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Conserved domains on  [gi|489820617|ref|WP_003724421|]
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MULTISPECIES: protein-glutamate O-methyltransferase CheR [Listeria]

Protein Classification

CheR family methyltransferase( domain architecture ID 11442594)

CheR family methyltransferase is a class I SAM-dependent methyltransferase that catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; such as chemotaxis protein methyltransferase that methylates membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:0032259|GO:1904047
SCOP:  3000118

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
1-261 5.43e-94

Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];


:

Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 277.43  E-value: 5.43e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617   1 MIPDLEKDYLYFTRVVKRDLGLDLALYKETQMKRRILSFIVKKQYITFGEFFKHLKKDAVLLDEFISLITINVSSFFRNR 80
Cdd:COG1352    1 MAELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617  81 NRWDALEKQVLPRLLEDSRGK--LRVWSAACSSGEEPYSLAMMME---RSVGTRHYDILATDLEPAILKRAVIGEYQSRQ 155
Cdd:COG1352   81 EHFEALREEVLPELLARRRAGrpLRIWSAGCSTGEEPYSLAMLLAeagGELAGWRVEILATDISEEALEKARAGIYPERS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617 156 MEELTEQERHTAFVEKGDTYQILPKYRKSIRFRRHDLLTDY-YEKGFDLIVCRNVLIYFTAEGKHQAYQKFAESLRRGGV 234
Cdd:COG1352  161 LRGLPPEYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDDPpPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGY 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 489820617 235 LFIGGSEQILNPADyGLATLNN---FFYIK 261
Cdd:COG1352  241 LFLGHSESLGGLSD-LFEPVDKkgrFIYRK 269
 
Name Accession Description Interval E-value
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
1-261 5.43e-94

Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 277.43  E-value: 5.43e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617   1 MIPDLEKDYLYFTRVVKRDLGLDLALYKETQMKRRILSFIVKKQYITFGEFFKHLKKDAVLLDEFISLITINVSSFFRNR 80
Cdd:COG1352    1 MAELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617  81 NRWDALEKQVLPRLLEDSRGK--LRVWSAACSSGEEPYSLAMMME---RSVGTRHYDILATDLEPAILKRAVIGEYQSRQ 155
Cdd:COG1352   81 EHFEALREEVLPELLARRRAGrpLRIWSAGCSTGEEPYSLAMLLAeagGELAGWRVEILATDISEEALEKARAGIYPERS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617 156 MEELTEQERHTAFVEKGDTYQILPKYRKSIRFRRHDLLTDY-YEKGFDLIVCRNVLIYFTAEGKHQAYQKFAESLRRGGV 234
Cdd:COG1352  161 LRGLPPEYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDDPpPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGY 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 489820617 235 LFIGGSEQILNPADyGLATLNN---FFYIK 261
Cdd:COG1352  241 LFLGHSESLGGLSD-LFEPVDKkgrFIYRK 269
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
6-248 1.08e-72

Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.


Pssm-ID: 214534 [Multi-domain]  Cd Length: 264  Bit Score: 222.93  E-value: 1.08e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617     6 EKDYLYFTRVVKRDLGLDLALYKETQMKRRILSFIVKKQYITFGEFFKHLKKD--AVLLDEFISLITINVSSFFRNRNRW 83
Cdd:smart00138   1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHrgEEELAELLDLMTTNETRFFRESKHF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617    84 DALEKQVLPRLLEDSR--GKLRVWSAACSSGEEPYSLAMMMERSVGTRH---YDILATDLEPAILKRAVIGEYQSRQMEE 158
Cdd:smart00138  81 EALEEKVLPLLIASRRhgRRVRIWSAGCSTGEEPYSLAMLLAETLPKGRepdVKILATDIDLKALEKARAGIYPERELED 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617   159 LTEQERHTAFVEKGDTYQILPKYRKSIRFRRHDLLTDYYEKG-FDLIVCRNVLIYFTAEGKHQAYQKFAESLRRGGVLFI 237
Cdd:smart00138 161 LPKALLARYFKEVEDKYRVKPELKERVRFAKHNLLAESPPLGdFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFL 240
                          250
                   ....*....|.
gi 489820617   238 GGSEQILNPAD 248
Cdd:smart00138 241 GHSESLPGLTD 251
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
72-243 1.95e-55

CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM.


