ID A0A1G0PE77_9BACT Unreviewed; 263 AA.
AC A0A1G0PE77;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 28-JUN-2023, entry version 17.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=A2068_10525 {ECO:0000313|EMBL:OGU34039.1};
OS Ignavibacteria bacterium GWB2_35_6b.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798424 {ECO:0000313|EMBL:OGU34039.1, ECO:0000313|Proteomes:UP000178800};
RN [1] {ECO:0000313|EMBL:OGU34039.1, ECO:0000313|Proteomes:UP000178800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGU34039.1}.
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DR EMBL; MGZW01000229; OGU34039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0PE77; -.
DR Proteomes; UP000178800; 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; IPR026024; Chemotaxis_MeTrfase_CheR.
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:SF18; CHEMOTAXIS PROTEIN METHYLTRANSFERASE 2; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR PIRSF; PIRSF000410; CheR; 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 S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..254
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
SQ SEQUENCE 263 AA; 30709 MW; C7114051F7DF6321 CRC64;
MYDQCGIYFQ DNKKYLLESR LQKRILYLKI DTFEKYLEYV KFNPRKADEL KYLYEVITIN
ETFFFRNQPQ LDALVTSIIP EVLNSPYKTN KNKIRIWSAA SSSGEEAYSI AMMFNEMIKP
KYPGLSIEIV GTDINYQVVE TAKSGIYKEY AVRNTPSYYM KKYFTQDGSN YYIDPQIKNM
ASFKLLNLYD QAAMKAMTSF DVIFCANVLI YFDLKSKIQV VSQLYNSLNK NGYLFIGYSE
TLHGISKAFK LASFPKTIGY KKE
//
