|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
89-1468 |
0e+00 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 1540.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 89 FDLRSLLHYLRSRQLEQGI--EPGDSGIAFKNLTAVGVDASAAYGPSVEEMFRNIASipaHLISKFTKKSDVPLRNIIQN 166
Cdd:TIGR00956 3 FNAKAWVKNFRKLIDSDPIyyKPYKLGVAYKNLSAYGVAADSDYQPTFPNALLKILT---RGFRKLKKFRDTKTFDILKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 167 CTGVVESGEMLFVVGRPGAGCSTFLKCLSGETSE-LVDVQGEFSYDGLDQSEMMSKYKGYVIYCPELDFHFPKITVKETI 245
Cdd:TIGR00956 80 MDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGfHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 246 DFALKCKTPRVRIDKMTRKQYVDNIRDMWCTVFGLRHTYATKVGNDFVRGVSGGERKRVSLVEAQAMNASIYSWDNATRG 325
Cdd:TIGR00956 160 DFAARCKTPQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 326 LDASTALEFAQAIRTATNMVNNSAIVAIYQAGENIYELFDKTTVLYNGRQIYFGPADKAVGYFQRMGWVKPNRMTSAEFL 405
Cdd:TIGR00956 240 LDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPDRQTTADFL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 406 TSVTVDFENRtldIKPGYEDKVPKSSSEFEEYWLNSEDYQELLRTYDDYQSRHPVNETRDRLDVAKKQRLQQGQRENSQY 485
Cdd:TIGR00956 320 TSLTSPAERQ---IKPGYEKKVPRTPQEFETYWRNSPEYAQLMKEIDEYLDRCSESDTKEAYRESHVAKQSKRTRPSSPY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 486 VVNYWTQVYYCMIRGFQRVKGDSTYTKVYLSSFLIKALIIGSMFHKIddksQSTTAGAYSRGGMLFYVLLFASVTSLAEI 565
Cdd:TIGR00956 397 TVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNL----PKNTSDFYSRGGALFFAILFNAFSSLLEI 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 566 GNSFSSRPVIVKHKSYSMYHLSAESLQEIITEFPTKFVAIVILCLITYWIPFMKYEAGAFFQYILYLLTVQQCTSFIFKF 645
Cdd:TIGR00956 473 ASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFICTLAMSHLFRS 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 646 VATMSKSGVDAHAVGGLWVLMLCVYAGFVLPIGEMHHWIRWLHFINPLTYAFESLVSTEFHHREMLCSALVPSGPGYEGI 725
Cdd:TIGR00956 553 IGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHGRRFECSQYVPSGGGYDNL 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 726 SIANQVCDAAGAVKGNLYVSGDSYILHQYHFAYKHAWRNWGVNIVWTFGYIVFNVILSEYLKPVEGGGDLLLYKRGHMP- 804
Cdd:TIGR00956 633 GVTNKVCTVVGAEPGQDYVDGDDYLKLSFQYYNSHKWRNFGIIIGFTVFFFFVYILLTEFNKGAKQKGEILVFRRGSLKr 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 805 -ELGTENADARTASREEMMEALNGP----------NVDLEKVIAEkDVFTWNHLDYTIPYDGATRKLLSDVFGYVKPGKM 873
Cdd:TIGR00956 713 aKKAGETSASNKNDIEAGEVLGSTDltdesddvndEKDMEKESGE-DIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTL 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 874 TALMGESGAGKTTLLNVLAQRINMGVIT-GDMLVNAKPLPASFNRSCGYVAQADNHMAELSVRESLRFAAELRQQSSVPL 952
Cdd:TIGR00956 792 TALMGASGAGKTTLLNVLAERVTTGVITgGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSK 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 953 EEKYEYVEKIITLLGMQNYAEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLLFLDEPTSGLDSQSAWSIVQFMRALADS 1032
Cdd:TIGR00956 872 SEKMEYVEEVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLADH 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1033 GQSILCTIHQPSATLFEQFDRLLLLKKGGKMVYFGDIGPNSETLLKYFERQSGMKCGVSENPAEYILNCIGAGATASVNS 1112
Cdd:TIGR00956 952 GQAILCTIHQPSAILFEEFDRLLLLQKGGQTVYFGDLGENSHTIINYFEKHGAPKCPEDANPAEWMLEVIGAAPGAHANQ 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1113 DWHDLWLASPECAAARAEVEELHRTLPGRAVNDDPELATRFAASYMTQIKCVLRRTALQFWRSPVYIRAKFFECVACALF 1192
Cdd:TIGR00956 1032 DYHEVWRNSSEYQAVKNELDRLEAELSKAEDDNDPDALSKYAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALF 1111
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1193 VGLSYVGVNHSVGGAIEAFSSIFMLLLIALAMINQLHVFAYDSRELYEVREAASNTFHWSVLLLCHAAVENFWSTLCQFM 1272
Cdd:TIGR00956 1112 IGFTFFKVGTSLQGLQNQMFAVFMATVLFNPLIQQYLPPFVAQRDLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAGTI 1191
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1273 CFICYYWPAQFSGRASHAGFFFFFYVL------IFPLYFVTYGLWILYMSPDVPSASMINSNLFAAMLLFCGILQPREKM 1346
Cdd:TIGR00956 1192 FFFIWYYPVGFYWNASKTGQVHERGVLfwllstMFFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRM 1271
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1347 PAFWrRLMYNVSPFTYVVQALVTPLVHNKKVVCNPHEYNIMDPPSGKTCGEFLSTYMDNNTGYLVNPTATENCQYCPYTV 1426
Cdd:TIGR00956 1272 PGFW-IFMYRCSPFTYLVQALLSTGLADVPVTCKVKELLTFNPPSGQTCGEYMKPYLENAGGYLLNPNATDSCSFCQYSY 1350
|
1370 1380 1390 1400
....*....|....*....|....*....|....*....|..
gi 6325199 1427 QDQVVAKYNVKWDHRWRNFGFMWAYICFNIAAMLICYYVVRV 1468
Cdd:TIGR00956 1351 TNDFLEPISSKYSGRWRNFGIFIAFIFFNIIATVFFYWLARV 1392
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
14-1369 |
1.41e-134 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 453.15 E-value: 1.41e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 14 SRSNHDDDYANSVQSYAASEGQVDNEdLAATSQLSRHLSNILSNEEG-----IERLESMARVishKTKKeMDSFEINDL- 87
Cdd:PLN03140 1 ARSRGGSMRRSISRSVSRSSRNMEDV-FSGGSQSRRRTSSVDEDEEAlkwaaIEKLPTYSRL---RTSI-MKSFVENDVy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 88 -------DFDLRSL-----------------------LHYLRSRQLEQGIEPGDSGIAFKNLTavgVDASAAYG----PS 133
Cdd:PLN03140 76 gnqllhkEVDVTKLdgndrqkfidmvfkvaeednekfLKKFRNRIDRVGIKLPTVEVRFEHLT---VEADCYIGsralPT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 134 VEEMFRNIASIPAHLIS-KFTKKSDVplrNIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGETSELVDVQGEFSYDG 212
Cdd:PLN03140 153 LPNAARNIAESALGMLGiNLAKKTKL---TILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKVSGEITYNG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 213 LDQSEMMSKYKGyvIYCPELDFHFPKITVKETIDFALKCKTPRVRID------------------------KMTRKQYVD 268
Cdd:PLN03140 230 YRLNEFVPRKTS--AYISQNDVHVGVMTVKETLDFSARCQGVGTRYDllselarrekdagifpeaevdlfmKATAMEGVK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 269 N--IRDMWCTVFGLRHTYATKVGNDFVRGVSGGERKRVSLVEAQAMNASIYSWDNATRGLDASTALEFAQAIRTATNMVN 346
Cdd:PLN03140 308 SslITDYTLKILGLDICKDTIVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 347 NSAIVAIYQAGENIYELFDKTTVLYNGRQIYFGPADKAVGYFQRMGWVKPNRMTSAEFLTSVTV--DFENRTLDI-KPGY 423
Cdd:PLN03140 388 ATVLMSLLQPAPETFDLFDDIILLSEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSkkDQEQYWADRnKPYR 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 424 EDKVPKSSSEFEEYWLNSEDYQELLRTYDDYQSrHPVNETRDRLDVAKKQRLQQgqrensqyvvnywtqvyyCMIRGFQR 503
Cdd:PLN03140 468 YISVSEFAERFKSFHVGMQLENELSVPFDKSQS-HKAALVFSKYSVPKMELLKA------------------CWDKEWLL 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 504 VKGDSTYTKVYLSSFLIKALIIGSMFHKIDDKSQSTTAGAYSRGGMLFYVLLfASVTSLAEIGNSFSSRPVIVKHKSYSM 583
Cdd:PLN03140 529 MKRNAFVYVFKTVQIIIVAAIASTVFLRTEMHTRNEEDGALYIGALLFSMII-NMFNGFAELALMIQRLPVFYKQRDLLF 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 584 YHLSAESLQEIITEFPTKFVAIVILCLITYWIPFMKYEAGAFFQYILYLLTVQQCTSFIFKFVATMSKSGVDAHAVGGLW 663
Cdd:PLN03140 608 HPPWTFTLPTFLLGIPISIIESVVWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALV 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 664 VLMLCVYAGFVLPIGEMHHWIRWLHFINPLTYAFESLVSTEfhhreMLCSALVPSGPGYEGISIANQVCDAAGAVKG-NL 742
Cdd:PLN03140 688 LLLVFLLGGFILPKGEIPNWWEWAYWVSPLSYGFNALAVNE-----MFAPRWMNKMASDNSTRLGTAVLNIFDVFTDkNW 762
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 743 YVSGDSYILHqyhFAYKhawrnwgVNIVWTFGYIVFN-------VILSEYLKPVEGGGDLLLY--------KRGHMPELG 807
Cdd:PLN03140 763 YWIGVGALLG---FTIL-------FNVLFTLALTYLNplgkkqaIISEETAEEMEGEEDSIPRslssadgnNTREVAIQR 832
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 808 TENADARTASREEMMEALNGPNVDLEKVIAekdvFT-----WNHLDYTIPYDGATR---------KLLSDVFGYVKPGKM 873
Cdd:PLN03140 833 MSNPEGLSKNRDSSLEAANGVAPKRGMVLP----FTplamsFDDVNYFVDMPAEMKeqgvtedrlQLLREVTGAFRPGVL 908
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 874 TALMGESGAGKTTLLNVLAQRINMGVITGDMLVNAKP-LPASFNRSCGYVAQADNHMAELSVRESLRFAAELRQQSSVPL 952
Cdd:PLN03140 909 TALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPkKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSK 988
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 953 EEKYEYVEKIITLLGMQNYAEALVGKTG-RGLNVEQRKKLSIGVELVAKPSLLlFLDEPTSGLDSQSAWSIVQFMRALAD 1031
Cdd:PLN03140 989 EEKMMFVDEVMELVELDNLKDAIVGLPGvTGLSTEQRKRLTIAVELVANPSII-FMDEPTSGLDARAAAIVMRTVRNTVD 1067
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1032 SGQSILCTIHQPSATLFEQFDRLLLLKKGGKMVYFGDIGPNSETLLKYFERQSGM-KCGVSENPAEYILNCIGAGATASV 1110
Cdd:PLN03140 1068 TGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYSGPLGRNSHKIIEYFEAIPGVpKIKEKYNPATWMLEVSSLAAEVKL 1147
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1111 NSDWHDLWLASPECAAARAEVEELHRTLPGRAvndDPELATRFAASYMTQIKCVLRRTALQFWRSPVYIRAKFFECVACA 1190
Cdd:PLN03140 1148 GIDFAEHYKSSSLYQRNKALVKELSTPPPGAS---DLYFATQYSQSTWGQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAA 1224
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1191 LFVGLSY--VGVNHS-------VGGAIeaFSSIFMLLLIALAMINQlhVFAYDSRELYevREAASNTFhwSVLLLCHAAV 1261
Cdd:PLN03140 1225 LMVGTIFwkVGTKRSnandltmVIGAM--YAAVLFVGINNCSTVQP--MVAVERTVFY--RERAAGMY--SALPYAIAQV 1296
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1262 ---------ENFWSTLCQFmCFICYYWPAqfsgrashAGFFFFFYVLIFP-LYFVTYGLWILYMSPDVPSASMINSNLFA 1331
Cdd:PLN03140 1297 vceipyvliQTTYYTLIVY-AMVAFEWTA--------AKFFWFYFISFFSfLYFTYYGMMTVSLTPNQQVAAIFAAAFYG 1367
|
1450 1460 1470
....*....|....*....|....*....|....*...
gi 6325199 1332 AMLLFCGILQPREKMPAFWrRLMYNVSPFTYVVQALVT 1369
Cdd:PLN03140 1368 LFNLFSGFFIPRPKIPKWW-VWYYWICPVAWTVYGLIV 1404
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
839-1067 |
1.44e-102 |
|
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: 325.35 E-value: 1.44e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 839 KDVFTWNHLDYTIPYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINMGVITGDMLVNAKPLPASFNRS 918
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRPLDKNFQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 919 CGYVAQADNHMAELSVRESLRFAAELRqqssvpleekyeyvekiitllgmqnyaealvgktgrGLNVEQRKKLSIGVELV 998
Cdd:cd03232 81 TGYVEQQDVHSPNLTVREALRFSALLR------------------------------------GLSVEQRKRLTIGVELA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6325199 999 AKPSLLlFLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQPSATLFEQFDRLLLLKKGGKMVYFG 1067
Cdd:cd03232 125 AKPSIL-FLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRGGKTVYFG 192
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
857-1470 |
1.40e-76 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 267.30 E-value: 1.40e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 857 TRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINMGV-ITGDMLVNAKPLPASFNRS-CGYVAQADNHMAELSV 934
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkGSGSVLLNGMPIDAKEMRAiSAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 935 RESLRFAAELRQQSSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGR--GLNVEQRKKLSIGVELVAKPSLLlFLDEPTS 1012
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLL-FCDEPTS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1013 GLDSQSAWSIVQFMRALADSGQSILCTIHQPSATLFEQFDRLLLLKKgGKMVYFGdigpNSETLLKYFeRQSGMKCGVSE 1092
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAE-GRVAYLG----SPDQAVPFF-SDLGHPCPENY 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1093 NPAEYILN--CIGAGATASVNSDWHDLWLASPECAAARaEVEELHRTLPGRA--VNDDPELA--TRFAASYMTQIKCVLR 1166
Cdd:TIGR00955 270 NPADFYVQvlAVIPGSENESRERIEKICDSFAVSDIGR-DMLVNTNLWSGKAggLVKDSENMegIGYNASWWTQFYALLK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1167 RTALQFWRSPVYIRAKFFECVACALFVGLSYVGVNHSVGGAIEAFSSIFMLL--LIALAMINQLHVFaydSRELYEV-RE 1243
Cdd:TIGR00955 349 RSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFLtnMTFQNVFPVINVF---TAELPVFlRE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1244 AASNTFHWSVLLLchaavENFWSTLCQF------MCFICyYWPAQFSGRASHAGFFFFFYVLIFpLYFVTYGLWILYMSP 1317
Cdd:TIGR00955 426 TRSGLYRVSAYFL-----AKTIAELPLFiilpalFTSIT-YWMIGLRSGATHFLTFLFLVTLVA-NVATSFGYLISCAFS 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1318 DVPSASMINSNLFAAMLLFCGILQPREKMPAFWRRLMYnVSPFTYVVQALVtplvhnkkvvcnpheYNIMDPPsgktcge 1397
Cdd:TIGR00955 499 STSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSY-LSWFRYGNEGLL---------------INQWSDV------- 555
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325199 1398 flstymDNNTGYLVNPTatencQYCPYTVQDqVVAKYNVKWDHRWRNFG--FMWaYICFNIAAmlicYYVVRVKV 1470
Cdd:TIGR00955 556 ------DNIECTSANTT-----GPCPSSGEV-ILETLSFRNADLYLDLIglVIL-IFFFRLLA----YFALRIRI 613
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
138-379 |
4.51e-76 |
|
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: 250.64 E-value: 4.51e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 138 FRNIASIPAHLISKFTkksdvplrnIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGETSELVDVQGEFSYDGLDQSE 217
Cdd:cd03233 6 WRNISFTTGKGRSKIP---------ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 218 MMSKYKGYVIYCPELDFHFPKITVKETIDFALKCKtprvridkmtrkqyvdnirdmwctvfglrhtyatkvGNDFVRGVS 297
Cdd:cd03233 77 FAEKYPGEIIYVSEEDVHFPTLTVRETLDFALRCK------------------------------------GNEFVRGIS 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 298 GGERKRVSLVEAQAMNASIYSWDNATRGLDASTALEFAQAIRTATNMVNNSAIVAIYQAGENIYELFDKTTVLYNGRQIY 377
Cdd:cd03233 121 GGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIY 200
|
..
gi 6325199 378 FG 379
Cdd:cd03233 201 YG 202
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
841-1067 |
1.25e-67 |
|
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: 226.28 E-value: 1.25e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 841 VFTWNHLDYTIPYD--GATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINMGVITGDMLVNAKPLPA-SFNR 917
Cdd:cd03213 3 TLSFRNLTVTVKSSpsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPLDKrSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 918 SCGYVAQADNHMAELSVRESLRFAAELRqqssvpleekyeyvekiitllgmqnyaealvgktgrGLNVEQRKKLSIGVEL 997
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKLR------------------------------------GLSGGERKRVSIALEL 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 998 VAKPSLLlFLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQPSATLFEQFDRLLLLKKgGKMVYFG 1067
Cdd:cd03213 127 VSNPSLL-FLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQ-GRVIYFG 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
852-1067 |
1.90e-52 |
|
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: 184.01 E-value: 1.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 852 PYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRI-NMGVITGDMLVNAKPL-PASFNRSCGYVAQADNHM 929
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeGGGTTSGQILFNGQPRkPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 930 AELSVRESLRFAAELRQQSSVPLEEKyeyvEKIITLLGMQNYAEALVGKTG-RGLNVEQRKKLSIGVELVAKPSLLlFLD 1008
Cdd:cd03234 94 PGLTVRETLTYTAILRLPRKSSDAIR----KKRVEDVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVL-ILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6325199 1009 EPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQPSATLFEQFDRLLLLKKgGKMVYFG 1067
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSS-GEIVYSG 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
148-775 |
7.20e-52 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 194.11 E-value: 7.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 148 LISKFTKKSdvPLRNIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGETSELVDVQGEFSYDGLD-QSEMMSKYKGYV 226
Cdd:TIGR00955 27 LRGCFCRER--PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPiDAKEMRAISAYV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 227 IycpELDFHFPKITVKETIDFALKCKTPRvRIDKMTRKQYVDNIRDMwctvFGLRHTYATKVGN-DFVRGVSGGERKRVS 305
Cdd:TIGR00955 105 Q---QDDLFIPTLTVREHLMFQAHLRMPR-RVTKKEKRERVDEVLQA----LGLRKCANTRIGVpGRVKGLSGGERKRLA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 306 LVEAQAMNASIYSWDNATRGLDASTAlefAQAIRTATNMVNN--SAIVAIYQAGENIYELFDKTTVLYNGRQIYFGPADK 383
Cdd:TIGR00955 177 FASELLTDPPLLFCDEPTSGLDSFMA---YSVVQVLKGLAQKgkTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 384 AVGYFQRMGWVKPNRMTSAEFLTSVtvdfenrtLDIKPGYEDKVPKSSSEFEEYWLNSEDYQELLRTYddyqsrhpvnet 463
Cdd:TIGR00955 254 AVPFFSDLGHPCPENYNPADFYVQV--------LAVIPGSENESRERIEKICDSFAVSDIGRDMLVNT------------ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 464 rdRLDVAKKQRLQQGQR--ENSQYVVNYWTQVYYCMIRGFQRVKGDSTYTKVYLSSFLIKALIIGSMFHKIddksQSTTA 541
Cdd:TIGR00955 314 --NLWSGKAGGLVKDSEnmEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQ----GLTQK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 542 GAYSRGGMLFYVLLFASVTSLAEIGNSFSS-RPVIVKHKSYSMYHLSAESLQEIITEFPTKFVAIVILCLITYWipfMKY 620
Cdd:TIGR00955 388 GVQNINGALFLFLTNMTFQNVFPVINVFTAeLPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYW---MIG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 621 EAGAFFQYILYLLTV----QQCTSFIFkFVATMSKSGVDAHAVGGLWVLMLCVYAGFVLPIGEMHHWIRWLHFINPLTYA 696
Cdd:TIGR00955 465 LRSGATHFLTFLFLVtlvaNVATSFGY-LISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 697 FESLVSTEF-HHREMLCSALVPSGPgyegisianqvCDAAGAVkgnlyvsgdsyILHQYHFAYKHAWRNWGVNIVWTFGY 775
Cdd:TIGR00955 544 NEGLLINQWsDVDNIECTSANTTGP-----------CPSSGEV-----------ILETLSFRNADLYLDLIGLVILIFFF 601
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
840-1067 |
8.34e-42 |
|
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: 152.42 E-value: 8.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 840 DVFTWNHLDYTIPYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINMGV-ITGDMLVN---AKPLPASF 915
Cdd:cd03233 2 STLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsVEGDIHYNgipYKEFAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 916 NRSCGYVAQADNHMAELSVRESLRFAAELRQQssvpleekyEYVekiitllgmqnyaealvgktgRGLNVEQRKKLSIGV 995
Cdd:cd03233 82 PGEIIYVSEEDVHFPTLTVRETLDFALRCKGN---------EFV---------------------RGISGGERKRVSIAE 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6325199 996 ELVAKPSLLLFlDEPTSGLDSQSAWSIVQFMRALAD-SGQSILCTIHQPSATLFEQFDRLLLLkKGGKMVYFG 1067
Cdd:cd03233 132 ALVSRASVLCW-DNSTRGLDSSTALEILKCIRTMADvLKTTTFVSLYQASDEIYDLFDKVLVL-YEGRQIYYG 202
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
858-1100 |
2.52e-41 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 163.13 E-value: 2.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINMGVITGDMLVNAKPLPASFNRSCGYVAQADNHMAELSVRES 937
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 938 LRFAAELRQQSSVPLEEKYEYVEKIITLLGMQNYAEALVGKTG-RGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGLDS 1016
Cdd:PLN03211 161 LVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFiRGISGGERKRVSIAHEMLINPSLLI-LDEPTSGLDA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1017 QSAWSIVQFMRALADSGQSILCTIHQPSATLFEQFDRLLLLKKgGKMVYFGdigpNSETLLKYFErQSGMKCGVSENPAE 1096
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSE-GRCLFFG----KGSDAMAYFE-SVGFSPSFPMNPAD 313
|
....
gi 6325199 1097 YILN 1100
Cdd:PLN03211 314 FLLD 317
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
142-379 |
9.07e-39 |
|
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: 143.46 E-value: 9.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 142 ASIPAHLISKFTKKSDVPL-RNIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGETSELvDVQGEFSYDGldQSEMMS 220
Cdd:cd03213 2 VTLSFRNLTVTVKSSPSKSgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGL-GVSGEVLING--RPLDKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 221 KYKGYVIYCPELDFHFPKITVKETIDFALKCktprvridkmtrkqyvdnirdmwctvfglrhtyatkvgndfvRGVSGGE 300
Cdd:cd03213 79 SFRKIIGYVPQDDILHPTLTVRETLMFAAKL------------------------------------------RGLSGGE 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6325199 301 RKRVSLVEAQAMNASIYSWDNATRGLDASTALEFAQAIRTATNMvNNSAIVAIYQAGENIYELFDKTTVLYNGRQIYFG 379
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
496-703 |
4.74e-38 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 141.64 E-value: 4.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 496 CMIRGFQRVKGDSTYTKVYLSSFLIKALIIGSMFHKIDdksqsTTAGAYSRGGMLFYVLLFASVTSLAEIGNSFSS-RPV 574
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG-----NQQGGLNRPGLLFFSILFNAFSALSGISPVFEKeRGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 575 IVKHKSYSMYHLSAESLQEIITEFPTKFVAIVILCLITYWIPFMKYEAGAFFQYILYLLTVQQCTSFIFKFVATMSKSGV 654
Cdd:pfam01061 76 LYRELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6325199 655 DAHAVGGLWVLMLCVYAGFVLPIGEMHHWIRWLHFINPLTYAFESLVST 703
Cdd:pfam01061 156 DASQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| PDR_CDR |
pfam06422 |
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters ... |
716-804 |
5.11e-37 |
|
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters comprising extracellular loop 3, transmembrane segment 6 and linker region.