Pssm-ID: 426403  Cd Length: 190  Bit Score: 176.32  E-value: 1.95e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617   72 NVSSFFRNRNRWDALEKQVLPRLLEDSRGK-LRVWSAACSSGEEPYSLAM---MMERSVGTRHYDILATDLEPAILKRAV 147
Cdd:pfam01739   1 NETRFFREPAHFEELKKYVLPLLAKAKNGKrVRIWSAGCSSGEEPYSLAMllkETFPNAARWDFKILATDIDLSVLEKAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617  148 IGEYQSRQMEELTEQERHTAFVE-KGDTYQILPKYRKSIRFRRHDLLTDY-YEKGFDLIVCRNVLIYFTAEGKHQAYQKF 225
Cdd:pfam01739  81 AGVYPERELEGLPEELLRRYFEKtAGGGYTVKPEIKSMVLFEYLNLLDEYpPLGDFDVIFCRNVLIYFDEETQRKILNRF 160
                         170
                  ....*....|....*...
gi 489820617  226 AESLRRGGVLFIGGSEQI 243
Cdd:pfam01739 161 AEKLKPGGYLFLGHSEAL 178
PRK10611 PRK10611
protein-glutamate O-methyltransferase CheR;
48-241 6.85e-29

protein-glutamate O-methyltransferase CheR;


Pssm-ID: 236725 [Multi-domain]  Cd Length: 287  Bit Score: 110.59  E-value: 6.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617  48 FGEFFKHLKKDAVLLD--EFISLITINVSSFFRnrnrwdalEKQVLPRLLEDSR---GKLRVWSAACSSGEEPYSLAMMM 122
Cdd:PRK10611  66 FGQYLALLESNQNSAEwqAFINALTTNLTAFFR--------EAHHFPILAEHARrrsGEYRVWSAAASTGEEPYSIAMTL 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617 123 ERSVGTR--HYDILATDLEPAILKRAVIGEYQSRQMEELTEQERHTAFVEKGDTYQILPKYRKS----IRFRRHDLLTDY 196
Cdd:PRK10611 138 ADTLGTApgRWKVFASDIDTEVLEKARSGIYRQEELKTLSPQQLQRYFMRGTGPHEGLVRVRQElanyVDFQQLNLLAKQ 217
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 489820617 197 Y--EKGFDLIVCRNVLIYFTAEGKHQAYQKFAESLRRGGVLFIGGSE 241
Cdd:PRK10611 218 WavPGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLLFAGHSE 264
 
Name Accession Description Interval E-value
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
1-261 5.43e-94

Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 277.43  E-value: 5.43e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617   1 MIPDLEKDYLYFTRVVKRDLGLDLALYKETQMKRRILSFIVKKQYITFGEFFKHLKKDAVLLDEFISLITINVSSFFRNR 80
Cdd:COG1352    1 MAELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617  81 NRWDALEKQVLPRLLEDSRGK--LRVWSAACSSGEEPYSLAMMME---RSVGTRHYDILATDLEPAILKRAVIGEYQSRQ 155
Cdd:COG1352   81 EHFEALREEVLPELLARRRAGrpLRIWSAGCSTGEEPYSLAMLLAeagGELAGWRVEILATDISEEALEKARAGIYPERS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617 156 MEELTEQERHTAFVEKGDTYQILPKYRKSIRFRRHDLLTDY-YEKGFDLIVCRNVLIYFTAEGKHQAYQKFAESLRRGGV 234
Cdd:COG1352  161 LRGLPPEYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDDPpPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGY 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 489820617 235 LFIGGSEQILNPADyGLATLNN---FFYIK 261
Cdd:COG1352  241 LFLGHSESLGGLSD-LFEPVDKkgrFIYRK 269
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
6-248 1.08e-72

Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.


