALMGVTGAGKTTLL-------DVLAG 937
Cdd:COG1117 1 MTAPASTLEpkIEVRNLNvYYGDK--------------QALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 938 RKtggvIEGDIRIGGypkvqqtfsrisgyceqNDVHSPQI---------------------TVGESVAYSawLRL----- 991
Cdd:COG1117 67 AR----VEGEILLDG-----------------EDIYDPDVdvvelrrrvgmvfqkpnpfpkSIYDNVAYG--LRLhgiks 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 992 PAEIDtktrkEFVDEVLEIIEL-DEIRDALvGTPGVnGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:COG1117 124 KSELD-----EIVEESLRKAALwDEVKDRL-KKSAL-GLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
894-1112 |
4.44e-10 |
|
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: 61.40 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 894 KKGYMGRKLqlLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIE-GDIRIGGYPKVQQtfSRIS-GYCEQ 969
Cdd:cd03218 7 SKRYGKRKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGlvKPDSGKILlDGQDITKLPMHKR--ARLGiGYLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 970 NDVHSPQITVGESvaysawLRLPAEIDTKTRKEF---VDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSN 1046
Cdd:cd03218 83 EASIFRKLTVEEN------ILAVLEIRGLSKKEReekLEELLEEFHITHLRKSKASS-----LSGGERRRVEIARALATN 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002313595 1047 PSIVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMLIkRGGELIYAG 1112
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVR-ETLSITDRAYII-YEGKVLAEG 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
228-471 |
6.02e-10 |
|
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: 60.85 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 228 LENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKS-----------LKETGEIEyngvkldefvpaKTSAYVSQYDL 296
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTsgratvaghdvVREPREVR------------RRIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 297 HVADMTVRETLDFSARFQGVGSRaeimkavIKREKeagitpdpdidaymkaismeglqrsmqTDYIMKIMGLDKCADVKV 376
Cdd:cd03265 84 VDDELTGWENLYIHARLYGVPGA-------ERRER---------------------------IDELLDFVGLLEAADRLV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 377 GNamrrgISGGEMKRLTTGE-MIVGPcKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILVSlLQPAPETYDLFDDI 455
Cdd:cd03265 130 KT-----YSGGMRRRLEIARsLVHRP-EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLT-THYMEEAEQLCDRV 202
|
250
....*....|....*..
gi 1002313595 456 IIMGEGKVVYHG-PKNL 471
Cdd:cd03265 203 AIIDHGRIIAEGtPEEL 219
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
218-439 |
6.74e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.59 E-value: 6.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 218 FSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKAL--AGRLNKSLKETGEIEYNGVKLDEfvpaktsayvsqyd 295
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEVRVEGRVEFFNQNIYE-------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 296 lhvadmtvretldfsarfqgvgSRAEIMKAvikREKEAGITPDPDI------DAYMKAISMEGLQRSMQTDYIMKimGLD 369
Cdd:PRK14258 79 ----------------------RRVNLNRL---RRQVSMVHPKPNLfpmsvyDNVAYGVKIVGWRPKLEIDDIVE--SAL 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002313595 370 KCADV--KVGNAMRRG---ISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILV 439
Cdd:PRK14258 132 KDADLwdEIKHKIHKSaldLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVI 206
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
897-1089 |
8.57e-10 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 60.96 E-value: 8.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 897 YMGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGviEGDIRIGGYPKV---QQTFSRISGYCEQNDVH 973
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE--NGRVLVDGHDLAladPAWLRRQVGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 974 SPQiTVGESVAYSawlrlpaeiDTKTRKEFVDEVLE-------IIELDEIRDALVGTPGVnGLSREQRKRLTIAVELVSN 1046
Cdd:cd03252 88 FNR-SIRDNIALA---------DPGMSMERVIEAAKlagahdfISELPEGYDTIVGEQGA-GLSGGQRQRIAIARALIHN 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1002313595 1047 PSIVFMDEPTSGLDARAAAIAMRAVKNVAEtGRTVVCTIHQPS 1089
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLS 198
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
895-1105 |
8.77e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 895 KGYMGrkLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGviEGDIRIGGypkVQQTFSRI-----SG---- 965
Cdd:PRK11288 12 KTFPG--VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD--AGSILIDG---QEMRFASTtaalaAGvaii 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 966 YCEQNDVhsPQITVGESVaysaWL-RLPAE---IDTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAV 1041
Cdd:PRK11288 85 YQELHLV--PEMTVAENL----YLgQLPHKggiVNRRLLNYEAREQLEHLGVDIDPDTPLKY-----LSIGQRQMVEIAK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002313595 1042 ELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMLIKRG 1105
Cdd:PRK11288 154 ALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRME-EIFALCDAITVFKDG 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
913-1114 |
1.02e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 61.28 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 913 QPGILSALMGVTGAGKTTLLDVLAGrktggVI---EGDIRIGGYPKVQQTFSRIsGYceqndvhsPQITVGESVAYSAWL 989
Cdd:COG4152 25 PKGEIFGLLGPNGAGKTTTIRIILG-----ILapdSGEVLWDGEPLDPEDRRRI-GYlpeerglyPKMKVGEQLVYLARL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 990 R-LPAEiDTKTRkefVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAM 1068
Cdd:COG4152 99 KgLSKA-EAKRR---ADEWLERLGLGDRANKKVEE-----LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002313595 1069 RAVKNVAETGRTVVCTIHQpsIEIFEAF-DELMLIKRgGELIYAGPL 1114
Cdd:COG4152 170 DVIRELAAKGTTVIFSSHQ--MELVEELcDRIVIINK-GRKVLSGSV 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
903-1060 |
1.03e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 62.09 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 903 QLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGrktggvIE----GDIRIGGypkvQQTFSRIS------GYCEQNDV 972
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAG------LEtpdsGRIVLNG----RDLFTNLPprerrvGFVFQHYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 973 HSPQITVGESVAYSAWLRLPAEIDTKTRkefVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFM 1052
Cdd:COG1118 86 LFPHMTVAENIAFGLRVRPPSKAEIRAR---VEELLELVQLEGLADRYPSQ-----LSGGQRQRVALARALAVEPEVLLL 157
|
....*...
gi 1002313595 1053 DEPTSGLD 1060
Cdd:COG1118 158 DEPFGALD 165
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
903-1060 |
1.09e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.70 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 903 QLLRNITGAFQPGILSALMGVTGAGKTTLLDV---LAGRKTGGVIEGDIRIGGYP-----------KVQQTFsrisgyce 968
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEARVSGEVYLDGQDifkmdvielrrRVQMVF-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 969 QNDVHSPQITVGESVAYSAWL-RLpaeidTKTRKEF---VDEVLEIIEL-DEIRDALVGTPGvnGLSREQRKRLTIAVEL 1043
Cdd:PRK14247 89 QIPNPIPNLSIFENVALGLKLnRL-----VKSKKELqerVRWALEKAQLwDEVKDRLDAPAG--KLSGGQQQRLCIARAL 161
|
170
....*....|....*..
gi 1002313595 1044 VSNPSIVFMDEPTSGLD 1060
Cdd:PRK14247 162 AFQPEVLLADEPTANLD 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
218-409 |
1.30e-09 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 60.49 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 218 FSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEfvPAKTSAYVSQydlh 297
Cdd:COG1116 17 FPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPT---SGEVLVDGKPVTG--PGPDRGVVFQ---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 298 vAD-----MTVRETLDFSARFQGVgSRAEimkavikREKEAgitpdpdidayMKAISMeglqrsmqtdyimkiMGLDKCA 372
Cdd:COG1116 88 -EPallpwLTVLDNVALGLELRGV-PKAE-------RRERA-----------RELLEL---------------VGLAGFE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1002313595 373 DVKVGNamrrgISGGeMKR-------LttgemIVGPcKVLLMDE 409
Cdd:COG1116 133 DAYPHQ-----LSGG-MRQrvaiaraL-----ANDP-EVLLMDE 164
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
897-1060 |
1.40e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.56 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 897 YMGRKlQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLagRKTGGVIegdiriggyPKVQQTFSRIsgYCEQNdVHSPQ 976
Cdd:PRK14239 14 YYNKK-KALNSVSLDFYPNEITALIGPSGSGKSTLLRSI--NRMNDLN---------PEVTITGSIV--YNGHN-IYSPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 977 ---------------------ITVGESVAYSawLRLPAEIDTKTRKEFVDEVLEIIEL-DEIRDALVGTpgVNGLSREQR 1034
Cdd:PRK14239 79 tdtvdlrkeigmvfqqpnpfpMSIYENVVYG--LRLKGIKDKQVLDEAVEKSLKGASIwDEVKDRLHDS--ALGLSGGQQ 154
|
170 180
....*....|....*....|....*.
gi 1002313595 1035 KRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALD 180
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
228-463 |
1.66e-09 |
|
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: 59.34 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 228 LENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRlnkSLKETGEIEYNGVKLDEFvPAKTSAY-------VSQYDLHVAD 300
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE---ELPTSGTIRVNGQDVSDL-RGRAIPYlrrkigvVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 301 MTVRETLDFSARFQGVGSRaEIMKAVikrekeagitpdpdidayMKAISMEGLQrsmqtdyimkimglDKcadvkvGNAM 380
Cdd:cd03292 93 RNVYENVAFALEVTGVPPR-EIRKRV------------------PAALELVGLS--------------HK------HRAL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 381 RRGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLaHISEYTILVsllqpAPETYDLFDD----II 456
Cdd:cd03292 134 PAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVV-----ATHAKELVDTtrhrVI 207
|
....*..
gi 1002313595 457 IMGEGKV 463
Cdd:cd03292 208 ALERGKL 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
220-468 |
1.94e-09 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 59.89 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 220 HHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVPAKT------SAYVSQ 293
Cdd:cd03256 9 TYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT---SGSVLIDGTDINKLKGKALrqlrrqIGMIFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 294 -YDLhVADMTVRETLdFSARFQGVGSRAEIMKAVIKREKEAGItpdpdidaymkaismEGLQRSmqtdyimkimGLDKCA 372
Cdd:cd03256 86 qFNL-IERLSVLENV-LSGRLGRRSTWRSLFGLFPKEEKQRAL---------------AALERV----------GLLDKA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 373 DVKVGNamrrgISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILVSLLQPapetyDL- 451
Cdd:cd03256 139 YQRADQ-----LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQV-----DLa 208
|
250 260
....*....|....*....|
gi 1002313595 452 ---FDDIIIMGEGKVVYHGP 468
Cdd:cd03256 209 reyADRIVGLKDGRIVFDGP 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
217-462 |
1.96e-09 |
|
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: 58.35 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 217 GFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrLNKslKETGEIEYNGV---KLDEFVPA--KTSAYV 291
Cdd:cd03229 5 NVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAG-LEE--PDSGSILIDGEdltDLEDELPPlrRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 292 SQYDLHVADMTVRETLDFsarfqgvgsraeimkavikrekeagitpdpdidaymkaismeglqrsmqtdyimkimgldkc 371
Cdd:cd03229 82 FQDFALFPHLTVLENIAL-------------------------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 372 advkvgnamrrGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILVSLLQPApETYDL 451
Cdd:cd03229 100 -----------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLD-EAARL 167
|
250
....*....|.
gi 1002313595 452 FDDIIIMGEGK 462
Cdd:cd03229 168 ADRVVVLRDGK 178
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
903-1089 |
1.98e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 59.76 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 903 QLLRNITGAFQPGILSALMGVTGAGKTTLLDV--LAGRKTGGVIE-GDIRIGGYPKVQQTFSRIS------GYCEQNDVH 973
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinLLEQPEAGTIRvGDITIDTARSLSQQKGLIRqlrqhvGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 974 SPQITVGESVaysawLRLPAEIDTKTRKEFVDEVLEIIeldeirdALVGTPGVNG-----LSREQRKRLTIAVELVSNPS 1048
Cdd:PRK11264 97 FPHRTVLENI-----IEGPVIVKGEPKEEATARARELL-------AKVGLAGKETsyprrLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1002313595 1049 IVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPS 1089
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
919-1113 |
2.36e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.86 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 919 ALMGVTGAGKTTLL---DVLAGRKTGGVIEGDIRIGG----YPKVQQT-FSRISGYCEQNDVHSPQITVGESVA----YS 986
Cdd:PRK14267 34 ALMGPSGCGKSTLLrtfNRLLELNEEARVEGEVRLFGrniySPDVDPIeVRREVGMVFQYPNPFPHLTIYDNVAigvkLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 987 AWLRLPAEIDtktrkEFVDEVLEIIEL-DEIRDALVGTPGvnGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAA 1065
Cdd:PRK14267 114 GLVKSKKELD-----ERVEWALKKAALwDEVKDRLNDYPS--NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTA 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002313595 1066 IAMRAVKNVaETGRTVVCTIHQPS----IEIFEAFDELmlikrgGELIYAGP 1113
Cdd:PRK14267 187 KIEELLFEL-KKEYTIVLVTHSPAqaarVSDYVAFLYL------GKLIEVGP 231
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
224-467 |
2.41e-09 |
|
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: 58.77 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 224 KVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVPA--KTSAYVSqYDLHVADM 301
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD---SGEITFDGKSYQKNIEAlrRIGALIE-APGFYPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 302 TVRETLDFSARFQGVgsraeimkavikREKEAgitpdpdidaymkaismeglqrsmqtDYIMKIMGLDKCADVKVGnamr 381
Cdd:cd03268 88 TARENLRLLARLLGI------------RKKRI--------------------------DEVLDVVGLKDSAKKKVK---- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 382 rGISGGeMK-RLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHiSEYTILVS--LLQpapETYDLFDDIIIM 458
Cdd:cd03268 126 -GFSLG-MKqRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISshLLS---EIQKVADRIGII 199
|
....*....
gi 1002313595 459 GEGKVVYHG 467
Cdd:cd03268 200 NKGKLIEEG 208
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
901-1060 |
2.44e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.00 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 901 KLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGgvIEGDIRIGGyPKVQQTFS----RISGYCEQNDVHSPQ 976
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP--AHGHVWLDG-EHIQHYASkevaRRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 977 ITVGESVAYSAWLRLPaeIDTKTRKEFVDEVLEIIELDEIRDalVGTPGVNGLSREQRKRLTIAVELVSNPSIVFMDEPT 1056
Cdd:PRK10253 96 ITVQELVARGRYPHQP--LFTRWRKEDEEAVTKAMQATGITH--LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
....
gi 1002313595 1057 SGLD 1060
Cdd:PRK10253 172 TWLD 175
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
905-1060 |
2.63e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.57 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGYPkvqQTF-----SRISG----YCEQNDVh 973
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGvyQPD----SGEILLDGEP---VRFrsprdAQAAGiaiiHQELNLV- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 974 sPQITVGESVAYSAWLRLPAEIDTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMD 1053
Cdd:COG1129 92 -PNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGD-----LSVAQQQLVEIARALSRDARVLILD 165
|
....*..
gi 1002313595 1054 EPTSGLD 1060
Cdd:COG1129 166 EPTASLT 172
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
225-429 |
2.93e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 59.49 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 225 VQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEfvPAKTSAYVSQYDLHVADMTVR 304
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS---SGEITLDGVPVTG--PGADRGVVFQKDALLPWLNVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 305 ETLDFSARFQGVGsRAEimkavikREKEAgitpdpdidaymkaismeglqrsmqtDYIMKIMGLDkcadvKVGNAMRRGI 384
Cdd:COG4525 95 DNVAFGLRLRGVP-KAE-------RRARA--------------------------EELLALVGLA-----DFARRRIWQL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1002313595 385 SGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIvsclQQL 429
Cdd:COG4525 136 SGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQM----QEL 176
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
226-471 |
3.73e-09 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 58.79 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 226 QILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRlnkslkET---GEIEYNGVKLDEFVPAK-TSAYVSQ-YDL--Hv 298
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF------ETptsGEILLDGKDITNLPPHKrPVNTVFQnYALfpH- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 299 adMTVRETLDFSARFQGVGsraeimKAVIKREkeagitpdpdIDAYMKAISMEGLqrsmqtdyimkimgldkcadvkvGN 378
Cdd:cd03300 87 --LTVFENIAFGLRLKKLP------KAEIKER----------VAEALDLVQLEGY-----------------------AN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 379 AMRRGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYT-ILVSLLQpaPETYDLFDDIII 457
Cdd:cd03300 126 RKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITfVFVTHDQ--EEALTMSDRIAV 203
|
250 260
....*....|....*....|..
gi 1002313595 458 MGEGKV--------VYHGPKNL 471
Cdd:cd03300 204 MNKGKIqqigtpeeIYEEPANR 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
225-471 |
4.53e-09 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 60.11 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 225 VQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAG--RLnkslkETGEIEYNGVKLDEFVPAKTS-AYVSQ-YDL--Hv 298
Cdd:COG3842 18 VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfeTP-----DSGRILLDGRDVTGLPPEKRNvGMVFQdYALfpH- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 299 adMTVRETLDFSARFQGVgSRAEIMKAVikreKEAgitpdpdidaymkaismeglqrsmqtdyiMKIMGLDKCADVKVGN 378
Cdd:COG3842 92 --LTVAENVAFGLRMRGV-PKAEIRARV----AEL-----------------------------LELVGLEGLADRYPHQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 379 amrrgISGGEMKR------LttgemIVGPcKVLLMDEISTGLD----SSTTFQIVScLQQLAHISeyTILVsllqpapeT 448
Cdd:COG3842 136 -----LSGGQQQRvalaraL-----APEP-RVLLLDEPLSALDaklrEEMREELRR-LQRELGIT--FIYV--------T 193
|
250 260 270
....*....|....*....|....*....|....*..
gi 1002313595 449 YD------LFDDIIIMGEGKV--------VYHGPKNL 471
Cdd:COG3842 194 HDqeealaLADRIAVMNDGRIeqvgtpeeIYERPATR 230
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
877-1105 |
4.64e-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: 57.86 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 877 ISFQDVNYYVDTPPEMRKKgymgrklqLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIEGDIRIggyp 954
Cdd:cd03250 1 ISVEDASFTWDSGEQETSF--------TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGelEKLSGSVSVPGSI---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 955 kvqqtfsrisGYCEQndvhSPQI---TVGESVAYSawlrlpAEIDtktrKEFVDEVLEIIELDEIRDAL-------VGTP 1024
Cdd:cd03250 69 ----------AYVSQ----EPWIqngTIRENILFG------KPFD----EERYEKVIKACALEPDLEILpdgdlteIGEK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1025 GVNgLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDAraaaiamravkNVAET------------GRTVVCTIHQpsIEI 1092
Cdd:cd03250 125 GIN-LSGGQKQRISLARAVYSDADIYLLDDPLSAVDA-----------HVGRHifencilglllnNKTRILVTHQ--LQL 190
|
250
....*....|...
gi 1002313595 1093 FEAFDELMLIKRG 1105
Cdd:cd03250 191 LPHADQIVVLDNG 203
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
226-469 |
5.08e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 59.78 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 226 QILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrLnkslkET---GEIEYNGVKLDEFVPAKTS--AYVSQ-YDL--H 297
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAG-L-----ETpdsGRIVLNGRDLFTNLPPRERrvGFVFQhYALfpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 298 vadMTVRETLDFSARFQGVgSRAEImkavikREKeagitpdpdIDAYMKAISMEGLqrsmqtdyimkimgldkcADVKVG 377
Cdd:COG1118 90 ---MTVAENIAFGLRVRPP-SKAEI------RAR---------VEELLELVQLEGL------------------ADRYPS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 378 NamrrgISGGEMKR------LttgemIVGPcKVLLMDEISTGLDSSTTFQIVSCLQQLaHiSEY---TILVS--LLqpap 446
Cdd:COG1118 133 Q-----LSGGQRQRvalaraL-----AVEP-EVLLLDEPFGALDAKVRKELRRWLRRL-H-DELggtTVFVThdQE---- 195
|
250 260
....*....|....*....|...