Pssm-ID: 461906 [Multi-domain] Cd Length: 92 Bit Score: 134.51 E-value: 5.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 716 VPSGPGYEGISIANQVCDAAGAVKGNLYVSGDSYILHQYHFAYKHAWRNWGVNIVWTFGYIVFNVILSEYLKPVEGGGDL 795
Cdd:pfam06422 1 VPSGPGYENVSGANQVCAVVGAVPGQTFVSGDDYLAASYGYSYSHLWRNFGILIAFWIFFLALYLIATEYNSAAKSKGEV 80
|
....*....
gi 6325199 796 LLYKRGHMP 804
Cdd:pfam06422 81 LVFKRGKAP 89
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
161-633 |
3.70e-34 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 141.17 E-value: 3.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 161 RNIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGETsELVDVQGEFSYDGLDQSEMMSKYKGYVIycpELDFHFPKIT 240
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRI-QGNNFTGTILANNRKPTKQILKRTGFVT---QDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 241 VKETIDFalkCKTprVRIDKMTRKQYVDNIRDMWCTVFGLRHTYATKVGNDFVRGVSGGERKRVSLVEAQAMNASIYSWD 320
Cdd:PLN03211 157 VRETLVF---CSL--LRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 321 NATRGLDASTALEFAQAIRTATNMvNNSAIVAIYQAGENIYELFDKTTVLYNGRQIYFGPADKAVGYFQRMGWVKPNRMT 400
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 401 SAEFLtsvtVDFENRTLDIKPGYEDKVPKSSSEFeeywlnSEDYQELL--RTYDDYQSRHPVNETRDRLDVAKKQRLQQG 478
Cdd:PLN03211 311 PADFL----LDLANGVCQTDGVSEREKPNVKQSL------VASYNTLLapKVKAAIEMSHFPQANARFVGSASTKEHRSS 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 479 QRENsqyVVNYWTQVYYCMIRGFQRVKGDStYTKVYLSSFLIKALIIGSMFHKIDDKSqsttagAYSRGGMLFYVLLFAS 558
Cdd:PLN03211 381 DRIS---ISTWFNQFSILLQRSLKERKHES-FNTLRVFQVIAAALLAGLMWWHSDFRD------VQDRLGLLFFISIFWG 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 559 VTSlaeignSFSS-------RPVIVKHKSYSMYHLSAESLQEIITEFPTKFVAIVILCLITYWIPFMKYEAGAFFQYILY 631
Cdd:PLN03211 451 VFP------SFNSvfvfpqeRAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLV 524
|
..
gi 6325199 632 LL 633
Cdd:PLN03211 525 LL 526
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
868-1069 |
4.22e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 131.72 E-value: 4.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLaqrinMGVIT---GDMLVNAKPL---PASFNRSCGYVAQADNHMAELSVRESLRFA 941
Cdd:COG1131 23 VEPGEIFGLLGPNGAGKTTTIRML-----LGLLRptsGEVRVLGEDVardPAEVRRRIGYVPQEPALYPDLTVRENLRFF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 942 AELRQqssVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLlFLDEPTSGLDSQSAWS 1021
Cdd:COG1131 98 ARLYG---LPRKEARERIDELLELFGLTDAADRKVGTLSGG----MKQRLGLALALLHDPELL-ILDEPTSGLDPEARRE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6325199 1022 IVQFMRALADSGQSILCTIHQPSaTLFEQFDRLLLLKKgGKMVYFGDI 1069
Cdd:COG1131 170 LWELLRELAAEGKTVLLSTHYLE-EAERLCDRVAIIDK-GRIVADGTP 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
868-1074 |
5.52e-34 |
|
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: 131.52 E-value: 5.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLA--QRINMGVITGDmLVNAKPLPASFNRSCGYVAQADNHMAELSVRESLRFAAELR 945
Cdd:COG4555 24 AKDGEITGLLGPNGAGKTTLLRMLAglLKPDSGSILID-GEDVRKEPREARRQIGVLPDERGLYDRLTVRENIRYFAELY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 946 QqssVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQF 1025
Cdd:COG4555 103 G---LFDEELKKRIEELIELLGLEEFLDRRVGELSTG----MKKKVALARALVHDPKVLL-LDEPTNGLDVMARRLLREI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6325199 1026 MRALADSGQSILCTIHQPSaTLFEQFDRLLLLKKgGKMVYFGDIGPNSE 1074
Cdd:COG4555 175 LRALKKEGKTVLFSSHIMQ-EVEALCDRVVILHK-GKVVAQGSLDELRE 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
853-1060 |
4.04e-31 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 122.19 E-value: 4.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 853 YDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRInmGVITGDMLVNAKPL----PASFNRSCGYVAQ-ADN 927
Cdd:cd03225 9 YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL--GPTSGEVLVDGKDLtklsLKELRRKVGLVFQnPDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 928 HMAELSVRESLRFAAELRQqssVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfL 1007
Cdd:cd03225 87 QFFGPTVEEEVAFGLENLG---LPEEEIEERVEEALELVGLEGLRDRSPFTLSGG----QKQRVAIAGVLAMDPDILL-L 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6325199 1008 DEPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQPSaTLFEQFDRLLLLKKG 1060
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDG 210
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
161-379 |
2.62e-29 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 117.37 E-value: 2.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 161 RNIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGETSELVDVQGEFSYDGLDQSEMMSKYKgyVIYCPELDFHFPKIT 240
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQFQKC--VAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 241 VKETIDFALKCKTPRVRIDKmtrkqyvdnIRDMWCTVFGLRHTYATKVGNDFVRGVSGGERKRVSLVEAQAMNASIYSWD 320
Cdd:cd03234 98 VRETLTYTAILRLPRKSSDA---------IRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 321 NATRGLDASTALEFAQAIR-TATNmvNNSAIVAIYQAGENIYELFDKTTVLYNGRQIYFG 379
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSqLARR--NRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
1164-1368 |
3.20e-28 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 113.52 E-value: 3.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1164 VLRRTALQFWRSPVYIRAKFFECVACALFVGLSYVGVNHSVGGAIEAFSSIFMLLLIALAMINQLHVFAYDSRELYEvRE 1243
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLY-RE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1244 AASNTFHWSVLLLCHAAVENFWSTLCQFMCFICYYWPAQFSGRASHAGFFFFFYVLIFpLYFVTYGLWILYMSPDVPSAS 1323
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTA-LAASSLGLFISALAPSFEDAS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6325199 1324 MINSNLFAAMLLFCGILQPREKMPAFWRRLMYnVSPFTYVVQALV 1368
Cdd:pfam01061 159 QLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYY-LNPLTYAIEALR 202
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
853-1067 |
1.32e-26 |
|
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: 109.52 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 853 YDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINMGviTGDMLVNAKPL---PASFNRSCGYVAQADNHM 929
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPT--SGTAYINGYSIrtdRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 930 AELSVRESLRFAAELRqqsSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSlLLFLDE 1009
Cdd:cd03263 88 DELTVREHLRFYARLK---GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGG----MKRKLSLAIALIGGPS-VLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325199 1010 PTSGLDSQS---AWSIVQFMRaladSGQSILCTIHqpSATLFEQF-DRLLLLKKgGKMVYFG 1067
Cdd:cd03263 160 PTSGLDPASrraIWDLILEVR----KGRSIILTTH--SMDEAEALcDRIAIMSD-GKLRCIG 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
858-1057 |
3.08e-26 |
|
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: 107.95 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKPL---PASFNRSCGYVAQADNHMAE 931
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILA-----GLLPpsaGEVLWNGEPIrdaREDYRRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 932 LSVRESLRFAAELRqqssvPLEEKYEYVEKIITLLGMQNYAEALVGK--TGrglnveQRKKLSIGVELVAKPSLLLfLDE 1009
Cdd:COG4133 90 LTVRENLRFWAALY-----GLRADREAIDEALEAVGLAGLADLPVRQlsAG------QKRRVALARLLLSPAPLWL-LDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6325199 1010 PTSGLDSQS-AWsIVQFMRALADSGQSILCTIHQPsatLFEQFDRLLLL 1057
Cdd:COG4133 158 PFTALDAAGvAL-LAELIAAHLARGGAVLLTTHQP---LELAAARVLDL 202
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
861-1012 |
1.49e-25 |
|
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: 103.88 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 861 LSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINmgVITGDMLVNAKPLP----ASFNRSCGYVAQADNHMAELSVRE 936
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS--PTEGTILLDGQDLTdderKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325199 937 SLRFAAELRQQSSVPLEEKyeyVEKIITLLGMQNYAEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLLfLDEPTS 1012
Cdd:pfam00005 79 NLRLGLLLKGLSKREKDAR---AEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLL-LDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
845-1060 |
4.74e-25 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 104.88 E-value: 4.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 845 NHLDYTIPYDGATRKLLSDV-FGyVKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKPLP-------A 913
Cdd:cd03255 4 KNLSKTYGGGGEKVQALKGVsLS-IEKGEFVAIVGPSGSGKSTLLNILG-----GLDRptsGEVRVDGTDISklsekelA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 914 SF-NRSCGYVAQADNHMAELSVRESLRFAAELRQqssVPLEEKYEYVEKIITLLGMQNYAEALVGKtgrgLNVEQRKKLS 992
Cdd:cd03255 78 AFrRRHIGFVFQSFNLLPDLTALENVELPLLLAG---VPKKERRERAEELLERVGLGDRLNHYPSE----LSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6325199 993 IGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQFMRALA-DSGQSILCTIHQPSatLFEQFDRLLLLKKG 1060
Cdd:cd03255 151 IARALANDPKIIL-ADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPE--LAEYADRIIELRDG 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
868-1060 |
7.06e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 104.74 E-value: 7.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKPLP-------ASF-NRSCGYVAQADNHMAELSVRE 936
Cdd:COG1136 31 IEAGEFVAIVGPSGSGKSTLLNILG-----GLDRptsGEVLIDGQDISslserelARLrRRHIGFVFQFFNLLPELTALE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 937 SLRFAAELRqqsSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLDEPTSGLDS 1016
Cdd:COG1136 106 NVALPLLLA---GVSRKERRERARELLERVGLGDRLDHRPSQLSGG----QQQRVAIARALVNRPKLIL-ADEPTGNLDS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6325199 1017 QSAWSIVQFMRALA-DSGQSILCTIHQPSatLFEQFDRLLLLKKG 1060
Cdd:COG1136 178 KTGEEVLELLRELNrELGTTIVMVTHDPE--LAARADRVIRLRDG 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
811-1060 |
4.92e-24 |
|
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: 108.69 E-value: 4.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 811 ADARTASrEEMMEALNGPNVDLEK-----VIAEKDVFTWNHLDYTipYDGAtRKLLSDVFGYVKPGKMTALMGESGAGKT 885
Cdd:COG4988 302 ANGIAAA-EKIFALLDAPEPAAPAgtaplPAAGPPSIELEDVSFS--YPGG-RPALDGLSLTIPPGERVALVGPSGAGKS 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 886 TLLNVLaqrinMGVIT---GDMLVNAKPL----PASFNRSCGYVAQaDNHMAELSVRESLRFAAElrqqsSVPLEEkyey 958
Cdd:COG4988 378 TLLNLL-----LGFLPpysGSILINGVDLsdldPASWRRQIAWVPQ-NPYLFAGTIRENLRLGRP-----DASDEE---- 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 959 VEKIITLLGMQNYAEAL-------VGKTGRGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQFMRALAD 1031
Cdd:COG4988 443 LEAALEAAGLDEFVAALpdgldtpLGEGGRGLSGGQAQRLALARALLRDAPLLL-LDEPTAHLDAETEAEILQALRRLAK 521
|
250 260
....*....|....*....|....*....
gi 6325199 1032 SGQSILCTiHQPSATlfEQFDRLLLLKKG 1060
Cdd:COG4988 522 GRTVILIT-HRLALL--AQADRILVLDDG 547
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
845-1068 |
7.89e-24 |
|
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: 101.64 E-value: 7.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 845 NHLDYTipYDGAtRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAqrinmGVI---TGDMLVNAKPL----PASFNR 917
Cdd:COG1122 4 ENLSFS--YPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN-----GLLkptSGEVLVDGKDItkknLRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 918 SCGYVAQ-ADNHMAELSVRESLRFAaeLRQQSsVPLEEKYEYVEKIITLLGMQNYAE----ALVGktgrGlnveQRKKLS 992
Cdd:COG1122 76 KVGLVFQnPDDQLFAPTVEEDVAFG--PENLG-LPREEIRERVEEALELVGLEHLADrpphELSG----G----QKQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6325199 993 I-GVeLVAKPSLLLfLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQPSAtLFEQFDRLLLLKKgGKMVYFGD 1068
Cdd:COG1122 145 IaGV-LAMEPEVLV-LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDD-GRIVADGT 217
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
163-709 |
9.63e-24 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 109.55 E-value: 9.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 163 IIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGETSELVdVQGEFSYDGL-DQSEMMSKYKGYviyCPELDFHFPKITV 241
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGY-IEGDIRISGFpKKQETFARISGY---CEQNDIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 242 KETIDFALKCKTPRvRIDKMTRKQYVDNIRDMwctvFGLRHTYATKVGNDFVRGVSGGERKRVSLVEAQAMNASIYSWDN 321
Cdd:PLN03140 971 RESLIYSAFLRLPK-EVSKEEKMMFVDEVMEL----VELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDE 1045
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 322 ATRGLDASTAlefAQAIRTATNMVNNSAIV--AIYQAGENIYELFDKTTVLYNGRQ-IYFGP----ADKAVGYFQRMGWV 394
Cdd:PLN03140 1046 PTSGLDARAA---AIVMRTVRNTVDTGRTVvcTIHQPSIDIFEAFDELLLMKRGGQvIYSGPlgrnSHKIIEYFEAIPGV 1122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 395 -----KPNRMTSAEFLTSVTVDFenrtldikpgyedkvpKSSSEFEEYWLNSEDYQellrtyddyqsrhpvnetRDRLDV 469
Cdd:PLN03140 1123 pkikeKYNPATWMLEVSSLAAEV----------------KLGIDFAEHYKSSSLYQ------------------RNKALV 1168
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 470 AKKQRLQQGQRE---NSQYVVNYWTQVYYCMIRGFQRVKGDSTYTKVYLSSFLIKALIIGSMFHKIDDKSQSTTAGAYSR 546
Cdd:PLN03140 1169 KELSTPPPGASDlyfATQYSQSTWGQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFWKVGTKRSNANDLTMVI 1248
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 547 GGMlFYVLLFASVTSLAEIGNSFS-SRPVIVKHKSYSMYHLSAESLQEIITEFPTKFVAIVILCLITYWIPFMKYEAGAF 625
Cdd:PLN03140 1249 GAM-YAAVLFVGINNCSTVQPMVAvERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKF 1327
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 626 FQYILYlltvqQCTSFI-FKFVATMSKSGVDAHAVGGLWVL----MLCVYAGFVLPIGEMHHWIRWLHFINPLTYAFESL 700
Cdd:PLN03140 1328 FWFYFI-----SFFSFLyFTYYGMMTVSLTPNQQVAAIFAAafygLFNLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGL 1402
|
....*....
gi 6325199 701 VSTEFHHRE 709
Cdd:PLN03140 1403 IVSQYGDVE 1411
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
853-1067 |
1.10e-23 |
|
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: 108.38 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 853 YDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKPL----PASFNRSCGYVAQa 925
Cdd:COG2274 483 YPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL-----GLYEptsGRILIDGIDLrqidPASLRRQIGVVLQ- 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 926 DNHMAELSVRESLRFAAElrqqsSVPLEEkyeyVEKIITLLGMQNYAEAL-------VGKTGRGLNVEQRKKLSIGVELV 998
Cdd:COG2274 557 DVFLFSGTIRENITLGDP-----DATDEE----IIEAARLAGLHDFIEALpmgydtvVGEGGSNLSGGQRQRLAIARALL 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6325199 999 AKPSLLLfLDEPTSGLDSQSAWSIVQFMRALAdSGQSILCTIHQPSaTLfEQFDRLLLLKKgGKMVYFG 1067
Cdd:COG2274 628 RNPRILI-LDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLS-TI-RLADRIIVLDK-GRIVEDG 691
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
868-1060 |
2.35e-22 |
|
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: 95.54 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLaqrinMGVIT---GDMLVNAKPL---PASFNRSCGYVAQADNHMAELSVRESLRFa 941
Cdd:cd03230 23 VEKGEIYGLLGPNGAGKTTLIKII-----LGLLKpdsGEIKVLGKDIkkePEEVKRRIGYLPEEPSLYENLTVRENLKL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 942 aelrqqsSvpleekyeyvekiitlLGMqnyaealvgktgrglnveqRKKLSIGVELVAKPSLLlFLDEPTSGLDSQSAWS 1021
Cdd:cd03230 97 -------S----------------GGM-------------------KQRLALAQALLHDPELL-ILDEPTSGLDPESRRE 133
|
170 180 190
....*....|....*....|....*....|....*....
gi 6325199 1022 IVQFMRALADSGQSILCTIHQPSaTLFEQFDRLLLLKKG 1060
Cdd:cd03230 134 FWELLRELKKEGKTILLSSHILE-EAERLCDRVAILNNG 171
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
853-1068 |
3.24e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 97.47 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 853 YDGatRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLaqrinMGVI---TGDMLVNAKPLPASFNRsCGYVAQADNHM 929
Cdd:COG1121 16 YGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAI-----LGLLpptSGTVRLFGKPPRRARRR-IGYVPQRAEVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 930 AE--LSVRE------------SLRFAAELRQQssvpleekyeyVEKIITLLGMQNYAEALVGK-TGrGlnveQRKKLSIG 994
Cdd:COG1121 88 WDfpITVRDvvlmgrygrrglFRRPSRADREA-----------VDEALERVGLEDLADRPIGElSG-G----QQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6325199 995 VELVAKPSLLLfLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQPSaTLFEQFDRLLLLKKGgkMVYFGD 1068
Cdd:COG1121 152 RALAQDPDLLL-LDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLG-AVREYFDRVLLLNRG--LVAHGP 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
848-1067 |
5.24e-22 |
|
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: 96.06 E-value: 5.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 848 DYTIPYDGatRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLaqrinMGVIT---GDMLVNAKPlPASFNRSCGYVAQ 924
Cdd:cd03235 4 DLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAI-----LGLLKptsGSIRVFGKP-LEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 925 AD--NHMAELSVRE--SLRFAAELRQQSSVPLEEKyEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAK 1000
Cdd:cd03235 76 RRsiDRDFPISVRDvvLMGLYGHKGLFRRLSKADK-AKVDEALERVGLSELADRQIGELSGG----QQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6325199 1001 PSLLLfLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQPSaTLFEQFDRLLLLKKggKMVYFG 1067
Cdd:cd03235 151 PDLLL-LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLG-LVLEYFDRVLLLNR--TVVASG 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
811-1057 |
6.04e-22 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 101.59 E-value: 6.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 811 ADARTASrEEMMEALNGPNV----DLEKVIAEKDVFTWNHLDYTipYDGaTRKLLSDVFGYVKPGKMTALMGESGAGKTT 886
Cdd:TIGR02857 288 ADGVAAA-EALFAVLDAAPRplagKAPVTAAPASSLEFSGVSVA--YPG-RRPALRPVSFTVPPGERVALVGPSGAGKST 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 887 LLNVLAQRINMGviTGDMLVNAKPL----PASFNRSCGYVAQADnHMAELSVRESLRFAAelrqqssvpLEEKYEYVEKI 962
Cdd:TIGR02857 364 LLNLLLGFVDPT--EGSIAVNGVPLadadADSWRDQIAWVPQHP-FLFAGTIAENIRLAR---------PDASDAEIREA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 963 ITLLGMQNYAEAL-------VGKTGRGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQFMRALAdSGQS 1035
Cdd:TIGR02857 432 LERAGLDEFVAALpqgldtpIGEGGAGLSGGQAQRLALARAFLRDAPLLL-LDEPTAHLDAETEAEVLEALRALA-QGRT 509
|
250 260
....*....|....*....|..
gi 6325199 1036 ILCTIHQPSatLFEQFDRLLLL 1057
Cdd:TIGR02857 510 VLLVTHRLA--LAALADRIVVL 529
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
857-1060 |
1.31e-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: 93.08 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 857 TRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINmgVITGDMLVNAKPLPASFN----RSCGYVAQadnhmaeL 932
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK--PTSGEILIDGKDIAKLPLeelrRRIGYVPQ-------L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 933 SvreslrfaaelrqqssvpleekyeyvekiitllgmqnyaealvgkTGrglnveQRKKLSIGVELVAKPSLLLfLDEPTS 1012
Cdd:cd00267 82 S---------------------------------------------GG------QRQRVALARALLLNPDLLL-LDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6325199 1013 GLDSQSAWSIVQFMRALADSGQSILCTIHQPSaTLFEQFDRLLLLKKG 1060
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPE-LAELAADRVIVLKDG 156
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
171-323 |
1.48e-21 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 92.71 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 171 VESGEMLFVVGRPGAGCSTFLKCLSGETSelvDVQGEFSYDGLD-QSEMMSKYKGYVIYCPELDFHFPKITVKETIDFAL 249
Cdd:pfam00005 8 LNPGEILALVGPNGAGKSTLLKLIAGLLS---PTEGTILLDGQDlTDDERKSLRKEIGYVFQDPQLFPRLTVRENLRLGL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6325199 250 KCKtprvRIDKMTRKQYVDNIRDMwctvFGLRHTYATKVGNdFVRGVSGGERKRVSLVEAQAMNASIYSWDNAT 323
Cdd:pfam00005 85 LLK----GLSKREKDARAEEALEK----LGLGDLADRPVGE-RPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
868-1067 |
1.94e-21 |
|
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: 94.36 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAQ--RINMGVITGDMLVNAKPlPASFNRSCGYVAQADNHMAELSVRESLRFAAELR 945
Cdd:cd03266 28 VKPGEVTGLLGPNGAGKTTTLRMLAGllEPDAGFATVDGFDVVKE-PAEARRRLGFVSDSTGLYDRLTARENLEYFAGLY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 946 QQSSVPLEEKyeyVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQF 1025
Cdd:cd03266 107 GLKGDELTAR---LEELADRLGMEELLDRRVGGFSTG----MRQKVAIARALVHDPPVLL-LDEPTTGLDVMATRALREF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6325199 1026 MRALADSGQSILCTIH--QPSATLfeqFDRLLLLKKgGKMVYFG 1067
Cdd:cd03266 179 IRQLRALGKCILFSTHimQEVERL---CDRVVVLHR-GRVVYEG 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
858-1060 |
4.26e-21 |
|
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: 93.09 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLA--QRINMGVItgdmLVNAKPLPASFN-RSCGYVAQ-ADNHMAELS 933
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAglIKESSGSI----LLNGKPIKAKERrKSIGYVMQdVDYQLFTDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 934 VRESLRFAAElrqqssvPLEEKYEYVEKIITLLGMQNYAEalvgKTGRGLNVEQRKKLSIGVELVAKPSLLLFlDEPTSG 1013
Cdd:cd03226 89 VREELLLGLK-------ELDAGNEQAETVLKDLDLYALKE----RHPLSLSGGQKQRLAIAAALLSGKDLLIF-DEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6325199 1014 LDSQSAWSIVQFMRALADSGQSILCTIHQPSaTLFEQFDRLLLLKKG 1060
Cdd:cd03226 157 LDYKNMERVGELIRELAAQGKAVIVITHDYE-FLAKVCDRVLLLANG 202
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
856-1067 |
6.31e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 92.73 E-value: 6.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 856 ATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLnvlaqRINMGVI---TGDMLVNAKPLPASFNRSCGYVAQADNHMAEL 932
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTI-----RMILGIIlpdSGEVLFDGKPLDIAARNRIGYLPEERGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 933 SVRESLRFAAELRqqsSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLDEPTS 1012
Cdd:cd03269 86 KVIDQLVYLAQLK---GLKKEEARRRIDEWLERLELSEYANKRVEELSKG----NQQKVQFIAAVIHDPELLI-LDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6325199 1013 GLDSQSAWSIVQFMRALADSGQSILCTIHQpsATLFEQF-DRLLLLKKgGKMVYFG 1067
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQ--MELVEELcDRVLLLNK-GRAVLYG 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
861-1037 |
1.29e-20 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 92.50 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 861 LSDVFGYVKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKP---LPA----------SFnrscgyvaQ 924
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIS-----GFLRptsGSVLFDGEDitgLPPheiarlgigrTF--------Q 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 925 ADNHMAELSVRESLRFAAELRQQSSV-------PLEEKYEYVEKIITLLGMQNYAEALVGktgrGLNVEQRKKLSIGVEL 997
Cdd:cd03219 83 IPRLFPELTVLENVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAG----ELSYGQQRRLEIARAL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6325199 998 VAKPSLLLfLDEPTSGLDSQSAWSIVQFMRALADSGQSIL 1037
Cdd:cd03219 159 ATDPKLLL-LDEPAAGLNPEETEELAELIRELRERGITVL 197
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
868-1068 |
1.32e-19 |
|
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: 89.03 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLaqrinMGVIT---GDMLVNAKPLP--ASFNRS---CGYVAQADNHMAELSVRESLR 939
Cdd:cd03224 23 VPEGEIVALLGRNGAGKTTLLKTI-----MGLLPprsGSIRFDGRDITglPPHERAragIGYVPEGRRIFPELTVEENLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 940 FAAELRQQSSVP--LEEKYEYVEKIITLLGmqNYAEALVGktGrglnveQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQ 1017
Cdd:cd03224 98 LGAYARRRAKRKarLERVYELFPRLKERRK--QLAGTLSG--G------EQQMLAIARALMSRPKLLL-LDEPSEGLAPK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6325199 1018 SAWSIVQFMRALADSGQSILctihqpsatLFEQF--------DRLLLLKKgGKMVYFGD 1068
Cdd:cd03224 167 IVEEIFEAIRELRDEGVTIL---------LVEQNarfaleiaDRAYVLER-GRVVLEGT 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
850-1094 |
1.61e-19 |
|
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: 89.72 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 850 TIPYDGatRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKPL----PASFNRSCGYV 922
Cdd:COG1120 8 SVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALA-----GLLKpssGEVLLDGRDLaslsRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 923 AQADNHMAELSVRESL---RFA--AELRQQSsvplEEKYEYVEKIITLLGMQNYAEALV-----GktgrglnveQRKKLS 992
Cdd:COG1120 81 PQEPPAPFGLTVRELValgRYPhlGLFGRPS----AEDREAVEEALERTGLEHLADRPVdelsgG---------ERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 993 IGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQFMRALA-DSGQSILCTIHQPS-ATLFeqFDRLLLLkKGGKMVYFGDig 1070
Cdd:COG1120 148 IARALAQEPPLLL-LDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNlAARY--ADRLVLL-KDGRIVAQGP-- 221
|
250 260
....*....|....*....|....*...