Pssm-ID: 214534 [Multi-domain]  Cd Length: 264  Bit Score: 222.93  E-value: 1.08e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617     6 EKDYLYFTRVVKRDLGLDLALYKETQMKRRILSFIVKKQYITFGEFFKHLKKD--AVLLDEFISLITINVSSFFRNRNRW 83
Cdd:smart00138   1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHrgEEELAELLDLMTTNETRFFRESKHF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617    84 DALEKQVLPRLLEDSR--GKLRVWSAACSSGEEPYSLAMMMERSVGTRH---YDILATDLEPAILKRAVIGEYQSRQMEE 158
Cdd:smart00138  81 EALEEKVLPLLIASRRhgRRVRIWSAGCSTGEEPYSLAMLLAETLPKGRepdVKILATDIDLKALEKARAGIYPERELED 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617   159 LTEQERHTAFVEKGDTYQILPKYRKSIRFRRHDLLTDYYEKG-FDLIVCRNVLIYFTAEGKHQAYQKFAESLRRGGVLFI 237
Cdd:smart00138 161 LPKALLARYFKEVEDKYRVKPELKERVRFAKHNLLAESPPLGdFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFL 240
                          250
                   ....*....|.
gi 489820617   238 GGSEQILNPAD 248
Cdd:smart00138 241 GHSESLPGLTD 251
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
72-243 1.95e-55

CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM.


Pssm-ID: 426403  Cd Length: 190  Bit Score: 176.32  E-value: 1.95e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617   72 NVSSFFRNRNRWDALEKQVLPRLLEDSRGK-LRVWSAACSSGEEPYSLAM---MMERSVGTRHYDILATDLEPAILKRAV 147
Cdd:pfam01739   1 NETRFFREPAHFEELKKYVLPLLAKAKNGKrVRIWSAGCSSGEEPYSLAMllkETFPNAARWDFKILATDIDLSVLEKAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617  148 IGEYQSRQMEELTEQERHTAFVE-KGDTYQILPKYRKSIRFRRHDLLTDY-YEKGFDLIVCRNVLIYFTAEGKHQAYQKF 225
Cdd:pfam01739  81 AGVYPERELEGLPEELLRRYFEKtAGGGYTVKPEIKSMVLFEYLNLLDEYpPLGDFDVIFCRNVLIYFDEETQRKILNRF 160
                         170
                  ....*....|....*...
gi 489820617  226 AESLRRGGVLFIGGSEQI 243
Cdd:pfam01739 161 AEKLKPGGYLFLGHSEAL 178
PRK10611 PRK10611
protein-glutamate O-methyltransferase CheR;
48-241 6.85e-29

protein-glutamate O-methyltransferase CheR;


Pssm-ID: 236725 [Multi-domain]  Cd Length: 287  Bit Score: 110.59  E-value: 6.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617  48 FGEFFKHLKKDAVLLD--EFISLITINVSSFFRnrnrwdalEKQVLPRLLEDSR---GKLRVWSAACSSGEEPYSLAMMM 122
Cdd:PRK10611  66 FGQYLALLESNQNSAEwqAFINALTTNLTAFFR--------EAHHFPILAEHARrrsGEYRVWSAAASTGEEPYSIAMTL 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617 123 ERSVGTR--HYDILATDLEPAILKRAVIGEYQSRQMEELTEQERHTAFVEKGDTYQILPKYRKS----IRFRRHDLLTDY 196
Cdd:PRK10611 138 ADTLGTApgRWKVFASDIDTEVLEKARSGIYRQEELKTLSPQQLQRYFMRGTGPHEGLVRVRQElanyVDFQQLNLLAKQ 217
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 489820617 197 Y--EKGFDLIVCRNVLIYFTAEGKHQAYQKFAESLRRGGVLFIGGSE 241
Cdd:PRK10611 218 WavPGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLLFAGHSE 264
CheR_N pfam03705
CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling ...
7-58 2.32e-07

CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase.