gi 1002313595 447 ETYDLFDDIIIMGEGKVVYHGPK 469
Cdd:COG1118 196 EALELADRVVVMNQGRIEQVGTP 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
905-1105 |
5.14e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.94 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGviEGDIRIGGYPKVQQTFSRisGYCEQNDVHSPQITVGESVA 984
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ--HGSITLDGKPVEGPGAER--GVVFQNEGLLPWRNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 985 YSawLRLpAEIDTKTRKEFVDEVLEIIELDEirdalVGTPGVNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAA 1064
Cdd:PRK11248 93 FG--LQL-AGVEKMQRLEIAHQMLKKVGLEG-----AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1002313595 1065 AIAMRAVKNV-AETGRTVVCTIHQPSIEIFEAfDELMLIKRG 1105
Cdd:PRK11248 165 EQMQTLLLKLwQETGKQVLLITHDIEEAVFMA-TELVLLSPG 205
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
226-468 |
5.26e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 58.63 E-value: 5.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 226 QILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVP---AKTSAYVSQYDLHVADMT 302
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD---SGEVRLNGRPLADWSPaelARRRAVLPQHSSLSFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 303 VRETldfsarfqgVGSRAEIMKAVIKREKEAgitpdpdIDAYMKAISMEGL-QRSMQTdyimkimgldkcadvkvgnamr 381
Cdd:PRK13548 93 VEEV---------VAMGRAPHGLSRAEDDAL-------VAAALAQVDLAHLaGRDYPQ---------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 382 rgISGGEMKR------LTTGEMIVGPCKVLLMDEISTGLDSS---TTFQIvscLQQLAHISEYTILVSLlqpapetYDL- 451
Cdd:PRK13548 135 --LSGGEQQRvqlarvLAQLWEPDGPPRWLLLDEPTSALDLAhqhHVLRL---ARQLAHERGLAVIVVL-------HDLn 202
|
250 260
....*....|....*....|..
gi 1002313595 452 -----FDDIIIMGEGKVVYHGP 468
Cdd:PRK13548 203 laaryADRIVLLHQGRLVADGT 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
915-1113 |
5.54e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 60.24 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 915 GILSALMGVTGAGKTTLLDVLAGRKTGGVieGDIRIGGYPkVQQTFSRISGyceQNDVHSPQITvgeSVAYSAWLRLPAE 994
Cdd:PRK09536 29 GSLVGLVGPNGAGKTTLLRAINGTLTPTA--GTVLVAGDD-VEALSARAAS---RRVASVPQDT---SLSFEFDVRQVVE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 995 ID-----------TKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARA 1063
Cdd:PRK09536 100 MGrtphrsrfdtwTETDRAAVERAMERTGVAQFADRPVTS-----LSGGERQRVLLARALAQATPVLLLDEPTASLDINH 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002313595 1064 AAIAMRAVKNVAETGRTVVCTIHqpSIEIFEAF-DELMLIKRGGeLIYAGP 1113
Cdd:PRK09536 175 QVRTLELVRRLVDDGKTAVAAIH--DLDLAARYcDELVLLADGR-VRAAGP 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
903-1060 |
6.44e-09 |
|
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: 57.54 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 903 QLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGVIEGDIRIGGypkvqqtfsrisgyceqNDVhsPQITVGES 982
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKG-----------------EDI--TDLPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 983 VA---YSAWLRlPAEIDTKTRKEFVDEVLEiieldeirdalvgtpgvnGLSREQRKRLTIAVELVSNPSIVFMDEPTSGL 1059
Cdd:cd03217 75 ARlgiFLAFQY-PPEIPGVKNADFLRYVNE------------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
.
gi 1002313595 1060 D 1060
Cdd:cd03217 136 D 136
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
226-471 |
7.34e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 59.58 E-value: 7.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 226 QILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrlnksLKE--TGEIEYNGVKLDEfVPAK-----TsayVSQ-YDL- 296
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAG-----FETpdSGRIMLDGQDITH-VPAEnrhvnT---VFQsYALf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 297 -HvadMTVRETLDFSARFQGVgSRAEIMKAVikrekeagitpdpdidaymkaisMEGLqrsmqtdyimKIMGLDKCADVK 375
Cdd:PRK09452 99 pH---MTVFENVAFGLRMQKT-PAAEITPRV-----------------------MEAL----------RMVQLEEFAQRK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 376 VgnamrRGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYT-ILVSLLQpaPETYDLFDD 454
Cdd:PRK09452 142 P-----HQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITfVFVTHDQ--EEALTMSDR 214
|
250 260
....*....|....*....|....*
gi 1002313595 455 IIIMGEGKV--------VYHGPKNL 471
Cdd:PRK09452 215 IVVMRDGRIeqdgtpreIYEEPKNL 239
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
899-1086 |
7.81e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 58.24 E-value: 7.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 899 GRKlQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGviEGDIRIGGYPKVQ---QTFSRISGYCEQNDVHSP 975
Cdd:PRK13548 13 GGR-TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD--SGEVRLNGRPLADwspAELARRRAVLPQHSSLSF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 976 QITVGESVAYSawlRLPAEIDTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELV------SNPSI 1049
Cdd:PRK13548 90 PFTVEEVVAMG---RAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQ-----LSGGEQQRVQLARVLAqlwepdGPPRW 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002313595 1050 VFMDEPTSGLDARAAAIAMRAVKNVA-ETGRTVVCTIH 1086
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLH 199
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
920-1088 |
7.84e-09 |
|
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: 57.12 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 920 LMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGYPKVQQTFSRISG--YCEQNDVHSPQITVGESVAYsaWLRLPAEi 995
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGlsPPL----AGRVLLNGGPLDFQRDSIARGllYLGHAPGIKTTLSVLENLRF--WHADHSD- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 996 dtktrkEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVA 1075
Cdd:cd03231 104 ------EQVEEALARVGLNGFEDRPVAQ-----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHC 172
|
170
....*....|...
gi 1002313595 1076 ETGRTVVCTIHQP 1088
Cdd:cd03231 173 ARGGMVVLTTHQD 185
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
905-1105 |
9.74e-09 |
|
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: 55.90 E-value: 9.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAGrktggVI---EGDIRIGGYPkvqQTFsrisgyceqndvHSPQitvge 981
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSG-----LYkpdSGEILVDGKE---VSF------------ASPR----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 982 svaysawlrlpaeidtktrkefvdevleiieldEIRDALVGTpgVNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDA 1061
Cdd:cd03216 71 ---------------------------------DARRAGIAM--VYQLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1002313595 1062 RAAAIAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMLIKRG 1105
Cdd:cd03216 116 AEVERLFKVIRRLRAQGVAVIFISHRLD-EVFEIADRVTVLRDG 158
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
919-1087 |
1.10e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 58.28 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 919 ALMGVTGAGKTTLLdvlagRKTGGVIE---GDIRIGGYPKVQQTFSRIS---GYCEQN---DVHSPqiTVGESVAYSAwl 989
Cdd:PRK13652 34 AVIGPNGAGKSTLF-----RHFNGILKptsGSVLIRGEPITKENIREVRkfvGLVFQNpddQIFSP--TVEQDIAFGP-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 990 rLPAEIDTKTRKEFVDEVLEIIELDEIRDALVgtpgvNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMR 1069
Cdd:PRK13652 105 -INLGLDEETVAHRVSSALHMLGLEELRDRVP-----HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELID 178
|
170
....*....|....*....
gi 1002313595 1070 AVKNVAET-GRTVVCTIHQ 1087
Cdd:PRK13652 179 FLNDLPETyGMTVIFSTHQ 197
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
897-1060 |
1.17e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 58.94 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 897 YMGRKlQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGviEGDIRIGGypkvqQTFSRIS------GYCEQN 970
Cdd:PRK10851 11 SFGRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT--SGHIRFHG-----TDVSRLHardrkvGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 971 DVHSPQITVGESVAYSawLR-LP-------AEIDTKtrkefVDEVLEIIELDEIRDALvgtPgvNGLSREQRKRLTIAVE 1042
Cdd:PRK10851 83 YALFRHMTVFDNIAFG--LTvLPrrerpnaAAIKAK-----VTQLLEMVQLAHLADRY---P--AQLSGGQKQRVALARA 150
|
170
....*....|....*...
gi 1002313595 1043 LVSNPSIVFMDEPTSGLD 1060
Cdd:PRK10851 151 LAVEPQILLLDEPFGALD 168
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
240-468 |
1.23e-08 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 58.58 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 240 ITLLLGPPGCGKTTLLKALAG--RLNKslketGEIEYNGVKLDE-----FVPAKTSA--YVSQYDLHVADMTVRETLDFS 310
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGltRPDE-----GEIVLNGRTLFDsrkgiFLPPEKRRigYVFQEARLFPHLSVRGNLRYG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 311 ARFqgvgSRAEimkavikrekeagitpdpdidaymkaismeglQRSMQTDYIMKIMGLDKCADVKVGNamrrgISGGEMK 390
Cdd:TIGR02142 100 MKR----ARPS--------------------------------ERRISFERVIELLGIGHLLGRLPGR-----LSGGEKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 391 RLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQL-AHISEYTILVS-LLQpapETYDLFDDIIIMGEGKVVYHGP 468
Cdd:TIGR02142 139 RVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLhAEFGIPILYVShSLQ---EVLRLADRVVVLEDGRVAAAGP 215
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
873-1060 |
1.24e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 59.45 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 873 TPLTISFQDVNYyvdtppemrkkGYMGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAgrKTGGVIEGDIRIGG 952
Cdd:PRK11160 335 DQVSLTLNNVSF-----------TYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT--RAWDPQQGEILLNG 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 953 YPkvqqtfsrISGYCEQnDVHSPQITVGESV-AYSAWLR--LPAEIDTKTRKEFVdEVLEIIELDEIrdaLVGTPGVNG- 1028
Cdd:PRK11160 402 QP--------IADYSEA-ALRQAISVVSQRVhLFSATLRdnLLLAAPNASDEALI-EVLQQVGLEKL---LEDDKGLNAw 468
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002313595 1029 -------LSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:PRK11160 469 lgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
905-1060 |
1.42e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 58.58 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAF-------------QPGILSALMGVTGAGKTTLLDVLAGRKTGgvIEGDIRIGGYpkvQQTFSRIsgycEQND 971
Cdd:PRK11432 9 LKNITKRFgsntvidnlnltiKQGTMVTLLGPSGCGKTTVLRLVAGLEKP--TEGQIFIDGE---DVTHRSI----QQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 972 V----HS----PQITVGESVAYS-AWLRLPAEidtkTRKEFVDEVLEIIELDEIRDALVgtpgvNGLSREQRKRLTIAVE 1042
Cdd:PRK11432 80 IcmvfQSyalfPHMSLGENVGYGlKMLGVPKE----ERKQRVKEALELVDLAGFEDRYV-----DQISGGQQQRVALARA 150
|
170
....*....|....*...
gi 1002313595 1043 LVSNPSIVFMDEPTSGLD 1060
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLD 168
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
895-1105 |
1.49e-08 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 57.53 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 895 KGYMGRKLqlLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKT--GGVIEGDIRIGGYPKV-------QQTFSRIS- 964
Cdd:TIGR02323 11 KSYGGGKG--CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLApdHGTATYIMRSGAELELyqlseaeRRRLMRTEw 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 965 GYCEQN--DVHSPQITVGESVAySAWLRLPAEIDTKTRKEFVDEvLEIIELDEIR-DALVGTpgvngLSREQRKRLTIAV 1041
Cdd:TIGR02323 89 GFVHQNprDGLRMRVSAGANIG-ERLMAIGARHYGNIRATAQDW-LEEVEIDPTRiDDLPRA-----FSGGMQQRLQIAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002313595 1042 ELVSNPSIVFMDEPTSGLDARAAAIAMRAVKN-VAETGRTVVCTIHQPSIEIFEAfDELMLIKRG 1105
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGlVRDLGLAVIIVTHDLGVARLLA-QRLLVMQQG 225
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
903-1060 |
1.54e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 57.00 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 903 QLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGVIEGDIRIGG---------------------YPkvqqtfS 961
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTSGSILLDGedilelspderaragiflafqYP------V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 962 RISGyceqndvhspqITVGE--SVAYSAwlRLPAEIDTKTRKEFVDEVLEIIELDEirDALvgTPGVN-GLSREQRKRLT 1038
Cdd:COG0396 88 EIPG-----------VSVSNflRTALNA--RRGEELSAREFLKLLKEKMKELGLDE--DFL--DRYVNeGFSGGEKKRNE 150
|
170 180
....*....|....*....|..
gi 1002313595 1039 IAVELVSNPSIVFMDEPTSGLD 1060
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLD 172
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
905-1060 |
1.68e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.17 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAGrktggVI---EGDIRIGGY-P-KVQQTFSRisgyceqndvhspQITV 979
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTG-----ILvptSGEVRVLGYvPfKRRKEFAR-------------RIGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 980 --G------------ESvaysawLRLPAEI---DTKTRKEFVDEVLEIIELDEIRDalvgTPgVNGLSREQRKRLTIAVE 1042
Cdd:COG4586 100 vfGqrsqlwwdlpaiDS------FRLLKAIyriPDAEYKKRLDELVELLDLGELLD----TP-VRQLSLGQRMRCELAAA 168
|
170
....*....|....*...
gi 1002313595 1043 LVSNPSIVFMDEPTSGLD 1060
Cdd:COG4586 169 LLHRPKILFLDEPTIGLD 186
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
868-1082 |
1.74e-08 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 56.67 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 868 MALPFTPLtISFQDVNYYVDTPpemrkkgymGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTggviE 945
Cdd:COG4181 1 MSSSSAPI-IELRGLTKTVGTG---------AGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGldRPT----S 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 946 GDIRIGGYPK------------------VQQTFSRIsgyceqndvhsPQITVGESVAysawlrLPAEI----DTKTRKEf 1003
Cdd:COG4181 67 GTVRLAGQDLfaldedararlrarhvgfVFQSFQLL-----------PTLTALENVM------LPLELagrrDARARAR- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1004 vdEVLEIIELDEIRDALvgtPGvnGLS-REQRkRLTIAVELVSNPSIVFMDEPTSGLDaraaaiamravknvAETGRTVV 1082
Cdd:COG4181 129 --ALLERVGLGHRLDHY---PA--QLSgGEQQ-RVALARAFATEPAILFADEPTGNLD--------------AATGEQII 186
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
920-1060 |
2.13e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 58.03 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 920 LMGVTGAGKTTLLDVLAGRKTggVIEGDIRIGGypkvqQTFSRISGycEQNDVHS--------PQITVGESVAYSawLRL 991
Cdd:PRK09452 45 LLGPSGCGKTTVLRLIAGFET--PDSGRIMLDG-----QDITHVPA--ENRHVNTvfqsyalfPHMTVFENVAFG--LRM 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002313595 992 ---PAEiDTKTRkefVDEVLEIIELDEIrdalvGTPGVNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:PRK09452 114 qktPAA-EITPR---VMEALRMVQLEEF-----AQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
235-468 |
2.48e-08 |
|
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: 57.80 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 235 IKPSRITLLLGPPGCGKTTLLKALAGrLNKSlkETGEIEYNG-VKLDE----FVPA-KTS-AYVSQYDL---HvadMTVR 304
Cdd:COG4148 22 LPGRGVTALFGPSGSGKTTLLRAIAG-LERP--DSGRIRLGGeVLQDSargiFLPPhRRRiGYVFQEARlfpH---LSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 305 ETLDFSARFQGVGSRAEIMKAVIKRekeAGITPDpdidaymkaismegLQRSMQTdyimkimgldkcadvkvgnamrrgI 384
Cdd:COG4148 96 GNLLYGRKRAPRAERRISFDEVVEL---LGIGHL--------------LDRRPAT------------------------L 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 385 SGGEMKR-------LTtgemivGPcKVLLMDEISTGLDSSTTFQIVSCLQQLAHisEYTI---LVSllqPAP-ETYDLFD 453
Cdd:COG4148 135 SGGERQRvaigralLS------SP-RLLLMDEPLAALDLARKAEILPYLERLRD--ELDIpilYVS---HSLdEVARLAD 202
|
250
....*....|....*
gi 1002313595 454 DIIIMGEGKVVYHGP 468
Cdd:COG4148 203 HVVLLEQGRVVASGP 217
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
903-1113 |
2.60e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 57.05 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 903 QLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTggVIEGDIRIGG---YPKVQQTFSRISGYCEQN-DVHSPQIT 978
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYL--PQRGRVKVMGrevNAENEKWVRSKVGLVFQDpDDQVFSST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 979 VGESVAYSAW-LRL-PAEIDTKtrkefVDEVLEIIELDEIRDAlvgTPgvNGLSREQRKRLTIAVELVSNPSIVFMDEPT 1056
Cdd:PRK13647 97 VWDDVAFGPVnMGLdKDEVERR-----VEEALKAVRMWDFRDK---PP--YHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002313595 1057 SGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSIEIfEAFDELMLIKRGGELIYAGP 1113
Cdd:PRK13647 167 AYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVLKEGRVLAEGDK 222
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
877-1105 |
2.83e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.49 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 877 ISFQDVNYYvdtppemrkkgYMGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAgrKTGGVIEGDIRIGGYPKV 956
Cdd:PRK11176 342 IEFRNVTFT-----------YPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLT--RFYDIDEGEILLDGHDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 957 QQTFSRISGYC---EQNdVHSPQITVGESVAYSA---WLRlpAEIDTKTRKEFVDEVleIIELDEIRDALVGTPGVNgLS 1030
Cdd:PRK11176 409 DYTLASLRNQValvSQN-VHLFNDTIANNIAYARteqYSR--EQIEEAARMAYAMDF--INKMDNGLDTVIGENGVL-LS 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002313595 1031 REQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAV----KNvaetgRTVVCTIHQPSieIFEAFDELMLIKRG 1105
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALdelqKN-----RTSLVIAHRLS--TIEKADEILVVEDG 554
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
226-471 |
3.35e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.19 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 226 QILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSLKEtGEIEYNGVKLDEFVPAKTS------AYvsQYDLHVA 299
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILE-GDILFKGESILDLEPEERAhlgiflAF--QYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 300 dmtvretldfsarfqGVgSRAEIMKAVIK-REKEAGitpDPDIDAymkaisMEGLQrsmqtdYIMKIMGLDKCADVKVGN 378
Cdd:CHL00131 98 ---------------GV-SNADFLRLAYNsKRKFQG---LPELDP------LEFLE------IINEKLKLVGMDPSFLSR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 379 AMRRGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILVSLLQpapetyDLFDDII-- 456
Cdd:CHL00131 147 NVNEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQ------RLLDYIKpd 220
|
250
....*....|....*...