gi 6325199 1071 P----NSETLLKYFerqsGMKCGVSENP 1094
Cdd:COG1120 222 PeevlTPELLEEVY----GVEARVIEDP 245
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
868-1060 |
3.05e-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: 87.96 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKP---LPASfNRSCGYVAQADNHMAELSVRESLRFA 941
Cdd:cd03259 23 VEPGEFLALLGPSGCGKTTLLRLIA-----GLERpdsGEILIDGRDvtgVPPE-RRNIGMVFQDYALFPHLTVAENIAFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 942 aeLRQQsSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWS 1021
Cdd:cd03259 97 --LKLR-GVPKAEIRARVRELLELVGLEGLLNRYPHELSGG----QQQRVALARALAREPSLLL-LDEPLSALDAKLREE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6325199 1022 IVQFMRALADSGQ--SILCTIHQPSAtlFEQFDRLLLLKKG 1060
Cdd:cd03259 169 LREELKELQRELGitTIYVTHDQEEA--LALADRIAVMNEG 207
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
845-1060 |
5.36e-19 |
|
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: 92.91 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 845 NHLDYTipYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLaqrinMGVI---TGDMLVNAKPL----PASFNR 917
Cdd:COG4987 337 EDVSFR--YPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALL-----LRFLdpqSGSITLGGVDLrdldEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 918 SCGYVAQaDNHMAELSVRESLRFA------AELRQqssvpleekyeyvekIITLLGMQNYAEAL-------VGKTGRGLN 984
Cdd:COG4987 410 RIAVVPQ-RPHLFDTTLRENLRLArpdatdEELWA---------------ALERVGLGDWLAALpdgldtwLGEGGRRLS 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325199 985 VEQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQFMRALADsGQSILCTIHQPSAtlFEQFDRLLLLKKG 1060
Cdd:COG4987 474 GGERRRLALARALLRDAPILL-LDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAG--LERMDRILVLEDG 545
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
857-1065 |
1.14e-18 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 86.12 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 857 TRKLLSDVFGYVKPGKMTALMGESGAGKTTLLnvlaqRINMGVI---TGDMLVNAKplpaSFNRScgyvAQADNHMA--- 930
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTM-----KIILGLIkpdSGEITFDGK----SYQKN----IEALRRIGali 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 931 -------ELSVRESLRFAAELRQQssvpleeKYEYVEKIITLLGMQNYAEALVGKTGRGLnveqRKKLSIGVELVAKPSL 1003
Cdd:cd03268 79 eapgfypNLTARENLRLLARLLGI-------RKKRIDEVLDVVGLKDSAKKKVKGFSLGM----KQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6325199 1004 LLfLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQPSAtlFEQF-DRLLLLKKgGKMVY 1065
Cdd:cd03268 148 LI-LDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSE--IQKVaDRIGIINK-GKLIE 206
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
853-1060 |
1.25e-18 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 86.49 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 853 YDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLaqrinMGVIT---GDMLVNAKPL----PASFNRSCGYVAQa 925
Cdd:cd03245 12 YPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLL-----AGLYKptsGSVLLDGTDIrqldPADLRRNIGYVPQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 926 DNHMAELSVRESLRFAAelrqqssvpLEEKYEYVEKIITLLGMQNYA-------EALVGKTGRGLNVEQRKKLSIGVELV 998
Cdd:cd03245 86 DVTLFYGTLRDNITLGA---------PLADDERILRAAELAGVTDFVnkhpnglDLQIGERGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325199 999 AKPSLLLfLDEPTSGLDSQSAWSIVQFMRALAdSGQSILCTIHQPSatLFEQFDRLLLLKKG 1060
Cdd:cd03245 157 NDPPILL-LDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSG 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
850-1067 |
3.99e-18 |
|
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: 83.64 E-value: 3.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 850 TIPYDGatRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINmgVITGDMLVNAKPL----PASFNRSCGYVAQA 925
Cdd:cd03214 6 SVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK--PSSGEILLDGKDLaslsPKELARKIAYVPQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 926 dnhmaelsvreslrfaaelrqqssvpleekyeyvekiITLLGMQNYAEalvgktgRGLNvE----QRKKLSIGVELVAKP 1001
Cdd:cd03214 82 -------------------------------------LELLGLAHLAD-------RPFN-ElsggERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6325199 1002 SLLLfLDEPTSGLDSQSAWSIVQFMRALADS-GQSILCTIHQPSATLfeQF-DRLLLLkKGGKMVYFG 1067
Cdd:cd03214 117 PILL-LDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAA--RYaDRVILL-KDGRIVAQG 180
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
853-1060 |
4.66e-18 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 83.20 E-value: 4.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 853 YDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLaqrinMGVIT---GDMLVNAKPL----PASFNRSCGYVAQa 925
Cdd:cd03228 10 YPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLL-----LRLYDptsGEILIDGVDLrdldLESLRKNIAYVPQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 926 DNHMAELSVRESLrfaaelrqqssvpleekyeyvekiitllgmqnyaealvgktgrgLNVEQRKKLSIGVELVAKPSLLL 1005
Cdd:cd03228 84 DPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6325199 1006 fLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTiHQPSatLFEQFDRLLLLKKG 1060
Cdd:cd03228 120 -LDEATSALDPETEALILEALRALAKGKTVIVIA-HRLS--TIRDADRIIVLDDG 170
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
161-379 |
8.09e-18 |
|
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: 83.06 E-value: 8.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 161 RNIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGETSELVdVQGEFSYDGLDQSEMMSKYKGYviyCPELDFHFPKIT 240
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGV-ITGEILINGRPLDKNFQRSTGY---VEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 241 VKETIDFALKCktprvridkmtrkqyvdnirdmwctvfglrhtyatkvgndfvRGVSGGERKRVSL-VEAQAmNASIYSW 319
Cdd:cd03232 96 VREALRFSALL------------------------------------------RGLSVEQRKRLTIgVELAA-KPSILFL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6325199 320 DNATRGLDASTALEFAQAIRTaTNMVNNSAIVAIYQAGENIYELFDKTTVLY-NGRQIYFG 379
Cdd:cd03232 133 DEPTSGLDSQAAYNIVRFLKK-LADSGQAILCTIHQPSASIFEKFDRLLLLKrGGKTVYFG 192
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
853-1060 |
1.29e-17 |
|
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: 83.69 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 853 YDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNvLAQRINMGViTGDMLVNAKPL----PASFNRSCGYVAQaDNH 928
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTK-LIQRFYVPE-NGRVLVDGHDLaladPAWLRRQVGVVLQ-ENV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 929 MAELSVRESLRFAAElrqqsSVPLEEkyeyVEKIITLLGMQNYA-------EALVGKTGRGLNVEQRKKLSIGVELVAKP 1001
Cdd:cd03252 87 LFNRSIRDNIALADP-----GMSMER----VIEAAKLAGAHDFIselpegyDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6325199 1002 SLLLFlDEPTSGLDSQSAWSIVQFMRALADsGQSILCTIHQPSATlfEQFDRLLLLKKG 1060
Cdd:cd03252 158 RILIF-DEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTV--KNADRIIVMEKG 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
848-1060 |
1.48e-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: 88.04 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 848 DYTIPYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRI-NMGVITGDMLVNAKPL----PASFNRSCGYV 922
Cdd:COG1123 9 DLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLpHGGRISGEVLLDGRDLlelsEALRGRRIGMV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 923 AQ-ADNHMAELSVRESLRFAAELRqqsSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKP 1001
Cdd:COG1123 89 FQdPMTQLNPVTVGDQIAEALENL---GLSRAEARARVLELLEAVGLERRLDRYPHQLSGG----QRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1002 SLLLfLDEPTSGLDSQSAWSIVQFMRAL-ADSGQSILCTIHQPsATLFEQFDRLLLLKKG 1060
Cdd:COG1123 162 DLLI-ADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDL-GVVAEIADRVVVMDDG 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
850-1081 |
1.56e-17 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 83.98 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 850 TIPYDGatRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVlaqrinmgvITGDMlvnakplPASFNRSC---------- 919
Cdd:COG1119 10 TVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLLSL---------ITGDL-------PPTYGNDVrlfgerrgge 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 920 ---------GYV--AQADNHMAELSVRE---SLRFAA-ELRQQssvPLEEKYEYVEKIITLLGMQNYAEALVGK--TGrg 982
Cdd:COG1119 72 dvwelrkriGLVspALQLRFPRDETVLDvvlSGFFDSiGLYRE---PTDEQRERARELLELLGLAHLADRPFGTlsQG-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 983 lnvEQRKKLsIGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQFMRALADSG--QSILCTiHQPSAtLFEQFDRLLLLKKg 1060
Cdd:COG1119 147 ---EQRRVL-IARALVKDPELLI-LDEPTAGLDLGARELLLALLDKLAAEGapTLVLVT-HHVEE-IPPGITHVLLLKD- 218
|
250 260
....*....|....*....|...
gi 6325199 1061 GKMVYFGDIGP--NSETLLKYFE 1081
Cdd:COG1119 219 GRVVAAGPKEEvlTSENLSEAFG 241
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
867-1060 |
7.43e-17 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 81.19 E-value: 7.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 867 YVKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKPLPASFN--------RSCGYVAQADNHMAELSVR 935
Cdd:cd03297 19 FDLNEEVTGIFGASGAGKSTLLRCIA-----GLEKpdgGTIVLNGTVLFDSRKkinlppqqRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 936 ESLRFAAELRQQSsvpleEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLDEPTSGLD 1015
Cdd:cd03297 94 ENLAFGLKRKRNR-----EDRISVDELLDLLGLDHLLNRYPAQLSGG----EKQRVALARALAAQPELLL-LDEPFSALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6325199 1016 SQSAWSIVQFMRALADSGQ--SILCTiHQPSaTLFEQFDRLLLLKKG 1060
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNipVIFVT-HDLS-EAEYLADRIVVMEDG 208
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
868-1041 |
8.27e-17 |
|
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: 82.82 E-value: 8.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAQRI----NMGVITG-DMLVNakplPASFNRSCGYVAQADNHMAELSVRESLRFAA 942
Cdd:TIGR01188 16 VREGEVFGFLGPNGAGKTTTIRMLTTLLrptsGTARVAGyDVVRE----PRKVRRSIGIVPQYASVDEDLTGRENLEMMG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 943 ELRqqsSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLlFLDEPTSGLDSQSAWSI 1022
Cdd:TIGR01188 92 RLY---GLPKDEAEERAEELLELFELGEAADRPVGTYSGG----MRRRLDIAASLIHQPDVL-FLDEPTTGLDPRTRRAI 163
|
170
....*....|....*....
gi 6325199 1023 VQFMRALADSGQSILCTIH 1041
Cdd:TIGR01188 164 WDYIRALKEEGVTILLTTH 182
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
868-1041 |
1.62e-16 |
|
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: 80.11 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAQ--RINMG--VITGDMLVNAkplPASFNRSCGYVAQ---ADNhmaELSVRESLRF 940
Cdd:cd03265 23 VRRGEIFGLLGPNGAGKTTTIKMLTTllKPTSGraTVAGHDVVRE---PREVRRRIGIVFQdlsVDD---ELTGWENLYI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 941 AAELrqqSSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGLnveqRKKLSIGVELVAKPSLLlFLDEPTSGLDSQS-- 1018
Cdd:cd03265 97 HARL---YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGM----RRRLEIARSLVHRPEVL-FLDEPTIGLDPQTra 168
|
170 180
....*....|....*....|....
gi 6325199 1019 -AWSIVQFMraLADSGQSILCTIH 1041
Cdd:cd03265 169 hVWEYIEKL--KEEFGMTILLTTH 190
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
846-1017 |
1.85e-16 |
|
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: 79.82 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 846 HLDYTIPYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKPLPASfNRSCGYV 922
Cdd:cd03293 5 NVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIA-----GLERptsGEVLVDGEPVTGP-GPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 923 AQADNHMAELSVRESLRFAAELRqqsSVPLEEKYEYVEKIITLLGMQNYAEA----LVGktGrglnveQRKKLSIGVELV 998
Cdd:cd03293 79 FQQDALLPWLTVLDNVALGLELQ---GVPKAEARERAEELLELVGLSGFENAyphqLSG--G------MRQRVALARALA 147
|
170
....*....|....*....
gi 6325199 999 AKPSLLLfLDEPTSGLDSQ 1017
Cdd:cd03293 148 VDPDVLL-LDEPFSALDAL 165
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
868-1037 |
2.13e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 80.85 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKPL----PASFNRsCGyVA---QADNHMAELSVRES 937
Cdd:COG0411 27 VERGEIVGLIGPNGAGKTTLFNLIT-----GFYRptsGRILFDGRDItglpPHRIAR-LG-IArtfQNPRLFPELTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 938 LRFAAELRQQSSVP------------LEEKYEYVEKIITLLGMQNYAEALVGktgrGLNVEQRKKLSIGVELVAKPSLLL 1005
Cdd:COG0411 100 VLVAAHARLGRGLLaallrlprarreEREARERAEELLERVGLADRADEPAG----NLSYGQQRRLEIARALATEPKLLL 175
|
170 180 190
....*....|....*....|....*....|...
gi 6325199 1006 fLDEPTSGLDSQSAWSIVQFMRAL-ADSGQSIL 1037
Cdd:COG0411 176 -LDEPAAGLNPEETEELAELIRRLrDERGITIL 207
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
858-1043 |
2.52e-16 |
|
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: 78.94 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLA--QRINMGVItgdmLVNAKPLP---ASFNRSCGYVAQADNHMAEL 932
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAglLRPDSGEV----RWNGTPLAeqrDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 933 SVRESLRFAAELRQQSSVPLEEKYEYVekiitllGMQNYAEALVGKtgrgLNVEQRKKLSIGVELVAKPSLLLfLDEPTS 1012
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRTIEDALAAV-------GLTGFEDLPAAQ----LSAGQQRRLALARLWLSRRPLWI-LDEPTT 156
|
170 180 190
....*....|....*....|....*....|.
gi 6325199 1013 GLDSQSAWSIVQFMRALADSGQSILCTIHQP 1043
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
848-1043 |
2.57e-16 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 83.95 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 848 DYTIPYDGATRkLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAqrinmGVI---TGDMLVNAKPlPASFN-----RSC 919
Cdd:TIGR02868 339 DLSAGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLA-----GLLdplQGEVTLDGVP-VSSLDqdevrRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 920 GYVAQaDNHMAELSVRESLRFAAElrqqsSVPLEEKYEYVEKIitllGMQNYAEAL-------VGKTGRGLNVEQRKKLS 992
Cdd:TIGR02868 412 SVCAQ-DAHLFDTTVRENLRLARP-----DATDEELWAALERV----GLADWLRALpdgldtvLGEGGARLSGGERQRLA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6325199 993 IGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQFMRAlADSGQSILCTIHQP 1043
Cdd:TIGR02868 482 LARALLADAPILL-LDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
855-1067 |
3.45e-16 |
|
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: 79.92 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 855 GATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQ--RINMGVIT-GDMLVNAKPLPA--SFNRSCGYVAQADNHM 929
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGlvEPTSGSVLiDGTDINKLKGKAlrQLRRQIGMIFQQFNLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 930 AELSVRESLRFAAeLRQQSSV-------PLEEKYEYVEkIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPS 1002
Cdd:cd03256 91 ERLSVLENVLSGR-LGRRSTWrslfglfPKEEKQRALA-ALERVGLLDKAYQRADQLSGG----QQQRVAIARALMQQPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325199 1003 LLLfLDEPTSGLDSQSAWSIVQFMRALADS-GQSILCTIHQPSATLfEQFDRLLLLKKgGKMVYFG 1067
Cdd:cd03256 165 LIL-ADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAR-EYADRIVGLKD-GRIVFDG 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
868-1054 |
3.63e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.00 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLaqrinMGVIT---GDMLVNAKPLP--ASFNRS-CGYVAQADNHMAELSVRESLRFA 941
Cdd:PRK13537 30 VQRGECFGLLGPNGAGKTTTLRML-----LGLTHpdaGSISLCGEPVPsrARHARQrVGVVPQFDNLDPDFTVRENLLVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 942 AELRQQSSVPLEEKyeyVEKIITLLGMQNYAEALVGKTGRGLnveqRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWS 1021
Cdd:PRK13537 105 GRYFGLSAAAARAL---VPPLLEFAKLENKADAKVGELSGGM----KRRLTLARALVNDPDVLV-LDEPTTGLDPQARHL 176
|
170 180 190
....*....|....*....|....*....|...
gi 6325199 1022 IVQFMRALADSGQSILCTIHqpsatLFEQFDRL 1054
Cdd:PRK13537 177 MWERLRSLLARGKTILLTTH-----FMEEAERL 204
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
846-1037 |
4.01e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 80.13 E-value: 4.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 846 HLDYTIPYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKPLPASfNRSCGYV 922
Cdd:COG1116 12 GVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA-----GLEKptsGEVLVDGKPVTGP-GPDRGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 923 AQADNHMAELSVRESLRFAAELRQqssVPLEEKYEYVEKIITLLGMQNYAEA----LVGktGrglnveQRKKLSIGVELV 998
Cdd:COG1116 86 FQEPALLPWLTVLDNVALGLELRG---VPKAERRERARELLELVGLAGFEDAyphqLSG--G------MRQRVAIARALA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6325199 999 AKPSLLLfLDEPTSGLDSQSAWSI-VQFMRALADSGQSIL 1037
Cdd:COG1116 155 NDPEVLL-MDEPFGALDALTRERLqDELLRLWQETGKTVL 193
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
868-1069 |
7.71e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.77 E-value: 7.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLnvlaqRINMGVIT---GDMLVNAKPLPASFNRSCGYvaqadnhMAE-------LSVRES 937
Cdd:COG4152 24 VPKGEIFGLLGPNGAGKTTTI-----RIILGILApdsGEVLWDGEPLDPEDRRRIGY-------LPEerglypkMKVGEQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 938 LRFAAELRQQSSVPLEEK-YEYVEKiitlLGMQNYAEALVGKTGRGlnvEQRKkLSIGVELVAKPSLLLfLDEPTSGLDS 1016
Cdd:COG4152 92 LVYLARLKGLSKAEAKRRaDEWLER----LGLGDRANKKVEELSKG---NQQK-VQLIAALLHDPELLI-LDEPFSGLDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6325199 1017 QSAWSIVQFMRALADSGQSILCTIHQ-PSAtlfEQF-DRLLLLKKgGKMVYFGDI 1069
Cdd:COG4152 163 VNVELLKDVIRELAAKGTTVIFSSHQmELV---EELcDRIVIINK-GRKVLSGSV 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
858-1043 |
1.20e-15 |
|
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: 77.15 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRinMGVITGDMLVNAKPL---PASFNRSCGYVAQADNHMAELSV 934
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGL--SPPLAGRVLLNGGPLdfqRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 935 RESLRFAAELRQQSSVpleekyeyvEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLDEPTSGL 1014
Cdd:cd03231 91 LENLRFWHADHSDEQV---------EEALARVGLNGFEDRPVAQLSAG----QQRRVALARLLLSGRPLWI-LDEPTTAL 156
|
170 180
....*....|....*....|....*....
gi 6325199 1015 DSQSAWSIVQFMRALADSGQSILCTIHQP 1043
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
845-1067 |
1.21e-15 |
|
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: 77.93 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 845 NHLDYTIPYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLA--QRINMGVIT---GDMLVNAKPLPASFNRSC 919
Cdd:cd03257 5 KNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILglLKPTSGSIIfdgKDLLKLSRRLRKIRRKEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 920 GYVAQadNHMAEL----SVRESLRFAAELRQQSSVPlEEKYEYVEKIITLLG-----MQNYAEALVGktGrglnveQRKK 990
Cdd:cd03257 85 QMVFQ--DPMSSLnprmTIGEQIAEPLRIHGKLSKK-EARKEAVLLLLVGVGlpeevLNRYPHELSG--G------QRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6325199 991 LSIGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQFMRALADS-GQSILCTIHQPSatLFEQF-DRLLLLkKGGKMVYFG 1067
Cdd:cd03257 154 VAIARALALNPKLLI-ADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLG--VVAKIaDRVAVM-YAGKIVEEG 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
855-1060 |
1.47e-15 |
|
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: 77.06 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 855 GATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINmgVITGDMLVNAKPLP-------ASFNRSCGYVAQADN 927
Cdd:cd03292 11 PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEEL--PTSGTIRVNGQDVSdlrgraiPYLRRKIGVVFQDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 928 HMAELSVRESLRFAAELrqqSSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnvEQrKKLSIGVELVAKPSLLLfL 1007
Cdd:cd03292 89 LLPDRNVYENVAFALEV---TGVPPREIRKRVPAALELVGLSHKHRALPAELSGG---EQ-QRVAIARAIVNSPTILI-A 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6325199 1008 DEPTSGLDSQSAWSIVQFMRALADSGQSILCTIHqpSATLFEQFD-RLLLLKKG 1060
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH--AKELVDTTRhRVIALERG 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
819-1041 |
2.37e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 82.37 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 819 EEMMEALNGPNvdlekviaEKDVFTWNHLdyTIPYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQriNMG 898
Cdd:TIGR01257 1923 EERQRIISGGN--------KTDILRLNEL--TKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG--DTT 1990
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 899 VITGDMLVNAKPLPASFN---RSCGYVAQADNHMAELSVRESLRFAAELRqqsSVPLEEKYEYVEKIITLLGMQNYAEAL 975
Cdd:TIGR01257 1991 VTSGDATVAGKSILTNISdvhQNMGYCPQFDAIDDLLTGREHLYLYARLR---GVPAEEIEKVANWSIQSLGLSLYADRL 2067
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325199 976 VGKTGRGlnveQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIH 1041
Cdd:TIGR01257 2068 AGTYSGG----NKRKLSTAIALIGCPPLVL-LDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
858-1067 |
5.86e-15 |
|
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: 75.31 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDVFGYVKPGkMTALMGESGAGKTTLLNVLA--QRINMGVITGDMlVNAKPLPASFNRSCGYVAQADNHMAELSVR 935
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILAtlTPPSSGTIRIDG-QDVLKQPQKLRRRIGYLPQEFGVYPNFTVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 936 ESLRFAAELRqqsSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLDEPTSGLD 1015
Cdd:cd03264 91 EFLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGG----MRRRVGIAQALVGDPSILI-VDEPTAGLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6325199 1016 SQSAwsiVQFMRALADSGQS---ILCTiHQPSATLFeQFDRLLLLKKgGKMVYFG 1067
Cdd:cd03264 163 PEER---IRFRNLLSELGEDrivILST-HIVEDVES-LCNQVAVLNK-GKLVFEG 211
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
858-1047 |
6.84e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.09 E-value: 6.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDVFGYVKPGKMTALMGESGAGKTTLLNV---LAQRINMGVITGDMLVNAKPLPASFNRSCGYVAQA--------- 925
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMvvgIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEasifrrlsv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 926 -DNHMAELSVRESLrfAAELRQQSSVPLEEKYeyvekiitllgmqnYAEALVGKTGRGLNVEQRKKLSIGVELVAKPSLL 1004
Cdd:PRK10895 96 yDNLMAVLQIRDDL--SAEQREDRANELMEEF--------------HIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6325199 1005 LfLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQPSATL 1047
Cdd:PRK10895 160 L-LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETL 201
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
868-1060 |
9.12e-15 |
|
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: 73.76 E-value: 9.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKPL------PASFNRSCGYVAQADNHMAELSVREsl 938
Cdd:cd03229 23 IEAGEIVALLGPSGSGKSTLLRCIA-----GLEEpdsGSILIDGEDLtdledeLPPLRRRIGMVFQDFALFPHLTVLE-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 939 rfaaelrqqssvpleekyeyvekiitllgmqNYAEALVGktgrGlnveQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQS 1018
Cdd:cd03229 96 -------------------------------NIALGLSG----G----QQQRVALARALAMDPDVLL-LDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6325199 1019 AWSIVQFMRALAD-SGQSILCTIHQPsATLFEQFDRLLLLKKG 1060
Cdd:cd03229 136 RREVRALLKSLQAqLGITVVLVTHDL-DEAARLADRVVVLRDG 177
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
868-1063 |
1.01e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 75.45 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKpLPasFNRSCGYVAQADNHMAE-------LSVRES 937
Cdd:cd03267 44 IEKGEIVGFIGPNGAGKTTTLKILS-----GLLQptsGEVRVAGL-VP--WKRRKKFLRRIGVVFGQktqlwwdLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 938 LRFAAELRQqssVPLEEKYEYVEKIITLLGMqnyaEALVGKTGRGLNVEQRKKLSIGVELVAKPSlLLFLDEPTSGLDSQ 1017
Cdd:cd03267 116 FYLLAAIYD---LPPARFKKRLDELSELLDL----EELLDTPVRQLSLGQRMRAEIAAALLHEPE-ILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6325199 1018 SAWSIVQFMRAL-ADSGQSILCTIH--QPSATLfeqFDRLLLLKKGGKM 1063
Cdd:cd03267 188 AQENIRNFLKEYnRERGTTVLLTSHymKDIEAL---ARRVLVIDKGRLL 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
868-1037 |
1.07e-14 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 78.79 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLaqrinMGVIT---GDMLVNAKPLP-------ASFNRSCGYVAQADNHM--AELSVR 935
Cdd:COG1123 288 LRRGETLGLVGESGSGKSTLARLL-----LGLLRptsGSILFDGKDLTklsrrslRELRRRVQMVFQDPYSSlnPRMTVG 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 936 ESLRFAaeLRQQSSVPLEEKYEYVEKIITLLG-----MQNYAEALVGktGrglnveQRKKLSIGVELVAKPSLLLfLDEP 1010
Cdd:COG1123 363 DIIAEP--LRLHGLLSRAERRERVAELLERVGlppdlADRYPHELSG--G------QRQRVAIARALALEPKLLI-LDEP 431
|
170 180
....*....|....*....|....*...
gi 6325199 1011 TSGLDSQSAWSIVQFMRALADS-GQSIL 1037
Cdd:COG1123 432 TSALDVSVQAQILNLLRDLQRElGLTYL 459
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
833-1015 |
1.14e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.98 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 833 EKVIAEKDVFTWNHLDYTIPydgaTRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQriNMGVITGDMLVNAKPLP 912
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVP----GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGR--HQPPSEGEILLDAQPLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 913 A----SFNRSCGYVAQADNHMAELSVRESL------------RFAAELRQQssvpleekyeyVEKIITLLGMQNYAEALV 976
Cdd:PRK10575 77 SwsskAFARKVAYLPQQLPAAEGMTVRELVaigrypwhgalgRFGAADREK-----------VEEAISLVGLKPLAHRLV 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 6325199 977 GKTGRGlnveQRKKLSIGVeLVAKPSLLLFLDEPTSGLD 1015
Cdd:PRK10575 146 DSLSGG----ERQRAWIAM-LVAQDSRCLLLDEPTSALD 179
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
857-1069 |
1.44e-14 |
|
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: 74.85 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 857 TRKLLSDVFGYVKPGKMTALMGESGAGKTTLLnvlaqRINMGVIT---GDMLVNAKPLPA-------SFNRSCGYVAQAD 926
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLL-----RLIVGLLRpdsGEVLIDGEDISGlseaelyRLRRRMGMLFQSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 927 NHMAELSVRESLRFAaeLRQQSSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSlLLF 1006
Cdd:cd03261 87 ALFDSLTVFENVAFP--LREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGG----MKKRVALARALALDPE-LLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325199 1007 LDEPTSGLDSQSAWSIVQFMRALADSGQ--SILCTiHQPSaTLFEQFDRLLLLkKGGKMVYFGDI 1069
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGltSIMVT-HDLD-TAFAIADRIAVL-YDGKIVAEGTP 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
858-1031 |
2.27e-14 |
|
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: 74.14 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLaQRINMGV----ITGDMLVNAKPL------PASFNRSCGYVAQADN 927
Cdd:cd03260 13 KHALKDISLDIPKGEITALIGPSGCGKSTLLRLL-NRLNDLIpgapDEGEVLLDGKDIydldvdVLELRRRVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 928 hMAELSVRESLRFAaeLRQQSSVPLEEKYEYVEKIITLLGMqnYAEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLLfL 1007
Cdd:cd03260 92 -PFPGSIYDNVAYG--LRLHGIKLKEELDERVEEALRKAAL--WDEVKDRLHALGLSGGQQQRLCLARALANEPEVLL-L 165
|
170 180
....*....|....*....|....