Pssm-ID: 461017 [Multi-domain]  Cd Length: 53  Bit Score: 46.66  E-value: 2.32e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489820617    7 KDYLYFTRVVKRDLGLDLALYKETQMKRRILSFIVKKQYITFGEFFKHLKKD 58
Cdd:pfam03705   1 AEFERLLELIYRRTGIDLSDYKRSLLERRLSRRMRALGLDSFSEYLDLLRSD 52
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
79-237 8.53e-06

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 44.24  E-value: 8.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617  79 NRNRWDALEKQVLPRLLEDSRgklRVWSAACSSGEepysLAMMMERsvgtRHYDILATDLEPAILKRAvigeyqsrqmee 158
Cdd:COG2227    6 ARDFWDRRLAALLARLLPAGG---RVLDVGCGTGR----LALALAR----RGADVTGVDISPEALEIA------------ 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617 159 lteQERHTAFvekgdtyqilpkyrkSIRFRRHDLLT-DYYEKGFDLIVCRNVLIYFTAEgkHQAYQKFAESLRRGGVLFI 237
Cdd:COG2227   63 ---RERAAEL---------------NVDFVQGDLEDlPLEDGSFDLVICSEVLEHLPDP--AALLRELARLLKPGGLLLL 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
185-233 1.52e-05

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 42.55  E-value: 1.52e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 489820617  185 IRFRRHDLLT-DYYEKGFDLIVCRNVLIYFTAEGKHQAYQKFAESLRRGG 233
Cdd:pfam13649  47 VEFVQGDAEDlPFPDGSFDLVVSSGVLHHLPDPDLEAALREIARVLKPGG 96
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
109-237 2.83e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 42.12  E-value: 2.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617 109 CSSGeepYSLAMMMERSVGtrhYDILATDLEPAILKRAvigeyqsrqmeelteQERHTAfvekgdtyqilpkyrksIRFR 188
Cdd:COG4106   10 CGTG---RLTALLAERFPG---ARVTGVDLSPEMLARA---------------RARLPN-----------------VRFV 51
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489820617 189 RHDLLTDYYEKGFDLIVCRNVLIYFtaEGKHQAYQKFAESLRRGGVLFI 237
Cdd:COG4106   52 VADLRDLDPPEPFDLVVSNAALHWL--PDHAALLARLAAALAPGGVLAV 98
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
185-237 2.61e-03

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 37.60  E-value: 2.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489820617 185 IRFRRHDLLTDYYEKGFDLIVCRNVLIYFTAEGKHQAYQKFAESLRRGGVLFI 237
Cdd:COG2230  103 VEVRLADYRDLPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
183-240 3.75e-03

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 37.59  E-value: 3.75e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617 183 KSIRFRRHDL--LTDYYEKGFDLIVCRNVLIYFTAEGKHQAYQKFAESLRRGGVLFIGGS 240
Cdd:COG0500   75 GNVEFLVADLaeLDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSAS 134
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
76-237 3.99e-03

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 36.90  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617  76 FFRNRNRWDALEKqvLPRLLEDSRGKlRVWSAACSSGEEPYSLAmmmersvgTRHYDILATDLEPAILKRAvigeyqsrq 155
Cdd:COG2226    1 FDRVAARYDGREA--LLAALGLRPGA-RVLDLGCGTGRLALALA--------ERGARVTGVDISPEMLELA--------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820617 156 meelteQERhtafvekgdtyqiLPKYRKSIRFRRHDLL-TDYYEKGFDLIVCRNVLIYFtaEGKHQAYQKFAESLRRGGV 234
Cdd:COG2226   61 ------RER-------------AAEAGLNVEFVVGDAEdLPFPDGSFDLVISSFVLHHL--PDPERALAEIARVLKPGGR 119

                 ...
gi 489820617 235 LFI 237
Cdd:COG2226  120 LVV 122
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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