gi 1002313595 457 ---IMGEGKVVYHGPKNL 471
Cdd:CHL00131 221 yvhVMQNGKIIKTGDAEL 238
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
905-1086 |
3.87e-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: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDvLAGRKTgGVIEGDIRIGGYPkVQQTFS-----RISGYCEQNDVHSpQITV 979
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLS-MISRLL-PPDSGEVLVDGLD-VATTPSrelakRLAILRQENHINS-RLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 980 GESVA-----YSAWlRLPAEiDtktrKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDE 1054
Cdd:COG4604 93 RELVAfgrfpYSKG-RLTAE-D----REIIDEAIAYLDLEDLADRYLDE-----LSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190
....*....|....*....|....*....|...
gi 1002313595 1055 PTSGLDARAAAIAMRAVKNVA-ETGRTVVCTIH 1086
Cdd:COG4604 162 PLNNLDMKHSVQMMKLLRRLAdELGKTVVIVLH 194
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
904-1115 |
4.24e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.37 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 904 LLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGV------IEGDIRIGGYPKVQ---QTFSRISGYCEQNDVHS 974
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarVTGDVTLNGEPLAAidaPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 975 PQITVGESVAYSAW--LRLPAEIDTKTRkEFVDEVLEIIELDEIRDALVGTPGVNGLSREQRKR----LTIAVELVSNPS 1048
Cdd:PRK13547 96 FAFSAREIVLLGRYphARRAGALTHRDG-EIAWQALALAGATALVGRDVTTLSGGELARVQFARvlaqLWPPHDAAQPPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002313595 1049 IVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTI-HQPSIEIFEAfDELMLIKRGGELIYAGPLG 1115
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIvHDPNLAARHA-DRIAMLADGAIVAHGAPAD 241
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
227-462 |
4.32e-08 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 55.17 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 227 ILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGvkldefvpakTSAYVSQYDLHVaDMTVRET 306
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKL---SGSVSVPG----------SIAYVSQEPWIQ-NGTIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 307 LDFSARFqgvgsraeimkavikrekeagitpdpDIDAYMKAISMEGLQRsmqtDyiMKIM-GLDKcadVKVGNamrRGI- 384
Cdd:cd03250 86 ILFGKPF--------------------------DEERYEKVIKACALEP----D--LEILpDGDL---TEIGE---KGIn 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 385 -SGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIV-SCLQQLAHISEYTILV----SLLQPApetydlfDDIIIM 458
Cdd:cd03250 128 lSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVthqlQLLPHA-------DQIVVL 200
|
....
gi 1002313595 459 GEGK 462
Cdd:cd03250 201 DNGR 204
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
901-1060 |
4.58e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.56 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 901 KLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGviEGDIRIGGYPKVQ-------QTFSRISGYCEQNDVH 973
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGS--SGEVSLVGQPLHQmdeearaKLRAKHVGFVFQSFML 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 974 SPQITVGESVAYSAWLRlpAEIDTKTRKEFVdEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMD 1053
Cdd:PRK10584 100 IPTLNALENVELPALLR--GESSRQSRNGAK-ALLEQLGLGKRLDHLPAQ-----LSGGEQQRVALARAFNGRPDVLFAD 171
|
....*..
gi 1002313595 1054 EPTSGLD 1060
Cdd:PRK10584 172 EPTGNLD 178
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
876-1112 |
4.80e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 57.66 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 876 TISFQDVNYyvdtppemrkkGYMGRKlQLLRNITGAFQPGILSALMGVTGAGKTTLLDVL-------AGRKTggvIEG-D 947
Cdd:PRK13657 334 AVEFDDVSF-----------SYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRIL---IDGtD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 948 IR----------IGgypKVQQT---FSR-IsgycEQNdvhspqITVGESVAYSAWLRLPAEIDtktrkefvdEVLEIIEL 1013
Cdd:PRK13657 399 IRtvtraslrrnIA---VVFQDaglFNRsI----EDN------IRVGRPDATDEEMRAAAERA---------QAHDFIER 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1014 DEIR-DALVGTPGvNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAEtGRTVVCTIHQPS--- 1089
Cdd:PRK13657 457 KPDGyDTVVGERG-RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHRLStvr 534
|
250 260 270
....*....|....*....|....*....|....*...
gi 1002313595 1090 ----IEIFEA--------FDElmLIKRGG---ELIYAG 1112
Cdd:PRK13657 535 nadrILVFDNgrvvesgsFDE--LVARGGrfaALLRAQ 570
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
877-1105 |
5.61e-08 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 54.24 E-value: 5.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 877 ISFQDVNYyvdtppemrkkGYMGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLdvlagrktgGVIEGDIriggypkv 956
Cdd:cd03247 1 LSINNVSF-----------SYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLL---------QLLTGDL-------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 957 qqtfsrisgyceqnDVHSPQITVGESvaysawlrlPAEIDTKTRKEFVDEVLEIIEL--DEIRDALvGTPgvngLSREQR 1034
Cdd:cd03247 53 --------------KPQQGEITLDGV---------PVSDLEKALSSLISVLNQRPYLfdTTLRNNL-GRR----FSGGER 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002313595 1035 KRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAEtGRTVVCTIHQpsIEIFEAFDELMLIKRG 1105
Cdd:cd03247 105 QRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHH--LTGIEHMDKILFLENG 172
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
225-467 |
5.68e-08 |
|
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: 54.98 E-value: 5.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 225 VQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLnksLKETGEIEYNGVKLDeFVPAKTSAYVSQYDLHVADMTVR 304
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGII---LPDSGEVLFDGKPLD-IAARNRIGYLPEERGLYPKMKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 305 ETLDFSARFQGVgSRAEIMKavikrekeagitpdpdidaymkaismeglqrsmQTDYIMKIMGLDKCADVKVgnamrRGI 384
Cdd:cd03269 89 DQLVYLAQLKGL-KKEEARR---------------------------------RIDEWLERLELSEYANKRV-----EEL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 385 SGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHiSEYTILVSLLQPApETYDLFDDIIIMGEGKVV 464
Cdd:cd03269 130 SKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQME-LVEELCDRVLLLNKGRAV 207
|
...
gi 1002313595 465 YHG 467
Cdd:cd03269 208 LYG 210
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
904-1105 |
5.85e-08 |
|
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: 55.69 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 904 LLRNITGAFQPGILSALMGVTGAGKTTL-------LDVLAGRKtggVIEGdIRIGGYPkVQQTFSRISgyceqndvhspq 976
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKI---VIDG-IDISKLP-LHTLRSRLS------------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 977 ITVGESVAYSAWLRLPAEIDTKTRKEFVDEVLEIIELDEIRDALVG------TPGVNGLSREQRKRLTIAVELVSNPSIV 1050
Cdd:cd03288 99 IILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGgldavvTEGGENFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002313595 1051 FMDEPTSGLDARAAAIAMRAVKnVAETGRTVVCTIHQPSiEIFEAfDELMLIKRG 1105
Cdd:cd03288 179 IMDEATASIDMATENILQKVVM-TAFADRTVVTIAHRVS-TILDA-DLVLVLSRG 230
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
914-1060 |
7.09e-08 |
|
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: 56.26 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 914 PGIlSALMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGYPkVQQTFSRIS--------GYCEQNDVHSPQITVGESV 983
Cdd:COG4148 25 RGV-TALFGPSGSGKTTLLRAIAGleRPD----SGRIRLGGEV-LQDSARGIFlpphrrriGYVFQEARLFPHLSVRGNL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002313595 984 AYSAWlRLPAEidtkTRKEFVDEVleiIELDEIRDALVGTPGvnGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:COG4148 99 LYGRK-RAPRA----ERRISFDEV---VELLGIGHLLDRRPA--TLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
907-1087 |
7.35e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 57.72 E-value: 7.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 907 NITgaFQPGILSALMGVTGAGKTTLLDVLAG---RKTGGVIEG--DIRIGgYPKVQQTFsrisGYCEQNDVHSPQITVGE 981
Cdd:TIGR01257 950 NIT--FYENQITAFLGHNGAGKTTTLSILTGllpPTSGTVLVGgkDIETN-LDAVRQSL----GMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 982 SVAYSAWLRLPAEIDTKTRKEFV--DEVLEIIELDEIRDalvgtpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGL 1059
Cdd:TIGR01257 1023 HILFYAQLKGRSWEEAQLEMEAMleDTGLHHKRNEEAQD----------LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180
....*....|....*....|....*...
gi 1002313595 1060 DARAAAIAMRAVKNVaETGRTVVCTIHQ 1087
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKY-RSGRTIIMSTHH 1119
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
902-1060 |
7.77e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.46 E-value: 7.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 902 LQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGgvieGDIRIGGYPKVQQTFSRISGYceQNDVH------ 973
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGleSPSQ----GNVSWRGEPLAKLNRAQRKAF--RRDIQmvfqds 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 974 ----SPQITVGESVAYSawLRLPAEIDTKTRKEFVDEVLEIIELD-EIRDALvgtPGvnGLSREQRKRLTIAVELVSNPS 1048
Cdd:PRK10419 99 isavNPRKTVREIIREP--LRHLLSLDKAERLARASEMLRAVDLDdSVLDKR---PP--QLSGGQLQRVCLARALAVEPK 171
|
170
....*....|..
gi 1002313595 1049 IVFMDEPTSGLD 1060
Cdd:PRK10419 172 LLILDEAVSNLD 183
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
224-476 |
8.07e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 56.27 E-value: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 224 KVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGvkldEFVpakTSAYVSQYDL------- 296
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPT---EGQIFIDG----EDV---THRSIQQRDIcmvfqsy 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 297 ----HvadMTVRETLDFSARFQGVgSRAEIMKAVikreKEAgitpdpdidayMKAISMEGLQrsmqtdyimkimglDKCA 372
Cdd:PRK11432 88 alfpH---MSLGENVGYGLKMLGV-PKEERKQRV----KEA-----------LELVDLAGFE--------------DRYV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 373 DvkvgnamrrGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDS----STTFQIVSCLQQLAHISEYtilVSLLQpaPET 448
Cdd:PRK11432 135 D---------QISGGQQQRVALARALILKPKVLLFDEPLSNLDAnlrrSMREKIRELQQQFNITSLY---VTHDQ--SEA 200
|
250 260 270
....*....|....*....|....*....|....*.
gi 1002313595 449 YDLFDDIIIMGEGKVV--------YHGPKNLIMTFF 476
Cdd:PRK11432 201 FAVSDTVIVMNKGKIMqigspqelYRQPASRFMASF 236
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
216-467 |
8.09e-08 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 54.93 E-value: 8.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 216 LGFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAgRLNKSlkETGEIEYNGVKLDEFVPA---KTSAYVS 292
Cdd:cd03251 6 VTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIP-RFYDV--DSGRILIDGHDVRDYTLAslrRQIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 293 QyDLHVADMTVRETLDFSARfqGVgSRAEIMKAvikrekeagitpdpdidaymkaismegLQRSMQTDYIMKimgLDKCA 372
Cdd:cd03251 83 Q-DVFLFNDTVAENIAYGRP--GA-TREEVEEA---------------------------ARAANAHEFIME---LPEGY 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 373 DVKVGNamrRGI--SGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAhiSEYTILV-----SLLQPA 445
Cdd:cd03251 129 DTVIGE---RGVklSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLM--KNRTTFViahrlSTIENA 203
|
250 260
....*....|....*....|..
gi 1002313595 446 petydlfDDIIIMGEGKVVYHG 467
Cdd:cd03251 204 -------DRIVVLEDGKIVERG 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
877-1105 |
8.24e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.51 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 877 ISFQDVNY-YVDTPPemrkkgYMGRKLqllRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIE-GDIRIGG 952
Cdd:PRK13643 2 IKFEKVNYtYQPNSP------FASRAL---FDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllQPTEGKVTvGDIVVSS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 953 YPK---VQQTFSRISGYCEQNDVHSPQITVGESVAYSawlrlPAE--IDTKTRKEFVDEVLEIIELDeiRDALVGTPgvN 1027
Cdd:PRK13643 73 TSKqkeIKPVRKKVGVVFQFPESQLFEETVLKDVAFG-----PQNfgIPKEKAEKIAAEKLEMVGLA--DEFWEKSP--F 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002313595 1028 GLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMLIKRG 1105
Cdd:PRK13643 144 ELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMD-DVADYADYVYLLEKG 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
901-1059 |
8.48e-08 |
|
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: 54.60 E-value: 8.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 901 KLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIE-GDIRIGGYPkvqqTFSRIS---GYCEQNDVHS 974
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGllPPRSGSIRfDGEDITGLP----PHRIARlgiGYVPEGRRIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 975 PQITVGESvaysawLRLPAEI--DTKTRKEFVDEVLEII-ELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVF 1051
Cdd:COG0410 91 PSLTVEEN------LLLGAYArrDRAEVRADLERVYELFpRLKERRRQRAGT-----LSGGEQQMLAIGRALMSRPKLLL 159
|
....*...
gi 1002313595 1052 MDEPTSGL 1059
Cdd:COG0410 160 LDEPSLGL 167
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
227-474 |
1.07e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.83 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 227 ILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSLKE-----TGEIEYNGVKLDEFVP---AKTSAYVSQydlhv 298
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPrgarvTGDVTLNGEPLAAIDAprlARLRAVLPQ----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 299 admTVRETLDFSARfqgvgsraEI-MKAVIKREKEAGITPDPDIDAYMKAISMEGlqrsmqtdyimkimgldkcADVKVG 377
Cdd:PRK13547 91 ---AAQPAFAFSAR--------EIvLLGRYPHARRAGALTHRDGEIAWQALALAG-------------------ATALVG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 378 NAMRRgISGGEMKRLT----------TGEMIVGPcKVLLMDEISTGLDSSTTFQIVSCLQQLA---HISEYTILVSLLQP 444
Cdd:PRK13547 141 RDVTT-LSGGELARVQfarvlaqlwpPHDAAQPP-RYLLLDEPTAALDLAHQHRLLDTVRRLArdwNLGVLAIVHDPNLA 218
|
250 260 270
....*....|....*....|....*....|
gi 1002313595 445 APETydlfDDIIIMGEGKVVYHGPKNLIMT 474
Cdd:PRK13547 219 ARHA----DRIAMLADGAIVAHGAPADVLT 244
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
228-439 |
1.15e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 54.72 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 228 LENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNkslKETGEIEYNGVKLdefvpaktsAYVSQYDLHVADMTVRETL 307
Cdd:cd03237 15 LEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLK---PDEGDIEIELDTV---------SYKPQYIKADYEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 308 dfsarfqgvgsraeimkavikrekeAGITPDPDIDAYMKaismeglqrsmqTDyIMKIMGLDKCADVKVGNamrrgISGG 387
Cdd:cd03237 83 -------------------------SSITKDFYTHPYFK------------TE-IAKPLQIEQILDREVPE-----LSGG 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002313595 388 EMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILV 439
Cdd:cd03237 120 ELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFV 171
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
875-1139 |
1.38e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.79 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 875 LTISFQDVNYYVD--TPPEMrkkgymgrklQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIE-GDIR 949
Cdd:PRK13646 1 MTIRFDNVSYTYQkgTPYEH----------QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAllKPTTGTVTvDDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 950 IGGYPKvqqtfsrisgyceqnDVHSPQI--TVG------ESVAYSAWLRLPAEIDTKTRKEFVDEVLE-----IIELDEI 1016
Cdd:PRK13646 71 ITHKTK---------------DKYIRPVrkRIGmvfqfpESQLFEDTVEREIIFGPKNFKMNLDEVKNyahrlLMDLGFS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1017 RDALVGTPgvNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNV-AETGRTVVCTIHQPSiEIFEA 1095
Cdd:PRK13646 136 RDVMSQSP--FQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMN-EVARY 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1096 FDELMLIKRGGELIYAGP--LGQHSCKVIQYFQSIPGVPK----IKDNYN 1139
Cdd:PRK13646 213 ADEVIVMKEGSIVSQTSPkeLFKDKKKLADWHIGLPEIVQlqydFEQKYQ 262
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
902-1105 |
1.41e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.95 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 902 LQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIegDIRIGGYPKVQQTFSRISG----YCEQNDVHsp 975
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGihEPTKGTI--TINNINYNKLDHKLAAQLGigiiYQELSVID-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 976 QITVGESVAYSawlRLPAE-------IDTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPS 1048
Cdd:PRK09700 94 ELTVLENLYIG---RHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVAN-----LSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002313595 1049 IVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMLIKRG 1105
Cdd:PRK09700 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLA-EIRRICDRYTVMKDG 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
226-276 |
1.51e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 54.27 E-value: 1.51e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1002313595 226 QILENVSGIIKPSRITLLLGPPGCGKTTLLKALaGRLN---KSLKETGEIEYNG 276
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCL-NRMNdliPGARVEGEILLDG 77
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
218-468 |
1.60e-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: 54.16 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 218 FSHHQSKvQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAgRLNKSlkETGEIEYNG-----VKLDEFvpAKTSAYVS 292
Cdd:cd03253 8 FAYDPGR-PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF-RFYDV--SSGSILIDGqdireVTLDSL--RRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 293 QydlhvaDMTV-RETLDFSARFQGVG-SRAEIMKAVikreKEAGITPdpdidaymkaismeglqrsmqtdyimKIMGLDK 370
Cdd:cd03253 82 Q------DTVLfNDTIGYNIRYGRPDaTDEEVIEAA----KAAQIHD--------------------------KIMRFPD 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 371 CADVKVGnamRRG--ISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHiSEYTILV----SLLQP 444
Cdd:cd03253 126 GYDTIVG---ERGlkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIahrlSTIVN 201
|
250 260
....*....|....*....|....
gi 1002313595 445 ApetydlfDDIIIMGEGKVVYHGP 468
Cdd:cd03253 202 A-------DKIIVLKDGRIVERGT 218
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
219-464 |
1.61e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.11 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 219 SHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVPAKTS----AYVSQY 294
Cdd:PRK11614 12 SAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRAT---SGRIVFDGKDITDWQTAKIMreavAIVPEG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 295 DLHVADMTVRETL---DFSARFQGVGSRAEIMKAVIKREKEagitpdpdidaymkaismeglqRSMQtdyimkimgldkc 371
Cdd:PRK11614 89 RRVFSRMTVEENLamgGFFAERDQFQERIKWVYELFPRLHE----------------------RRIQ------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 372 advkvgnamRRG-ISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILVSllQPAPETYD 450
Cdd:PRK11614 134 ---------RAGtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVE--QNANQALK 202
|
250
....*....|....