gi 6325199 1008 DEPTSGLDSQSAWSIVQFMRALAD 1031
Cdd:cd03260 166 DEPTSALDPISTAKIEELIAELKK 189
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
845-1015 |
9.02e-14 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 72.91 E-value: 9.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 845 NHLDYTIPYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAqrinmGVI---TGDMLVNAKPL----PASFNR 917
Cdd:COG1124 5 RNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALA-----GLErpwSGEVTFDGRPVtrrrRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 918 SCGYVAQaD-------NHMAELSVRESLRFAAELRQQssvpleekyEYVEKIITLLGMqnyAEALVGKTGRGLNVEQRKK 990
Cdd:COG1124 80 RVQMVFQ-DpyaslhpRHTVDRILAEPLRIHGLPDRE---------ERIAELLEQVGL---PPSFLDRYPHQLSGGQRQR 146
|
170 180
....*....|....*....|....*
gi 6325199 991 LSIGVELVAKPSLLLfLDEPTSGLD 1015
Cdd:COG1124 147 VAIARALILEPELLL-LDEPTSALD 170
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
868-1060 |
9.22e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.04 E-value: 9.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLaqrinMGVI--TGDMLVNAKPL----PASFNRSCGYVAQaDNHMAELSVRESLRFA 941
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNAL-----LGFLpyQGSLKINGIELreldPESWRKHLSWVGQ-NPQLPHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 942 ------AELRQQssvpLEEKY--EYVEKIItlLGMqNYAealVGKTGRGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSG 1013
Cdd:PRK11174 447 npdasdEQLQQA----LENAWvsEFLPLLP--QGL-DTP---IGDQAAGLSVGQAQRLALARALLQPCQLLL-LDEPTAS 515
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6325199 1014 LDSQSAWSIvqfMRAL--ADSGQSILCTIHQPSATlfEQFDRLLLLKKG 1060
Cdd:PRK11174 516 LDAHSEQLV---MQALnaASRRQTTLMVTHQLEDL--AQWDQIWVMQDG 559
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
859-1041 |
1.17e-13 |
|
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: 70.91 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 859 KLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAqrinmGVI---TGDMLVNAKPLPAS------FNRSCGYVAQ-ADNH 928
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLN-----GLLrpqSGAVLIDGEPLDYSrkglleRRQRVGLVFQdPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 929 MAELSVRESLRFAAelrQQSSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLD 1008
Cdd:TIGR01166 81 LFAADVDQDVAFGP---LNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGG----EKKRVAIAGAVAMRPDVLL-LD 152
|
170 180 190
....*....|....*....|....*....|...
gi 6325199 1009 EPTSGLDSQSAWSIVQFMRALADSGQSILCTIH 1041
Cdd:TIGR01166 153 EPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
868-1031 |
2.22e-13 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 73.60 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLA--QRINMGVIT--GDMLVNAKP---LPASfNRSCGYVAQADNHMAELSVRESLRF 940
Cdd:COG4148 22 LPGRGVTALFGPSGSGKTTLLRAIAglERPDSGRIRlgGEVLQDSARgifLPPH-RRRIGYVFQEARLFPHLSVRGNLLY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 941 AA--ELRQQSSVPLEEkyeyvekIITLLGMqnyaEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQS 1018
Cdd:COG4148 101 GRkrAPRAERRISFDE-------VVELLGI----GHLLDRRPATLSGGERQRVAIGRALLSSPRLLL-MDEPLAALDLAR 168
|
170
....*....|...
gi 6325199 1019 AWSIVQFMRALAD 1031
Cdd:COG4148 169 KAEILPYLERLRD 181
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
868-1042 |
2.85e-13 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 70.64 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLL---NVLaQRINMGVIT--GDMLVNAKPLPASFNRSCGYVAQADNHMAELSVRESLRFAa 942
Cdd:cd03262 23 VKKGEVVVIIGPSGSGKSTLLrciNLL-EEPDSGTIIidGLKLTDDKKNINELRQKVGMVFQQFNLFPHLTVLENITLA- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 943 eLRQQSSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLFlDEPTSGLDSQSAWSI 1022
Cdd:cd03262 101 -PIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGG----QQQRVAIARALAMNPKVMLF-DEPTSALDPELVGEV 174
|
170 180
....*....|....*....|
gi 6325199 1023 VQFMRALADSGQSILCTIHQ 1042
Cdd:cd03262 175 LDVMKDLAEEGMTMVVVTHE 194
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
853-1060 |
3.60e-13 |
|
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: 70.72 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 853 YDGaTRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLaqrinMGVIT---GDMLVNAKPLP----ASFNRSCGYVAQa 925
Cdd:cd03254 12 YDE-KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLL-----MRFYDpqkGQILIDGIDIRdisrKSLRSMIGVVLQ- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 926 DNHMAELSVRESLRFAAELRQQssvpleekyEYVEKIITLLGMQNYAEAL-------VGKTGRGLNVEQRKKLSIGVELV 998
Cdd:cd03254 85 DTFLFSGTIMENIRLGRPNATD---------EEVIEAAKEAGAHDFIMKLpngydtvLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325199 999 AKPSLLLfLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTiHQPSATLFEqfDRLLLLKKG 1060
Cdd:cd03254 156 RDPKILI-LDEATSNIDTETEKLIQEALEKLMKGRTSIIIA-HRLSTIKNA--DKILVLDDG 213
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
853-1060 |
3.96e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 74.05 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 853 YDGAtRKLLSDV-FgYVKPGKMTALMGESGAGKTTLLNVLaqrinMG---VITGDMLVNAKPL----PASFNRSCGYVAQ 924
Cdd:COG1132 349 YPGD-RPVLKDIsL-TIPPGETVALVGPSGSGKSTLVNLL-----LRfydPTSGRILIDGVDIrdltLESLRRQIGVVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 925 aDNHMAELSVRESLRFAAElrqqsSVPLEEkyeyVEKIITLLGMQNYAEAL-------VGKTGRGLNVEQRKKLSIGVEL 997
Cdd:COG1132 422 -DTFLFSGTIRENIRYGRP-----DATDEE----VEEAAKAAQAHEFIEALpdgydtvVGERGVNLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6325199 998 VAKPSLLLfLDEPTSGLDSQSAWSIVQFMRALADSGQSILctI-HQPSaTLfEQFDRLLLLKKG 1060
Cdd:COG1132 492 LKDPPILI-LDEATSALDTETEALIQEALERLMKGRTTIV--IaHRLS-TI-RNADRILVLDDG 550
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
861-1060 |
5.62e-13 |
|
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: 70.45 E-value: 5.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 861 LSDVFGYVKPGKMTALMGESGAGKTTLLNVLA--QRINMG-VITGDMLVNAKPLPasfNRSCGYVAQadnHMA---ELSV 934
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAglERPDSGtILFGGEDATDVPVQ---ERNVGFVFQ---HYAlfrHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 935 RESLRFAAELRQQSSVPLE-EKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLDEPTSG 1013
Cdd:cd03296 92 FDNVAFGLRVKPRSERPPEaEIRAKVHELLKLVQLDWLADRYPAQLSGG----QRQRVALARALAVEPKVLL-LDEPFGA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6325199 1014 LDSQSAWSIVQFMRALAD--SGQSILCTIHQPSAtlFEQFDRLLLLKKG 1060
Cdd:cd03296 167 LDAKVRKELRRWLRRLHDelHVTTVFVTHDQEEA--LEVADRVVVMNKG 213
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
838-1041 |
7.55e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 70.65 E-value: 7.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 838 EKDVFTWNHLDYTIPyDGAtrKLLSDVFGYVKPGKMTALMGESGAGKTTLLnvlaQRINmGVI---TGDMLVNAKPLPAS 914
Cdd:PRK13636 2 EDYILKVEELNYNYS-DGT--HALKGININIKKGEVTAILGGNGAGKSTLF----QNLN-GILkpsSGRILFDGKPIDYS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 915 ------FNRSCGYVAQA-DNHMAELSVRESLRFAAelrQQSSVPLEEKYEYVEKIITLLGMqnyaEALVGKTGRGLNVEQ 987
Cdd:PRK13636 74 rkglmkLRESVGMVFQDpDNQLFSASVYQDVSFGA---VNLKLPEDEVRKRVDNALKRTGI----EHLKDKPTHCLSFGQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6325199 988 RKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQFMRALADS-GQSILCTIH 1041
Cdd:PRK13636 147 KKRVAIAGVLVMEPKVLV-LDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATH 200
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
161-379 |
8.54e-13 |
|
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: 69.10 E-value: 8.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 161 RNIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGetseLVD-VQGEFSYDGLDQsEMMSKYKGYVIYCPELDFHFPkI 239
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILG----LLKpTSGSIRVFGKPL-EKERKRIGYVPQRRSIDRDFP-I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 240 TVKETIdfALKCKTPRVRIDKMTRKQY--VDNIRDMwctvfglrhTYATKVGNDFVRGVSGGERKRVSLVEAQAMNASIY 317
Cdd:cd03235 86 SVRDVV--LMGLYGHKGLFRRLSKADKakVDEALER---------VGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6325199 318 SWDNATRGLDASTALEFAQAIRT--ATNMvnnsAIVAIYQAGENIYELFDKTTVLyNGRQIYFG 379
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRElrREGM----TILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
868-1028 |
1.01e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 71.26 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLA--QRINMGVIT-GDMLVNAKPlPAsfNRSCGYVAQadN-----HMaelSVRESLR 939
Cdd:COG3839 26 IEDGEFLVLLGPSGCGKSTLLRMIAglEDPTSGEILiGGRDVTDLP-PK--DRNIAMVFQ--SyalypHM---TVYENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 940 FAAELRQqssVPLEEKYEYVEKIITLLGMQNYAE----ALVGktGrglnveQRKKLSIGVELVAKPSLLLFlDEPTSGLD 1015
Cdd:COG3839 98 FPLKLRK---VPKAEIDRRVREAAELLGLEDLLDrkpkQLSG--G------QRQRVALGRALVREPKVFLL-DEPLSNLD 165
|
170
....*....|...
gi 6325199 1016 SQSAWSivqfMRA 1028
Cdd:COG3839 166 AKLRVE----MRA 174
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
848-1061 |
1.12e-12 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 69.18 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 848 DYTIPYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINmgVITGDMLVNAKPLP----ASFNRSCGYVA 923
Cdd:cd03251 5 NVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYD--VDSGRILIDGHDVRdytlASLRRQIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 924 QaDNHMAELSVRESLRFAAELRQQSSVPLEEKYEYVEKIITllGMQNYAEALVGKTGRGLNVEQRKKLSIGVELVAKPSL 1003
Cdd:cd03251 83 Q-DVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIM--ELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6325199 1004 LLfLDEPTSGLDSQSAWSIVQFMRALADSGQSI-----LCTIhqpsatlfEQFDRLLLLKKGG 1061
Cdd:cd03251 160 LI-LDEATSALDTESERLVQAALERLMKNRTTFviahrLSTI--------ENADRIVVLEDGK 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
858-1060 |
1.41e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 68.54 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDV-FGyVKPGKMTALMGESGAGKTTLLNVL--AQRINMGVIT--GDMLVNAKP--LPAsFNRSCGYVAQaDNH-M 929
Cdd:COG2884 15 REALSDVsLE-IEKGEFVFLTGPSGAGKSTLLKLLygEERPTSGQVLvnGQDLSRLKRreIPY-LRRRIGVVFQ-DFRlL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 930 AELSVRESLRFAAELRQQSSVPLEEKyeyVEKIITLLGMQNYAEALVGKTGRGlnvEQrKKLSIGVELVAKPSLLLfLDE 1009
Cdd:COG2884 92 PDRTVYENVALPLRVTGKSRKEIRRR---VREVLDLVGLSDKAKALPHELSGG---EQ-QRVAIARALVNRPELLL-ADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6325199 1010 PTSGLDSQSAWSIVQFMRALADSGQSILCTIHQPSatLFEQFD-RLLLLKKG 1060
Cdd:COG2884 164 PTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE--LVDRMPkRVLELEDG 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
868-1068 |
1.62e-12 |
|
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: 68.86 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLaqrinMGVI---TGDMLVNAKP---LPAS--FNRSCGYVAQADNHMAELSVRESLR 939
Cdd:COG0410 26 VEEGEIVALLGRNGAGKTTLLKAI-----SGLLpprSGSIRFDGEDitgLPPHriARLGIGYVPEGRRIFPSLTVEENLL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 940 FAAELRQQSSVP---LEEKYEY----VEKiitllgMQNYAEALVGktGrglnveQRKKLSIGVELVAKPSLLLfLDEPTS 1012
Cdd:COG0410 101 LGAYARRDRAEVradLERVYELfprlKER------RRQRAGTLSG--G------EQQMLAIGRALMSRPKLLL-LDEPSL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6325199 1013 GLdsqsAWSIVQFM----RALADSGQSILctihqpsatLFEQF--------DRLLLLKKgGKMVYFGD 1068
Cdd:COG0410 166 GL----APLIVEEIfeiiRRLNREGVTIL---------LVEQNarfaleiaDRAYVLER-GRIVLEGT 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
868-1064 |
2.04e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 70.24 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLlnvlaQRINMGVIT---GDMLVNAKPLPA---SFNRSCGYVAQADNHMAELSVRESLRFA 941
Cdd:PRK13536 64 VASGECFGLLGPNGAGKSTI-----ARMILGMTSpdaGKITVLGVPVPArarLARARIGVVPQFDNLDLEFTVRENLLVF 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 942 AELRQQSSVPLEEkyeYVEKIITLLGMQNYAEALVGKTGRGLnveqRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWS 1021
Cdd:PRK13536 139 GRYFGMSTREIEA---VIPSLLEFARLESKADARVSDLSGGM----KRRLTLARALINDPQLLI-LDEPTTGLDPHARHL 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6325199 1022 IVQFMRALADSGQSILCTIHqpsatLFEQF----DRLLLLKKGGKMV 1064
Cdd:PRK13536 211 IWERLRSLLARGKTILLTTH-----FMEEAerlcDRLCVLEAGRKIA 252
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
161-422 |
2.27e-12 |
|
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: 71.47 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 161 RNIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGETSELVDVQGEFSYDGLDQSEM----MSKYKGYVIYCPELDFhF 236
Cdd:COG1123 19 VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELsealRGRRIGMVFQDPMTQL-N 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 237 PkITVKETIDFALkcktprvRIDKMTRKQYVDNIRDMWCTVfGLRHtyatkVGNDFVRGVSGGERKRVSLVEAQAMNASI 316
Cdd:COG1123 98 P-VTVGDQIAEAL-------ENLGLSRAEARARVLELLEAV-GLER-----RLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 317 YSWDNATRGLDASTALEFAQAIRTATNMvNNSAIVAIYQAGENIYELFDKTTVLYNGRQIYFGPAD---------KAVGY 387
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRE-RGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEeilaapqalAAVPR 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 6325199 388 FQRMGWVKPNRMTSAEFL---TSVTVDFENR-----------TLDIKPG 422
Cdd:COG1123 243 LGAARGRAAPAAAAAEPLlevRNLSKRYPVRgkggvravddvSLTLRRG 291
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
858-1069 |
3.28e-12 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 68.08 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDVFGYVKPGKMTALMGESGAGKTTLLnvlaqRINMGVIT---GDMLVNAKPLPA-------SFNRSCGYVAQA-- 925
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLL-----KLIIGLLRpdsGEILVDGQDITGlsekelyELRRRIGMLFQGga 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 926 --DNhmaeLSVRESLRFAaeLRQQSSVPLEEKYEYVEKIITLLGMQNYAE----ALVGktgrGlnveQRKKLSIGVELVA 999
Cdd:COG1127 93 lfDS----LTVFENVAFP--LREHTDLSEAEIRELVLEKLELVGLPGAADkmpsELSG----G----MRKRVALARALAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325199 1000 KPSLLlFLDEPTSGLDSQSAWSIVQFMRALADSGQ--SILCTiHQpSATLFEQFDRLLLLKKgGKMVYFGDI 1069
Cdd:COG1127 159 DPEIL-LYDEPTAGLDPITSAVIDELIRELRDELGltSVVVT-HD-LDSAFAIADRVAVLAD-GKIIAEGTP 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
857-1060 |
3.57e-12 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 67.57 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 857 TRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLA--QRINMG-VITGDMLVNAKPLPASFNRSCGYVAQADNHMAELS 933
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVglVKPDSGkILLDGQDITKLPMHKRARLGIGYLPQEASIFRKLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 934 VRESLRFAAELRQQSSVPLEEKYEYVekiITLLGMqnyaEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSG 1013
Cdd:cd03218 92 VEENILAVLEIRGLSKKEREEKLEEL---LEEFHI----THLRKSKASSLSGGERRRVEIARALATNPKFLL-LDEPFAG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6325199 1014 LDSQSAWSIVQFMRALADSGQSILCTIHQPSATLfEQFDRLLLLKKG 1060
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDRGIGVLITDHNVRETL-SITDRAYIIYEG 209
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
868-1024 |
5.50e-12 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 67.18 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLaQR---INMGVITGDMlVNAKPLPASFNRS-CGYVAQaDNHMAELSVRESLRFAAE 943
Cdd:cd03249 26 IPPGKTVALVGSSGCGKSTVVSLL-ERfydPTSGEILLDG-VDIRDLNLRWLRSqIGLVSQ-EPVLFDGTIAENIRYGKP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 944 LRQQSSVPLEEKYEYVEKIITLLgMQNYaEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAwSIV 1023
Cdd:cd03249 103 DATDEEVEEAAKKANIHDFIMSL-PDGY-DTLVGERGSQLSGGQKQRIAIARALLRNPKILL-LDEATSALDAESE-KLV 178
|
.
gi 6325199 1024 Q 1024
Cdd:cd03249 179 Q 179
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
868-1015 |
7.34e-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: 68.59 E-value: 7.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKP---LPAsFNRSCGYVAQAD---NHMaelSVRESL 938
Cdd:COG3842 28 IEPGEFVALLGPSGCGKTTLLRMIA-----GFETpdsGRILLDGRDvtgLPP-EKRNVGMVFQDYalfPHL---TVAENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 939 RFAaeLRQQsSVPLEEKYEYVEKIITLLGMQNYAEALVGktgrglnveqrkKLSIG----VE----LVAKPSLLLfLDEP 1010
Cdd:COG3842 99 AFG--LRMR-GVPKAEIRARVAELLELVGLEGLADRYPH------------QLSGGqqqrVAlaraLAPEPRVLL-LDEP 162
|
....*
gi 6325199 1011 TSGLD 1015
Cdd:COG3842 163 LSALD 167
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
161-374 |
8.04e-12 |
|
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: 64.96 E-value: 8.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 161 RNIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGETSElvdVQGEFSYDGLDQSEMMSK-YKGYVIYCPELdfhfpki 239
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKP---TSGEILIDGKDIAKLPLEeLRRRIGYVPQL------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 240 tvketidfalkcktprvridkmtrkqyvdnirdmwctvfglrhtyatkvgndfvrgvSGGERKRVSLVEAQAMNASIYSW 319
Cdd:cd00267 82 ---------------------------------------------------------SGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6325199 320 DNATRGLDASTALEFAQAIRTATNmvNNSAIVAIYQAGENIYELFDKTTVLYNGR 374
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAE--EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
845-1067 |
8.34e-12 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 67.06 E-value: 8.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 845 NHLDYTIpydgATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKPLpASFNRscgy 921
Cdd:COG4559 5 ENLSVRL----GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLT-----GELTpssGEVRLNGRPL-AAWSP---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 922 vaqadnhmAELSVReslRfaAELRQQSSVPL-------------------EEKYEYVEKIITLLGMQNYAE----ALVGk 978
Cdd:COG4559 71 --------WELARR---R--AVLPQHSSLAFpftveevvalgraphgssaAQDRQIVREALALVGLAHLAGrsyqTLSG- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 979 tgrGlnvEQRKklsigVEL----------VAKPSLLLFLDEPTSGLD--SQSAwsIVQFMRALADSGQSILCTIHQPSAT 1046
Cdd:COG4559 137 ---G---EQQR-----VQLarvlaqlwepVDGGPRWLFLDEPTSALDlaHQHA--VLRLARQLARRGGGVVAVLHDLNLA 203
|
250 260
....*....|....*....|..
gi 6325199 1047 LfeQF-DRLLLLkKGGKMVYFG 1067
Cdd:COG4559 204 A--QYaDRILLL-HQGRLVAQG 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
858-1043 |
1.33e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.67 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLA--QRINMGVITGDMLVNAKPLPASfnrSCGYVAQADNHMAELSVR 935
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAglLPPAAGTIKLDGGDIDDPDVAE---ACHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 936 ESLRFAAELRQQSSVPLEEKyeyvekiITLLGMQNYAEalvgKTGRGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGLD 1015
Cdd:PRK13539 92 ENLEFWAAFLGGEELDIAAA-------LEAVGLAPLAH----LPFGYLSAGQKRRVALARLLVSNRPIWI-LDEPTAALD 159
|
170 180
....*....|....*....|....*...
gi 6325199 1016 SQSAWSIVQFMRALADSGQSILCTIHQP 1043
Cdd:PRK13539 160 AAAVALFAELIRAHLAQGGIVIAATHIP 187
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
858-1060 |
1.54e-11 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 65.96 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAqriNMGVIT-GDMLVNAKPLPASFNRscgYVaqadnHMAELSV-R 935
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLE---NFYQPQgGQVLLDGKPISQYEHK---YL-----HSKVSLVgQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 936 ESLRFAAELRQQ-----SSVPLEEKYEYVEK-----IITLLGMQNYAEalVGKTGRGLNVEQRKKLSIGVELVAKPSLLL 1005
Cdd:cd03248 96 EPVLFARSLQDNiayglQSCSFECVKEAAQKahahsFISELASGYDTE--VGEKGSQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6325199 1006 fLDEPTSGLDSQSAWSIVQfmrALAD--SGQSILCTIHQPSatLFEQFDRLLLLKKG 1060
Cdd:cd03248 174 -LDEATSALDAESEQQVQQ---ALYDwpERRTVLVIAHRLS--TVERADQILVLDGG 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
171-335 |
1.74e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 65.51 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 171 VESGEMLFVVGRPGAGCSTFLKCLSGE---TSELVDVQGefsydgldqsEMMSKYKGYVIycPEL---------DFHF-P 237
Cdd:cd03292 24 ISAGEFVFLVGPSGAGKSTLLKLIYKEelpTSGTIRVNG----------QDVSDLRGRAI--PYLrrkigvvfqDFRLlP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 238 KITVKETIDFALKC--KTPRVridkmTRKQYVDNIRdmwctVFGLRHTYatkvgNDFVRGVSGGERKRVSLVEAQAMNAS 315
Cdd:cd03292 92 DRNVYENVAFALEVtgVPPRE-----IRKRVPAALE-----LVGLSHKH-----RALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180
....*....|....*....|
gi 6325199 316 IYSWDNATRGLDASTALEFA 335
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIM 176
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
835-1060 |
1.96e-11 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 64.80 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 835 VIAEKDVFTWNhldytiPYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQriNMGVITGDMLVnakplpas 914
Cdd:cd03250 1 ISVEDASFTWD------SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG--ELEKLSGSVSV-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 915 fNRSCGYVAQADNHMAElSVRESLRFAAELRqqssvplEEKYEYV------EKIITLL--GMQnyaeALVGKTGRGLNVE 986
Cdd:cd03250 65 -PGSIAYVSQEPWIQNG-TIRENILFGKPFD-------EERYEKVikacalEPDLEILpdGDL----TEIGEKGINLSGG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325199 987 QRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQ--FMRALADSGQSILCTiHQPSatLFEQFDRLLLLKKG 1060
Cdd:cd03250 132 QKQRISLARAVYSDADIYL-LDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVT-HQLQ--LLPHADQIVVLDNG 203
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
853-1060 |
2.03e-11 |
|
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: 64.16 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 853 YDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAqrinmGVI---TGDMLVNAKPL----PASFNRSCGYVAQA 925
Cdd:cd03246 10 YPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLIL-----GLLrptSGRVRLDGADIsqwdPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 926 DnhmaELsvreslrFAAELRqqssvpleekyeyvEKIITllgmqnyaealvgktgRGlnveQRKKLSIGVELVAKPSlLL 1005
Cdd:cd03246 85 D----EL-------FSGSIA--------------ENILS----------------GG----QRQRLGLARALYGNPR-IL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6325199 1006 FLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQPSatLFEQFDRLLLLKKG 1060
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDG 171
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
161-374 |
3.02e-11 |
|
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: 64.41 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 161 RNIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGEtseLVDVQGEFSYDGLD----QSEMMSKYKGYViycpeldFHF 236
Cdd:cd03225 14 RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL---LGPTSGEVLVDGKDltklSLKELRRKVGLV-------FQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 237 P-----KITVKETIDFALK-CKTPRVRIDKmtrkqyvdnIRDMWCTVFGL-----RHTYAtkvgndfvrgVSGGERKRVS 305
Cdd:cd03225 84 PddqffGPTVEEEVAFGLEnLGLPEEEIEE---------RVEEALELVGLeglrdRSPFT----------LSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6325199 306 LVEAQAMNASIYSWDNATRGLDASTALEFAQAIRTATNmvNNSAIVAIYQAGENIYELFDKTTVLYNGR 374
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA--EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
859-1042 |
3.24e-11 |
|
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: 64.91 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 859 KLLSDVFGYVKPGKMTALMGESGAGKTTLL---NVLaQRINMGVITGD----MLVNAKPLPAsFNRSCGYVAQADNHMAE 931
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIrciNGL-ERPTSGSVLVDgtdlTLLSGKELRK-ARRRIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 932 LSVRESLRFAAELrqqSSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLDEPT 1011
Cdd:cd03258 97 RTVFENVALPLEI---AGVPKAEIEERVLELLELVGLEDKADAYPAQLSGG----QKQRVGIARALANNPKVLL-CDEAT 168
|
170 180 190
....*....|....*....|....*....|..
gi 6325199 1012 SGLDSQSAWSIVQFMRALADS-GQSILCTIHQ 1042
Cdd:cd03258 169 SALDPETTQSILALLRDINRElGLTIVLITHE 200
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
857-1015 |
3.49e-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: 64.58 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 857 TRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLA--QRINMGVI-TGDMLVNAkpLPASfNRSCGYVAQadN-----H 928
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAglEEPTSGRIyIGGRDVTD--LPPK-DRDIAMVFQ--NyalypH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 929 MaelSVRESLRFAAELRQQSSVPLEEKyeyVEKIITLLGMqnyaEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLLfLD 1008
Cdd:cd03301 87 M---TVYDNIAFGLKLRKVPKDEIDER---VREVAELLQI----EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL-MD 155
|
....*..
