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Database: UniProt
Entry: A0A7C9RJ88_9BRAD
LinkDB: A0A7C9RJ88_9BRAD
Original site: A0A7C9RJ88_9BRAD 
ID   A0A7C9RJ88_9BRAD        Unreviewed;       247 AA.
AC   A0A7C9RJ88;
DT   10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2021, sequence version 1.
DT   02-APR-2025, entry version 14.
DE   RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE            EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
DE   Flags: Fragment;
GN   ORFNames=G4V63_27230 {ECO:0000313|EMBL:NGX98764.1};
OS   Candidatus Afipia apatlaquensis.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Nitrobacteraceae; Afipia.
OX   NCBI_TaxID=2712852 {ECO:0000313|EMBL:NGX98764.1, ECO:0000313|Proteomes:UP000480266};
RN   [1] {ECO:0000313|EMBL:NGX98764.1, ECO:0000313|Proteomes:UP000480266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT-C3 {ECO:0000313|EMBL:NGX98764.1};
RA   Sanchez-Reyes A., Breton-Deval L., Mangelson H., Sanchez-Flores A.;
RT   "Draft genome sequence of Candidatus Afipia apatlaquensis IBT-C3, a
RT   potential strain for decolorization of textile dyes.";
RL   Submitted (FEB-2020) 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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:NGX98764.1}.
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DR   EMBL; JAAMRR010001389; NGX98764.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7C9RJ88; -.
DR   Proteomes; UP000480266; Unassembled WGS sequence.
DR   GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; IPR050903; Bact_Chemotaxis_MeTrfase.
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:SF21; CHEMOTAXIS PROTEIN METHYLTRANSFERASE 1; 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:NGX98764.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000480266};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:NGX98764.1}.
FT   DOMAIN          1..247
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   NON_TER         247
FT                   /evidence="ECO:0000313|EMBL:NGX98764.1"
SQ   SEQUENCE   247 AA;  28157 MW;  F14B3D086547D091 CRC64;
     MTPLDYEYLR KLLKDRSGLL LSSDKQYLIE SRLLPLARKA GISGISELVQ KIKSGSEALT
     VDVVEAMTTN ETFFFRDKVP FENVRDTVLP QLLKARANRR SLRIWCAAAS TGQEPYSLAM
     LLKEALPPDW RAEIVATDLS LEVLEKAKAG IYSQFEVQRG LPIQLLVKHF KQVGDVWQLN
     PDIRAMVRYQ QANLLQDFSH FGIFDIIFCR NVLIYFDQPT KIDVFGRMQK INEPDGFLFL
     GAAETVI
//
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