gi 1002313595 451 LFDDIIIMGEGKVV 464
Cdd:PRK11614 203 LADRGYVLENGHVV 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
903-1086 |
1.68e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 54.31 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 903 QLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGYP---------KVQQTFsrisGYCEQN- 970
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGilKPT----SGEVLIKGEPikydkksllEVRKTV----GIVFQNp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 971 --DVHSPqiTVGESVAYSAW-LRLPAEiDTKTRkefvdevleiieldeIRDAL--VGTPGVNG-----LSREQRKRLTIA 1040
Cdd:PRK13639 88 ddQLFAP--TVEEDVAFGPLnLGLSKE-EVEKR---------------VKEALkaVGMEGFENkpphhLSGGQKKRVAIA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1002313595 1041 VELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIH 1086
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
906-1060 |
1.70e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 55.04 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 906 RNITGAFQPGILSALMGVTGAGKTTLLDVLAGRK---TGGVIEGDIRIGGYPKVQqtfsRISGYCEQNDVHSPQITVGES 982
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEditSGDLFIGEKRMNDVPPAE----RGVGMVFQSYALYPHLSVAEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002313595 983 VAYSawLRLpAEIDTKTRKEFVDEVLEIIELDEIRDAlvgTPgvNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:PRK11000 96 MSFG--LKL-AGAKKEEINQRVNQVAEVLQLAHLLDR---KP--KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
225-467 |
1.98e-07 |
|
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: 53.70 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 225 VQILENVSGIIKPSRITLLLGPPGCGKTTLLkalagrlnkSLKE------TGEIEYNGVKLDEFVPAKTS---AYVSQyD 295
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVV---------SLLErfydptSGEILLDGVDIRDLNLRWLRsqiGLVSQ-E 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 296 LHVADMTVRETLDFsarfqgvGSRAEIMKAVIKREKEAGItpdpdidaymkaismeglqrsmqTDYIMKimgLDKCADVK 375
Cdd:cd03249 86 PVLFDGTIAENIRY-------GKPDATDEEVEEAAKKANI-----------------------HDFIMS---LPDGYDTL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 376 VGNamrRG--ISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLahISEYTILV-----SLLQPApet 448
Cdd:cd03249 133 VGE---RGsqLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA--MKGRTTIViahrlSTIRNA--- 204
|
250
....*....|....*....
gi 1002313595 449 ydlfDDIIIMGEGKVVYHG 467
Cdd:cd03249 205 ----DLIAVLQNGQVVEQG 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
904-1060 |
2.54e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.90 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 904 LLRNITGAFQPGILSALMGVTGAGKTTLLDVLagRKTGGVIEGDIRIGGypKV---QQTFSRIS--------GYCEQNDV 972
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL--NRLIEIYDSKIKVDG--KVlyfGKDIFQIDaiklrkevGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 973 HSPQITVGESVAYSawLRLPAEIDTKTRKEFVDEVLEIIEL-DEIRDALvGTPGvNGLSREQRKRLTIAVELVSNPSIVF 1051
Cdd:PRK14246 101 PFPHLSIYDNIAYP--LKSHGIKEKREIKKIVEECLRKVGLwKEVYDRL-NSPA-SQLSGGQQQRLTIARALALKPKVLL 176
|
....*....
gi 1002313595 1052 MDEPTSGLD 1060
Cdd:PRK14246 177 MDEPTSMID 185
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
925-1060 |
3.16e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 54.31 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 925 GAGKTTLLDVLAG--RKTGGVIE-GDIRIGGYPKVQ------------QTF----SRisgyceqndvhspqiTVGESVAY 985
Cdd:COG1135 41 GAGKSTLIRCINLleRPTSGSVLvDGVDLTALSERElraarrkigmifQHFnllsSR---------------TVAENVAL 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002313595 986 SawLRLpAEIDTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:COG1135 106 P--LEI-AGVPKAEIRKRVAELLELVGLSDKADAYPSQ-----LSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
905-1105 |
3.64e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 53.45 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTL---LDVLAGRKTGGVIEGDIRIGGYPKVQQtFSRISGYCEQNdvhsPQI---- 977
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLRPQKGKVLVSGIDTGDFSKLQG-IRKLVGIVFQN----PETqfvg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 978 -TVGESVAYSAW-LRLPAeidTKTRKEfVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEP 1055
Cdd:PRK13644 93 rTVEEDLAFGPEnLCLPP---IEIRKR-VDRALAEIGLEKYRHRSPKT-----LSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1056 TSGLDARAAAIAMRAVKNVAETGRTVVCTIHqpSIEIFEAFDELMLIKRG 1105
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKGKTIVYITH--NLEELHDADRIIVMDRG 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
211-417 |
3.78e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 52.79 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 211 LLAAKLGFSHHQSKvqILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNkslKETGEIEYNGVKLDEFVPA---KT 287
Cdd:PRK10247 8 LQLQNVGYLAGDAK--ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIS---PTSGTLLFEGEDISTLKPEiyrQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 288 SAYVSQYDLHVADmTVRETLDFSARFQgvgsraeimkavikrekeaGITPDPdiDAYMKAISMEGLQRSMQTDYImkimg 367
Cdd:PRK10247 83 VSYCAQTPTLFGD-TVYDNLIFPWQIR-------------------NQQPDP--AIFLDDLERFALPDTILTKNI----- 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1002313595 368 ldkcadvkvgNAMrrgiSGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSS 417
Cdd:PRK10247 136 ----------AEL----SGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
896-1084 |
4.15e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.18 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 896 GYMGRKLqlLRNITGAFQPGILSALMGVTGAGKTTLL-------DVLAG-RKTGGVIEGDIRIGGYPKVQQtFSRISGYC 967
Cdd:PRK14271 30 GFAGKTV--LDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmnDKVSGyRYSGDVLLGGRSIFNYRDVLE-FRRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 968 EQNDVHSPQITVGESVAYSAWLRLPAeidtktRKEFVD----EVLEIIELDEIRDALVGTPgvNGLSREQRKRLTIAVEL 1043
Cdd:PRK14271 107 FQRPNPFPMSIMDNVLAGVRAHKLVP------RKEFRGvaqaRLTEVGLWDAVKDRLSDSP--FRLSGGQQQLLCLARTL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1002313595 1044 VSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCT 1084
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVT 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
220-467 |
4.35e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 53.31 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 220 HHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGvkldefvpaktsayvsqydlhva 299
Cdd:PRK13636 14 NYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPS---SGRILFDG----------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 300 dmtvrETLDFSArfqgvgsraeimKAVIKREKEAGIT-PDPDIDAYMKA----ISMEGLQRSMQTDYIMKimgldkcadv 374
Cdd:PRK13636 68 -----KPIDYSR------------KGLMKLRESVGMVfQDPDNQLFSASvyqdVSFGAVNLKLPEDEVRK---------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 375 KVGNAMRR-GI-----------SGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILVSll 442
Cdd:PRK13636 121 RVDNALKRtGIehlkdkpthclSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIA-- 198
|
250 260 270
....*....|....*....|....*....|.
gi 1002313595 443 qpapeTYDL------FDDIIIMGEGKVVYHG 467
Cdd:PRK13636 199 -----THDIdivplyCDNVFVMKEGRVILQG 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
901-1081 |
4.64e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.57 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 901 KLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIEGDIR-IGGYPKVQQTFSRISGYCEQNDVHSpQI 977
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGdpRATSGRIVFDGKdITDWQTAKIMREAVAIVPEGRRVFS-RM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 978 TVGESVAYSAWLrlpaeIDTKTRKEFVDEVLEII-ELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPT 1056
Cdd:PRK11614 96 TVEENLAMGGFF-----AERDQFQERIKWVYELFpRLHERRIQRAGT-----MSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
170 180
....*....|....*....|....*
gi 1002313595 1057 SGLDARAAAIAMRAVKNVAETGRTV 1081
Cdd:PRK11614 166 LGLAPIIIQQIFDTIEQLREQGMTI 190
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
216-315 |
4.65e-07 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 51.55 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 216 LGFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSLketGEIEYNGVKLDEFVPAKTSAY-VSQY 294
Cdd:cd03247 6 VSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQ---GEITLDGVPVSDLEKALSSLIsVLNQ 82
|
90 100
....*....|....*....|.
gi 1002313595 295 DLHVADMTVRETLdfSARFQG 315
Cdd:cd03247 83 RPYLFDTTLRNNL--GRRFSG 101
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
227-415 |
5.14e-07 |
|
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: 51.98 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 227 ILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrLNKSLKetGEIEYNGVKLDE--FVPAKTSAYVSQYDLHVADMTVR 304
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAG-LLRPDS--GEVRWNGTPLAEqrDEPHENILYLGHLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 305 ETLDFSARFQGVGSRaeimkavikrekeagitpdpDIDAYMKAismeglqrsmqtdyimkiMGLDKCADVKVGNamrrgI 384
Cdd:TIGR01189 92 ENLHFWAAIHGGAQR--------------------TIEDALAA------------------VGLTGFEDLPAAQ-----L 128
|
170 180 190
....*....|....*....|....*....|.
gi 1002313595 385 SGGEMKRLTTGEMIVGPCKVLLMDEISTGLD 415
Cdd:TIGR01189 129 SAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
203-467 |
5.14e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 54.06 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 203 NAALSRFSLLAAKLGFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNkslKETGEIEYNGVKLDEF 282
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD---PQQGEILLNGQPIADY 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 283 VPA---KTSAYVSQyDLHVADMTVRETLDFSArfqgvgsraeimkavikrekeagitPDPDiDAYMKAIsmegLQRsmqt 359
Cdd:PRK11160 408 SEAalrQAISVVSQ-RVHLFSATLRDNLLLAA-------------------------PNAS-DEALIEV----LQQ---- 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 360 dyimkiMGLDKCADVKVG-NAMR----RGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQlaHISE 434
Cdd:PRK11160 453 ------VGLEKLLEDDKGlNAWLgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE--HAQN 524
|
250 260 270
....*....|....*....|....*....|....*...
gi 1002313595 435 YTILVSllqpapeTYDL-----FDDIIIMGEGKVVYHG 467
Cdd:PRK11160 525 KTVLMI-------THRLtgleqFDRICVMDNGQIIEQG 555
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
872-1105 |
5.61e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.27 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 872 FTPLTISFQDVnyyVDTPPEMRK------KGYMGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGVIE 945
Cdd:COG2401 10 LMRVTKVYSSV---LDLSERVAIvleafgVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 946 GdiriggypkvqqtfsrisgyceQNDVHSPQITVGESVaysawlrlpaeIDTKTRKEFVDEVLEIIELDEIRDALVGTPG 1025
Cdd:COG2401 87 G----------------------CVDVPDNQFGREASL-----------IDAIGRKGDFKDAVELLNAVGLSDAVLWLRR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1026 VNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVA-ETGRT-VVCTIH-------QPSIEIFEAF 1096
Cdd:COG2401 134 FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLArRAGITlVVATHHydviddlQPDLLIFVGY 213
|
....*....
gi 1002313595 1097 DELMLIKRG 1105
Cdd:COG2401 214 GGVPEEKRR 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
224-472 |
5.71e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 51.76 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 224 KVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrlNKSLKET-GEIEYNGVKLdefvpaktsayvsqydlhvADMT 302
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPKYEVTeGEILFKGEDI-------------------TDLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 303 VREtldfsarfqgvgsRAeimkavikrekEAGITpdpdidaymkaismeglqRSMQtdYIMKIMGldkcadVKVGNAMR- 381
Cdd:cd03217 71 PEE-------------RA-----------RLGIF------------------LAFQ--YPPEIPG------VKNADFLRy 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 382 --RGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILVSLLQpapetyDLFDDII--- 456
Cdd:cd03217 101 vnEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQ------RLLDYIKpdr 174
|
250
....*....|....*...
gi 1002313595 457 --IMGEGKVVYHGPKNLI 472
Cdd:cd03217 175 vhVLYDGRIVKSGDKELA 192
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
882-1086 |
6.03e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 53.69 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 882 VNYYVDTPPEmrKKGYMGRKLQLLRNITGAF--QP-----------GILSALMGVTGAGKTTLLDVLAGRKTGgvIEGDI 948
Cdd:PRK11607 1 MNDAIPRPQA--KTRKALTPLLEIRNLTKSFdgQHavddvsltiykGEIFALLGASGCGKSTLLRMLAGFEQP--TAGQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 949 RIGGypkvqQTFSRISGYCE------QNDVHSPQITVGESVAYSAwlrlpaEIDTKTRKEFVDEVLEIIELDEIRDALVG 1022
Cdd:PRK11607 77 MLDG-----VDLSHVPPYQRpinmmfQSYALFPHMTVEQNIAFGL------KQDKLPKAEIASRVNEMLGLVHMQEFAKR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002313595 1023 TPgvNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAE-TGRTVVCTIH 1086
Cdd:PRK11607 146 KP--HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErVGVTCVMVTH 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
243-415 |
7.04e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 52.91 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 243 LLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYngvkLDEFVPAKTSA------YVSQYDLHVADMTVRETLDFSARFQGv 316
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPD---AGKITV----LGVPVPARARLararigVVPQFDNLDLEFTVRENLLVFGRYFG- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 317 gsraeiMKAvikREKEAGITPdpdidaymkaismeglqrsmqtdyIMKIMGLDKCADVKVGNamrrgISGGEMKRLTTGE 396
Cdd:PRK13536 144 ------MST---REIEAVIPS------------------------LLEFARLESKADARVSD-----LSGGMKRRLTLAR 185
|
170
....*....|....*....
gi 1002313595 397 MIVGPCKVLLMDEISTGLD 415
Cdd:PRK13536 186 ALINDPQLLILDEPTTGLD 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
226-307 |
7.63e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 53.53 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 226 QILENVSGIIKP-SRItLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYN-GVKLdefvpaktsAYVSQY--DLHVaDM 301
Cdd:COG0488 329 TLLDDLSLRIDRgDRI-GLIGPNGAGKSTLLKLLAGELEPD---SGTVKLGeTVKI---------GYFDQHqeELDP-DK 394
|
....*.
gi 1002313595 302 TVRETL 307
Cdd:COG0488 395 TVLDEL 400
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
895-1060 |
8.03e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 53.53 E-value: 8.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 895 KGYMGRKLqlLRNITGAFQPG--IlsALMGVTGAGKTTLLDVLAGRKTggVIEGDIRIGgyPKVQQtfsrisGYCEQndv 972
Cdd:COG0488 323 KSYGDKTL--LDDLSLRIDRGdrI--GLIGPNGAGKSTLLKLLAGELE--PDSGTVKLG--ETVKI------GYFDQ--- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 973 HSPQITVGESVAysAWLRlpaeidtktrkEFVDEVLEIieldEIRDAL---------VGTPgVNGLSREQRKRLTIAVEL 1043
Cdd:COG0488 386 HQEELDPDKTVL--DELR-----------DGAPGGTEQ----EVRGYLgrflfsgddAFKP-VGVLSGGEKARLALAKLL 447
|
170
....*....|....*..
gi 1002313595 1044 VSNPSIVFMDEPTSGLD 1060
Cdd:COG0488 448 LSPPNVLLLDEPTNHLD 464
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
877-1060 |
9.68e-07 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 51.32 E-value: 9.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 877 ISFQDVNYYVDTPPEMrkkgymgrklQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIEGDirigGYP 954
Cdd:cd03248 12 VKFQNVTFAYPTRPDT----------LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENfyQPQGGQVLLD----GKP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 955 kvqqtfsrISGYcEQNDVHSPQITVG-ESVAYSAWLRlpAEIDTKTRKEFVDEVLE----------IIELDEIRDALVGT 1023
Cdd:cd03248 78 --------ISQY-EHKYLHSKVSLVGqEPVLFARSLQ--DNIAYGLQSCSFECVKEaaqkahahsfISELASGYDTEVGE 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 1002313595 1024 PGvNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:cd03248 147 KG-SQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
877-1105 |
1.19e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 53.19 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 877 ISFQDVNYYVDTPPEmrkkgymgrkLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGviegDIRIGGYP 954
Cdd:TIGR00958 479 IEFQDVSFSYPNRPD----------VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNlyQPTGG----QVLLDGVP 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 955 KVQ------QTFSRISGyceqndvHSPQI---TVGESVAYSAWLRLPAEIDTKTRKEFVDEVleIIELDEIRDALVGTPG 1025
Cdd:TIGR00958 545 LVQydhhylHRQVALVG-------QEPVLfsgSVRENIAYGLTDTPDEEIMAAAKAANAHDF--IMEFPNGYDTEVGEKG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1026 vNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKnvaETGRTVVCTIHQPSieIFEAFDELMLIKRG 1105
Cdd:TIGR00958 616 -SQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS---RASRTVLLIAHRLS--TVERADQILVLKKG 689
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
903-1060 |
1.21e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.57 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 903 QLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGVIEGDIRIGGYPKVQQTFSRIS------GYceQNDVHSPQ 976
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGESILDLEPEERAhlgiflAF--QYPIEIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 977 ITVGE--SVAYSA---WLRLPaEIDTKTRKEFVDEVLEIIELDEI---RDalvgtpgVN-GLSREQRKRLTIAVELVSNP 1047
Cdd:CHL00131 99 VSNADflRLAYNSkrkFQGLP-ELDPLEFLEIINEKLKLVGMDPSflsRN-------VNeGFSGGEKKRNEILQMALLDS 170
|
170
....*....|...
gi 1002313595 1048 SIVFMDEPTSGLD 1060
Cdd:CHL00131 171 ELAILDETDSGLD 183
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
875-1113 |
1.32e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 51.75 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 875 LTISFQDVNYYVDTPPEMRKKGymgrklqlLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIEgdirIGG 952
Cdd:PRK13641 1 MSIKFENVDYIYSPGTPMEKKG--------LDNISFELEEGSFVALVGHTGSGKSTLMQHFNAllKPSSGTIT----IAG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 953 YPKVQQTFS--------RISGYCEQNDVHSPQITVGESVAYSAwlrLPAEIDTKTRKEFVDEVLEIIELDEirDALVGTP 1024
Cdd:PRK13641 69 YHITPETGNknlkklrkKVSLVFQFPEAQLFENTVLKDVEFGP---KNFGFSEDEAKEKALKWLKKVGLSE--DLISKSP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1025 gvNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMLIKR 1104
Cdd:PRK13641 144 --FELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMD-DVAEYADDVLVLEH 220
|
....*....
gi 1002313595 1105 GGELIYAGP 1113
Cdd:PRK13641 221 GKLIKHASP 229
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
877-1060 |
1.50e-06 |
|
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: 50.96 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 877 ISFQDVN--YYVDTPPEmrkkgymgrklqlLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGrktggVIE---GDIRIG 951
Cdd:cd03244 3 IEFKNVSlrYRPNLPPV-------------LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFR-----LVElssGSILID 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 952 GYP-------KVQQTFSRIsgyceqndvhsPQitvgESVAYSAWLRLPAEIDTKTRKEFVDEVLEIIELDEIRDALVG-- 1022
Cdd:cd03244 65 GVDiskiglhDLRSRISII-----------PQ----DPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGgl 129
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1002313595 1023 ----TPGVNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:cd03244 130 dtvvEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVD 171
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1250-1419 |
1.73e-06 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 52.01 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1250 NDQQGLFTILGCMYGITIFTGInnSQSAMPFVAVERSVMYRERFAGM-YSPWAYSFAQVAMEIPYVLMLALLFMLIAYpt 1328
Cdd:pfam12698 154 NPQSGYAYYLVGLILMIIILIG--AAIIAVSIVEEKESRIKERLLVSgVSPLQYWLGKILGDFLVGLLQLLIILLLLF-- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1329 iGYAWTAAKFCWFFYTMFCTLLYFVYFGMLIVSITPNLQVASIYASSFYMTQHLLSGFVMPPSQIPKWWIWLYYISPMSW 1408
Cdd:pfam12698 230 -GIGIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFS 308
|
170
....*....|.