gi 6325199 1009 EPTSGLD 1015
Cdd:cd03301 156 EPLSNLD 162
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
868-1017 |
3.57e-11 |
|
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: 64.95 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKP---LPAsFNRSCGYVAQADNHMAELSVRESLRFA 941
Cdd:cd03300 23 IKEGEFFTLLGPSGCGKTTLLRLIA-----GFETptsGEILLDGKDitnLPP-HKRPVNTVFQNYALFPHLTVFENIAFG 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325199 942 AELRQQSSVPLEEKyeyVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQ 1017
Cdd:cd03300 97 LRLKKLPKAEIKER---VAEALDLVQLEGYANRKPSQLSGG----QQQRVAIARALVNEPKVLL-LDEPLGALDLK 164
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
864-1059 |
3.79e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.48 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 864 VFG----YVKPGKMTALMGESGAGKTTLLNVLAQRINMGviTGDMLVNAKPLP-ASFNRSCGYVAQADNHMAELSVRESL 938
Cdd:PRK13543 26 VFGpldfHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVE--SGQIQIDGKTATrGDRSRFMAYLGHLPGLKADLSTLENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 939 RFAAEL--RQQSSVPleekyeyvEKIITLLGMQNYAEALVgktgRGLNVEQRKKLSIGvELVAKPSLLLFLDEPTSGLDS 1016
Cdd:PRK13543 104 HFLCGLhgRRAKQMP--------GSALAIVGLAGYEDTLV----RQLSAGQKKRLALA-RLWLSPAPLWLLDEPYANLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6325199 1017 QSAWSIVQFMRALADSGQSILCTIHQPSATLFEQfDRLLLLKK 1059
Cdd:PRK13543 171 EGITLVNRMISAHLRGGGAALVTTHGAYAAPPVR-TRMLTLEA 212
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
171-382 |
7.91e-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: 7.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 171 VESGEMLFVVGRPGAGCSTFLKCLSGEtseLVDVQGEFSYDGLDQSEMMSKYK-------GYVIYCPELdfhFPKITVKE 243
Cdd:cd03261 23 VRRGEILAIIGPSGSGKSTLLRLIVGL---LRPDSGEVLIDGEDISGLSEAELyrlrrrmGMLFQSGAL---FDSLTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 244 TIDFALKCKT--PRVRIDKMTRkqyvdnirdMWCTVFGLRHTyatkvGNDFVRGVSGGERKRVSLVEAQAMNASIYSWDN 321
Cdd:cd03261 97 NVAFPLREHTrlSEEEIREIVL---------EKLEAVGLRGA-----EDLYPAELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6325199 322 ATRGLDASTALEFAQAIRTATNMVNNSAIV------AIYQAGENIYelfdkttVLYNGRQIYFGPAD 382
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKELGLTSIMvthdldTAFAIADRIA-------VLYDGKIVAEGTPE 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
868-1037 |
1.09e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.81 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKPLP-----ASFNRSCGYVAQADNHMAELSVRESLR 939
Cdd:COG1129 27 LRPGEVHALLGENGAGKSTLMKILS-----GVYQpdsGEILLDGEPVRfrsprDAQAAGIAIIHQELNLVPNLSVAENIF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 940 FAAELRQQSSVPLEEKYEYVEKIITLLGMQNYAEALVGktgrGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSA 1019
Cdd:COG1129 102 LGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVG----DLSVAQQQLVEIARALSRDARVLI-LDEPTASLTEREV 176
|
170
....*....|....*...
gi 6325199 1020 WSIVQFMRALADSGQSIL 1037
Cdd:COG1129 177 ERLFRIIRRLKAQGVAII 194
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
868-1064 |
1.18e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.41 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT--GDMLVNAKPL----PASFNRSCGYVAQADNHMAELSVRESLrfa 941
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMA-----GLLPgsGSIQFAGQPLeawsAAELARHRAYLSQQQTPPFAMPVFQYL--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 942 aELRQQSSVPLEEKYEYVEKIITLLGMQNyaealvgKTGRGLNV----E-QRKKLSiGVELVAKPSL-----LLFLDEPT 1011
Cdd:PRK03695 91 -TLHQPDKTRTEAVASALNEVAEALGLDD-------KLGRSVNQlsggEwQRVRLA-AVVLQVWPDInpagqLLLLDEPM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6325199 1012 SGLD-SQSAWsIVQFMRALADSGQSILCTIHQPSATLfEQFDRLLLLkKGGKMV 1064
Cdd:PRK03695 162 NSLDvAQQAA-LDRLLSELCQQGIAVVMSSHDLNHTL-RHADRVWLL-KQGKLL 212
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
868-1041 |
1.89e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.56 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTL---LNvlaqrinmGVI---TGDMLVNAKPLPAS------FNRSCGYVAQ-ADNHMAELSV 934
Cdd:PRK13639 25 AEKGEMVALLGPNGAGKSTLflhFN--------GILkptSGEVLIKGEPIKYDkkslleVRKTVGIVFQnPDDQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 935 RESLRFAAelrQQSSVPLEEKYEYVEKIITLLGMQNYAEalvgKTGRGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGL 1014
Cdd:PRK13639 97 EEDVAFGP---LNLGLSKEEVEKRVKEALKAVGMEGFEN----KPPHHLSGGQKKRVAIAGILAMKPEIIV-LDEPTSGL 168
|
170 180
....*....|....*....|....*..
gi 6325199 1015 DSQSAWSIVQFMRALADSGQSILCTIH 1041
Cdd:PRK13639 169 DPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
173-379 |
2.01e-10 |
|
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: 62.31 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 173 SGEMLFVVGRPGAGCSTFLKCLSGETSelVDVqGEFSYDG--LDQSEM---MSKYK---GYVIYCPELdfhFPKITVKET 244
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEK--PDG-GTIVLNGtvLFDSRKkinLPPQQrkiGLVFQQYAL---FPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 245 IDFALKCKTPRVridkmtRKQYVDNIRDmwctVFGLRHtyatkVGNDFVRGVSGGERKRVSLVEAQAMNASIYSWDNATR 324
Cdd:cd03297 96 LAFGLKRKRNRE------DRISVDELLD----LLGLDH-----LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6325199 325 GLDASTALEFAQAIRtatNMVNNSAIVAIY--QAGENIYELFDKTTVLYNGRQIYFG 379
Cdd:cd03297 161 ALDRALRLQLLPELK---QIKKNLNIPVIFvtHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
856-1060 |
2.34e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.21 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 856 ATRKLLsDVFGYVKPGKMTALMGESGAGKTTLL---NVLAQRINMGVITGDMLVNA-------KPLpasfNRSCGYVAQ- 924
Cdd:PRK13643 18 ASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLqhlNGLLQPTEGKVTVGDIVVSStskqkeiKPV----RKKVGVVFQf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 925 ADNHMAELSVRESLRFAAelrQQSSVPLEEKYEYVEKIITLLGMqnyAEALVGKTGRGLNVEQRKKLSIGVELVAKPSLL 1004
Cdd:PRK13643 93 PESQLFEETVLKDVAFGP---QNFGIPKEKAEKIAAEKLEMVGL---ADEFWEKSPFELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6325199 1005 LfLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQPSaTLFEQFDRLLLLKKG 1060
Cdd:PRK13643 167 V-LDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMD-DVADYADYVYLLEKG 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
868-1060 |
2.50e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 65.13 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAqriNMGVIT-GDMLVNAKPLPA----SFNRSCGYVAQADNHMAElSVRESLRFAA 942
Cdd:TIGR00958 504 LHPGEVVALVGPSGSGKSTVAALLQ---NLYQPTgGQVLLDGVPLVQydhhYLHRQVALVGQEPVLFSG-SVRENIAYGL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 943 ELRQQSSVPLEEKYEYVEKIITllGMQNYAEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWSI 1022
Cdd:TIGR00958 580 TDTPDEEIMAAAKAANAHDFIM--EFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLI-LDEATSALDAECEQLL 656
|
170 180 190
....*....|....*....|....*....|....*...
gi 6325199 1023 VQFMRAladSGQSILCTIHQPSatLFEQFDRLLLLKKG 1060
Cdd:TIGR00958 657 QESRSR---ASRTVLLIAHRLS--TVERADQILVLKKG 689
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
845-1063 |
2.57e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 63.11 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 845 NHLDYTipYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTllnvLAQRINmGVI---TGDMLVNAKPLPAS----FNR 917
Cdd:PRK13635 9 EHISFR--YPDAATYALKDVSFSVYEGEWVAIVGHNGSGKST----LAKLLN-GLLlpeAGTITVGGMVLSEEtvwdVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 918 SCGYVAQ-ADNHMAELSVRESLRFAAELRQqssVPLEEKYEYVEKIITLLGMQNYAE----ALVGKtgrglnveQRKKLS 992
Cdd:PRK13635 82 QVGMVFQnPDNQFVGATVQDDVAFGLENIG---VPREEMVERVDQALRQVGMEDFLNrephRLSGG--------QKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6325199 993 IGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQFMRALAD-SGQSILCTIHQpsatLFE--QFDRLLLLKKGGKM 1063
Cdd:PRK13635 151 IAGVLALQPDIII-LDEATSMLDPRGRREVLETVRQLKEqKGITVLSITHD----LDEaaQADRVIVMNKGEIL 219
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
861-1064 |
3.03e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.17 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 861 LSDVFGYVKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT--GDMLVNAKPL----PASFNRSCGYVAQADNHMAELSV 934
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMA-----GLLPgqGEILLNGRPLsdwsAAELARHRAYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 935 RESLRfaaeLRQQSSVPLEEKYEYVEKIITLLGmqnyaeaLVGKTGRGLNveqrkKLSIG----VELVAK-----PSL-- 1003
Cdd:COG4138 87 FQYLA----LHQPAGASSEAVEQLLAQLAEALG-------LEDKLSRPLT-----QLSGGewqrVRLAAVllqvwPTInp 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325199 1004 ---LLFLDEPTSGLD--SQSAwsIVQFMRALADSGQSILCTIHQPSATLFeQFDRLLLLkKGGKMV 1064
Cdd:COG4138 151 egqLLLLDEPMNSLDvaQQAA--LDRLLRELCQQGITVVMSSHDLNHTLR-HADRVWLL-KQGKLV 212
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
840-1060 |
3.44e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.90 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 840 DVFTWNHLDYTipYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTT---LLN--VLAQRINMGVITGD-MLVNAKPLpA 913
Cdd:PRK13640 4 NIVEFKHVSFT--YPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINglLLPDDNPNSKITVDgITLTAKTV-W 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 914 SFNRSCGYVAQ-ADNHMAELSVRESLRFAAELRQqssVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLS 992
Cdd:PRK13640 81 DIREKVGIVFQnPDNQFVGATVGDDVAFGLENRA---VPRPEMIKIVRDVLADVGMLDYIDSEPANLSGG----QKQRVA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6325199 993 IGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQFMRALA-DSGQSILCTIHQPSATlfEQFDRLLLLKKG 1060
Cdd:PRK13640 154 IAGILAVEPKIII-LDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEA--NMADQVLVLDDG 219
|
|
| ABC_trans_N |
pfam14510 |
ABC-transporter N-terminal; This domain is found at the N-terminus of ABC-transporter proteins ... |
46-134 |
3.59e-10 |
|
ABC-transporter N-terminal; This domain is found at the N-terminus of ABC-transporter proteins from fungi, plants to higher eukaryotes. It is predicted to be an intracellular domain.
Pssm-ID: 464194 Cd Length: 80 Bit Score: 57.71 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 46 QLSRHLSNILSNEegierlesmarviSHKTKKEMDSFEINDLDFDLRSLLHYLRSRQLEQG-IEPGDSGIAFKNLTAVGV 124
Cdd:pfam14510 1 ELARILTRQSSSS-------------SSSSSPESTDPDEEDSEFDLRKWLKNLRRLIDEDGyIKPRKLGVAFKNLTVSGV 67
|
90
....*....|
gi 6325199 125 DASAAYGPSV 134
Cdd:pfam14510 68 GAGADYQPTV 77
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
868-1060 |
4.12e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 62.34 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAqrinmGVITGDMLVNAK------------PLPASFNRS---CGYVAQADNHMAEL 932
Cdd:PRK09984 27 IHHGEMVALLGPSGSGKSTLLRHLS-----GLITGDKSAGSHiellgrtvqregRLARDIRKSranTGYIFQQFNLVNRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 933 SVRESLRFAAelrqQSSVPL---------EEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSL 1003
Cdd:PRK09984 102 SVLENVLIGA----LGSTPFwrtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSGG----QQQRVAIARALMQQAKV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6325199 1004 LLfLDEPTSGLDSQSAWSIVQFMRAL-ADSGQSILCTIHQPSATLfEQFDRLLLLKKG 1060
Cdd:PRK09984 174 IL-ADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYAL-RYCERIVALRQG 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
868-1037 |
4.88e-10 |
|
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: 59.75 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKPLpaSFNrscgyvaqadnhmaelSVRESLRFAAEL 944
Cdd:cd03216 23 VRRGEVHALLGENGAGKSTLMKILS-----GLYKpdsGEILVDGKEV--SFA----------------SPRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 945 RQQssvpleekyeyvekiitllgmqnyaealvgktgrgLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQ 1024
Cdd:cd03216 80 VYQ-----------------------------------LSVGERQMVEIARALARNARLLI-LDEPTAALTPAEVERLFK 123
|
170
....*....|...
gi 6325199 1025 FMRALADSGQSIL 1037
Cdd:cd03216 124 VIRRLRAQGVAVI 136
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
845-1060 |
6.11e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 63.69 E-value: 6.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 845 NHLDYTipYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQriNMGVITGDMLVNAKPLPAsFNRScgyvaQ 924
Cdd:PRK11160 342 NNVSFT--YPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTR--AWDPQQGEILLNGQPIAD-YSEA-----A 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 925 ADNHMAELSVRESLrFAAELRQQSSVPLEEKYEyvEKIITLL---GMQNYAE------ALVGKTGRGLNVEQRKKLSIGV 995
Cdd:PRK11160 412 LRQAISVVSQRVHL-FSATLRDNLLLAAPNASD--EALIEVLqqvGLEKLLEddkglnAWLGEGGRQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325199 996 ELVAKPSLLLfLDEPTSGLDSQSAWSIVQFMRALAdSGQSILCTIHQpsATLFEQFDRLLLLKKG 1060
Cdd:PRK11160 489 ALLHDAPLLL-LDEPTEGLDAETERQILELLAEHA-QNKTVLMITHR--LTGLEQFDRICVMDNG 549
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
873-1039 |
6.99e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.65 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 873 MTALMGESGAGKTTLLNVLaQRINMGV----ITGDMLVNAKPL-----PASFNRSCGYVAQADNHMAeLSVRESLrfAAE 943
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTL-NRMNDKVsgyrYSGDVLLGGRSIfnyrdVLEFRRRVGMLFQRPNPFP-MSIMDNV--LAG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 944 LRQQSSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWSIV 1023
Cdd:PRK14271 125 VRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL-LDEPTSALDPTTTEKIE 203
|
170
....*....|....*.
gi 6325199 1024 QFMRALADSGQSILCT 1039
Cdd:PRK14271 204 EFIRSLADRLTVIIVT 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
868-1044 |
7.18e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 61.30 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLL---NVLAQ----RINMGVITGDM---LVNAKPLPASFNRSCGYVAQADNHMAELSVRES 937
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLrciNLLEQpeagTIRVGDITIDTarsLSQQKGLIRQLRQHVGFVFQNFNLFPHRTVLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 938 LrfaaeLRQQSSVPLEEKYEYVEKIITLLgmqnyaeALVGKTG------RGLNVEQRKKLSIGVELVAKPSLLLFlDEPT 1011
Cdd:PRK11264 106 I-----IEGPVIVKGEPKEEATARARELL-------AKVGLAGketsypRRLSGGQQQRVAIARALAMRPEVILF-DEPT 172
|
170 180 190
....*....|....*....|....*....|...
gi 6325199 1012 SGLDSQSAWSIVQFMRALADSGQSILCTIHQPS 1044
Cdd:PRK11264 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
858-1060 |
8.14e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.38 E-value: 8.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINMGV------ITGDMLVNAKPL----PASFNRSCGYVAQADN 927
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarVTGDVTLNGEPLaaidAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 928 HMAELSVRE--SLRFAAELRQQSSVPLEEKyEYVEKIITLLGmqnyAEALVGKTGRGLNVEQRKKLSIGVELV------- 998
Cdd:PRK13547 94 PAFAFSAREivLLGRYPHARRAGALTHRDG-EIAWQALALAG----ATALVGRDVTTLSGGELARVQFARVLAqlwpphd 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6325199 999 -AKPSLLLFLDEPTSGLDSQSAWSIVQFMRALA-DSGQSILCTIHQPSATLfEQFDRLLLLKKG 1060
Cdd:PRK13547 169 aAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLArDWNLGVLAIVHDPNLAA-RHADRIAMLADG 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
848-1016 |
8.94e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.06 E-value: 8.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 848 DYTIPYDGaTRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLaQRI---NMGVITGDMLVNAKPLPASFNRSCGYVAQ 924
Cdd:PRK13657 339 DVSFSYDN-SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL-QRVfdpQSGRILIDGTDIRTVTRASLRRNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 925 aDNHMAELSVRESLRFA------AELRQQSSvpLEEKYEYVEKiitllGMQNYaEALVGKTGRGLNVEQRKKLSIGVELV 998
Cdd:PRK13657 417 -DAGLFNRSIEDNIRVGrpdatdEEMRAAAE--RAQAHDFIER-----KPDGY-DTVVGERGRQLSGGERQRLAIARALL 487
|
170
....*....|....*...
gi 6325199 999 AKPSLLLfLDEPTSGLDS 1016
Cdd:PRK13657 488 KDPPILI-LDEATSALDV 504
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
853-1078 |
9.49e-10 |
|
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: 60.71 E-value: 9.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 853 YDGaTRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINmgVITGDMLVNAKPLP----ASFNRSCGYVAQaDNH 928
Cdd:cd03253 10 YDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYD--VSSGSILIDGQDIRevtlDSLRRAIGVVPQ-DTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 929 MAELSVRESLRFAAElrqqsSVPLEEKYEYVEKII---TLLGMQNYAEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLL 1005
Cdd:cd03253 86 LFNDTIGYNIRYGRP-----DATDEEVIEAAKAAQihdKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6325199 1006 FlDEPTSGLDSQSAWSIVQFMRALADSGQSILCTiHQPSATLfeQFDRLLLLKKgGKMVyfgDIGPNSETLLK 1078
Cdd:cd03253 161 L-DEATSALDTHTEREIQAALRDVSKGRTTIVIA-HRLSTIV--NADKIIVLKD-GRIV---ERGTHEELLAK 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
859-1074 |
1.22e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.70 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 859 KLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINM---GVITGDMLVNAKPL----PASFNRSCGYVAQADNHMAE 931
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypeARVSGEVYLDGQDIfkmdVIELRRRVQMVFQIPNPIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 932 LSVRESLRFAAELRQ--QSSVPLEEKYEY-VEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLD 1008
Cdd:PRK14247 97 LSIFENVALGLKLNRlvKSKKELQERVRWaLEKAQLWDEVKDRLDAPAGKLSGG----QQQRLCIARALAFQPEVLL-AD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325199 1009 EPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQPSATLFEQFDRLLLlkkGGKMVyfgDIGPNSE 1074
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLY---KGQIV---EWGPTRE 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
868-1037 |
1.35e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.35 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLaqrinMGVIT---GDMLVNAKPL-PASFN--RSCG--YVAQ----ADNhmaeLSVR 935
Cdd:COG3845 28 VRPGEIHALLGENGAGKSTLMKIL-----YGLYQpdsGEILIDGKPVrIRSPRdaIALGigMVHQhfmlVPN----LTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 936 ESLRFAAELRQQSSVPLEEKYEYVEKIitllgMQNYaealvgktgrGLNVEQRKK---LSIG----VELV------AKps 1002
Cdd:COG3845 99 ENIVLGLEPTKGGRLDRKAARARIREL-----SERY----------GLDVDPDAKvedLSVGeqqrVEILkalyrgAR-- 161
|
170 180 190
....*....|....*....|....*....|....*
gi 6325199 1003 lLLFLDEPTSGLDSQSAWSIVQFMRALADSGQSIL 1037
Cdd:COG3845 162 -ILILDEPTAVLTPQEADELFEILRRLAAEGKSII 195
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
868-1067 |
1.43e-09 |
|
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: 59.81 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKPLPAS--FNRSCGYVAQADNHMAELSVRE------ 936
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIA-----GFETpqsGRVLINGVDVTAAppADRPVSMLFQENNLFAHLTVEQnvglgl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 937 --SLRFAAELRQQssvpleekyeyVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELV-AKPSLLlfLDEPTSG 1013
Cdd:cd03298 96 spGLKLTAEDRQA-----------IEVALARVGLAGLEKRLPGELSGG----ERQRVALARVLVrDKPVLL--LDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6325199 1014 LDSQSAWSIVQFMRAL-ADSGQSILCTIHQPSATLfEQFDRLLLLKKgGKMVYFG 1067
Cdd:cd03298 159 LDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAK-RLAQRVVFLDN-GRIAAQG 211
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
806-1060 |
1.68e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 63.11 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 806 LGTENADARTASREEMMEALNGPNVDLEKVIAEKDVFTWNHLDYTIPydGATRKLLSDVFG-YVKPG-----------KM 873
Cdd:TIGR01257 881 LGGEGCSTREERALEKTEPLTEEMEDPEHPEGINDSFFERELPGLVP--GVCVKNLVKIFEpSGRPAvdrlnitfyenQI 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 874 TALMGESGAGKTTLLNVLAqrinmGVI---TGDMLVNAKPLPASFN---RSCGYVAQADNHMAELSVRESLRFAAELRQQ 947
Cdd:TIGR01257 959 TAFLGHNGAGKTTTLSILT-----GLLpptSGTVLVGGKDIETNLDavrQSLGMCPQHNILFHHLTVAEHILFYAQLKGR 1033
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 948 SSvplEEKYEYVEKIITLLGMQNYAEalvgKTGRGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQFMR 1027
Cdd:TIGR01257 1034 SW---EEAQLEMEAMLEDTGLHHKRN----EEAQDLSGGMQRKLSVAIAFVGDAKVVV-LDEPTSGVDPYSRRSIWDLLL 1105
|
250 260 270
....*....|....*....|....*....|...
gi 6325199 1028 ALADSGQSILCTIHQPSATLFEqfDRLLLLKKG 1060
Cdd:TIGR01257 1106 KYRSGRTIIMSTHHMDEADLLG--DRIAIISQG 1136
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
855-1042 |
1.76e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.11 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 855 GATrKLLSDVFGYVKPGKMTALMGESGAGKTTLL---NVLAQrINMG-VITGDMLVNAkplPASFNR----SCGYVAQAD 926
Cdd:PRK09493 12 GPT-QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKLEE-ITSGdLIVDGLKVND---PKVDERlirqEAGMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 927 NHMAELSVRESLRFA---------AELRQQSS-----VPLEEKyeyvekiitllgMQNYAEALVGKtgrglnveQRKKLS 992
Cdd:PRK09493 87 YLFPHLTALENVMFGplrvrgaskEEAEKQARellakVGLAER------------AHHYPSELSGG--------QQQRVA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6325199 993 IGVELVAKPSLLLFlDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQ 1042
Cdd:PRK09493 147 IARALAVKPKLMLF-DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
868-1068 |
2.39e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 59.70 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAQRINMGVITGDMLVNAKPL-------------------PASFnrscgyvaqadnh 928
Cdd:COG0396 23 IKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTSGSILLDGEDIlelspderaragiflafqyPVEI------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 929 mAELSVRESLRFAAELRQQSSVPLEEKYEYVEKIITLLGM-QNYAEalvgktgRGLNVE----QRKKLSIGVELVAKPSL 1003
Cdd:COG0396 90 -PGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLdEDFLD-------RYVNEGfsggEKKRNEILQMLLLEPKL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6325199 1004 LLfLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQPsatlfeqfdRLL-LLK-------KGGKMVYFGD 1068
Cdd:COG0396 162 AI-LDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQ---------RILdYIKpdfvhvlVDGRIVKSGG 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
858-1060 |
2.42e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.79 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINmgVITGDMLVNAKPLpasfnrscgyvaqadnhmAELSVRES 937
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELS--PDSGEVRLNGRPL------------------ADWSPAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 938 LRFAAELRQQSSV--PLEekyeyVEKIITLLGM---------QNYAEALVGKTG-RGLnvEQRK--KLSIG----VEL-- 997
Cdd:PRK13548 75 ARRRAVLPQHSSLsfPFT-----VEEVVAMGRAphglsraedDALVAAALAQVDlAHL--AGRDypQLSGGeqqrVQLar 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325199 998 -------VAKPSLLLFLDEPTSGLDSQSAWSIVQFMRALA-DSGQSILCTIHQPS-ATLFEqfDRLLLLKKG 1060
Cdd:PRK13548 148 vlaqlwePDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNlAARYA--DRIVLLHQG 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
171-333 |
2.87e-09 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 58.91 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 171 VESGEMLFVVGRPGAGCSTFLKCLSGEtsELVDvQGEFSYDGLDqsemMSKYKGYVIycPEL---------DFHF-PKIT 240
Cdd:COG2884 25 IEKGEFVFLTGPSGAGKSTLLKLLYGE--ERPT-SGQVLVNGQD----LSRLKRREI--PYLrrrigvvfqDFRLlPDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 241 VKETIDFALkcktprvRIDKMTRKQYVDNIRDM--WctvFGLRHtyatkVGNDFVRGVSGGERKRVSLVEAQAMNASIYS 318
Cdd:COG2884 96 VYENVALPL-------RVTGKSRKEIRRRVREVldL---VGLSD-----KAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170
....*....|....*
gi 6325199 319 WDNATRGLDASTALE 333
Cdd:COG2884 161 ADEPTGNLDPETSWE 175
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
858-1043 |
5.52e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.89 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAqrinmGVI---TGDMLVNAKPL---PASFNRSCGYVAQADNHMAE 931
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILA-----GLArpdAGEVLWQGEPIrrqRDEYHQDLLYLGHQPGIKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 932 LSVRESLRFAAELRQQSSVplEEKYEYVEKIitllGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLDEPT 1011
Cdd:PRK13538 89 LTALENLRFYQRLHGPGDD--EALWEALAQV----GLAGFEDVPVRQLSAG----QQRRVALARLWLTRAPLWI-LDEPF 157
|
170 180 190
....*....|....*....|....*....|..
gi 6325199 1012 SGLDSQSAWSIVQFMRALADSGQSILCTIHQP 1043
Cdd:PRK13538 158 TAIDKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
161-339 |
6.39e-09 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 60.38 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 161 RNIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGetseLVDV-QGEFSYDGLDQSEMMSK-YKGYVIYCPELDFHFPK 238
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG----FVDPtEGSIAVNGVPLADADADsWRDQIAWVPQHPFLFAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 239 iTVKETIDFALKCKTPrVRIDKMTRKQYVDNIrdmwctVFGLRHTYATKVGNDfVRGVSGGERKRVSLVEAQAMNASIYS 318
Cdd:TIGR02857 411 -TIAENIRLARPDASD-AEIREALERAGLDEF------VAALPQGLDTPIGEG-GAGLSGGQAQRLALARAFLRDAPLLL 481
|
170 180
....*....|....*....|.
