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Database: UniProt
Entry: A0A095TMY1_9GAMM
LinkDB: A0A095TMY1_9GAMM
Original site: A0A095TMY1_9GAMM 
ID   A0A095TMY1_9GAMM        Unreviewed;       292 AA.
AC   A0A095TMY1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE            EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN   ORFNames=Y5S_02990 {ECO:0000313|EMBL:KGD63783.1};
OS   Alcanivorax nanhaiticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=1177154 {ECO:0000313|EMBL:KGD63783.1, ECO:0000313|Proteomes:UP000029444};
RN   [1] {ECO:0000313|EMBL:KGD63783.1, ECO:0000313|Proteomes:UP000029444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=19-m-6 {ECO:0000313|EMBL:KGD63783.1,
RC   ECO:0000313|Proteomes:UP000029444};
RA   Lai Q., Shao Z.;
RT   "Genome Sequence of alkane-degrading Bacterium Alcanivorax sp. 19-m-6.";
RL   Submitted (SEP-2012) 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:KGD63783.1}.
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DR   EMBL; ARXV01000014; KGD63783.1; -; Genomic_DNA.
DR   RefSeq; WP_035234125.1; NZ_ARXV01000014.1.
DR   AlphaFoldDB; A0A095TMY1; -.
DR   STRING; 1177154.Y5S_02990; -.
DR   PATRIC; fig|1177154.3.peg.3031; -.
DR   eggNOG; COG1352; Bacteria.
DR   OrthoDB; 9816309at2; -.
DR   Proteomes; UP000029444; 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; 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:SF19; 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:KGD63783.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KGD63783.1}.
FT   DOMAIN          10..292
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
SQ   SEQUENCE   292 AA;  33583 MW;  511236B63F36F694 CRC64;
     MGAAVTDRWS IRSTPAMDAE QFQLWQALLE DRTGMTLSDA RKSFLETSLS IRMRELGFED
     YEAYYEHLMV GTTESRAMEW SILVDRLTVQ ETSFFRHQSS YALVEEYVQR FVAEQPDGAN
     LDVWSVGCST GEEAYSLAML INEQLTDNTR KLFYGITATD ISLPTLAKAR KGEYAARRAL
     QVDPLLREKY FQPGESGQTV MVSPELKQHI CFARLNVLDL GNAPMNNMDL IFCQNMLIYF
     RRWRKRQIVN RLAERLAPGG LMVLGPGEVT DWQHPDLERV HFADTLAFRR CR
//
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