gi 1002313595 1409 TLNLLFTTQFG 1419
Cdd:pfam12698 309 PIDGLLRLIYG 319
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
908-1086 |
2.26e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.70 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 908 ITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGgviEGDIRIGG-----YPKVQQtfSRISGYCEQNDVHSPQITVGES 982
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG---SGSIQFAGqpleaWSAAEL--ARHRAYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 983 VAysawLRLPAEIDTKTRKEFVDEVLEIIELDeirDALvGTPgVNGLS--REQRKRLTiAVEL----VSNPS--IVFMDE 1054
Cdd:PRK03695 90 LT----LHQPDKTRTEAVASALNEVAEALGLD---DKL-GRS-VNQLSggEWQRVRLA-AVVLqvwpDINPAgqLLLLDE 159
|
170 180 190
....*....|....*....|....*....|..
gi 1002313595 1055 PTSGLDARAAAIAMRAVKNVAETGRTVVCTIH 1086
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQGIAVVMSSH 191
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1028-1112 |
2.48e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.39 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1028 GLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMLIKRgGE 1107
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME-HVLEVADEVIVMDK-GK 253
|
....*
gi 1002313595 1108 LIYAG 1112
Cdd:PRK13631 254 ILKTG 258
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
905-1112 |
2.63e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.00 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGgvIEGDIRIGGYP-----KVQQTFSRISGYCEQNDVHSP-QIT 978
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP--SSGRILFDGKPidysrKGLMKLRESVGMVFQDPDNQLfSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 979 VGESVAYSAW-LRLPaeidTKTRKEFVDEVLEIIELDEIRDalvgTPgVNGLSREQRKRLTIAVELVSNPSIVFMDEPTS 1057
Cdd:PRK13636 100 VYQDVSFGAVnLKLP----EDEVRKRVDNALKRTGIEHLKD----KP-THCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002313595 1058 GLDARAAAIAMRAVKNVA-ETGRTVVCTIHqpSIEIFEAFDELMLIKRGGELIYAG 1112
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQkELGLTIIIATH--DIDIVPLYCDNVFVMKEGRVILQG 224
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
217-293 |
2.92e-06 |
|
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: 48.21 E-value: 2.92e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002313595 217 GFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNkslKETGEIEYNgvkldefvPAKTSAYVSQ 293
Cdd:cd03221 5 NLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELE---PDEGIVTWG--------STVKIGYFEQ 70
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
899-1087 |
4.07e-06 |
|
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: 49.64 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 899 GRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIEGDIRIGGYPKVQQTFSRISGyceqndvhspq 976
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGemQTLEGKVHWSNKNESEPSFEATRSRNRY----------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 977 itvgeSVAYSA---WLrLPAEID------TKTRKEFVDEVLEIIELDEIRDAL-------VGTPGVNgLSREQRKRLTIA 1040
Cdd:cd03290 80 -----SVAYAAqkpWL-LNATVEenitfgSPFNKQRYKAVTDACSLQPDIDLLpfgdqteIGERGIN-LSGGQRQRICVA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1002313595 1041 VELVSNPSIVFMDEPTSGLDARAA--AIAMRAVKNVAETGRTVVCTIHQ 1087
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIHLSdhLMQEGILKFLQDDKRTLVLVTHK 201
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
917-1060 |
4.17e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 50.04 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 917 LSALMGVTGAGKTTLLDVLAGRKTggvIEGDIRIGGYPKV--QQTFSR---ISGYCEQNDVHSPQ-----ITVGESVAYS 986
Cdd:PRK14258 35 VTAIIGPSGCGKSTFLKCLNRMNE---LESEVRVEGRVEFfnQNIYERrvnLNRLRRQVSMVHPKpnlfpMSVYDNVAYG 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002313595 987 AWL---RLPAEIDtktrkEFVDEVLEIIEL-DEIRDALvgTPGVNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:PRK14258 112 VKIvgwRPKLEID-----DIVESALKDADLwDEIKHKI--HKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLD 182
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
237-283 |
4.34e-06 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 49.88 E-value: 4.34e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1002313595 237 PSRITLLLGPPGCGKTTLLKALAGRLNKSLKEtgeieyngVKLDEFV 283
Cdd:COG1223 34 PPRKILFYGPPGTGKTMLAEALAGELKLPLLT--------VRLDSLI 72
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
905-1114 |
4.84e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGYPkVQQTFSRISGYCEQNDVHSPQITVGE- 981
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGiyQKD----SGSILFQGKE-IDFKSSKEALENGISMVHQELNLVLQr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 982 SVAYSAWL-RLPaeidtkTRKEFVDEVLEIIELDEIRDAL---------VGTpgvngLSREQRKRLTIAVELVSNPSIVF 1051
Cdd:PRK10982 89 SVMDNMWLgRYP------TKGMFVDQDKMYRDTKAIFDELdididprakVAT-----LSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002313595 1052 MDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMlIKRGGELIYAGPL 1114
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKME-EIFQLCDEIT-ILRDGQWIATQPL 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
227-467 |
5.02e-06 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 49.41 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 227 ILENVSGIIKPSRITLLLGPPGCGKTTLLKaLAGRLnkslketgeieyngvkldeFVPAKTSAYVSQYDLHVADMTvret 306
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTK-LIQRF-------------------YVPENGRVLVDGHDLALADPA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 307 ldfSARFQ-GVGSRAEIMKAVIKREKEAGITPDPDIDAYMKAISMEGLQrsmqtDYIMKimgLDKCADVKVGNaMRRGIS 385
Cdd:cd03252 73 ---WLRRQvGVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAH-----DFISE---LPEGYDTIVGE-QGAGLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 386 GGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILVSLLQpapeTYDLFDDIIIMGEGKVVY 465
Cdd:cd03252 141 GGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLS----TVKNADRIIVMEKGRIVE 216
|
..
gi 1002313595 466 HG 467
Cdd:cd03252 217 QG 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
223-468 |
5.47e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.82 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 223 SKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLnksLKETGEIEYNGVKLDEFVPAKTSAY----VSQYDLHV 298
Cdd:PRK15439 22 SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIV---PPDSGTLEIGGNPCARLTPAKAHQLgiylVPQEPLLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 299 ADMTVRETLDFsarfqGVGSRAEIMKAVIKREKEAGITPDPDidayMKAISMEGLQRSMqtdyiMKIM-GLdkcadvkvg 377
Cdd:PRK15439 99 PNLSVKENILF-----GLPKRQASMQKMKQLLAALGCQLDLD----SSAGSLEVADRQI-----VEILrGL--------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 378 naMRRGisggemkrlttgemivgpcKVLLMDEISTGL---DSSTTFQIVSCLQQLAHiseytILVSLLQPAPETYDLFDD 454
Cdd:PRK15439 156 --MRDS-------------------RILILDEPTASLtpaETERLFSRIRELLAQGV-----GIVFISHKLPEIRQLADR 209
|
250
....*....|....
gi 1002313595 455 IIIMGEGKVVYHGP 468
Cdd:PRK15439 210 ISVMRDGTIALSGK 223
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
243-468 |
5.96e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.46 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 243 LLGPPGCGKTTLLKALAG--RLNKSLKETGEIEYNGV-----KLDEFVPAKTSAYVSQYDLHVADMTVRETLDFSARFQG 315
Cdd:PRK14267 35 LMGPSGCGKSTLLRTFNRllELNEEARVEGEVRLFGRniyspDVDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 316 -VGSRAEIMKAVIKREKEAGITPDPDidaymkaismeglqrsmqtdyimkimglDKCADvKVGNamrrgISGGEMKRLTT 394
Cdd:PRK14267 115 lVKSKKELDERVEWALKKAALWDEVK----------------------------DRLND-YPSN-----LSGGQRQRLVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002313595 395 GEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAhiSEYTILVSLLQPApETYDLFDDIIIMGEGKVVYHGP 468
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELK--KEYTIVLVTHSPA-QAARVSDYVAFLYLGKLIEVGP 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
225-467 |
6.08e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.55 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 225 VQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGV---KLDEFVPAKTSAYVSQYDLHVAD- 300
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT---KGTITINNInynKLDHKLAAQLGIGIIYQELSVIDe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 301 MTVRETLdfsarFQGvgsraeimKAVIKreKEAGItpdPDID-AYMKaismeglqrsMQTDYIMKIMGLDKCADVKVGNa 379
Cdd:PRK09700 95 LTVLENL-----YIG--------RHLTK--KVCGV---NIIDwREMR----------VRAAMMLLRVGLKVDLDEKVAN- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 380 mrrgISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAhiSEYTILVSLLQPAPETYDLFDDIIIMG 459
Cdd:PRK09700 146 ----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLR--KEGTAIVYISHKLAEIRRICDRYTVMK 219
|
....*...
gi 1002313595 460 EGKVVYHG 467
Cdd:PRK09700 220 DGSSVCSG 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
875-1134 |
6.27e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 49.74 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 875 LTISFQDVN--YYVDTPPEMRKkgymgrklqlLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKT---GGVIEGDIR 949
Cdd:PRK13649 1 MGINLQNVSytYQAGTPFEGRA----------LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVptqGSVRVDDTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 950 IGGYPK------VQQTFSRISGYCEQndvhspQI---TVGESVAYSawlrlPAEIDTkTRKEFVDEVLEIIELDEIRDAL 1020
Cdd:PRK13649 71 ITSTSKnkdikqIRKKVGLVFQFPES------QLfeeTVLKDVAFG-----PQNFGV-SQEEAEALAREKLALVGISESL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1021 VGTPGVNgLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQpsIEIFEAFDELM 1100
Cdd:PRK13649 139 FEKNPFE-LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHL--MDDVANYADFV 215
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1002313595 1101 LIKRGGELIYAGplgqhscKVIQYFQSIP-------GVPKI 1134
Cdd:PRK13649 216 YVLEKGKLVLSG-------KPKDIFQDVDfleekqlGVPKI 249
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
905-1105 |
6.66e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 49.36 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTggVIEGDIRIGGYPKVQQTFSRIS---GYCEQNdvhsPQIT-VG 980
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEK--VKSGEIFYNNQAITDDNFEKLRkhiGIVFQN----PDNQfVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 981 ESVAYSAWLRLPAE-IDTKTRKEFVDEVLEIIELDEIRDAlvgTPgvNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGL 1059
Cdd:PRK13648 99 SIVKYDVAFGLENHaVPYDEMHRRVSEALKQVDMLERADY---EP--NALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1002313595 1060 DARAAAIAMRAVKNVAETGRTVVCTIHQPSIEIFEAfDELMLIKRG 1105
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEA-DHVIVMNKG 218
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
913-1090 |
1.02e-05 |
|
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: 48.90 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 913 QPGILSALMGVTGAGKTTLLDVLAGRktggVIEGDIRIGGYPKVQQTFSRISGYCEQN---DVHSPQITVGESVAYSAwl 989
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGK----LKPNLGKFDDPPDWDEILDEFRGSELQNyftKLLEGDVKVIVKPQYVD-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 990 RLPAEIDTKTR--------KEFVDEVLEIIELDEIRDAlvgtpGVNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDA 1061
Cdd:cd03236 98 LIPKAVKGKVGellkkkdeRGKLDELVDQLELRHVLDR-----NIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*....
gi 1002313595 1062 RAAAIAMRAVKNVAETGRTVVCTIHQPSI 1090
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHDLAV 201
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
217-467 |
1.13e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.61 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 217 GFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLnksLKETGEIEYNGvkldEFVPA----------K 286
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQI---APDHGEILFDG----ENIPAmsrsrlytvrK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 287 TSAYVSQYDLHVADMTVRETLDFSARfqgvgsraeimkavikrekEAGITPDPDIdaymkaismeglqrsmQTDYIMKI- 365
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNVAYPLR-------------------EHTQLPAPLL----------------HSTVMMKLe 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 366 -MGLDKCAdvkvgNAMRRGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYT-ILVSllQ 443
Cdd:PRK11831 130 aVGLRGAA-----KLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTcVVVS--H 202
|
250 260
....*....|....*....|....
gi 1002313595 444 PAPETYDLFDDIIIMGEGKVVYHG 467
Cdd:PRK11831 203 DVPEVLSIADHAYIVADKKIVAHG 226
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
237-265 |
1.13e-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: 46.98 E-value: 1.13e-05
10 20
....*....|....*....|....*....
gi 1002313595 237 PSRITLLLGPPGCGKTTLLKALAGRLNKS 265
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPP 29
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
186-468 |
1.20e-05 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 49.80 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 186 VEAECQVVSGKPLPTLWNAAlsrfsllaaKLGFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKS 265
Cdd:TIGR03269 267 VEKECEVEVGEPIIKVRNVS---------KRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 266 lkeTGEIEyngVKL-DEFVpaktsayvsqydlhvaDMTVRetldfsarfqGVGSRAEIMKAVIKREKEAGITPDPDI-DA 343
Cdd:TIGR03269 338 ---SGEVN---VRVgDEWV----------------DMTKP----------GPDGRGRAKRYIGILHQEYDLYPHRTVlDN 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 344 YMKAISME---GLQRsMQTDYIMKIMGLDKCADVKVGNAMRRGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTF 420
Cdd:TIGR03269 386 LTEAIGLElpdELAR-MKAVITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKV 464
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1002313595 421 QIV-SCLQQLAHISEYTILVSllQPAPETYDLFDDIIIMGEGKVVYHGP 468
Cdd:TIGR03269 465 DVThSILKAREEMEQTFIIVS--HDMDFVLDVCDRAALMRDGKIVKIGD 511
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
227-446 |
1.37e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 48.54 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 227 ILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEfvPAKTSAYVSQYDLHVADMTVRET 306
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ---HGSITLDGKPVEG--PGAERGVVFQNEGLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 307 LDFSARFQGVGsraeimkaviKREKEAgitpdpdidaymKAISMeglqrsmqtdyiMKIMGLDkcadvkvGNAMRR--GI 384
Cdd:PRK11248 91 VAFGLQLAGVE----------KMQRLE------------IAHQM------------LKKVGLE-------GAEKRYiwQL 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002313595 385 SGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAH------------ISEYTILVS---LLQPAP 446
Cdd:PRK11248 130 SGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQetgkqvllithdIEEAVFMATelvLLSPGP 206
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
225-470 |
1.48e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 48.87 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 225 VQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrlnksLKE--TGEIEYNGVKLDEFVPAKTS-AYVSQ-YDLHvAD 300
Cdd:PRK11000 16 VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAG-----LEDitSGDLFIGEKRMNDVPPAERGvGMVFQsYALY-PH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 301 MTVRETLDFSARFQGVGsRAEIMKAVikrekeagitpdpdidaymkaismeglqrsmqtDYIMKIMGLDKCADVKvgnam 380
Cdd:PRK11000 90 LSVAENMSFGLKLAGAK-KEEINQRV---------------------------------NQVAEVLQLAHLLDRK----- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 381 RRGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQI---VSCLQQlaHISEYTILVSLLQpaPETYDLFDDIII 457
Cdd:PRK11000 131 PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMrieISRLHK--RLGRTMIYVTHDQ--VEAMTLADKIVV 206
|
250 260
....*....|....*....|.
gi 1002313595 458 MGEGKV--------VYHGPKN 470
Cdd:PRK11000 207 LDAGRVaqvgkpleLYHYPAN 227
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
211-415 |
1.49e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.92 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 211 LLAAKlGFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNkslKETGEIEYNGVKLDEFVPAKTSAY 290
Cdd:PRK13543 11 LLAAH-ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLH---VESGQIQIDGKTATRGDRSRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 291 VSQYDLHVADMTVRETLDFSARFQgvGSRAEIMKAvikrekeagitpdpdidaymKAISMEGLqrsmqTDYimkimgldk 370
Cdd:PRK13543 87 LGHLPGLKADLSTLENLHFLCGLH--GRRAKQMPG--------------------SALAIVGL-----AGY--------- 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1002313595 371 cadvkvGNAMRRGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLD 415
Cdd:PRK13543 131 ------EDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
228-468 |
1.53e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 48.51 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 228 LENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNG-------VKLDEFvpAKTSAYVSQYDLH-VA 299
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPT---SGKIIIDGvditdkkVKLSDI--RKKVGLVFQYPEYqLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 300 DMTVRETLDFSARFQGVgSRAEIMKAVikreKEAgitpdpdidaymkaismeglqrsmqtdyiMKIMGLDKcADVKVGNA 379
Cdd:PRK13637 98 EETIEKDIAFGPINLGL-SEEEIENRV----KRA-----------------------------MNIVGLDY-EDYKDKSP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 380 MRrgISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLaHiSEY---TILVSllQPAPETYDLFDDII 456
Cdd:PRK13637 143 FE--LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKEL-H-KEYnmtIILVS--HSMEDVAKLADRII 216
|
250
....*....|..
gi 1002313595 457 IMGEGKVVYHGP 468
Cdd:PRK13637 217 VMNKGKCELQGT 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
877-1112 |
1.82e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 48.06 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 877 ISFQDVNYyvdtppemrkkGYMGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVIEgdirIGGYP 954
Cdd:PRK13632 8 IKVENVSF-----------SYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGllKPQSGEIK----IDGIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 955 KVQQTFSRIS---GYCEQN-DVHSPQITVGESVAYSAWLRLpaeIDTKTRKEFVDEVLEIIELDEIRDAlvgTPgvNGLS 1030
Cdd:PRK13632 73 ISKENLKEIRkkiGIIFQNpDNQFIGATVEDDIAFGLENKK---VPPKKMKDIIDDLAKKVGMEDYLDK---EP--QNLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1031 REQRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSIEIFEAfDELmLIKRGGELIY 1110
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILA-DKV-IVFSEGKLIA 222
|
..
gi 1002313595 1111 AG 1112
Cdd:PRK13632 223 QG 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
229-325 |
1.89e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.11 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 229 ENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrLnkSLKETGEIEYNGVKL----DEFvpaktsayvsQYDL----HVA- 299
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAG-L--ARPDAGEVLWQGEPIrrqrDEY----------HQDLlylgHQPg 84
|
90 100
....*....|....*....|....*....
gi 1002313595 300 ---DMTVRETLDFSARFQGVGSRAEIMKA 325
Cdd:PRK13538 85 iktELTALENLRFYQRLHGPGDDEALWEA 113
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
899-1060 |
2.16e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 899 GRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTggVIEGDIRIG-GYpKVqqtfsrisGYCEQNDVHSPQI 977
Cdd:PRK11819 17 PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK--EFEGEARPApGI-KV--------GYLPQEPQLDPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 978 TVGESVA----------------YSAWLRLPAEIDtKTRKEFVdEVLEII------ELD---EI-RDALVGTPG---VNG 1028
Cdd:PRK11819 86 TVRENVEegvaevkaaldrfneiYAAYAEPDADFD-ALAAEQG-ELQEIIdaadawDLDsqlEIaMDALRCPPWdakVTK 163
|
170 180 190
....*....|....*....|....*....|..