gi 6325199 319 WDNATRGLDASTALEFAQAIR 339
Cdd:TIGR02857 482 LDEPTAHLDAETEAEVLEALR 502
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
861-1069 |
1.10e-08 |
|
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: 57.35 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 861 LSDVFGYVKPGKMTALMGESGAGKTTLLNVLAqrinmGVI---TGDMLVNAK---PLPASfNRSCGYVAQADNHMAELSV 934
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIA-----GFIkpdSGKILLNGKditNLPPE-KRDISYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 935 RESLRFAAELRqqssvpLEEKYEYVEKIITLLGMQNYAEALVGKTGRgLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGL 1014
Cdd:cd03299 89 YKNIAYGLKKR------KVDKKEIERKVLEIAEMLGIDHLLNRKPET-LSGGEQQRVAIARALVVNPKILL-LDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1015 DSQSAWSIVQFMRALADS-GQSILCTIHQpsatlFEQF----DRLLLLKKgGKMVYFGDI 1069
Cdd:cd03299 161 DVRTKEKLREELKKIRKEfGVTVLHVTHD-----FEEAwalaDKVAIMLN-GKLIQVGKP 214
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
853-1064 |
1.27e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 57.79 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 853 YDGatRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLA--QRINMGVITGDMLVNAKPlpaSFNRscGYVAQADNHMA 930
Cdd:PRK11248 11 YGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAgfVPYQHGSITLDGKPVEGP---GAER--GVVFQNEGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 931 ELSVRESLRFAAELRqqsSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLDEP 1010
Cdd:PRK11248 84 WRNVQDNVAFGLQLA---GVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGG----QRQRVGIARALAANPQLLL-LDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6325199 1011 TSGLDsqsAWSIVQ----FMRALADSGQSILCTIHQPSATLFEQFDRLLLLKKGGKMV 1064
Cdd:PRK11248 156 FGALD---AFTREQmqtlLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVV 210
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
842-1060 |
1.87e-08 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 55.78 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 842 FTWNHLDYTipYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLnvlaqrinmGVITGDMlvnaKPlpasfnrSCGY 921
Cdd:cd03247 1 LSINNVSFS--YPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLL---------QLLTGDL----KP-------QQGE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 922 VAQADNHMAELSvreslrfaAELRQQSSVPLEEKYEYVEKIitllgMQNyaealvgkTGRGLNVEQRKKLSIGVELVAKP 1001
Cdd:cd03247 59 ITLDGVPVSDLE--------KALSSLISVLNQRPYLFDTTL-----RNN--------LGRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1002 SLLLfLDEPTSGLDSQSAWSIV-QFMRALADsgQSILCTIHQPSAtlFEQFDRLLLLKKG 1060
Cdd:cd03247 118 PIVL-LDEPTVGLDPITERQLLsLIFEVLKD--KTLIWITHHLTG--IEHMDKILFLENG 172
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
868-1016 |
2.37e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.12 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLA--QRINMG-VITGDMLVNAKPlPAsfNRSCGYVAQADNHMAELSVRESLRFAAEL 944
Cdd:PRK11000 26 IHEGEFVVFVGPSGCGKSTLLRMIAglEDITSGdLFIGEKRMNDVP-PA--ERGVGMVFQSYALYPHLSVAENMSFGLKL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325199 945 RQQSSVPLEEKYEYVEKIITLlgmqnyaEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGLDS 1016
Cdd:PRK11000 103 AGAKKEEINQRVNQVAEVLQL-------AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL-LDEPLSNLDA 166
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
171-374 |
3.10e-08 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 54.89 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 171 VESGEMLFVVGRPGAGCSTFLKCLSG---ETSELVDVQGEFSYDGLDQSEMMSKYKGYVIYCPELdfhFPKITVKETIDF 247
Cdd:cd03229 23 IEAGEIVALLGPSGSGKSTLLRCIAGleePDSGSILIDGEDLTDLEDELPPLRRRIGMVFQDFAL---FPHLTVLENIAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 248 ALkcktprvridkmtrkqyvdnirdmwctvfglrhtyatkvgndfvrgvSGGERKRVSLVEAQAMNASIYSWDNATRGLD 327
Cdd:cd03229 100 GL-----------------------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6325199 328 ASTALEFAQAIRTATNMVNNSAIVAIYQAGEnIYELFDKTTVLYNGR 374
Cdd:cd03229 133 PITRREVRALLKSLQAQLGITVVLVTHDLDE-AARLADRVVVLRDGK 178
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
850-1017 |
3.94e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 57.15 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 850 TIPYDGatRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLA--QRINMG--VITGDMLVNAKPlpasFNRSCGYVAQA 925
Cdd:PRK11607 26 TKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAgfEQPTAGqiMLDGVDLSHVPP----YQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 926 DNHMAELSVRESLRFAAelrQQSSVPLEEKYEYVEKIITLLGMQNYAealvGKTGRGLNVEQRKKLSIGVELVAKPSLLL 1005
Cdd:PRK11607 100 YALFPHMTVEQNIAFGL---KQDKLPKAEIASRVNEMLGLVHMQEFA----KRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170
....*....|..
gi 6325199 1006 fLDEPTSGLDSQ 1017
Cdd:PRK11607 173 -LDEPMGALDKK 183
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
868-1060 |
5.00e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.56 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAQRINMGviTGDMLVNAKPL--------PASFNRSCGYVAQADNHMAELSVRESLR 939
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGS--SGEVSLVGQPLhqmdeearAKLRAKHVGFVFQSFMLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 940 FAAELRQQSSvplEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnvEQrKKLSIGVELVAKPSlLLFLDEPTSGLDSQSA 1019
Cdd:PRK10584 111 LPALLRGESS---RQSRNGAKALLEQLGLGKRLDHLPAQLSGG---EQ-QRVALARAFNGRPD-VLFADEPTGNLDRQTG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6325199 1020 WSIVQFMRAL-ADSGQSILCTIHQPsaTLFEQFDRLLLLKKG 1060
Cdd:PRK10584 183 DKIADLLFSLnREHGTTLILVTHDL--QLAARCDRRLRLVNG 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
868-1015 |
7.27e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 54.97 E-value: 7.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVN----AKPLPAsfNRSCGYVAQADNHMAELSVRE---- 936
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLLNLIA-----GFLTpasGSLTLNgqdhTTTPPS--RRPVSMLFQENNLFSHLTVAQnigl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 937 ----SLRFAAELRQQssvpleekyeyVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLDEPTS 1012
Cdd:PRK10771 95 glnpGLKLNAAQREK-----------LHAIARQMGIEDLLARLPGQLSGG----QRQRVALARCLVREQPILL-LDEPFS 158
|
...
gi 6325199 1013 GLD 1015
Cdd:PRK10771 159 ALD 161
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
162-331 |
8.04e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.82 E-value: 8.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 162 NIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGETSElvdVQGEFSYDGLDQSEMMSKYKGYV-------IYcpelDF 234
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTP---TSGDVIFNGQPMSKLSSAAKAELrnqklgfIY----QF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 235 H--FPKITVKETIDFALkcktprvRIDKMTRKQYVDNIRDMWCTVfGLRHTyatkvGNDFVRGVSGGERKRVSLVEAQAM 312
Cdd:PRK11629 96 HhlLPDFTALENVAMPL-------LIGKKKPAEINSRALEMLAAV-GLEHR-----ANHRPSELSGGERQRVAIARALVN 162
|
170
....*....|....*....
gi 6325199 313 NASIYSWDNATRGLDASTA 331
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNA 181
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
852-1041 |
8.85e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 55.52 E-value: 8.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 852 PYDGATrklLSDVFGYVKPGKMTALMGESGAGKTT---LLNVLAQRINMGVITGDMLVNAKPLPA---SFNRSCGYVAQ- 924
Cdd:PRK13649 17 PFEGRA---LFDVNLTIEDGSYTAFIGHTGSGKSTimqLLNGLHVPTQGSVRVDDTLITSTSKNKdikQIRKKVGLVFQf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 925 ADNHMAELSVRESLRFAAelrQQSSVPLEEKYEYVEKIITLLGMqnyAEALVGKTGRGLNVEQRKKLSIGVELVAKPSLL 1004
Cdd:PRK13649 94 PESQLFEETVLKDVAFGP---QNFGVSQEEAEALAREKLALVGI---SESLFEKNPFELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 6325199 1005 LfLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIH 1041
Cdd:PRK13649 168 V-LDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
858-1084 |
9.37e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 54.07 E-value: 9.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINMGVITGDMLVNAKPLpasfnrscgyvaqadnhmAELSVRES 937
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGEDI------------------TDLPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 938 LRFAAELRQQSsvPLEekYEYVeKIITLLgmqnyaealvgktgRGLNVE----QRKKLSIGVELVAKPSLLLfLDEPTSG 1013
Cdd:cd03217 75 ARLGIFLAFQY--PPE--IPGV-KNADFL--------------RYVNEGfsggEKKRNEILQLLLLEPDLAI-LDEPDSG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6325199 1014 LDSQSAWSIVQFMRALADSGQSILCTIHQPSATLFEQFDRLLLLKKgGKMVYFGDigpnsETLLKYFERQS 1084
Cdd:cd03217 135 LDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYD-GRIVKSGD-----KELALEIEKKG 199
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
171-342 |
1.08e-07 |
|
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: 56.21 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 171 VESGEMLFVVGRPGAGCSTFLKCLSGETSELvdvQGEFSYDGLD-QSEMMSKYKGYVIYCPElDFHFPKITVKETIDFAL 249
Cdd:TIGR02868 358 LPPGERVAILGPSGSGKSTLLATLAGLLDPL---QGEVTLDGVPvSSLDQDEVRRRVSVCAQ-DAHLFDTTVRENLRLAR 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 250 KCKTPRVRIDKMTRKQYVDNIRDmwctvfgLRHTYATKVGNDFVRgVSGGERKRVSLVEAQAMNASIYSWDNATRGLDAS 329
Cdd:TIGR02868 434 PDATDEELWAALERVGLADWLRA-------LPDGLDTVLGEGGAR-LSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
170
....*....|...
gi 6325199 330 TALEFAQAIRTAT 342
Cdd:TIGR02868 506 TADELLEDLLAAL 518
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
870-1063 |
1.39e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 54.63 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 870 PGKMTALMGESGAGKTTLLNVLAqRINMGViTGDMLVNAKPLpasfnrscgyvaqadnhmAELSVRESLRFAAELRQQSS 949
Cdd:PRK11231 27 TGKITALIGPNGCGKSTLLKCFA-RLLTPQ-SGTVFLGDKPI------------------SMLSSRQLARRLALLPQHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 950 VP----LEEKYEY-------------------VEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELvAKPSLLLF 1006
Cdd:PRK11231 87 TPegitVRELVAYgrspwlslwgrlsaednarVNQAMEQTRINHLADRRLTDLSGG----QRQRAFLAMVL-AQDTPVVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1007 LDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIH---QPSatlfEQFDRLLLLKKGGKM 1063
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQAS----RYCDHLVVLANGHVM 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
859-1068 |
2.87e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.94 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 859 KLLSDVFGYVKPGKMTALMGESGAGKTTL---LNVL---------------------------AQRINMGVITGDMLVNA 908
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALllpdtgtiewifkdeknkkktkekekvLEKLVIQKTRFKKIKKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 909 KPLpasfNRSCGYVAQ-ADNHMAELSVRESLRFAAelrQQSSVPLEEKYEYVEKIITLLGM-QNYAEalvgKTGRGLNVE 986
Cdd:PRK13651 101 KEI----RRRVGVVFQfAEYQLFEQTIEKDIIFGP---VSMGVSKEEAKKRAAKYIELVGLdESYLQ----RSPFELSGG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 987 QRKKLSIGVELVAKPSLLlFLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQPSATLfEQFDRLLLLKKgGKMVYF 1066
Cdd:PRK13651 170 QKRRVALAGILAMEPDFL-VFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVL-EWTKRTIFFKD-GKIIKD 246
|
..
gi 6325199 1067 GD 1068
Cdd:PRK13651 247 GD 248
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
163-339 |
2.95e-07 |
|
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: 52.88 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 163 IIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGetselVDV--QGEFSYDGLDQSEM----MSKYK----GYViycpel 232
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG-----LDRptSGEVRVDGTDISKLsekeLAAFRrrhiGFV------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 233 dFHF----PKITVKETIDFALkcktprvRIDKMTRKQYVDNIRDMwCTVFGLRHTYATKVGNdfvrgVSGGERKRVSLVE 308
Cdd:cd03255 88 -FQSfnllPDLTALENVELPL-------LLAGVPKKERRERAEEL-LERVGLGDRLNHYPSE-----LSGGQQQRVAIAR 153
|
170 180 190
....*....|....*....|....*....|.
gi 6325199 309 AQAMNASIYSWDNATRGLDASTALEFAQAIR 339
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLR 184
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
875-1044 |
3.01e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 53.31 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 875 ALMGESGAGKTTLLNVLAQRINMGV---------ITGDMLVNAKPLPASFNRSCGYVAQADNHMAELSVRESLRFAAELR 945
Cdd:PRK14267 34 ALMGPSGCGKSTLLRTFNRLLELNEearvegevrLFGRNIYSPDVDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 946 Q--QSSVPLEEKYEYVEKIITLLG-----MQNYAEALVGKtgrglnveQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQS 1018
Cdd:PRK14267 114 GlvKSKKELDERVEWALKKAALWDevkdrLNDYPSNLSGG--------QRQRLVIARALAMKPKILL-MDEPTANIDPVG 184
|
170 180
....*....|....*....|....*.
gi 6325199 1019 AWSIVQFMRALADSGQSILCTiHQPS 1044
Cdd:PRK14267 185 TAKIEELLFELKKEYTIVLVT-HSPA 209
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
161-382 |
3.21e-07 |
|
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: 53.06 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 161 RNIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCL-------SGEtselVDVQGEfSYDGLDQSEMMSKYK--GYViycpe 231
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIigllrpdSGE----ILVDGQ-DITGLSEKELYELRRriGML----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 232 ldFH----FPKITVKETIDFALKCKTprvridKMTRKQyvdnIRDMwctV------FGLRHtyatkVGNDFVRGVSGGER 301
Cdd:COG1127 88 --FQggalFDSLTVFENVAFPLREHT------DLSEAE----IREL---VleklelVGLPG-----AADKMPSELSGGMR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 302 KRVSLVEAQAMNASIYSWDNATRGLDASTALEFAQAIRTATNMVNNSAIV------AIYQAGENIYelfdkttVLYNGRQ 375
Cdd:COG1127 148 KRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVvthdldSAFAIADRVA-------VLADGKI 220
|
....*..
gi 6325199 376 IYFGPAD 382
Cdd:COG1127 221 IAEGTPE 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
861-1060 |
3.57e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.58 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 861 LSDVFGYVKPGKMTALMGESGAGKTTLLnvlaqRINMGVI---TGDMLVNAKPLPAS----FNRSCGYVAQ-ADNHMAEL 932
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTV-----RLIDGLLeaeSGQIIIDGDLLTEEnvwdIRHKIGMVFQnPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 933 SVRESLRFAAElrqQSSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLDEPTS 1012
Cdd:PRK13650 98 TVEDDVAFGLE---NKGIPHEEMKERVNEALELVGMQDFKEREPARLSGG----QKQRVAIAGAVAMRPKIII-LDEATS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6325199 1013 GLDSQSAWSIVQFMRALADSGQSILCTI-HQPSATLFEqfDRLLLLKKG 1060
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISItHDLDEVALS--DRVLVMKNG 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
868-1069 |
3.79e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.94 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAK-PLP--ASFNRSCGYVaqadnhMA-------ELSV 934
Cdd:COG4586 45 IEPGEIVGFIGPNGAGKSTTIKMLT-----GILVptsGEVRVLGYvPFKrrKEFARRIGVV------FGqrsqlwwDLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 935 RESLRFAAELRQqssVPlEEKY-EYVEKIITLLGMQNYaealvgktgrgLNVEQRKkLSIG----VELVAkpSLL----- 1004
Cdd:COG4586 114 IDSFRLLKAIYR---IP-DAEYkKRLDELVELLDLGEL-----------LDTPVRQ-LSLGqrmrCELAA--ALLhrpki 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6325199 1005 LFLDEPTSGLD--SQSAwsIVQFMRAL-ADSGQSILCTIHqpsatlfeqfD---------RLLLLKKgGKMVYFGDI 1069
Cdd:COG4586 176 LFLDEPTIGLDvvSKEA--IREFLKEYnRERGTTILLTSH----------DmddiealcdRVIVIDH-GRIIYDGSL 239
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
859-1069 |
4.63e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 859 KLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAqrinmGVI---TGDMLVNAKPL-----PASFNRSCGYVAQADNHMA 930
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILS-----GNYqpdAGSILIDGQEMrfastTAALAAGVAIIYQELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 931 ELSVRESL-------RFA----AELRQQSSVPLEEkyeyvekiitlLGMQNYAEALVgktgrglnveqrKKLSIG----V 995
Cdd:PRK11288 93 EMTVAENLylgqlphKGGivnrRLLNYEAREQLEH-----------LGVDIDPDTPL------------KYLSIGqrqmV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6325199 996 EL---VAKPSLLLFLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQpSATLFEQFDRLLLLKKGGKMVYFGDI 1069
Cdd:PRK11288 150 EIakaLARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHR-MEEIFALCDAITVFKDGRYVATFDDM 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
861-1069 |
5.21e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.02 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 861 LSDVFGYVKPGKMTALMGESGAGKTTLLNVL--AQRINMGVITGDMLVNAKPLPA-SFNRSCGYVAQADNHMAELSVRES 937
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLsgIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQELSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 938 LrFAAEL--RQQSSVPL---EEKYEYVEKIITLLGMQNYAEALVGKtgrgLNVEQRKKLSIGVELVAKPSLLLfLDEPTS 1012
Cdd:PRK09700 101 L-YIGRHltKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVII-MDEPTS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6325199 1013 GLDSQSAWSIVQFMRALADSGQSILCTIHQpSATLFEQFDRLLLLKKGGKmVYFGDI 1069
Cdd:PRK09700 175 SLTNKEVDYLFLIMNQLRKEGTAIVYISHK-LAEIRRICDRYTVMKDGSS-VCSGMV 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
857-1020 |
5.45e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 53.92 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 857 TRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAkplpasfNRSCGYVAQADNHMAELS 933
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILA-----GELEpdsGEVSIPK-------GLRIGYLPQEPPLDDDLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 934 VRESLRFA--------AELRQQSSVP------------LEEKYEY---------VEKIITLLGM-QNYAEALVGK-TGrG 982
Cdd:COG0488 78 VLDTVLDGdaelraleAELEELEAKLaepdedlerlaeLQEEFEAlggweaearAEEILSGLGFpEEDLDRPVSElSG-G 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 6325199 983 lnveQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQS-AW 1020
Cdd:COG0488 157 ----WRRRVALARALLSEPDLLL-LDEPTNHLDLESiEW 190
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
832-1043 |
8.35e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 52.36 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 832 LEKVIAEKDVFTWNHLdYTIPYDGAtrkLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINMG----VITGDMLVN 907
Cdd:PRK14246 1 MEAGKSAEDVFNISRL-YLYINDKA---ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYdskiKVDGKVLYF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 908 AKPL----PASFNRSCGYVAQADNHMAELSVRESLrfAAELRQQSSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGL 983
Cdd:PRK14246 77 GKDIfqidAIKLRKEVGMVFQQPNPFPHLSIYDNI--AYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 984 NVEQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQFMRALADSgQSILCTIHQP 1043
Cdd:PRK14246 155 SGGQQQRLTIARALALKPKVLL-MDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNP 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
878-1015 |
1.14e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.59 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 878 GESGAGKTTllnvlaqriNMGVITGdmLvnakpLPAS------FNRS-----------CGYVAQADNHMAELSVRESLRF 940
Cdd:NF033858 299 GSNGCGKST---------TMKMLTG--L-----LPASegeawlFGQPvdagdiatrrrVGYMSQAFSLYGELTVRQNLEL 362
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325199 941 AAELRQqssVPLEEKYEYVEKIITLLGMQNYAEALVGktgrGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGLD 1015
Cdd:NF033858 363 HARLFH---LPAAEIAARVAEMLERFDLADVADALPD----SLPLGIRQRLSLAVAVIHKPELLI-LDEPTSGVD 429
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
171-382 |
1.21e-06 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 51.57 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 171 VESGEMLFVVGRPGAGCSTFLKCLSG-ETSElvdvQGEFSYDGLDQSEMMSKYK--GYVIYCPELdfhFPKITVKETIDF 247
Cdd:cd03296 25 IPSGELVALLGPSGSGKTTLLRLIAGlERPD----SGTILFGGEDATDVPVQERnvGFVFQHYAL---FRHMTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 248 ALKCKTPRVRIDKMTRKQYVDNIrdmwctvfgLRHTYATKVGNDFVRGVSGGERKRVSLVEAQAMNASIYSWDNATRGLD 327
Cdd:cd03296 98 GLRVKPRSERPPEAEIRAKVHEL---------LKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6325199 328 ASTALEFAQAIRTATNMVNNSAIVAIYQAGENIyELFDKTTVLYNGRQIYFGPAD 382
Cdd:cd03296 169 AKVRKELRRWLRRLHDELHVTTVFVTHDQEEAL-EVADRVVVMNKGRIEQVGTPD 222
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
161-353 |
1.37e-06 |
|
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: 50.72 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 161 RNIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGETSElvdVQGEFSYDGLDQSE-MMSKYKGYVIycPELDFHFPKI 239
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE---SSGSILLNGKPIKAkERRKSIGYVM--QDVDYQLFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 240 TVKETIDFALKcktprvriDKMTRKQYVDNI-RDMWCTVFGLRHTyatkvgndfvRGVSGGERKRVSLVEAQAMNASIYS 318
Cdd:cd03226 88 SVREELLLGLK--------ELDAGNEQAETVlKDLDLYALKERHP----------LSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190
....*....|....*....|....*....|....*
gi 6325199 319 WDNATRGLDASTALEFAQAIRTATNMvnNSAIVAI 353
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQ--GKAVIVI 182
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
868-1015 |
1.49e-06 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 50.91 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKPL----PAsfNRSCGYVAQADNHMAELSVRE---- 936
Cdd:COG3840 22 IAAGERVAILGPSGAGKSTLLNLIA-----GFLPpdsGRILWNGQDLtalpPA--ERPVSMLFQENNLFPHLTVAQnigl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 937 ----SLRFAAELRQQssvpleekyeyVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELV-AKPSLLlfLDEPT 1011
Cdd:COG3840 95 glrpGLKLTAEQRAQ-----------VEQALERVGLAGLLDRLPGQLSGG----QRQRVALARCLVrKRPILL--LDEPF 157
|
....
gi 6325199 1012 SGLD 1015
Cdd:COG3840 158 SALD 161
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
869-1042 |
1.81e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.12 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 869 KPGKMTALMGESGAGKTTLLN--------------VLAQRINMGVIT-GDMLVNAKPLPASFNRSCGYVAQADNHMAELS 933
Cdd:PRK10619 29 NAGDVISIIGSSGSGKSTFLRcinflekpsegsivVNGQTINLVRDKdGQLKVADKNQLRLLRTRLTMVFQHFNLWSHMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 934 VRESLRFAaelrqqssvPLE----EKYEYVEKIITLLGMQNYAEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLLFlDE 1009
Cdd:PRK10619 109 VLENVMEA---------PIQvlglSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLF-DE 178
|
170 180 190
....*....|....*....|....*....|...
gi 6325199 1010 PTSGLDSQSAWSIVQFMRALADSGQSILCTIHQ 1042
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
858-1060 |
2.10e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 51.62 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLA--QRINMGVI----TGDMLVNAKplpasfNRSCGYVAQadnHMA- 930
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAglEHQTSGHIrfhgTDVSRLHAR------DRKVGFVFQ---HYAl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 931 --ELSVRESLRFAAELRQQSSVPleEKYEYVEKIITLLGMQNYAEaLVGKTGRGLNVEQRKKLSIGVELVAKPSLLLfLD 1008
Cdd:PRK10851 86 frHMTVFDNIAFGLTVLPRRERP--NAAAIKAKVTQLLEMVQLAH-LADRYPAQLSGGQKQRVALARALAVEPQILL-LD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6325199 1009 EPTSGLDSQSAWSIVQFMRALADSGQ--SILCTIHQPSATlfEQFDRLLLLKKG 1060
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKftSVFVTHDQEEAM--EVADRVVVMSQG 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
838-1060 |
2.11e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.91 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 838 EKDVFTWNHLDYTipYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTL--LNVLAQRINMG-VITGDMLVNAKPLpAS 914
Cdd:PRK13648 4 KNSIIVFKNVSFQ--YQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIakLMIGIEKVKSGeIFYNNQAITDDNF-EK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 915 FNRSCGYVAQ-ADNHMAELSVRESLRFAAElrqQSSVPLEEKYEYVEKIITLLGMQNYAE----ALVGKtgrglnveQRK 989
Cdd:PRK13648 81 LRKHIGIVFQnPDNQFVGSIVKYDVAFGLE---NHAVPYDEMHRRVSEALKQVDMLERADyepnALSGG--------QKQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325199 990 KLSIGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQFMRAL-ADSGQSILCTIHQPSATLfeQFDRLLLLKKG 1060
Cdd:PRK13648 150 RVAIAGVLALNPSVII-LDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAM--EADHVIVMNKG 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
870-1070 |
2.11e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.16 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 870 PGKMTALMGESGAGKTTLLNVLAqrinmGVI---TGDMLVNAKPLPAS------FNRSCGYVAQ-ADNHMAELSVRESLR 939
Cdd:PRK13638 26 LSPVTGLVGANGCGKSTLFMNLS-----GLLrpqKGAVLWQGKPLDYSkrgllaLRQQVATVFQdPEQQIFYTDIDSDIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 940 FAaeLRQQSsVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSA 1019
Cdd:PRK13638 101 FS--LRNLG-VPEAEITRRVDEALTLVDAQHFRHQPIQCLSHG----QKKRVAIAGALVLQARYLL-LDEPTAGLDPAGR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6325199 1020 WSIVQFMRALADSGQSILCTIHQPSaTLFEQFDRLLLLKKGGKMVYfGDIG 1070
Cdd:PRK13638 173 TQMIAIIRRIVAQGNHVIISSHDID-LIYEISDAVYVLRQGQILTH-GAPG 221
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
856-1015 |
2.12e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.08 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 856 ATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRI--NMGVITGDM----LVNAKPLPASFNRSC-----GYVAQ 924
Cdd:PRK11701 17 GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLapDAGEVHYRMrdgqLRDLYALSEAERRRLlrtewGFVHQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 925 --ADNHMAELS----VRESL-----RFAAELRQQSSVPLEEkyeyVEkiITLL-----------GMQnyaealvgktgrg 982
Cdd:PRK11701 97 hpRDGLRMQVSaggnIGERLmavgaRHYGDIRATAGDWLER----VE--IDAAriddlpttfsgGMQ------------- 157
|
170 180 190
....*....|....*....|....*....|...
