ID F4GZC8_CELFA Unreviewed; 359 AA.
AC F4GZC8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN OrderedLocusNames=Celf_0709 {ECO:0000313|EMBL:AEE44849.1};
OS Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 /
OS NCIMB 8980 / NCTC 7547).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=590998 {ECO:0000313|EMBL:AEE44849.1, ECO:0000313|Proteomes:UP000008460};
RN [1] {ECO:0000313|EMBL:AEE44849.1, ECO:0000313|Proteomes:UP000008460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 /
RC NCTC 7547 {ECO:0000313|Proteomes:UP000008460};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA Woyke T.;
RT "Complete sequence of Cellulomonas fimi ATCC 484.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-
CC glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:24452, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:82795; EC=2.1.1.80;
CC Evidence={ECO:0000256|ARBA:ARBA00001541};
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DR EMBL; CP002666; AEE44849.1; -; Genomic_DNA.
DR AlphaFoldDB; F4GZC8; -.
DR STRING; 590998.Celf_0709; -.
DR KEGG; cfi:Celf_0709; -.
DR eggNOG; COG1352; Bacteria.
DR HOGENOM; CLU_025854_4_1_11; -.
DR Proteomes; UP000008460; Chromosome.
DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR022641; CheR_N.
DR InterPro; IPR036804; CheR_N_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF25; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00138; MeTrc; 1.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50123; CHER; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:AEE44849.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008460};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEE44849.1}.
FT DOMAIN 1..272
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT REGION 295..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..338
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 359 AA; 38232 MW; BC5E2087E6D50F77 CRC64;
MSLASDVFQY VADLVQRRAG IQLDSGKEYL VESRLLPLAQ AAGHARVDAY VRQVRTSARA
ADEQAVVEAL TTNETSFFRD GSPFQALTEE ILPGLRRPDG SLPRLRIWSA ACSTGQEPYS
IAMTLADALG PETAVEIVAT DINQTVLDRA ATGTYSRLET NRGLPSPMLV RHFEADGMGW
RVKEPLRRQV TFHRHNLLDA PPFVGGFDVV FLRNVLIYFD LPVKQAVLDR VLAAMRPGGY
LVLGAAETTI GLDDSWERIP VGRGAVYRAG SPGTAGAPAV RPFLAAPRTL TPAAGSIGTL
PRPASPPSVP VRAVPAPAAP PAATVRPVAP PTVPPGAAPR GVLPTTRTPV PAPVRGESR
//