gi 1002313595 1029 LSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
827-1105 |
2.89e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 48.56 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 827 IGLTIKQSPgASQAIISNDKI-RICHGRDQEKSKDIKigtrrmalPFTPLTISFQDVNYyvdtppemrkkGYMGRKLqLL 905
Cdd:PRK10790 299 IELTTQQSM-LQQAVVAGERVfELMDGPRQQYGNDDR--------PLQSGRIDIDNVSF-----------AYRDDNL-VL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 906 RNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTggVIEGDIRIGGYPkvqqtFSRISGYCEQNDVHSPQ---ITVGES 982
Cdd:PRK10790 358 QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP--LTEGEIRLDGRP-----LSSLSHSVLRQGVAMVQqdpVVLADT 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 983 vaYSAWLRLPAEIDtktrKEFVDEVLEIIELDEIRDAL-------VGTPGvNGLSREQRKRLTIAVELVSNPSIVFMDEP 1055
Cdd:PRK10790 431 --FLANVTLGRDIS----EEQVWQALETVQLAELARSLpdglytpLGEQG-NNLSVGQKQLLALARVLVQTPQILILDEA 503
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1056 TSGLDARAAAIAMRAVKNVAETgRTVVCTIHQPSIeIFEAfDELMLIKRG 1105
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREH-TTLVVIAHRLST-IVEA-DTILVLHRG 550
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
903-1060 |
2.90e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 903 QLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGVIEGDIRIGGYPKVQQTFSRISG----YCEQNDVHSP--- 975
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLELSPEDRAGegifMAFQYPVEIPgvs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 976 -----QITVGESVAYsawlRLPAEIDtktRKEFVDEVLEIIELDEIRDALVgTPGVN-GLSREQRKRLTIAVELVSNPSI 1049
Cdd:PRK09580 95 nqfflQTALNAVRSY----RGQEPLD---RFDFQDLMEEKIALLKMPEDLL-TRSVNvGFSGGEKKRNDILQMAVLEPEL 166
|
170
....*....|.
gi 1002313595 1050 VFMDEPTSGLD 1060
Cdd:PRK09580 167 CILDESDSGLD 177
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
226-283 |
3.13e-05 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 47.69 E-value: 3.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002313595 226 QILENVsGIIKPSRItLLLGPPGCGKTTLLKALAGRLNKSLketgeieYNgVKLDEFV 283
Cdd:COG1222 102 ELFRKY-GIEPPKGV-LLYGPPGTGKTLLAKAVAGELGAPF-------IR-VRGSELV 149
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
226-463 |
3.27e-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: 46.75 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 226 QILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrlnksLKET--GEIEYNGVKLD------EFVPAKTSAYVSQYDLH 297
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINL-----LEEPdsGTIIIDGLKLTddkkniNELRQKVGMVFQQFNLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 298 vADMTVRETldfsarfqgvgsraeIMKAVIKREKEagitpdPDIDAymKAISMEGLQRsmqtdyimkiMGLDKCADVKVG 377
Cdd:cd03262 89 -PHLTVLEN---------------ITLAPIKVKGM------SKAEA--EERALELLEK----------VGLADKADAYPA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 378 NamrrgISGGEMKRLTTGE-MIVGPcKVLLMDEISTGLDSSTTFQIVSCLQQLAHiSEYTILVSllqpapeTYDL-F--- 452
Cdd:cd03262 135 Q-----LSGGQQQRVAIARaLAMNP-KVMLFDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVV-------THEMgFare 200
|
250
....*....|...
gi 1002313595 453 --DDIIIMGEGKV 463
Cdd:cd03262 201 vaDRVIFMDDGRI 213
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
229-266 |
3.38e-05 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 45.74 E-value: 3.38e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1002313595 229 ENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSL 266
Cdd:cd19481 17 RLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPL 54
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
903-1060 |
3.44e-05 |
|
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: 46.64 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 903 QLLRNITGAFQPGILSALMGVTGAGKTTLldVLAGRKTGGVIEGDIRIGGypkvqQTFSRIsgycEQNDVHS-----PQi 977
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTL--ILALFRFLEAEEGKIEIDG-----IDISTI----PLEDLRSsltiiPQ- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 978 tvgESVAYSAWLRLPAEIdtktRKEFVDEvleiieldEIRDALVGTPGVNGLSREQRKRLTIAVELVSNPSIVFMDEPTS 1057
Cdd:cd03369 90 ---DPTLFSGTIRSNLDP----FDEYSDE--------EIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
...
gi 1002313595 1058 GLD 1060
Cdd:cd03369 155 SID 157
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
235-266 |
3.68e-05 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 47.98 E-value: 3.68e-05
10 20 30
....*....|....*....|....*....|..
gi 1002313595 235 IKPSRITLLLGPPGCGKTTLLKALAGRLNKSL 266
Cdd:COG0464 188 LPPPRGLLLYGPPGTGKTLLARALAGELGLPL 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
913-1060 |
3.68e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 46.88 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 913 QPGILSALMGVTGAGKTTLLDVLAGRKTGGviEGDIRIGGYPKVQQTFSR--ISGYCEQNDVHsPQITVGESVAY--SAW 988
Cdd:PRK10771 23 ERGERVAILGPSGAGKSTLLNLIAGFLTPA--SGSLTLNGQDHTTTPPSRrpVSMLFQENNLF-SHLTVAQNIGLglNPG 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002313595 989 LRLPAEidtktRKEFVDEVLEIIELDEIRDALvgtPGvnGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:PRK10771 100 LKLNAA-----QREKLHAIARQMGIEDLLARL---PG--QLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
635-829 |
3.94e-05 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 46.35 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 635 LVMSISRLPVFykhrdhylypgWAYAIPAFILkipaSLVAALSWTSISYYLIGYTPEAPRYFRQLLVLFLVHTGALSLYR 714
Cdd:COG0842 39 LVTPVSRLEIL-----------LGKVLAYLLR----GLLQALLVLLVALLFFGVPLRGLSLLLLLLVLLLFALAFSGLGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 715 CVGSYCQTIAVGPIAATMSLLVILLFGGFLIPRPSMPNWLKWGFWLSPLSYAeigltgneflaprwlkitisgVTIGRRI 794
Cdd:COG0842 104 LISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYF---------------------VEALRAL 162
|
170 180 190
....*....|....*....|....*....|....*
gi 1002313595 795 LIdRGLDFSVyfYWISVAALIGFILlynIGFAIGL 829
Cdd:COG0842 163 FL-GGAGLAD--VWPSLLVLLAFAV---VLLALAL 191
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
920-1096 |
4.07e-05 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 47.87 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 920 LMGVTGAGKTTLLDVLAG--RKTGGVIEgdIRIGGY--------PKVQQTFSRISGYCEQNDVHSPQITVGESVAYSAWL 989
Cdd:TIGR03269 315 IVGTSGAGKTTLSKIIAGvlEPTSGEVN--VRVGDEwvdmtkpgPDGRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 990 RLPAEIdtKTRKEFVDEVLEIIELDEIRDALVGTPgvNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDARaaaiamr 1069
Cdd:TIGR03269 393 ELPDEL--ARMKAVITLKMVGFDEEKAEEILDKYP--DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPI------- 461
|
170 180
....*....|....*....|....*..
gi 1002313595 1070 avknvaeTGRTVVCTIHQPSIEIFEAF 1096
Cdd:TIGR03269 462 -------TKVDVTHSILKAREEMEQTF 481
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
224-326 |
4.53e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 47.03 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 224 KVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDE-------FVPAKTSAYvsqydl 296
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD---SGEVLWDGEPLDPedrrrigYLPEERGLY------ 83
|
90 100 110
....*....|....*....|....*....|
gi 1002313595 297 hvADMTVRETLDFSARFQGVgSRAEIMKAV 326
Cdd:COG4152 84 --PKMKVGEQLVYLARLKGL-SKAEAKRRA 110
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
235-262 |
4.59e-05 |
|
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410926 [Multi-domain] Cd Length: 169 Bit Score: 45.47 E-value: 4.59e-05
10 20
....*....|....*....|....*...
gi 1002313595 235 IKPSRITLLLGPPGCGKTTLLKALAGRL 262
Cdd:cd19518 31 VEPPRGVLLHGPPGCGKTMLANAIAGEL 58
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
228-474 |
5.71e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.80 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 228 LENVSGIIKPSRITLLLGPPGCGKTTLLKALAG--RLNKslketGEIEYNGVKLDEFVPAKTSAYVSQydlhvadmtvRE 305
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGfvRLAS-----GKISILGQPTRQALQKNLVAYVPQ----------SE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 306 TLDFSarFQGVGSRAEIMKavikREKEAGITPDPDidAYMKAISMEGLQRSMQTDYIMKIMGldkcadvkvgnamrrGIS 385
Cdd:PRK15056 88 EVDWS--FPVLVEDVVMMG----RYGHMGWLRRAK--KRDRQIVTAALARVDMVEFRHRQIG---------------ELS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 386 GGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEyTILVSllqpapeTYDL-----FDDIIIMGE 460
Cdd:PRK15056 145 GGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGK-TMLVS-------THNLgsvteFCDYTVMVK 216
|
250
....*....|....
gi 1002313595 461 GKVVYHGPKNLIMT 474
Cdd:PRK15056 217 GTVLASGPTETTFT 230
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
994-1121 |
6.45e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.04 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 994 EIDTKTRKEFVDEVLEIIELDEI--RDALVGTPGVnglsreqRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAV 1071
Cdd:NF000106 115 DLSRKDARARADELLERFSLTEAagRAAAKYSGGM-------RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV 187
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1072 KNVAETGRTVVCTIhQPSIEIFEAFDELMLIKRgGELIYAGPLGQHSCKV 1121
Cdd:NF000106 188 RSMVRDGATVLLTT-QYMEEAEQLAHELTVIDR-GRVIADGKVDELKTKV 235
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
216-295 |
6.47e-05 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 45.29 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 216 LGFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVPA---KTSAYVS 292
Cdd:cd03246 6 VSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT---SGRVRLDGADISQWDPNelgDHVGYLP 82
|
...
gi 1002313595 293 QYD 295
Cdd:cd03246 83 QDD 85
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
218-464 |
6.96e-05 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 47.47 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 218 FSHHQSKvQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVPA---KTSAYVSQy 294
Cdd:COG1132 347 FSYPGDR-PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT---SGRILIDGVDIRDLTLEslrRQIGVVPQ- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 295 DLHVADMTVRETLDF---SArfqgvgSRAEIMKAVikreKEAGITPDpdidaymkaismeglqrsmqtdyimkIMGLDKC 371
Cdd:COG1132 422 DTFLFSGTIRENIRYgrpDA------TDEEVEEAA----KAAQAHEF--------------------------IEALPDG 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 372 ADVKVGnamRRGI--SGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHisEYTILV-----SLLQP 444
Cdd:COG1132 466 YDTVVG---ERGVnlSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIViahrlSTIRN 540
|
250 260
....*....|....*....|
gi 1002313595 445 ApetydlfDDIIIMGEGKVV 464
Cdd:COG1132 541 A-------DRILVLDDGRIV 553
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
903-1087 |
7.35e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 46.12 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 903 QLLRNITGAFQPGILSALMGVTGAGKTTLL---DVLAGRKTGGVI------------EGDIRIGGYPKVQQTFSRISGYC 967
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLrciNFLEKPSEGSIVvngqtinlvrdkDGQLKVADKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 968 EQNDVHSpQITVGESVaysawLRLPAEIDTKTRKEFVDEVLEIIELDEIRDALVGTPGVNgLSREQRKRLTIAVELVSNP 1047
Cdd:PRK10619 99 QHFNLWS-HMTVLENV-----MEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVH-LSGGQQQRVSIARALAMEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1002313595 1048 SIVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQ 1087
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| rad24 |
TIGR00602 |
checkpoint protein rad24; All proteins in this family for which functions are known are ... |
224-281 |
7.46e-05 |
|
checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).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: 129690 [Multi-domain] Cd Length: 637 Bit Score: 47.26 E-value: 7.46e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002313595 224 KVQILENvsgiiKPSRITLLLGPPGCGKTTLLKALAGRLNKSLKETgeieYNGVKLDE 281
Cdd:TIGR00602 101 KAQVLEN-----APKRILLITGPSGCGKSTTIKILSKELGIQVQEW----SNPTLPDF 149
|
|
| RecA-like_CDC48_r2-like |
cd19511 |
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ... |
235-260 |
7.63e-05 |
|
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410919 [Multi-domain] Cd Length: 159 Bit Score: 44.58 E-value: 7.63e-05
10 20
....*....|....*....|....*.
gi 1002313595 235 IKPSRITLLLGPPGCGKTTLLKALAG 260
Cdd:cd19511 24 IRPPKGVLLYGPPGCGKTLLAKALAS 49
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
914-1060 |
7.89e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 45.61 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 914 PGILSALMGVTGAGKTTLLDVLAGRKTGGviEGDIRIGGYPKVQQTFSRISGYCEQNDVHSPQITVGESVAYSAWLRlpa 993
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVE--SGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLH--- 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002313595 994 eidTKTRKEFVDEVLEIIELDEIRDALVgtpgvNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:PRK13543 111 ---GRRAKQMPGSALAIVGLAGYEDTLV-----RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
902-1086 |
8.37e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 46.23 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 902 LQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGR--KTGGVIEGDIRiggYPKVQQTFSRISGYCEQNDVHSP---- 975
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllPDTGTIEWIFK---DEKNKKKTKEKEKVLEKLVIQKTrfkk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 976 --------------------QI---TVGESVAYSAwlrLPAEIDTKTRKEFVDEVLEIIELDEirDALVGTPgvNGLSRE 1032
Cdd:PRK13651 97 ikkikeirrrvgvvfqfaeyQLfeqTIEKDIIFGP---VSMGVSKEEAKKRAAKYIELVGLDE--SYLQRSP--FELSGG 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002313595 1033 QRKRLTIAVELVSNPSIVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIH 1086
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
226-415 |
1.05e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.55 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 226 QILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSLKEtGEIEYNGVKLDEFVPAKTsayvsqydlhvADMTVRE 305
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTG-GTVEFKGKDLLELSPEDR-----------AGEGIFM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 306 TLDFSARFQGVGSRAEIMKAVikrekeagitpdpdiDAYMKAISMEGLQRSMQTDYIM-KIMGLDKCADVkVGNAMRRGI 384
Cdd:PRK09580 83 AFQYPVEIPGVSNQFFLQTAL---------------NAVRSYRGQEPLDRFDFQDLMEeKIALLKMPEDL-LTRSVNVGF 146
|
170 180 190
....*....|....*....|....*....|.
gi 1002313595 385 SGGEMKRLTTGEMIVGPCKVLLMDEISTGLD 415
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLD 177
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
228-327 |
1.15e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 45.31 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 228 LENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlketGEIEYNGVKLDEFVPAKTS---AYVSQYDLHVADMTVR 304
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS----GSIQFAGQPLEAWSAAELArhrAYLSQQQTPPFAMPVF 87
|
90 100
....*....|....*....|...
gi 1002313595 305 ETLdfsARFQGVGSRAEIMKAVI 327
Cdd:PRK03695 88 QYL---TLHQPDKTRTEAVASAL 107
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
242-268 |
1.44e-04 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 42.97 E-value: 1.44e-04
10 20
....*....|....*....|....*..
gi 1002313595 242 LLLGPPGCGKTTLLKALAGRLNKSLKE 268
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAPFIE 28
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
903-1087 |
1.48e-04 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 45.01 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 903 QLLRNITGAFQPGILSALMGVTGAGKTTLLDVLagrktgGVIE----GDIRIGGY---------PKVQQTFSRISGYCEQ 969
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVL------NLLEmprsGTLNIAGNhfdfsktpsDKAIRELRRNVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 970 NDVHSPQITVGESVAySAWLRLpAEIDTKTRKEFVDEVLEIIELDEIRDALvgtPgvNGLSREQRKRLTIAVELVSNPSI 1049
Cdd:PRK11124 90 QYNLWPHLTVQQNLI-EAPCRV-LGLSKDQALARAEKLLERLRLKPYADRF---P--LHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002313595 1050 VFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQ 1087
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
891-1060 |
1.57e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 44.70 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 891 EMRKKGYMGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG--RKTGGVI--EGDiRIGGYPKvqQTFSRISGY 966
Cdd:PRK10247 9 QLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASliSPTSGTLlfEGE-DISTLKP--EIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 967 CEQndvhSPQItVGESVaYSAwLRLPAEIDTKT--RKEFVDEvLEIIELDEIrdalVGTPGVNGLSREQRKRLTIAVELV 1044
Cdd:PRK10247 86 CAQ----TPTL-FGDTV-YDN-LIFPWQIRNQQpdPAIFLDD-LERFALPDT----ILTKNIAELSGGEKQRISLIRNLQ 153
|
170
....*....|....*.
gi 1002313595 1045 SNPSIVFMDEPTSGLD 1060
Cdd:PRK10247 154 FMPKVLLLDEITSALD 169
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
914-1109 |
1.64e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.15 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 914 PGILSALMGVTGAGKTTLLDVLAG--RKTGGVIE--GDIRIGGYPKVQQT--FSRIsgYCEQNDVhsPQITVGESV---- 983
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGiyTRDAGSILylGKEVTFNGPKSSQEagIGII--HQELNLI--PQLTIAENIflgr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 984 -AYSAWLRlpaeIDTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDAR 1062
Cdd:PRK10762 105 eFVNRFGR----IDWKKMYAEADKLLARLNLRFSSDKLVGE-----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002313595 1063 AAAIAMRAVKNVAETGRTVVCTIHQPSiEIFEAFDELMLIkRGGELI 1109
Cdd:PRK10762 176 ETESLFRVIRELKSQGRGIVYISHRLK-EIFEICDDVTVF-RDGQFI 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
905-1060 |
1.65e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 45.42 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAG---RKTGGVIEGDIRIGGyPKVQQTFSRIS-GYCEQNDVHspQI--- 977
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGllkPTSGKIIIDGVDITD-KKVKLSDIRKKvGLVFQYPEY--QLfee 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 978 TVGESVAYSAWLRLPAEIDTKTRkefVDEVLEIIELD--EIRDAlvgTPgvNGLSREQRKRLTIAVELVSNPSIVFMDEP 1055
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENR---VKRAMNIVGLDyeDYKDK---SP--FELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
....*
gi 1002313595 1056 TSGLD 1060
Cdd:PRK13637 172 TAGLD 176
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
925-1060 |
1.68e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 925 GAGKTT-------LLDVLAGRKT--GGVIE-GDI----RIGgYpkVQQTFSRisgYCE----QN-DVHspqitvgesvay 985
Cdd:NF033858 302 GCGKSTtmkmltgLLPASEGEAWlfGQPVDaGDIatrrRVG-Y--MSQAFSL---YGEltvrQNlELH------------ 363
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002313595 986 sAWL-RLPAEiDTKTRkefVDEVLEIIELDEIRDALvgtPGvnGLSREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:NF033858 364 -ARLfHLPAA-EIAAR---VAEMLERFDLADVADAL---PD--SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| SpoIIIAA |
COG3854 |
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome ... |
234-259 |
1.69e-04 |
|
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443063 Cd Length: 309 Bit Score: 45.53 E-value: 1.69e-04
10 20
....*....|....*....|....*...