gi 6325199 983 lnveQRkkLSIGVELVAKPSlLLFLDEPTSGLD 1015
Cdd:PRK11701 158 ----QR--LQIARNLVTHPR-LVFMDEPTGGLD 183
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
874-1015 |
2.36e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.41 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 874 TALMGESGAGKTTLLNVLA--QRINMGVIT--GDMLVNAKP---LPASfNRSCGYVAQaDnhmAEL----SVRESLRF-- 940
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISglTRPQKGRIVlnGRVLFDAEKgicLPPE-KRRIGYVFQ-D---ARLfphyKVRGNLRYgm 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325199 941 AAELRQQssvpleekyeyVEKIITLLGMqnyaEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGLD 1015
Cdd:PRK11144 102 AKSMVAQ-----------FDKIVALLGI----EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLL-MDEPLASLD 160
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
163-374 |
2.42e-06 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 49.62 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 163 IIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGEtseLVDVQGEFSYDGLDQSEmmskykgyviycpeldfhfpkitvk 242
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGD---LKPQQGEITLDGVPVSD------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 243 etidfalkcktprvridkmtrkqYVDNIRDMWCTVFGLRHTYATKVGNDFVRGVSGGERKRVSLVEAQAMNASIYSWDNA 322
Cdd:cd03247 69 -----------------------LEKALSSLISVLNQRPYLFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6325199 323 TRGLDASTALEFaqaIRTATNMVNNSAIVAIYQAGENIyELFDKTTVLYNGR 374
Cdd:cd03247 126 TVGLDPITERQL---LSLIFEVLKDKTLIWITHHLTGI-EHMDKILFLENGK 173
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
851-1064 |
4.56e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.57 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 851 IPYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRinmgvitgdmlvnakplpASFNRSCGYVAQADNHMA 930
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA------------------LKGTPVAGCVDVPDNQFG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 931 -ELSVRESLrfaaelrqqssVPLEEKYEYVEkiitLLGMQNYAEA-LVGKTGRGLNVEQRKKLSIGVELVAKPSLLLfLD 1008
Cdd:COG2401 98 rEASLIDAI-----------GRKGDFKDAVE----LLNAVGLSDAvLWLRRFKELSTGQKFRFRLALLLAERPKLLV-ID 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6325199 1009 EPTSGLDSQSAWSIVQFMRALADSG--QSILCTiHQPSATLFEQFDRLLLLKKGGKMV 1064
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKLARRAgiTLVVAT-HHYDVIDDLQPDLLIFVGYGGVPE 218
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
853-1061 |
5.27e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.87 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 853 YDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNvLAQRiNMGVITGDMLVNAKPLPAsfnrscgyvAQADNHMAEL 932
Cdd:PRK10789 323 YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLS-LIQR-HFDVSEGDIRFHDIPLTK---------LQLDSWRSRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 933 SVRESLRFAAELRQQSSVPL------EEKYEYV-------EKIITLlgMQNYaEALVGKTGRGLNVEQRKKLSIGVELVA 999
Cdd:PRK10789 392 AVVSQTPFLFSDTVANNIALgrpdatQQEIEHVarlasvhDDILRL--PQGY-DTEVGERGVMLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325199 1000 KPSLLLfLDEPTSGLDSQSAWSIVQFMRALADsGQSILCTIHQPSAtLFEQfDRLLLLKKGG 1061
Cdd:PRK10789 469 NAEILI-LDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSA-LTEA-SEILVMQHGH 526
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
143-339 |
5.28e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.47 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 143 SIPAHLISKFTKKSDVpLRNIIQNctgvVESGEMLFVVGRPGAGCSTFLKCLSGETSElvdVQGEFSYDGLDQSEMMSKY 222
Cdd:PRK10851 2 SIEIANIKKSFGRTQV-LNDISLD----IPSGQMVALLGPSGSGKTTLLRIIAGLEHQ---TSGHIRFHGTDVSRLHARD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 223 K--GYVIYCPELdfhFPKITVKETIDFALKCKTPRVRIDKMTRKQYVDNIRDMwctvFGLRHtyatkVGNDFVRGVSGGE 300
Cdd:PRK10851 74 RkvGFVFQHYAL---FRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLEM----VQLAH-----LADRYPAQLSGGQ 141
|
170 180 190
....*....|....*....|....*....|....*....
gi 6325199 301 RKRVSLVEAQAMNASIYSWDNATRGLDASTALEFAQAIR 339
Cdd:PRK10851 142 KQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLR 180
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
872-1068 |
5.29e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 872 KMTALMGESGAGKTTLLNVLAQRINM---------GVITGDM---------------LVNAKPLPAS-----------FN 916
Cdd:PTZ00265 1195 KTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkNEHTNDMtneqdyqgdeeqnvgMKNVNEFSLTkeggsgedstvFK 1274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 917 RS----------CGY----------VAQADNHMAELSVRESLRFAAELRQQSSVPLEEKYEYVEKIITLLgmQNYAEALV 976
Cdd:PTZ00265 1275 NSgkilldgvdiCDYnlkdlrnlfsIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESL--PNKYDTNV 1352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 977 GKTGRGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQpsatlfeqfdRLLL 1056
Cdd:PTZ00265 1353 GPYGKSLSGGQKQRIAIARALLREPKILL-LDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH----------RIAS 1421
|
250
....*....|..
gi 6325199 1057 LKKGGKMVYFGD 1068
Cdd:PTZ00265 1422 IKRSDKIVVFNN 1433
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
843-1015 |
5.31e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 50.02 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 843 TWNHLDYTipYDGAT---RKLLSDVFGYVKPGKMTALMGESGAGKTTL---LNVLAQRINMGVITGDMLVNA-------K 909
Cdd:PRK13634 4 TFQKVEHR--YQYKTpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLlqhLNGLLQPTSGTVTIGERVITAgkknkklK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 910 PLpasfNRSCGYVAQ-ADNHMAELSVRESLRFAAelrQQSSVPLEEKYEYVEKIITLLGMqnyAEALVGKTGRGLNVEQR 988
Cdd:PRK13634 82 PL----RKKVGIVFQfPEHQLFEETVEKDICFGP---MNFGVSEEDAKQKAREMIELVGL---PEELLARSPFELSGGQM 151
|
170 180
....*....|....*....|....*..
gi 6325199 989 KKLSIGVELVAKPSLLLfLDEPTSGLD 1015
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLV-LDEPTAGLD 177
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
1298-1367 |
5.53e-06 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 48.66 E-value: 5.53e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1298 VLIFPLYFVTYGLWILYMSPDVPSASMINSNLFAAMLLFCGILQPREKMPAFWRRLMYnVSPFTYVVQAL 1367
Cdd:COG0842 91 LLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAY-LNPLTYFVEAL 159
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
161-379 |
5.73e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 49.60 E-value: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 161 RNIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGetsELVDVQGEFSYDGLDQS----EMMSKYKGYVIYCPelDFHF 236
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTG---LLKPQSGEIKIDGITISkenlKEIRKKIGIIFQNP--DNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 237 PKITVKETIDFALKCKtprvridKMTRKQYVDNIRDmwctvfglrhtYATKVG-NDFVR----GVSGGERKRVSLVEAQA 311
Cdd:PRK13632 97 IGATVEDDIAFGLENK-------KVPPKKMKDIIDD-----------LAKKVGmEDYLDkepqNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6325199 312 MNASIYSWDNATRGLDASTALEFAQAIRTATNMVNNSAIVAIYQAGENIyeLFDKTTVLYNGRQIYFG 379
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI--LADKVIVFSEGKLIAQG 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
858-1015 |
5.84e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 49.76 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINMGviTGDMLVNAKPLPAsFNRSCGYVAQADNHM-------- 929
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD--HGEILFDGENIPA-MSRSRLYTVRKRMSMlfqsgalf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 930 AELSVRESLRFAaeLRQQSSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGLnvEQRKKLSIGVELvaKPSLLLFlDE 1009
Cdd:PRK11831 97 TDMNVFDNVAYP--LREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGM--ARRAALARAIAL--EPDLIMF-DE 169
|
....*.
gi 6325199 1010 PTSGLD 1015
Cdd:PRK11831 170 PFVGQD 175
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
171-379 |
6.37e-06 |
|
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: 49.04 E-value: 6.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 171 VESGEMLFVVGRPGAGCSTFLKCLSGetseLVDV-QGEFSYDGLD----QSEMMSKYKGYVIYCPE-----LDfhfPKIT 240
Cdd:cd03257 28 IKKGETLGLVGESGSGKSTLARAILG----LLKPtSGSIIFDGKDllklSRRLRKIRRKEIQMVFQdpmssLN---PRMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 241 VKETIDFALKCKTPRVRIDKMTRKQYVDNIRdmwctvFGLRHTYATKvgndFVRGVSGGERKRVSLVEAQAMNASIYSWD 320
Cdd:cd03257 101 IGEQIAEPLRIHGKLSKKEARKEAVLLLLVG------VGLPEEVLNR----YPHELSGGQRQRVAIARALALNPKLLIAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6325199 321 NATRGLDASTALEFAQAIRTATNMVNNSAI-----VAIyqagenIYELFDKTTVLYNGRQIYFG 379
Cdd:cd03257 171 EPTSALDVSVQAQILDLLKKLQEELGLTLLfithdLGV------VAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
171-327 |
6.88e-06 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 48.68 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 171 VESGEMLFVVGRPGAGCSTFLKCLSG-ETSElvdvQGEFSYDGLD------QSEMMSKYKGYVIYcpelDFH-FPKITVK 242
Cdd:cd03262 23 VKKGEVVVIIGPSGSGKSTLLRCINLlEEPD----SGTIIIDGLKltddkkNINELRQKVGMVFQ----QFNlFPHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 243 ETIDFALkcktprVRIDKMTRKQYVDNIRDmwctvfglrhtYATKVG-----NDFVRGVSGGERKRVSLVEAQAMNASIY 317
Cdd:cd03262 95 ENITLAP------IKVKGMSKAEAEERALE-----------LLEKVGladkaDAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170
....*....|
gi 6325199 318 SWDNATRGLD 327
Cdd:cd03262 158 LFDEPTSALD 167
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
851-1015 |
7.72e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 48.94 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 851 IPYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINmgVITGDMLVNAKPL----PASFNRSCGYVAQAD 926
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIS--PTSGTLLFEGEDIstlkPEIYRQQVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 927 NHMAElSVRESLRFAAELRQQSSVPleekyeyvEKIITLLGMQNYAEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLLf 1006
Cdd:PRK10247 91 TLFGD-TVYDNLIFPWQIRNQQPDP--------AIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL- 160
|
....*....
gi 6325199 1007 LDEPTSGLD 1015
Cdd:PRK10247 161 LDEITSALD 169
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
853-1042 |
8.06e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.41 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 853 YDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINMGviTGDMLV---NAKPLPASFNRSCGYVAQADNHM 929
Cdd:PRK13540 9 FDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPE--KGEILFerqSIKKDLCTYQKQLCFVGHRSGIN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 930 AELSVRESLRFAAELrqqSSVPLEekyeyVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIgVELVAKPSLLLFLDE 1009
Cdd:PRK13540 87 PYLTLRENCLYDIHF---SPGAVG-----ITELCRLFSLEHLIDYPCGLLSSG----QKRQVAL-LRLWMSKAKLWLLDE 153
|
170 180 190
....*....|....*....|....*....|...
gi 6325199 1010 PTSGLDSQSAWSIVQFMRALADSGQSILCTIHQ 1042
Cdd:PRK13540 154 PLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
171-382 |
8.34e-06 |
|
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: 50.29 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 171 VESGEMLFVVGRPGAGCSTFLKCLSGetseLVDV-QGEFSYDGLDQSEM-------MSKYKGYVIYCPELDFhFPKITVK 242
Cdd:COG1123 288 LRRGETLGLVGESGSGKSTLARLLLG----LLRPtSGSILFDGKDLTKLsrrslreLRRRVQMVFQDPYSSL-NPRMTVG 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 243 ETIDFALKCKTprvRIDKMTRKQYVDNIRDMwctvFGLRHTYATKVGNDFvrgvSGGERKRVSLVEAQAMNASIYSWDNA 322
Cdd:COG1123 363 DIIAEPLRLHG---LLSRAERRERVAELLER----VGLPPDLADRYPHEL----SGGQRQRVAIARALALEPKLLILDEP 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6325199 323 TRGLDASTA---LEFAQAIRTATNMvnnsAIV------AIyqagenIYELFDKTTVLYNGRQIYFGPAD 382
Cdd:COG1123 432 TSALDVSVQaqiLNLLRDLQRELGL----TYLfishdlAV------VRYIADRVAVMYDGRIVEDGPTE 490
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
861-1041 |
1.06e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.11 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 861 LSDVFGYVKPGKMTALMGESGAGKTTLLNVLaqrinMGVI---TGDMLVNAKPLPASFNRS-CGYVAQADnhmaelSVRE 936
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKAL-----MGFVrlaSGKISILGQPTRQALQKNlVAYVPQSE------EVDW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 937 SLRFAAE-------------LRQqssvPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGvELVAKPSL 1003
Cdd:PRK15056 92 SFPVLVEdvvmmgryghmgwLRR----AKKRDRQIVTAALARVDMVEFRHRQIGELSGG----QKKRVFLA-RAIAQQGQ 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 6325199 1004 LLFLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIH 1041
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
858-1060 |
1.42e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 47.95 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLA--QRINMGVI--TGDMLVNAKPLPASF-NRSCGYVAQADNHMAEL 932
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICgiERPSAGKIwfSGHDITRLKNREVPFlRRQIGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 933 SVRESLRF--------AAELRQQSSVPLeekyeyvEKIITLLGMQNYAEALVGKtgrglnveQRKKLSIGVELVAKPSLL 1004
Cdd:PRK10908 95 TVYDNVAIpliiagasGDDIRRRVSAAL-------DKVGLLDKAKNFPIQLSGG--------EQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6325199 1005 LfLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQpSATLFEQFDRLLLLKKG 1060
Cdd:PRK10908 160 L-ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHD-IGLISRRSYRMLTLSDG 213
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
859-1060 |
1.57e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 859 KLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINMGviTGDMLVNAKplPASFN--RSC-----GYVAQADNHMAE 931
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRD--AGSILYLGK--EVTFNgpKSSqeagiGIIHQELNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 932 LSVRESLRFAAELRQQ-SSVPLEEKYEYVEKIITLLGMQNYAEALVGktgrglnveqrkKLSIG----VElVAK----PS 1002
Cdd:PRK10762 94 LTIAENIFLGREFVNRfGRIDWKKMYAEADKLLARLNLRFSSDKLVG------------ELSIGeqqmVE-IAKvlsfES 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6325199 1003 LLLFLDEPTSGL-DSQSAwSIVQFMRALADSGQSILCTIHQpSATLFEQFDRLLLLKKG 1060
Cdd:PRK10762 161 KVIIMDEPTDALtDTETE-SLFRVIRELKSQGRGIVYISHR-LKEIFEICDDVTVFRDG 217
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
861-1060 |
1.84e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 47.95 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 861 LSDVFGYVKPGKMTALMGESGAGKTTLLNVL--AQRINMGVITGD-MLVNAKPLPASFNRSCGYVAQADNHMAELSVRES 937
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLcgDPRATSGRIVFDgKDITDWQTAKIMREAVAIVPEGRRVFSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 938 LR---FAAElRQQSSVPLEEKYEYVEKIitllgmqnyAEALVGKTGRGLNVEQrKKLSIGVELVAKPSLLLfLDEPTSGL 1014
Cdd:PRK11614 101 LAmggFFAE-RDQFQERIKWVYELFPRL---------HERRIQRAGTMSGGEQ-QMLAIGRALMSQPRLLL-LDEPSLGL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6325199 1015 DSQSAWSIVQFMRALADSGQSILcTIHQPSATLFEQFDRLLLLKKG 1060
Cdd:PRK11614 169 APIIIQQIFDTIEQLREQGMTIF-LVEQNANQALKLADRGYVLENG 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
868-1019 |
1.91e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 48.16 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLA--QRINMGVIT-GDMLVNAKPlpaSFNRS--CGYVAQadNHMA----ELSVRESL 938
Cdd:COG1101 29 IEEGDFVTVIGSNGAGKSTLLNAIAgsLPPDSGSILiDGKDVTKLP---EYKRAkyIGRVFQ--DPMMgtapSMTIEENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 939 RFAAeLRQQS-----SVPLEEKYEYVEKIITL-LGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLDEPTS 1012
Cdd:COG1101 104 ALAY-RRGKRrglrrGLTKKRRELFRELLATLgLGLENRLDTKVGLLSGG----QRQALSLLMATLTKPKLLL-LDEHTA 177
|
....*..
gi 6325199 1013 GLDSQSA 1019
Cdd:COG1101 178 ALDPKTA 184
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
870-1042 |
1.99e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.89 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 870 PGKMTALMGESGAGKTTLLNVLAqrinmGVIT---GDMLVNAKPL----PASFNRSCGY-VAQADNHMAELSVRESLRFA 941
Cdd:PRK15439 36 AGEVHALLGGNGAGKSTLMKIIA-----GIVPpdsGTLEIGGNPCarltPAKAHQLGIYlVPQEPLLFPNLSVKENILFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 942 AELRQQSsvpleekYEYVEKIITLLGMQNYAEALVGKtgrgLNVEQRKKLSIGVELVaKPSLLLFLDEPTSGLDSQSAWS 1021
Cdd:PRK15439 111 LPKRQAS-------MQKMKQLLAALGCQLDLDSSAGS----LEVADRQIVEILRGLM-RDSRILILDEPTASLTPAETER 178
|
170 180
....*....|....*....|.
gi 6325199 1022 IVQFMRALADSGQSILCTIHQ 1042
Cdd:PRK15439 179 LFSRIRELLAQGVGIVFISHK 199
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
868-1037 |
2.04e-05 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 46.66 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAqrinmGVI---TGDMLVNAKPLPASFNRSC-----GYVAqADNH----MAELSVR 935
Cdd:cd03215 23 VRAGEIVGIAGLVGNGQTELAEALF-----GLRppaSGEITLDGKPVTRRSPRDAiragiAYVP-EDRKreglVLDLSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 936 ESLRFAAEL---RQQssvpleekyeyvekiitllgmqnyaealvgktgrglnveqrkKLSIGVELVAKPSLLLfLDEPTS 1012
Cdd:cd03215 97 ENIALSSLLsggNQQ------------------------------------------KVVLARWLARDPRVLI-LDEPTR 133
|
170 180
....*....|....*....|....*
gi 6325199 1013 GLDSQSAWSIVQFMRALADSGQSIL 1037
Cdd:cd03215 134 GVDVGAKAEIYRLIRELADAGKAVL 158
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
868-1014 |
2.56e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.77 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAQRINMGVITGDMLVNAKPLPASFNRSCGYVAQADNH-----MAELSVRESLRFAA 942
Cdd:PRK13549 28 VRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEELQASNIRDTERAGIAIIHqelalVKELSVLENIFLGN 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6325199 943 ELRQQSSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGLN--VEQRKKLSigvelvaKPSLLLFLDEPTSGL 1014
Cdd:PRK13549 108 EITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQqlVEIAKALN-------KQARLLILDEPTASL 174
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
875-1042 |
2.60e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 47.88 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 875 ALMGESGAGKTTLLnvlaQRINmGVIT---GDMLVNAKPLPAS----FNRSCGYVAQ-ADNHMAELSVRESLRFAAelrq 946
Cdd:PRK13652 34 AVIGPNGAGKSTLF----RHFN-GILKptsGSVLIRGEPITKEnireVRKFVGLVFQnPDDQIFSPTVEQDIAFGP---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 947 qSSVPLEEKY--EYVEKIITLLGMQNYAEalvgKTGRGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQ 1024
Cdd:PRK13652 105 -INLGLDEETvaHRVSSALHMLGLEELRD----RVPHHLSGGEKKRVAIAGVIAMEPQVLV-LDEPTAGLDPQGVKELID 178
|
170
....*....|....*....
gi 6325199 1025 FMRALADS-GQSILCTIHQ 1042
Cdd:PRK13652 179 FLNDLPETyGMTVIFSTHQ 197
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
868-1078 |
3.32e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.70 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLnvlaQRINMGVI--TGDMLVNAKPLPAS---------FNRSCGYVAQ-ADNHMAELSVR 935
Cdd:PRK13645 34 FKKNKVTCVIGTTGSGKSTMI----QLTNGLIIseTGQTIVGDYAIPANlkkikevkrLRKEIGLVFQfPEYQLFQETIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 936 ESLRFAaelrqqssvPL---EEKYEYVEKIITLLGMQNYAEALVGKTGRGLNVEQRKKLSIGvELVAKPSLLLFLDEPTS 1012
Cdd:PRK13645 110 KDIAFG---------PVnlgENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALA-GIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1013 GLDSQSAWSIVQ-FMRALADSGQSILCTIHQPSATLfEQFDRLLLLKKgGKMVYFG---DIGPNSETLLK 1078
Cdd:PRK13645 180 GLDPKGEEDFINlFERLNKEYKKRIIMVTHNMDQVL-RIADEVIVMHE-GKVISIGspfEIFSNQELLTK 247
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
871-1094 |
3.56e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 47.29 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 871 GKMTALMGESGAGKTTLLNVLAQRinMGVITGDMLVNAKPL----PASFNRSCGYVAQADNHMAELSVRESLRFAAELRQ 946
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRL--MTPAHGHVWLDGEHIqhyaSKEVARRIGLLAQNATTPGDITVQELVARGRYPHQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 947 qssvPL-----EEKYEYVEKIITLLGMQNYAEALVGKTGRGlnveQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWS 1021
Cdd:PRK10253 111 ----PLftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGG----QRQRAWIAMVLAQETAIML-LDEPTTWLDISHQID 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6325199 1022 IVQFMRAL-ADSGQSILCTIHQPSATLfeQFDRLLLLKKGGKMVYFGdiGPNSETLLKYFERQSGMKCGVSENP 1094
Cdd:PRK10253 182 LLELLSELnREKGYTLAAVLHDLNQAC--RYASHLIALREGKIVAQG--APKEIVTAELIERIYGLRCMIIDDP 251
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
174-327 |
4.20e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 47.52 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 174 GEMLFVVGRPGAGCSTFLKCLSG-ETSelvdVQGEFSYDGLDQSE---------MMskYKGYVIycpeldfhFPKITVKE 243
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAGfEQP----TAGQIMLDGVDLSHvppyqrpinMM--FQSYAL--------FPHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 244 TIDFALKcktprvrIDKMTRKQYVDNIRDMwctvFGLRHT--YATKVGNDfvrgVSGGERKRVSLVEAQAMNASIYSWDN 321
Cdd:PRK11607 111 NIAFGLK-------QDKLPKAEIASRVNEM----LGLVHMqeFAKRKPHQ----LSGGQRQRVALARSLAKRPKLLLLDE 175
|
....*.
gi 6325199 322 ATRGLD 327
Cdd:PRK11607 176 PMGALD 181
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
842-1042 |
5.02e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 46.17 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 842 FTWnhldytipydGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVL---AQRINMGVITGDMLVNAKPLPASFNRS 918
Cdd:cd03290 8 FSW----------GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAIlgeMQTLEGKVHWSNKNESEPSFEATRSRN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 919 CGYVAQADNH--MAELSVRESLRFAAELRQQSSVPLEEKYEyVEKIITLLGMQNYAEalVGKTGRGLNVEQRKKLSIGVE 996
Cdd:cd03290 78 RYSVAYAAQKpwLLNATVEENITFGSPFNKQRYKAVTDACS-LQPDIDLLPFGDQTE--IGERGINLSGGQRQRICVARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6325199 997 LVAKPSlLLFLDEPTSGLDSQSAWSIVQ--FMRALADSGQSILCTIHQ 1042
Cdd:cd03290 155 LYQNTN-IVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHK 201
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
858-1037 |
5.49e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.47 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 858 RKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLaqrinMGV---ITGDMLVNAKPL-PAS----FNRSCGYVAQA--DN 927
Cdd:PRK09700 276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL-----FGVdkrAGGEIRLNGKDIsPRSpldaVKKGMAYITESrrDN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 928 -HMAELSVRESLRFAAELRQ---QSSVPL---EEKYEYVEKIITLLGM------QNYAEalvgktgrgLNVEQRKKLSIG 994
Cdd:PRK09700 351 gFFPNFSIAQNMAISRSLKDggyKGAMGLfheVDEQRTAENQRELLALkchsvnQNITE---------LSGGNQQKVLIS 421
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6325199 995 VELVAKPSLLLFlDEPTSGLDSQSAWSIVQFMRALADSGQSIL 1037
Cdd:PRK09700 422 KWLCCCPEVIIF-DEPTRGIDVGAKAEIYKVMRQLADDGKVIL 463
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
171-261 |
5.55e-05 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 46.27 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 171 VESGEMLFVVGRPGAGCSTFLKCLSGetseLVDV-QGEFSYDGLD----QSEMMSKyKGyVIYCPELDFHFPKITVKETI 245
Cdd:cd03224 23 VPEGEIVALLGRNGAGKTTLLKTIMG----LLPPrSGSIRFDGRDitglPPHERAR-AG-IGYVPEGRRIFPELTVEENL 96
|
90
....*....|....*....
gi 6325199 246 D---FALKCKTPRVRIDKM 261
Cdd:cd03224 97 LlgaYARRRAKRKARLERV 115
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
602-700 |
6.12e-05 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 45.58 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 602 FVAIVILCLITYW---IPFMKYEAGAFF-QYILYLLtvqqCTSFIFKFVATMSKSGVDAHAVGGLWVLMLCVYAGFVLPI 677
Cdd:COG0842 61 LLQALLVLLVALLffgVPLRGLSLLLLLlVLLLFAL----AFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPI 136
|
90 100
....*....|....*....|...
gi 6325199 678 GEMHHWIRWLHFINPLTYAFESL 700
Cdd:COG0842 137 ESLPGWLQAIAYLNPLTYFVEAL 159
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
868-1015 |
6.84e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 46.95 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAQRI--NMGVITGDMLVNAKPLPASF----NRSCGYVAQADNHMAELSVRESLRFA 941
Cdd:PRK10070 51 IEEGEIFVIMGLSGSGKSTMVRLLNRLIepTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPHMTVLDNTAFG 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6325199 942 AELrqqSSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGLnveqRKKLSIGVELVAKPSLLLfLDEPTSGLD 1015
Cdd:PRK10070 131 MEL---AGINAEERREKALDALRQVGLENYAHSYPDELSGGM----RQRVGLARALAINPDILL-MDEAFSALD 196
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
868-1033 |
6.95e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.13 E-value: 6.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAQRINMGVITGDMLVNAKPLPASFNRSCGYVAQADNH-----MAELSVRESLRFAA 942
Cdd:TIGR02633 24 VRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTERAGIVIIHqeltlVPELSVAENIFLGN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 943 ELRQQSS-VPLEEKYEYVEKIITLLGMQNYAEAL-VGKTGRGLN--VEQRKKLSigvelvaKPSLLLFLDEPTSGLDSQS 1018
Cdd:TIGR02633 104 EITLPGGrMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQqlVEIAKALN-------KQARLLILDEPSSSLTEKE 176
|
170
....*....|....*
gi 6325199 1019 AWSIVQFMRALADSG 1033
Cdd:TIGR02633 177 TEILLDIIRDLKAHG 191
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
868-1060 |
8.60e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 46.13 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTL---LNVL-----AQRINMGVITGDMlvnaKPLPAsFNRSCGYVAQ-ADNHMAELSVRESL 938
Cdd:PRK13644 25 IKKGEYIGIIGKNGSGKSTLalhLNGLlrpqkGKVLVSGIDTGDF----SKLQG-IRKLVGIVFQnPETQFVGRTVEEDL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 939 RFAAElrqQSSVPLEEKYEYVEKIITLLGMQNYAEalvgKTGRGLNVEQRKKLSIGVELVAKPSLLLFlDEPTSGLDSQS 1018
Cdd:PRK13644 100 AFGPE---NLCLPPIEIRKRVDRALAEIGLEKYRH----RSPKTLSGGQGQCVALAGILTMEPECLIF-DEVTSMLDPDS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6325199 1019 AWSIVQFMRALADSGQSILCTIHQPSAtlFEQFDRLLLLKKG 1060
Cdd:PRK13644 172 GIAVLERIKKLHEKGKTIVYITHNLEE--LHDADRIIVMDRG 211
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
1041-1067 |
9.51e-05 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 46.82 E-value: 9.51e-05
10 20
....*....|....*....|....*..
