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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//