gi 1002313595 234 IIKPSRI--TLLLGPPGCGKTTLLKALA 259
Cdd:COG3854 134 IISGGRIynTLIISPPGCGKTTLLRDIA 161
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
902-1090 |
1.73e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 46.26 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 902 LQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLA--GRKTGGVIegdiRIGGypkvqQTFSRIS------------GYC 967
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGclDKPTSGTY----RVAG-----QDVATLDadalaqlrrehfGFI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 968 EQNDVHSPQITVGESVAYSAwlrLPAEIDTKTRKEFVDEVLEIIELDEIRDAlvgTPgvNGLSREQRKRLTIAVELVSNP 1047
Cdd:PRK10535 92 FQRYHLLSHLTAAQNVEVPA---VYAGLERKQRLLRAQELLQRLGLEDRVEY---QP--SQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1002313595 1048 SIVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSI 1090
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQV 206
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
157-308 |
1.93e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 157 VRMLRKQR-ERMERvgvrpatvevrwRDVCVEAECQVV----SGKPLPTLWNAALSrfslLAAKlgfshhqskvQILENV 231
Cdd:PRK11147 285 VRALKALRrERSER------------REVMGTAKMQVEeasrSGKIVFEMENVNYQ----IDGK----------QLVKDF 338
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002313595 232 SG-IIKPSRITLLlGPPGCGKTTLLKALAGRLNkslKETGEIeYNGVKLDefvpaktSAYVSQYdlhvadmtvRETLD 308
Cdd:PRK11147 339 SAqVQRGDKIALI-GPNGCGKTTLLKLMLGQLQ---ADSGRI-HCGTKLE-------VAYFDQH---------RAELD 395
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
884-1060 |
2.02e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 45.00 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 884 YYVDTPPEMRKkgymgrklqlLRNITGAFQPGILSALMGVTGAGKTTLLDVLAG---RKTGGVIEGDIRI-GGYPKVQQT 959
Cdd:PRK13645 16 YAKKTPFEFKA----------LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGliiSETGQTIVGDYAIpANLKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 960 --FSRISGYCEQ-NDVHSPQITVGESVAYSAwLRLPAEIDTKTRKefVDEVLEIIELDeiRDALVGTPgvNGLSREQRKR 1036
Cdd:PRK13645 86 krLRKEIGLVFQfPEYQLFQETIEKDIAFGP-VNLGENKQEAYKK--VPELLKLVQLP--EDYVKRSP--FELSGGQKRR 158
|
170 180
....*....|....*....|....
gi 1002313595 1037 LTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLD 182
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
224-463 |
2.05e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 45.59 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 224 KVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKslKETGEIEYNGVKLDEFVPAKTSAyvsqydlhvadmtv 303
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPG--KFEGNVFINGKPVDIRNPAQAIR-------------- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 304 retldfsarfQGVGsraeimkAVIKREKEAGITPDPDIDaymKAISMEGLQRsmqtdyIMKIMGLDKCADVK-VGNAMRR 382
Cdd:TIGR02633 336 ----------AGIA-------MVPEDRKRHGIVPILGVG---KNITLSVLKS------FCFKMRIDAAAELQiIGSAIQR 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 383 -------------GISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILVSllQPAPETY 449
Cdd:TIGR02633 390 lkvktaspflpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVS--SELAEVL 467
|
250
....*....|....
gi 1002313595 450 DLFDDIIIMGEGKV 463
Cdd:TIGR02633 468 GLSDRVLVIGEGKL 481
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
236-265 |
2.25e-04 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 43.29 E-value: 2.25e-04
10 20 30
....*....|....*....|....*....|
gi 1002313595 236 KPSRITLLLGPPGCGKTTLLKALAGRLNKS 265
Cdd:cd00009 17 PPPKNLLLYGPPGTGKTTLARAIANELFRP 46
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
904-1087 |
2.30e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.17 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 904 LLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGviEGDIRIGG--YPKVQQTFSRISGYCEQNDVHSPQITVGE 981
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPE--KGEILFERqsIKKDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 982 SVAYsawlrlpaEIDTKTRKEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNPSIVFMDEPTSGLDA 1061
Cdd:PRK13540 94 NCLY--------DIHFSPGAVGITELCRLFSLEHLIDYPCGL-----LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180
....*....|....*....|....*.
gi 1002313595 1062 RAAAIAMRAVKNVAETGRTVVCTIHQ 1087
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
895-1059 |
2.89e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.43 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 895 KGYMGrkLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGviEGDIRIGGYPKVQQTFSRISGY----CEQN 970
Cdd:PRK15439 19 KQYSG--VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD--SGTLEIGGNPCARLTPAKAHQLgiylVPQE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 971 DVHSPQITVGESVAYsawlRLPAEIDTKTR-KEFVDEVLEIIELdeirDALVGTpgvngLSREQRKRLTIAVELVSNPSI 1049
Cdd:PRK15439 95 PLLFPNLSVKENILF----GLPKRQASMQKmKQLLAALGCQLDL----DSSAGS-----LEVADRQIVEILRGLMRDSRI 161
|
170
....*....|
gi 1002313595 1050 VFMDEPTSGL 1059
Cdd:PRK15439 162 LILDEPTASL 171
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
893-1112 |
2.94e-04 |
|
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: 44.06 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 893 RKKGYMGRKlQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLAgrktgGVI---EGDIRIGGypkvqqtfsRISGYCEQ 969
Cdd:cd03220 27 GRKGEVGEF-WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLA-----GIYppdSGTVTVRG---------RVSSLLGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 970 NDVHSPQITVGESVAYSAWL--RLPAEIDtktrkEFVDEVLEIIELDEIRDALVGTpgvngLSREQRKRLTIAVELVSNP 1047
Cdd:cd03220 92 GGGFNPELTGRENIYLNGRLlgLSRKEID-----EKIDEIIEFSELGDFIDLPVKT-----YSSGMKARLAFAIATALEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002313595 1048 SIVFMDEPTSGLDARAAAIAMRAVKNVAETGRTVVCTIHQPSIeIFEAFDELMLIKRgGELIYAG 1112
Cdd:cd03220 162 DILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEK-GKIRFDG 224
|
|
| Rad17 |
pfam03215 |
Rad17 P-loop domain; |
224-268 |
2.99e-04 |
|
Rad17 P-loop domain;
Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 43.41 E-value: 2.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1002313595 224 KVQILENvsgiiKPSRITLLLGPPGCGKTTLLKALAGRLNKSLKE 268
Cdd:pfam03215 36 DAMFLEN-----AKHRILLISGPSGCGKSTVIKELSKELGPKYRE 75
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
224-415 |
3.00e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.83 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 224 KVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrlnksLKET--GEIEYNGVKLDEFVPA-KTSAYVSQ-YDL--H 297
Cdd:PRK11650 16 KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG-----LERItsGEIWIGGRVVNELEPAdRDIAMVFQnYALypH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 298 vadMTVRETLDFSARFQGVGsRAEIMkaviKREKEAGitpdpdidaymkaismeglqrsmqtdyimKIMGLDKCADVKvg 377
Cdd:PRK11650 91 ---MSVRENMAYGLKIRGMP-KAEIE----ERVAEAA-----------------------------RILELEPLLDRK-- 131
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002313595 378 namRRGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLD 415
Cdd:PRK11650 132 ---PRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
81-264 |
3.19e-04 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 45.57 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 81 ELKRKWAAIERLPTADRLRLSLLSSTRGGGSSGDVSEGGGGGAASSELEVVDVRWLGAAERRAVVQRLVADVKHDHVRML 160
Cdd:COG5635 26 AIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAAALLARALSALLLVLLLLESLLLLLLLLLLLAEALL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 161 RKQRERMERVGVRPATVEVRWRDVCVEAECQVVSGKPLPTLWNAALSRFSLLAAKLGFSHHQSKVQILEnvsGIIKPSRI 240
Cdd:COG5635 106 ALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLERIESLKRLE---LLEAKKKR 182
|
170 180
....*....|....*....|....
gi 1002313595 241 TLLLGPPGCGKTTLLKALAGRLNK 264
Cdd:COG5635 183 LLILGEPGSGKTTLLRYLALELAE 206
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
218-467 |
3.25e-04 |
|
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: 43.75 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 218 FSHhQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNkslKETGEIEYNGV---KLDEFVPAKTSAYVSQy 294
Cdd:cd03254 10 FSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD---PQKGQILIDGIdirDISRKSLRSMIGVVLQ- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 295 DLHVADMTVRETLDFSarfqgvGSRAEiMKAVIKREKEAGItpdpdidaymkaismeglqrsmqTDYIMKimgLDKCADV 374
Cdd:cd03254 85 DTFLFSGTIMENIRLG------RPNAT-DEEVIEAAKEAGA-----------------------HDFIMK---LPNGYDT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 375 KVGNAmRRGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHisEYTILV-----SLLQPApety 449
Cdd:cd03254 132 VLGEN-GGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIiahrlSTIKNA---- 204
|
250
....*....|....*...
gi 1002313595 450 dlfDDIIIMGEGKVVYHG 467
Cdd:cd03254 205 ---DKILVLDDGKIIEEG 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
227-394 |
3.62e-04 |
|
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: 43.25 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 227 ILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNkslKETGEIEYNGVKLDEFVP--AKTSAYVSQYDLHVADMTVR 304
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP---PLAGRVLLNGGPLDFQRDsiARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 305 ETLDFSARFqgvGSRAEIMKAVikreKEAGITPDPDID-AYMKAismeGLQR---------SMQTDYIMK--IMGLDKCA 372
Cdd:cd03231 92 ENLRFWHAD---HSDEQVEEAL----ARVGLNGFEDRPvAQLSA----GQQRrvalarlllSGRPLWILDepTTALDKAG 160
|
170 180
....*....|....*....|..
gi 1002313595 373 DVKVGNAMRRGISGGEMKRLTT 394
Cdd:cd03231 161 VARFAEAMAGHCARGGMVVLTT 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
225-280 |
3.87e-04 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 42.80 E-value: 3.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002313595 225 VQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNkslKETGEIEYNGVKLD 280
Cdd:cd03216 13 VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK---PDSGEILVDGKEVS 65
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
225-467 |
4.35e-04 |
|
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: 43.48 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 225 VQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGvkldeFVPAK-TSAYVSQYDLHVA---- 299
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPT---SGEVRVAG-----LVPWKrRKKFLRRIGVVFGqktq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 300 ---DMTVRETLDFSARFQGVgsraeimkavikrekeagitpdpDIDAYMKAIsmeglqrsmqtDYIMKIMGLDKCADVKV 376
Cdd:cd03267 106 lwwDLPVIDSFYLLAAIYDL-----------------------PPARFKKRL-----------DELSELLDLEELLDTPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 377 gnamrRGISGGE-MKRLTTGEMIVGPcKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILVSllqpapeTYDLfDDI 455
Cdd:cd03267 152 -----RQLSLGQrMRAEIAAALLHEP-EILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLT-------SHYM-KDI 217
|
250
....*....|....*....
gi 1002313595 456 -------IIMGEGKVVYHG 467
Cdd:cd03267 218 ealarrvLVIDKGRLLYDG 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
898-1059 |
5.11e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.53 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 898 MGRKLQLLRNITGAF-------------QPGILSALMGVTGAGKTTLLDVLAGRKTGGVIEGDIRIGGYPkvqQTFSRIS 964
Cdd:PRK13549 1 MMEYLLEMKNITKTFggvkaldnvslkvRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEE---LQASNIR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 965 GyCEQNDV---HS-----PQITVGESVAysawlrLPAEIDTKTRKEFVDEVLEIIE-LDEIR-DALVGTPgVNGLSREQR 1034
Cdd:PRK13549 78 D-TERAGIaiiHQelalvKELSVLENIF------LGNEITPGGIMDYDAMYLRAQKlLAQLKlDINPATP-VGNLGLGQQ 149
|
170 180
....*....|....*....|....*
gi 1002313595 1035 KRLTIAVELVSNPSIVFMDEPTSGL 1059
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASL 174
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
225-357 |
5.46e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.52 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 225 VQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLdEFVPAKTS-----AYVSQyDLH-V 298
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD---AGSILIDGQEM-RFASTTAAlaagvAIIYQ-ELHlV 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002313595 299 ADMTVRETL---DFSARFqGVGSRAEIMKAVIKREKEAGITPDPdiDAYMKAISMEglQRSM 357
Cdd:PRK11288 92 PEMTVAENLylgQLPHKG-GIVNRRLLNYEAREQLEHLGVDIDP--DTPLKYLSIG--QRQM 148
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
905-1109 |
6.35e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 44.05 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTGGVIEGDIRIGGYPKVQQTFSRIS----GYCEQNDVHSPQITVG 980
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTEragiVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 981 ESVAYSAWLRLPAEI---DTKTRKefVDEVLEIIELDEIRDALvgtpGVNGLSREQRKRLTIAVELVSNPSIVFMDEPTS 1057
Cdd:TIGR02633 97 ENIFLGNEITLPGGRmayNAMYLR--AKNLLRELQLDADNVTR----PVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002313595 1058 GLDARAAAIAMRAVKNVAETGrtVVCTIHQPSIEIFEAFDELMLIKRGGELI 1109
Cdd:TIGR02633 171 SLTEKETEILLDIIRDLKAHG--VACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
227-260 |
6.57e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 44.03 E-value: 6.57e-04
10 20 30
....*....|....*....|....*....|....
gi 1002313595 227 ILENVSGIIKPSRITLLLGPPGCGKTTLLKALAG 260
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG 411
|
|
| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
232-259 |
6.66e-04 |
|
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410928 [Multi-domain] Cd Length: 166 Bit Score: 42.03 E-value: 6.66e-04
10 20
....*....|....*....|....*...
gi 1002313595 232 SGIIKPSRITLLLGPPGCGKTTLLKALA 259
Cdd:cd19520 29 SRLLQPPKGVLLYGPPGCGKTMLAKATA 56
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
895-1060 |
6.81e-04 |
|
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: 41.67 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 895 KGYMGRKLqlLRNITGAFQPGILSALMGVTGAGKTTLLDVLAGRKTggVIEGDIRIGGYPKVqqtfsrisGYCEQndvhs 974
Cdd:cd03221 8 KTYGGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELE--PDEGIVTWGSTVKI--------GYFEQ----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 975 pqitvgesvaysawlrlpaeidtktrkefvdevleiieldeirdalvgtpgvngLSREQRKRLTIAVELVSNPSIVFMDE 1054
Cdd:cd03221 71 ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
....*.
gi 1002313595 1055 PTSGLD 1060
Cdd:cd03221 97 PTNHLD 102
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
224-276 |
6.97e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 43.53 E-value: 6.97e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1002313595 224 KVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNG 276
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT---SGHIRFHG 63
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
226-471 |
7.25e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 43.23 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 226 QILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKldefVPAKTSayvsqyDLHVAdmTVRE 305
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPT---TGTVTVDDIT----ITHKTK------DKYIR--PVRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 306 TLDFSARFqgvgSRAEIMKAVIKREKEAGitpDPDIDAYMKAISMEGLQRSMQTDYIMKIMGLDKCAdvkvgnamrrgIS 385
Cdd:PRK13646 86 RIGMVFQF----PESQLFEDTVEREIIFG---PKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQ-----------MS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 386 GGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTI-LVSllQPAPETYDLFDDIIIMGEGKVV 464
Cdd:PRK13646 148 GGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIiLVS--HDMNEVARYADEVIVMKEGSIV 225
|
....*...
gi 1002313595 465 YHG-PKNL 471
Cdd:PRK13646 226 SQTsPKEL 233
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
217-284 |
7.26e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 42.64 E-value: 7.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002313595 217 GFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLnKSLKETGEIEYNGVKLDEFVP 284
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL-KGTPVAGCVDVPDNQFGREAS 101
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
232-259 |
8.25e-04 |
|
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410917 [Multi-domain] Cd Length: 163 Bit Score: 41.57 E-value: 8.25e-04
10 20
....*....|....*....|....*...
gi 1002313595 232 SGIIKPSRITLLLGPPGCGKTTLLKALA 259
Cdd:cd19509 26 PGLRGPPRGILLYGPPGTGKTLLARAVA 53
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
227-260 |
8.35e-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: 41.76 E-value: 8.35e-04
10 20 30
....*....|....*....|....*....|....
gi 1002313595 227 ILENVSGIIKPSRITLLLGPPGCGKTTLLKALAG 260
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG 49
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
228-326 |
1.19e-03 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 42.90 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 228 LENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVPAK--TSAYVSQYDLhVADMTVRE 305
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPT---AGQIMLDGVDLSHVPPYQrpINMMFQSYAL-FPHMTVEQ 110
|
90 100
....*....|....*....|.
gi 1002313595 306 TLDFSARfQGVGSRAEIMKAV 326
Cdd:PRK11607 111 NIAFGLK-QDKLPKAEIASRV 130
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
221-335 |
1.29e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 42.38 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 221 HQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGvkldefvpaKTSAYVsqyDLHVA- 299
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT---SGRVEVNG---------RVSALL---ELGAGf 99
|
90 100 110
....*....|....*....|....*....|....*...
gi 1002313595 300 --DMTVRETLDFSARFQGVgSRAEImkavikREKEAGI 335
Cdd:COG1134 100 hpELTGRENIYLNGRLLGL-SRKEI------DEKFDEI 130
|
|
| pup_AAA |
TIGR03689 |
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ... |
235-270 |
1.30e-03 |
|
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some proteins are modified by ligation between an epsilon-amino group of a lysine side chain and the C-terminal carboxylate of the ubiquitin-like protein Pup. This modification leads to protein degradation by the archaeal-like proteasome found in the Actinobacteria. Members of this protein family belong to the AAA family of ATPases and tend to be clustered with the genes for Pup, the Pup ligase PafA, and structural components of the proteasome. This protein forms hexameric rings with ATPase activity. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 200312 [Multi-domain] Cd Length: 512 Bit Score: 43.16 E-value: 1.30e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1002313595 235 IKPSRITLLLGPPGCGKTTLLKALAGRLNKSLKETG 270
Cdd:TIGR03689 213 LKPPKGVLLYGPPGCGKTLIAKAVANSLAARIGAEG 248
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
235-468 |
1.42e-03 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 42.05 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 235 IKPSRITLLLGPPGCGKTTLLKALAGRLNkslKETGEIEYNGVKLDEFVPAKTSayVS----QYDL--HvadMTVRETLD 308
Cdd:COG3840 22 IAAGERVAILGPSGAGKSTLLNLIAGFLP---PDSGRILWNGQDLTALPPAERP--VSmlfqENNLfpH---LTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 309 FsarfqgvgsraeimkavikrekeaGITPDPDIDAYMKAISMEGLQRsmqtdyimkiMGLDKCADVKVGNamrrgISGGE 388
Cdd:COG3840 94 L------------------------GLRPGLKLTAEQRAQVEQALER----------VGLAGLLDRLPGQ-----LSGGQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 389 MKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILVSLLQPApETYDLFDDIIIMGEGKVVYHGP 468
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPE-DAARIADRVLLVADGRIAADGP 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
905-1112 |
1.42e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 42.71 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAFQPGILSALMGVTGAGKTT---LLDVLAGRKTGGV-IEG-DIRIGGYPKVQQTFSRISGYCEQNDVHSPQITV 979
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTmvrLLNRLIEPTRGQVlIDGvDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 980 GESVAYSAWLrlpAEIDTKTRKEFVDEVLEIIELDEIRDalvGTPgvNGLSREQRKRLTIAVELVSNPSIVFMDEPTSGL 1059
Cdd:PRK10070 124 LDNTAFGMEL---AGINAEERREKALDALRQVGLENYAH---SYP--DELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1060 D-ARAAAIAMRAVKNVAETGRTVVCTIHQpsieifeaFDELM------LIKRGGELIYAG 1112
Cdd:PRK10070 196 DpLIRTEMQDELVKLQAKHQRTIVFISHD--------LDEAMrigdriAIMQNGEVVQVG 247
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
221-436 |
1.44e-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: 43.00 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 221 HQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrLNKslketgeiEYNGvkldEFVPAK--TSAYVSQYDLHV 298
Cdd:TIGR03719 14 VPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDK--------DFNG----EARPQPgiKVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 299 ADMTVRETLdfsarFQGVGSraeiMKAVIKREKE---AGITPDPDIDAYMKaiSMEGLQRSMQT----DYIMKI-MGLD- 369
Cdd:TIGR03719 81 PTKTVRENV-----EEGVAE----IKDALDRFNEisaKYAEPDADFDKLAA--EQAELQEIIDAadawDLDSQLeIAMDa 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002313595 370 -KCA--DVKVGNamrrgISGGEMKRlttgemiVGPCK-------VLLMDEISTGLDSSTtfqiVSCLQQlaHISEYT 436
Cdd:TIGR03719 150 lRCPpwDADVTK-----LSGGERRR-------VALCRlllskpdMLLLDEPTNHLDAES----VAWLER--HLQEYP 208
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
443-497 |
1.47e-03 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 42.97 E-value: 1.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002313595 443 QPAPETYDLFDDIIIMGEG-KVVYHGPKNLIMTFFESCGFKCPERKGPADFLQEVL 497
Cdd:pfam19055 2 QPSYTLFKMFDDLILLAKGgLTVYHGPVKKVEEYFAGLGINVPERVNPPDHFIDIL 57
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
221-435 |
1.58e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 221 HQSKVQILENVS---------GIikpsritllLGPPGCGKTTLLKALAGrLNKslketgeiEYNGvkldEFVPAK--TSA 289
Cdd:PRK11819 16 VPPKKQILKDISlsffpgakiGV---------LGLNGAGKSTLLRIMAG-VDK--------EFEG----EARPAPgiKVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 290 YVSQYDLHVADMTVRETLDfsarfQGVGsraEImKAVIKR-----EKEAgiTPDPDIDAYMKaiSMEGLQRSMQT----- 359
Cdd:PRK11819 74 YLPQEPQLDPEKTVRENVE-----EGVA---EV-KAALDRfneiyAAYA--EPDADFDALAA--EQGELQEIIDAadawd 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 360 -DYIMKI-MGLDKC--ADVKVGNamrrgISGGEMKRlttgemiVGPCK-------VLLMDEISTGLDSSTtfqiVSCLQQ 428
Cdd:PRK11819 141 lDSQLEIaMDALRCppWDAKVTK-----LSGGERRR-------VALCRlllekpdMLLLDEPTNHLDAES----VAWLEQ 204
|
....*..
gi 1002313595 429 laHISEY 435
Cdd:PRK11819 205 --FLHDY 209
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
235-259 |
1.62e-03 |
|
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410911 [Multi-domain] Cd Length: 165 Bit Score: 40.74 E-value: 1.62e-03
10 20
....*....|....*....|....*
gi 1002313595 235 IKPSRITLLLGPPGCGKTTLLKALA 259
Cdd:cd19503 31 LKPPRGVLLHGPPGTGKTLLARAVA 55
|
|
| RNA_helicase |
pfam00910 |
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ... |
242-316 |
1.75e-03 |
|
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.