gi 6325199 1041 HQPSATLFEQFDRLLLLKKGGKMVYFG 1067
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLTVYHG 27
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
531-701 |
1.02e-04 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 46.23 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 531 KIDDKSQSTTAGAYSRGGMLFYVLLFASVTSLA-EIGNSFSSRpviVKHKSYSMyHLSAES--LQEIITEFPTKFVAIVI 607
Cdd:pfam12698 148 ESTPLFNPQSGYAYYLVGLILMIIILIGAAIIAvSIVEEKESR---IKERLLVS-GVSPLQywLGKILGDFLVGLLQLLI 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 608 LCLITY--WIPFMKYEAGAFFqYILYLLTvqqCTSFIFkFVATMSKSGVDAHAVGGLWVLMLCVYAGFVLPIGEMHHWIR 685
Cdd:pfam12698 224 ILLLLFgiGIPFGNLGLLLLL-FLLYGLA---YIALGY-LLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQ 298
|
170
....*....|....*.
gi 6325199 686 WLHFINPLTYAFESLV 701
Cdd:pfam12698 299 WIFSIIPFFSPIDGLL 314
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
147-379 |
1.04e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 46.00 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 147 HLISKFTKKSDVPLRnIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSG-ETSELVDVQGE-------FSYDGLDQSEM 218
Cdd:PRK13631 26 NLYCVFDEKQENELV-ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGlIKSKYGTIQVGdiyigdkKNNHELITNPY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 219 MSKYK---------GYVIYCPEldFHFPKITVKETIDFA-LKCKTPRVRIDKMTrKQYVDNIrdmwctvfGLRHTYATKv 288
Cdd:PRK13631 105 SKKIKnfkelrrrvSMVFQFPE--YQLFKDTIEKDIMFGpVALGVKKSEAKKLA-KFYLNKM--------GLDDSYLER- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 289 gNDFvrGVSGGERKRVSLVEAQAMNASIYSWDNATRGLDASTALEFAQAIRTATNmvNNSAIVAIYQAGENIYELFDKTT 368
Cdd:PRK13631 173 -SPF--GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKA--NNKTVFVITHTMEHVLEVADEVI 247
|
250
....*....|.
gi 6325199 369 VLYNGRQIYFG 379
Cdd:PRK13631 248 VMDKGKILKTG 258
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
811-1015 |
1.48e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 46.21 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 811 ADARTA----SREEMMEALNG-------PNVDLEKVIAE---KDVFTWNHLDYTipYDGatRKLLSDVFGYVKPGKMTAL 876
Cdd:COG0488 271 AKARKAkqaqSRIKALEKLEReepprrdKTVEIRFPPPErlgKKVLELEGLSKS--YGD--KTLLDDLSLRIDRGDRIGL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 877 MGESGAGKTTLLNVLAQRInmgvitgdmlvnaKPLPASFNR----SCGYVAQadnHMAEL----SVRESLR-FAAELRQQ 947
Cdd:COG0488 347 IGPNGAGKSTLLKLLAGEL-------------EPDSGTVKLgetvKIGYFDQ---HQEELdpdkTVLDELRdGAPGGTEQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325199 948 SsvpleekyeyvekIITLLG--------MQNYAEALVGktGrglnveQRKKLSIGVELVAKPSLLLfLDEPTSGLD 1015
Cdd:COG0488 411 E-------------VRGYLGrflfsgddAFKPVGVLSG--G------EKARLALAKLLLSPPNVLL-LDEPTNHLD 464
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
958-1059 |
1.64e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.89 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 958 YVEKIITLLGMQNYAEALVGKTGRGLNVEQ--------RKKLSIG-VELVA----------KPSLLLFLDEPTSGLDSQS 1018
Cdd:cd03227 37 ILDAIGLALGGAQSATRRRSGVKAGCIVAAvsaeliftRLQLSGGeKELSAlalilalaslKPRPLYILDEIDRGLDPRD 116
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 6325199 1019 AWSIVQFMRALADSGQSILCTIHQPsaTLFEQFDRLLLLKK 1059
Cdd:cd03227 117 GQALAEAILEHLVKGAQVIVITHLP--ELAELADKLIHIKK 155
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
171-328 |
1.94e-04 |
|
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: 44.55 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 171 VESGEMLFVVGRPGAGCSTFLKCLSGetSELVDvQGEFSYDGLDQSEMMSK-------YKGYVIYcpeldfhfPKITVKE 243
Cdd:cd03301 23 IADGEFVVLLGPSGCGKTTTLRMIAG--LEEPT-SGRIYIGGRDVTDLPPKdrdiamvFQNYALY--------PHMTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 244 TIDFALKC-KTPRVRIDKMTRKQyvdnirdmwCTVFGLRHtyatkVGNDFVRGVSGGERKRVSLVEAQAMNASIYSWDNA 322
Cdd:cd03301 92 NIAFGLKLrKVPKDEIDERVREV---------AELLQIEH-----LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
....*.
gi 6325199 323 TRGLDA 328
Cdd:cd03301 158 LSNLDA 163
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
871-1015 |
2.09e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.22 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 871 GKMTALMGESGAGKTTLLNVLA--QRINMGVIT-GDMLVNAKPlPAsfNRSCGYVAQadN-----HMaelSVRESLRFAA 942
Cdd:PRK11650 30 GEFIVLVGPSGCGKSTLLRMVAglERITSGEIWiGGRVVNELE-PA--DRDIAMVFQ--NyalypHM---SVRENMAYGL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6325199 943 ELRQQSSVPLEEKYEYVEKIITLlgmqnyaEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLLFlDEPTSGLD 1015
Cdd:PRK11650 102 KIRGMPKAEIEERVAEAARILEL-------EPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF-DEPLSNLD 166
|
|
| PDR_CDR |
pfam06422 |
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters ... |
1434-1462 |
2.18e-04 |
|
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters comprising extracellular loop 3, transmembrane segment 6 and linker region.
Pssm-ID: 461906 [Multi-domain] Cd Length: 92 Bit Score: 41.68 E-value: 2.18e-04
10 20
....*....|....*....|....*....
gi 6325199 1434 YNVKWDHRWRNFGFMWAYICFNIAAMLIC 1462
Cdd:pfam06422 39 YGYSYSHLWRNFGILIAFWIFFLALYLIA 67
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
843-1041 |
2.30e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 44.77 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 843 TWNHLDYT----IPYDgatRKLLSDVFGYVKPGKMTALMGESGAGKTTL---LNVLAQRINMGVITGDMLVNAKPLPA-- 913
Cdd:PRK13646 4 RFDNVSYTyqkgTPYE---HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLiqnINALLKPTTGTVTVDDITITHKTKDKyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 914 -SFNRSCGYVAQ-ADNHMAELSVRESLRFAAelrQQSSVPLEEKYEYVEKIITLLGmqnYAEALVGKTGRGLNVEQRKKL 991
Cdd:PRK13646 81 rPVRKRIGMVFQfPESQLFEDTVEREIIFGP---KNFKMNLDEVKNYAHRLLMDLG---FSRDVMSQSPFQMSGGQMRKI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6325199 992 SIGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQFMRALA-DSGQSILCTIH 1041
Cdd:PRK13646 155 AIVSILAMNPDIIV-LDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSH 204
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
859-1060 |
2.36e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 859 KLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLaqrinMGVI---TGDML-----VNAKPLPASFNRSCGYVAQADNHMA 930
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCL-----FGIYqkdSGSILfqgkeIDFKSSKEALENGISMVHQELNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 931 ELSVRESLRFAAELRQQSSVPLEEKYEYVEKIITLLGMQNYAEALVGKtgrgLNVEQRKKLSIGvELVAKPSLLLFLDEP 1010
Cdd:PRK10982 87 QRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVAT----LSVSQMQMIEIA-KAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6325199 1011 TSGLDSQSAWSIVQFMRALADSGQSILCTIHQpSATLFEQFDRLLLLKKG 1060
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKLKERGCGIVYISHK-MEEIFQLCDEITILRDG 210
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
144-340 |
3.05e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 44.26 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 144 IPAHLISKFTKKSDVplRNIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSgETSEL---VDVQGEFSYDGLDQSE--- 217
Cdd:PRK14258 5 IPAIKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELeseVRVEGRVEFFNQNIYErrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 218 ---MMSKYKGYVIYCPELdfhFPkITVKETIDFALKCK--TPRVRIDKMTRKQYVDniRDMWCTVFGLRHTYATKvgndf 292
Cdd:PRK14258 82 nlnRLRRQVSMVHPKPNL---FP-MSVYDNVAYGVKIVgwRPKLEIDDIVESALKD--ADLWDEIKHKIHKSALD----- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6325199 293 vrgVSGGERKRVSLVEAQAMNASIYSWDNATRGLDASTALEFAQAIRT 340
Cdd:PRK14258 151 ---LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQS 195
|
|
| HypB |
COG0378 |
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ... |
876-905 |
3.08e-04 |
|
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440147 [Multi-domain] Cd Length: 200 Bit Score: 43.51 E-value: 3.08e-04
10 20 30
....*....|....*....|....*....|....
gi 6325199 876 LMGESGAGKTTLL----NVLAQRINMGVITGDML 905
Cdd:COG0378 18 LMGSPGSGKTTLLektiRALKDRLRIAVIEGDIY 51
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
872-1029 |
4.20e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.00 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 872 KMTALMGESGAGKTTLL---NVLAQRINMGVITGDMLVNAKPL------PASFNRSCGYVAQADNHMAElSVRESLRFAA 942
Cdd:PRK14243 37 QITAFIGPSGCGKSTILrcfNRLNDLIPGFRVEGKVTFHGKNLyapdvdPVEVRRRIGMVFQKPNPFPK-SIYDNIAYGA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 943 ELRQQSSvpleEKYEYVEKIITLLGMQNYAEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWSI 1022
Cdd:PRK14243 116 RINGYKG----DMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVIL-MDEPCSALDPISTLRI 190
|
....*..
gi 6325199 1023 VQFMRAL 1029
Cdd:PRK14243 191 EELMHEL 197
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
171-339 |
4.29e-04 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 43.59 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 171 VESGEMLFVVGRPGAGCSTFLKCLSG-ETSELVDVQ-GEFSYDGldqSEMMSKYKGYViycPELDFH----------FPK 238
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLRCINLlEQPEAGTIRvGDITIDT---ARSLSQQKGLI---RQLRQHvgfvfqnfnlFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 239 ITVKETIdfalkCKTPrVRIDKMTRKQYVDNIRDMWCTVfGLrhtyaTKVGNDFVRGVSGGERKRVSLVEAQAMNASIYS 318
Cdd:PRK11264 100 RTVLENI-----IEGP-VIVKGEPKEEATARARELLAKV-GL-----AGKETSYPRRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180
....*....|....*....|.
gi 6325199 319 WDNATRGLDASTALEFAQAIR 339
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIR 188
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
171-379 |
4.99e-04 |
|
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: 43.25 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 171 VESGEMLFVVGRPGAGCSTFLKCLSG-ETSElvdvQGEFSYDGLDQSEMMSKYKGYVIYCPELDFhFPKITVKETIDFAL 249
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGfETPQ----SGRVLINGVDVTAAPPADRPVSMLFQENNL-FAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 250 kckTPRVRIDKMTRKQYVDNIRDMwctvfGLRHTYATKVGNdfvrgVSGGERKRVSLVEAQAMNASIYSWDNATRGLDAS 329
Cdd:cd03298 96 ---SPGLKLTAEDRQAIEVALARV-----GLAGLEKRLPGE-----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6325199 330 TALEFAQAIRTATNMVNNSAIVAIYQAgENIYELFDKTTVLYNGRQIYFG 379
Cdd:cd03298 163 LRAEMLDLVLDLHAETKMTVLMVTHQP-EDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
872-1068 |
5.63e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 43.69 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 872 KMTALMGESGAGKTTLLNVLAQRI--NMGVI-TGDMLVNAKPlpaSFNRSCGYVAQAD-NHMAELSVRESLRFAAELRQQ 947
Cdd:PRK13631 53 KIYFIIGNSGSGKSTLVTHFNGLIksKYGTIqVGDIYIGDKK---NNHELITNPYSKKiKNFKELRRRVSMVFQFPEYQL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 948 SSVPLEE------------KYEYVEKIITLLGMQNYAEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLLFlDEPTSGLD 1015
Cdd:PRK13631 130 FKDTIEKdimfgpvalgvkKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIF-DEPTAGLD 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6325199 1016 SQSAWSIVQFMRALADSGQSILCTIHQPSATLfEQFDRLLLLKKgGKMVYFGD 1068
Cdd:PRK13631 209 PKGEHEMMQLILDAKANNKTVFVITHTMEHVL-EVADEVIVMDK-GKILKTGT 259
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
171-331 |
7.52e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.20 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 171 VESGEMLFVVGRPGAGCSTFLKCLSGETSELVDVQGEFsydgldqsemmskyKGYVIYCPELDFHFpKITVKETIDFALK 250
Cdd:PLN03232 640 IPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVI--------------RGSVAYVPQVSWIF-NATVRENILFGSD 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 251 CKTPRV--RIDKMTRKQYVDNI--RDMwctvfglrhtyaTKVGNdfvRGV--SGGERKRVSLVEAQAMNASIYSWDNATR 324
Cdd:PLN03232 705 FESERYwrAIDVTALQHDLDLLpgRDL------------TEIGE---RGVniSGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
....*..
gi 6325199 325 GLDASTA 331
Cdd:PLN03232 770 ALDAHVA 776
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
870-1060 |
7.84e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.59 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 870 PGKMTALMGESGAGKTTLLNVLAQRIN---MGVITGDMlvnakplpasfnrscgyvaqaDNHMAELSVRESlrfaaelrq 946
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGppgGGVIYIDG---------------------EDILEEVLDQLL--------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 947 qssvpleekyeyvekiitllgmqnyaeaLVGKTGRGLNVEQRKKLSIGVELVAKPSL-LLFLDEPTSGLDSQSAWSIVQ- 1024
Cdd:smart00382 51 ----------------------------LIIVGGKKASGSGELRLRLALALARKLKPdVLILDEITSLLDAEQEALLLLl 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6325199 1025 -----FMRALADSGQSILCTIHQP----SATLFEQFDRLLLLKKG 1060
Cdd:smart00382 103 eelrlLLLLKSEKNLTVILTTNDEkdlgPALLRRRFDRRIVLLLI 147
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
871-897 |
9.99e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 41.76 E-value: 9.99e-04
10 20
....*....|....*....|....*..
gi 6325199 871 GKMTALMGESGAGKTTLLNVLAQRINM 897
Cdd:pfam03193 106 GKTTVLAGQSGVGKSTLLNALLPELDL 132
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
163-333 |
1.19e-03 |
|
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: 42.07 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 163 IIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGetseLVDVQ-GEFSYDGLDQSEmMSKYKGYVIYCPELdfhFPKITV 241
Cdd:cd03293 19 ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAG----LERPTsGEVLVDGEPVTG-PGPDRGYVFQQDAL---LPWLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 242 KETIDFALKCKtprvRIDKMTRKQYVDNIRDMwctvFGLRHTyatkvGNDFVRGVSGGERKRVSLVEAQAMNASIYSWDN 321
Cdd:cd03293 91 LDNVALGLELQ----GVPKAEARERAEELLEL----VGLSGF-----ENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170
....*....|..
gi 6325199 322 ATRGLDASTALE 333
Cdd:cd03293 158 PFSALDALTREQ 169
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
171-327 |
1.32e-03 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 42.00 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 171 VESGEMLFVVGRPGAGCSTFLKCLSgeTSELVDvQGEFSYDGLD------QSEMMSKYKGYVIYcpelDFH-FPKITVKE 243
Cdd:PRK09493 24 IDQGEVVVIIGPSGSGKSTLLRCIN--KLEEIT-SGDLIVDGLKvndpkvDERLIRQEAGMVFQ----QFYlFPHLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 244 TIDFAlkcktPRvRIDKMTRKQYVDNIRDMWCTVfGLR---HTYATKvgndfvrgVSGGERKRVSLVEAQAMNASIYSWD 320
Cdd:PRK09493 97 NVMFG-----PL-RVRGASKEEAEKQARELLAKV-GLAeraHHYPSE--------LSGGQQQRVAIARALAVKPKLMLFD 161
|
....*..
gi 6325199 321 NATRGLD 327
Cdd:PRK09493 162 EPTSALD 168
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
795-1173 |
1.35e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 795 LLLYKRGHMPELGTE--NADARTASREEMM---EALNGPNVDLE----KVIAEKDVFTWNhldytipyDGATRKLLSDVF 865
Cdd:PLN03232 566 VLRSPLNMLPNLLSQvvNANVSLQRIEELLlseERILAQNPPLQpgapAISIKNGYFSWD--------SKTSKPTLSDIN 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 866 GYVKPGKMTALMGESGAGKTTLLNVLAQRinmgvitgdmLVNAKPLPASFNRSCGYVAQAdNHMAELSVRESLRFAAELR 945
Cdd:PLN03232 638 LEIPVGSLVAIVGGTGEGKTSLISAMLGE----------LSHAETSSVVIRGSVAYVPQV-SWIFNATVRENILFGSDFE 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 946 qqssvplEEKYeyvEKIITLLGMQNYAEALVGKT-----GRGLNVE--QRKKLSIGVELVAKPSLLLFlDEPTSGLDSQS 1018
Cdd:PLN03232 707 -------SERY---WRAIDVTALQHDLDLLPGRDlteigERGVNISggQKQRVSMARAVYSNSDIYIF-DDPLSALDAHV 775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1019 AWSIVQFMRALADSGQSILCTIHQpsATLFEQFDRLLLLKKGgkMV----YFGDIGPNSETLLKYFERQSGMKCGVSENP 1094
Cdd:PLN03232 776 AHQVFDSCMKDELKGKTRVLVTNQ--LHFLPLMDRIILVSEG--MIkeegTFAELSKSGSLFKKLMENAGKMDATQEVNT 851
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 1095 AEYILNCIGAGATAsvnsDWHDLWLASPECAAARAEV----EELHRTLPG--------RAVNDDPELATRFAASYMTQIK 1162
Cdd:PLN03232 852 NDENILKLGPTVTI----DVSERNLGSTKQGKRGRSVlvkqEERETGIISwnvlmrynKAVGGLWVVMILLVCYLTTEVL 927
|
410
....*....|.
gi 6325199 1163 CVLRRTALQFW 1173
Cdd:PLN03232 928 RVSSSTWLSIW 938
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
859-891 |
1.37e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 1.37e-03
10 20 30
....*....|....*....|....*....|...
gi 6325199 859 KLLSDVFGYVKPGKMTALMGESGAGKTTLLNVL 891
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVL 47
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
830-897 |
1.39e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 41.61 E-value: 1.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 830 VDL-EKVIAEKDVFTWNHLDY-TIPYDGATRKLLSDVFGYVKpGKMTALMGESGAGKTTLLNVLAQRINM 897
Cdd:cd01854 43 ADLvDDEELEELLEIYEKLGYpVLAVSAKTGEGLDELRELLK-GKTSVLVGQSGVGKSTLLNALLPELVL 111
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
868-1076 |
1.65e-03 |
|
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: 42.87 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 868 VKPGKMTALMGESGAGKTTLLNVLAQRI-----NMGVITGDMLVN-AKPLPASFNRSCGYVAQADNHMAELSVRESLrfa 941
Cdd:TIGR03269 307 VKEGEIFGIVGTSGAGKTTLSKIIAGVLeptsgEVNVRVGDEWVDmTKPGPDGRGRAKRYIGILHQEYDLYPHRTVL--- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 942 AELRQQSSVPLEEKYEYVEKIITLLGM---QNYAEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGLDS-- 1016
Cdd:TIGR03269 384 DNLTEAIGLELPDELARMKAVITLKMVgfdEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVI-LDEPTGTMDPit 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325199 1017 --QSAWSIvqfMRALADSGQSILCTIHQPSATLfEQFDRLLLLkKGGKMVyfgDIGPNSETL 1076
Cdd:TIGR03269 463 kvDVTHSI---LKAREEMEQTFIIVSHDMDFVL-DVCDRAALM-RDGKIV---KIGDPEEIV 516
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
290-382 |
2.44e-03 |
|
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: 40.97 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 290 NDFVRGV----SGGERKRVSLVEAQAMNASIYSWDNATRGLDAStalefaqAIRTATNMVN-----NSAIVAI--YQage 358
Cdd:cd03217 95 ADFLRYVnegfSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID-------ALRLVAEVINklreeGKSVLIIthYQ--- 164
|
90 100
....*....|....*....|....*.
gi 6325199 359 NIYELF--DKTTVLYNGRQIYFGPAD 382
Cdd:cd03217 165 RLLDYIkpDRVHVLYDGRIVKSGDKE 190
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
875-1067 |
2.90e-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: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 875 ALMGESGAGKTTLLNVLAqrinmGVI---TGDMLVNAKPLP-----ASFNrscgyvaqadnhmAELSVRESLRFAAELRQ 946
Cdd:cd03220 52 GLIGRNGAGKSTLLRLLA-----GIYppdSGTVTVRGRVSSllglgGGFN-------------PELTGRENIYLNGRLLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 947 QSsvpLEEKYEYVEKIITLLGMQNYAEALVgktgRGLNVEQRKKLSIGVELVAKPSLLLfLDEPTSGLDSQSAWSIVQFM 1026
Cdd:cd03220 114 LS---RKEIDEKIDEIIEFSELGDFIDLPV----KTYSSGMKARLAFAIATALEPDILL-IDEVLAVGDAAFQEKCQRRL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6325199 1027 RALADSGQSILCTIHQPSatLFEQF-DRLLLLKKgGKMVYFG 1067
Cdd:cd03220 186 RELLKQGKTVILVSHDPS--SIKRLcDRALVLEK-GKIRFDG 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
853-1015 |
3.08e-03 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 41.86 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 853 YDGATrkLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLA--QRINMGVITGDMlVNAKPLPASfNRSCGYVAQADNHMA 930
Cdd:PRK09452 24 FDGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAgfETPDSGRIMLDG-QDITHVPAE-NRHVNTVFQSYALFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 931 ELSVRESLRFAaeLRQQsSVPLEEKYEYVEKIITLLGMQNYAEalvgKTGRGLNVEQRKKLSIGVELVAKPSLLLfLDEP 1010
Cdd:PRK09452 100 HMTVFENVAFG--LRMQ-KTPAAEITPRVMEALRMVQLEEFAQ----RKPHQLSGGQQQRVAIARAVVNKPKVLL-LDES 171
|
....*
gi 6325199 1011 TSGLD 1015
Cdd:PRK09452 172 LSALD 176
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
171-310 |
3.45e-03 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 40.91 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 171 VESGEMLFVVGRPGAGCSTFLKCLSGetsELVDVQGEFSYDGLDQSEM----MSKYKGYVIYCPELDFHFpkiTVKETID 246
Cdd:PRK13548 25 LRPGEVVAILGPNGAGKSTLLRALSG---ELSPDSGEVRLNGRPLADWspaeLARRRAVLPQHSSLSFPF---TVEEVVA 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325199 247 FALkckTPRVRidkmtRKQYVDNIRDMWCTVFGLRHtYATKvgndFVRGVSGGERKRVSL--VEAQ 310
Cdd:PRK13548 99 MGR---APHGL-----SRAEDDALVAAALAQVDLAH-LAGR----DYPQLSGGEQQRVQLarVLAQ 151
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
867-891 |
3.56e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.46 E-value: 3.56e-03
10 20
....*....|....*....|....*
gi 6325199 867 YVKPGKMTALMGESGAGKTTLLNVL 891
Cdd:PRK01889 191 WLSGGKTVALLGSSGVGKSTLVNAL 215
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
850-895 |
3.65e-03 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 39.35 E-value: 3.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 6325199 850 TIPYDGatRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRI 895
Cdd:cd03221 7 SKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGEL 50
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
156-211 |
4.50e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.47 E-value: 4.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 6325199 156 SDVPLrniIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGETseLVDvQGEFSYD 211
Cdd:PRK11147 14 SDAPL---LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEV--LLD-DGRIIYE 63
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
861-1015 |
5.15e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 40.46 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 861 LSDVFGYVKPGKMTALMGESGAGKTTllnvLAQRINMGVITGDMLVNAKPLPAS-------FNRSCGYVAQ-ADNHMAEL 932
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKST----IAKHMNALLIPSEGKVYVDGLDTSdeenlwdIRNKAGMVFQnPDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 933 SVRESLRFAAElrqQSSVPLEEKYEYVEKIITLLGMQNY---AEALvgktgrgLNVEQRKKLSIGVELVAKPSLLLFlDE 1009
Cdd:PRK13633 102 IVEEDVAFGPE---NLGIPPEEIRERVDESLKKVGMYEYrrhAPHL-------LSGGQKQRVAIAGILAMRPECIIF-DE 170
|
....*.
gi 6325199 1010 PTSGLD 1015
Cdd:PRK13633 171 PTAMLD 176
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
171-339 |
8.22e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.88 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 171 VESGEMLFVVGRPGAGCSTFLKCLSGETSELVDvqGEFSYdgldqsemmskyKGYVIYCPELDFHFpKITVKETIDFALK 250
Cdd:PLN03130 640 VPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD--ASVVI------------RGTVAYVPQVSWIF-NATVRDNILFGSP 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325199 251 CKTPRvridkmtrkqYVDNIRdmwctVFGLRHTYATKVGNDFV----RGV--SGGERKRVSLVEAQAMNASIYSWDNATR 324
Cdd:PLN03130 705 FDPER----------YERAID-----VTALQHDLDLLPGGDLTeigeRGVniSGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170
....*....|....*.
gi 6325199 325 GLDASTALE-FAQAIR 339
Cdd:PLN03130 770 ALDAHVGRQvFDKCIK 785
|
|
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