Pssm-ID: 459992 Cd Length: 102 Bit Score: 39.12 E-value: 1.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002313595 242 LLLGPPGCGKTTLLKALAGRLNKSLKETGEIEYNGVKLDEFvpakTSAYVSQyDLHVADmtvretlDFSARFQGV 316
Cdd:pfam00910 2 WLYGPPGCGKSTLAKYLARALLKKLGLPKDSVYSRNPDDDF----WDGYTGQ-PVVIID-------DFGQNPDGP 64
|
|
| RecA-like_Pch2-like |
cd19508 |
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ... |
232-262 |
1.77e-03 |
|
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as Thyroid hormone receptor interactor 13 (TRIP13) and 16E1BP) is a key regulator of specific chromosomal events, like the control of G2/prophase processes such as DNA break formation and recombination, checkpoint signaling, and chromosome synapsis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion
Pssm-ID: 410916 [Multi-domain] Cd Length: 199 Bit Score: 41.28 E-value: 1.77e-03
10 20 30
....*....|....*....|....*....|.
gi 1002313595 232 SGIIKPSRITLLLGPPGCGKTTLLKALAGRL 262
Cdd:cd19508 46 TNLITWNRLVLLHGPPGTGKTSLCKALAQKL 76
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
245-308 |
1.81e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 40.16 E-value: 1.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002313595 245 GPPGCGKTTLLKALAGRLNKSLKETGEIeyngvKLDEFvpaktSAYVSQYDLHVAdmtVRETLD 308
Cdd:cd02020 6 GPAGSGKSTVAKLLAKKLGLPYLDTGGI-----RTEEV-----GKLASEVAAIPE---VRKALD 56
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
217-415 |
1.96e-03 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 41.55 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 217 GFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVPAKTS-------A 289
Cdd:cd03290 6 GYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTL---EGKVHWSNKNESEPSFEATRsrnrysvA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 290 YVSQYDLhVADMTVRETLDFSARFQgvgsrAEIMKAVIKrekeaGITPDPDIDAymkaismegLQRSMQTDyimkimgld 369
Cdd:cd03290 83 YAAQKPW-LLNATVEENITFGSPFN-----KQRYKAVTD-----ACSLQPDIDL---------LPFGDQTE--------- 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1002313595 370 kcadvkVGnamRRGI--SGGEMKRLTTGEMIVGPCKVLLMDEISTGLD 415
Cdd:cd03290 134 ------IG---ERGInlSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
226-431 |
2.01e-03 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 41.64 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 226 QILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLDEFVPAKtsayvsqydLHVaDMTVRE 305
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPD---EGVIKRNGKLRIGYVPQK---------LYL-DTTLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 306 TLDFSARFQGVGSRAEIMKAvIKREKEAGItpdpdidaymkaismegLQRSMQTdyimkimgldkcadvkvgnamrrgIS 385
Cdd:PRK09544 85 TVNRFLRLRPGTKKEDILPA-LKRVQAGHL-----------------IDAPMQK------------------------LS 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1002313595 386 GGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAH 431
Cdd:PRK09544 123 GGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRR 168
|
|
| RecA-like_BCS1 |
cd19510 |
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ... |
242-265 |
2.45e-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: 2.45e-03
10 20
....*....|....*....|....
gi 1002313595 242 LLLGPPGCGKTTLLKALAGRLNKS 265
Cdd:cd19510 27 LLYGPPGTGKSSFIAALAGELDYD 50
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
224-322 |
2.59e-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: 40.98 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 224 KVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLnksLKETGEIEYNGvkldefvpaKTSAYVsqyDLHVA---D 300
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIY---PPDSGTVTVRG---------RVSSLL---GLGGGfnpE 98
|
90 100
....*....|....*....|..
gi 1002313595 301 MTVRETLDFSARFQGVgSRAEI 322
Cdd:cd03220 99 LTGRENIYLNGRLLGL-SRKEI 119
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
384-467 |
2.74e-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: 40.38 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 384 ISGGEMKRLTTGEMIVGPCK--VLLMDEISTGLDSSTTFQIVSCLQQLAHISEYTILVsllQPAPETYDLFDDIIIMGE- 460
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILI---EHNLDVLSSADWIIDFGPg 164
|
90
....*....|..
gi 1002313595 461 -----GKVVYHG 467
Cdd:cd03238 165 sgksgGKVVFSG 176
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
220-469 |
2.98e-03 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 40.81 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 220 HHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGrlnkSLKET-GEIEYNGVKLDEfVPAKTSAY-------V 291
Cdd:COG2884 10 RYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG----EERPTsGQVLVNGQDLSR-LKRREIPYlrrrigvV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 292 SQyDLH-VADMTVRETLDFSARFQGVgSRAEIMKAVikrekeagitpdpdidayMKAISMEGLqrsmqtdyimkimgLDK 370
Cdd:COG2884 85 FQ-DFRlLPDRTVYENVALPLRVTGK-SRKEIRRRV------------------REVLDLVGL--------------SDK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 371 cadvkvGNAMRRGISGGEMKRLTTGEMIVG-PcKVLLMDEiSTG-LDSSTTFQIVSCLQQLaHISEYTILVSllqpapeT 448
Cdd:COG2884 131 ------AKALPHELSGGEQQRVAIARALVNrP-ELLLADE-PTGnLDPETSWEIMELLEEI-NRRGTTVLIA-------T 194
|
250 260
....*....|....*....|....*..
gi 1002313595 449 YD--LFDD----IIIMGEGKVVYHGPK 469
Cdd:COG2884 195 HDleLVDRmpkrVLELEDGRLVRDEAR 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
877-1060 |
3.02e-03 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 41.15 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 877 ISFQDVNYYvdtppemrkkgYMGRKLQLLRNITGAFQPGILSALMGVTGAGKTTLLDVLagrktGGVI---EGDIRIGGY 953
Cdd:PRK13635 6 IRVEHISFR-----------YPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLL-----NGLLlpeAGTITVGGM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 954 PKVQQTFSRIS---GYCEQN-DVHSPQITVGESVAYSAwlrlpaEIDTKTRKEFVDEVLEIIELDEIRDALVGTPgvNGL 1029
Cdd:PRK13635 70 VLSEETVWDVRrqvGMVFQNpDNQFVGATVQDDVAFGL------ENIGVPREEMVERVDQALRQVGMEDFLNREP--HRL 141
|
170 180 190
....*....|....*....|....*....|.
gi 1002313595 1030 SREQRKRLTIAVELVSNPSIVFMDEPTSGLD 1060
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
|
| AAA_28 |
pfam13521 |
AAA domain; |
243-263 |
3.11e-03 |
|
AAA domain;
Pssm-ID: 433278 [Multi-domain] Cd Length: 164 Bit Score: 39.94 E-value: 3.11e-03
|
| RecA-like_CDC48_r2-like |
cd19528 |
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ... |
237-259 |
3.15e-03 |
|
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP in metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the second of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r2-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410936 [Multi-domain] Cd Length: 161 Bit Score: 39.80 E-value: 3.15e-03
|
| RecA-like_FtsH |
cd19501 |
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ... |
236-260 |
3.18e-03 |
|
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410909 [Multi-domain] Cd Length: 171 Bit Score: 39.91 E-value: 3.18e-03
10 20
....*....|....*....|....*
gi 1002313595 236 KPSRITLLLGPPGCGKTTLLKALAG 260
Cdd:cd19501 35 KIPKGVLLVGPPGTGKTLLAKAVAG 59
|
|
| RecA-like_PAN_like |
cd19502 |
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ... |
235-263 |
3.25e-03 |
|
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410910 [Multi-domain] Cd Length: 171 Bit Score: 40.01 E-value: 3.25e-03
10 20
....*....|....*....|....*....
gi 1002313595 235 IKPSRITLLLGPPGCGKTTLLKALAGRLN 263
Cdd:cd19502 34 IEPPKGVLLYGPPGTGKTLLAKAVANHTD 62
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
1086-1140 |
3.84e-03 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 41.43 E-value: 3.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1002313595 1086 HQPSIEIFEAFDELMLIKRGGELIYAGPLGqhscKVIQYFQSIpGVpKIKDNYNP 1140
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLTVYHGPVK----KVEEYFAGL-GI-NVPERVNP 49
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
974-1060 |
4.59e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 41.21 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 974 SPQITVGESVAYSawLRL-PAEIDTKTRKEFVDEVLEIIELD-EIRDalvgtpgvnglsR---E----QRKRLTIAVELV 1044
Cdd:COG4172 376 SPRMTVGQIIAEG--LRVhGPGLSAAERRARVAEALEEVGLDpAARH------------RyphEfsggQRQRIAIARALI 441
|
90
....*....|....*.
gi 1002313595 1045 SNPSIVFMDEPTSGLD 1060
Cdd:COG4172 442 LEPKLLVLDEPTSALD 457
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
228-324 |
4.77e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 41.31 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 228 LENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNkslKETGEIEYNgVKLdefvpaktsAYVSQYDLHVADMTVRETL 307
Cdd:COG1245 356 LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLK---PDEGEVDED-LKI---------SYKPQYISPDYDGTVEEFL 422
|
90 100
....*....|....*....|
gi 1002313595 308 dFSARFQGVGS---RAEIMK 324
Cdd:COG1245 423 -RSANTDDFGSsyyKTEIIK 441
|
|
| PRK03992 |
PRK03992 |
proteasome-activating nucleotidase; Provisional |
226-263 |
4.81e-03 |
|
proteasome-activating nucleotidase; Provisional
Pssm-ID: 179699 [Multi-domain] Cd Length: 389 Bit Score: 40.97 E-value: 4.81e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1002313595 226 QILENVsGIIKPSRItLLLGPPGCGKTTLLKALAGRLN 263
Cdd:PRK03992 155 ELFEEV-GIEPPKGV-LLYGPPGTGKTLLAKAVAHETN 190
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
192-429 |
5.15e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 41.38 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 192 VVSGKPLPTLWNAaLSRFSLLAAKlgFSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAgRLNKSlkETGE 271
Cdd:PRK10261 307 VVDGEPILQVRNL-VTRFPLRSGL--LNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALL-RLVES--QGGE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 272 IEYNGVKLDEFVPAKTSAyvsqydlhvadmtVRETLDFsarfqgvgsraeimkavIKREKEAGITPDPDI-DAYMKAISM 350
Cdd:PRK10261 381 IIFNGQRIDTLSPGKLQA-------------LRRDIQF-----------------IFQDPYASLDPRQTVgDSIMEPLRV 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 351 EGL----QRSMQTDYIMKIMGLdkcadvKVGNAMR--RGISGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVS 424
Cdd:PRK10261 431 HGLlpgkAAAARVAWLLERVGL------LPEHAWRypHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIIN 504
|
....*
gi 1002313595 425 CLQQL 429
Cdd:PRK10261 505 LLLDL 509
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
905-1059 |
6.01e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 40.78 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 905 LRNITGAF-------------QPG-ILsALMGVTGAGKTTLLDVLAG--RKTggviEGDIRIGGYP-------------- 954
Cdd:COG3845 8 LRGITKRFggvvanddvsltvRPGeIH-ALLGENGAGKSTLMKILYGlyQPD----SGEILIDGKPvrirsprdaialgi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 955 -KVQQTFSRIsgyceqndvhsPQITVGESVAYSAWLRLPAEIDTKTRKEFVDEVLEIIELDeIR-DALVGTpgvngLSRE 1032
Cdd:COG3845 83 gMVHQHFMLV-----------PNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLD-VDpDAKVED-----LSVG 145
|
170 180
....*....|....*....|....*..
gi 1002313595 1033 QRKRLTIAVELVSNPSIVFMDEPTSGL 1059
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVL 172
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1008-1105 |
6.02e-03 |
|
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: 38.89 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 1008 LEIIELDEIRDALVGTPGVNGLSREQRKRLTIAVELV--SNPSIVFMDEPTSGLD------ARAAAIAMRAVKNVAETGR 1079
Cdd:smart00382 38 GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALArkLKPDVLILDEITSLLDaeqealLLLLEELRLLLLLKSEKNL 117
|
90 100 110
....*....|....*....|....*....|
gi 1002313595 1080 TVVCTIHQPSI----EIFEAFDELMLIKRG 1105
Cdd:smart00382 118 TVILTTNDEKDlgpaLLRRRFDRRIVLLLI 147
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
233-337 |
6.32e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 40.16 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 233 GIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSLKetgeieyngvkldefvpaktSAYVSQYDLHVADM--TVRETLDFS 310
Cdd:COG3267 38 ALAQGGGFVVLTGEVGTGKTTLLRRLLERLPDDVK--------------------VAYIPNPQLSPAELlrAIADELGLE 97
|
90 100
....*....|....*....|....*..
gi 1002313595 311 ARFQGVGSRAEIMKAVIKREKEAGITP 337
Cdd:COG3267 98 PKGASKADLLRQLQEFLLELAAAGRRV 124
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
225-305 |
6.71e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 40.77 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 225 VQILENVSGIIKPSRITLLLGPPGCGKTTLLKALAGRLNKSlkeTGEIEYNGVKLdEFVPAKTS-----AYVSQyDLH-V 298
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPD---SGEILLDGEPV-RFRSPRDAqaagiAIIHQ-ELNlV 91
|
....*..
gi 1002313595 299 ADMTVRE 305
Cdd:COG1129 92 PNLSVAE 98
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
900-1060 |
7.12e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.99 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 900 RKLQLLRNITGAFQPGILSALMGVTGAGKTTL---LDVLAGRKTGGVIEGDIRIGGYPKVQ-QTFSRISGYCEQNDVHS- 974
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTgraLLRLVESQGGEIIFNGQRIDTLSPGKlQALRRDIQFIFQDPYASl 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 975 -PQITVGESVAYSawLRLPAEIDTKTRKEFVDEVLEIIELDEirDALVGTPgvNGLSREQRKRLTIAVELVSNPSIVFMD 1053
Cdd:PRK10261 415 dPRQTVGDSIMEP--LRVHGLLPGKAAAARVAWLLERVGLLP--EHAWRYP--HEFSGGQRQRICIARALALNPKVIIAD 488
|
....*..
gi 1002313595 1054 EPTSGLD 1060
Cdd:PRK10261 489 EAVSALD 495
|
|
| ruvB |
TIGR00635 |
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ... |
224-270 |
7.34e-03 |
|
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129721 [Multi-domain] Cd Length: 305 Bit Score: 40.36 E-value: 7.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1002313595 224 KVQILENVSGIIKPSRI-------TLLLGPPGCGKTTLLKALAGRLNKSLKETG 270
Cdd:TIGR00635 9 QEKVKEQLQLFIEAAKMrqealdhLLLYGPPGLGKTTLAHIIANEMGVNLKITS 62
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
234-265 |
7.82e-03 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 40.73 E-value: 7.82e-03
10 20 30
....*....|....*....|....*....|..
gi 1002313595 234 IIKPSRITLLLGPPGCGKTTLLKALAGRLNKS 265
Cdd:COG0507 136 ALTTRRVSVLTGGAGTGKTTTLRALLAALEAL 167
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
218-467 |
8.76e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 40.39 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 218 FSHHQSKVQILENVSGIIKPSRITLLLGPPGCGKTTLlkalAGRLNKSLK-ETGEIEYNGVKLDEFVPA---KTSAYVSQ 293
Cdd:PRK11176 349 FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTI----ANLLTRFYDiDEGEILLDGHDLRDYTLAslrNQVALVSQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 294 yDLHVADMTVRETLDFSArfQGVGSRAEIMKAvikrekeagitpdpdidAYMkAISMeglqrsmqtDYIMKimgLDKCAD 373
Cdd:PRK11176 425 -NVHLFNDTIANNIAYAR--TEQYSREQIEEA-----------------ARM-AYAM---------DFINK---MDNGLD 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002313595 374 VKVGnamRRGI--SGGEMKRLTTGEMIVGPCKVLLMDEISTGLDSSTTFQIVSCLQQLAhiSEYTILV-----SLLQPAp 446
Cdd:PRK11176 472 TVIG---ENGVllSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQ--KNRTSLViahrlSTIEKA- 545
|
250 260
....*....|....*....|.
gi 1002313595 447 etydlfDDIIIMGEGKVVYHG 467
Cdd:PRK11176 546 ------DEILVVEDGEIVERG 560
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
236-263 |
8.84e-03 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 40.29 E-value: 8.84e-03
10 20
....*....|....*....|....*...
gi 1002313595 236 KPSRITLLLGPPGCGKTTLLKALAGRLN 263
Cdd:PRK04195 37 KPKKALLLYGPPGVGKTSLAHALANDYG 64
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