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Database: UniProt
Entry: A0A2S6IG25_9ACTN
LinkDB: A0A2S6IG25_9ACTN
Original site: A0A2S6IG25_9ACTN 
ID   A0A2S6IG25_9ACTN        Unreviewed;       274 AA.
AC   A0A2S6IG25;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE            EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN   ORFNames=CLV92_11127 {ECO:0000313|EMBL:PPK93110.1};
OS   Kineococcus xinjiangensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC   Kineococcus.
OX   NCBI_TaxID=512762 {ECO:0000313|EMBL:PPK93110.1, ECO:0000313|Proteomes:UP000239485};
RN   [1] {ECO:0000313|EMBL:PPK93110.1, ECO:0000313|Proteomes:UP000239485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22857 {ECO:0000313|EMBL:PPK93110.1,
RC   ECO:0000313|Proteomes:UP000239485};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (FEB-2018) 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:PPK93110.1}.
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DR   EMBL; PTJD01000011; PPK93110.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S6IG25; -.
DR   OrthoDB; 9816309at2; -.
DR   Proteomes; UP000239485; 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   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:SF21; 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:PPK93110.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239485};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PPK93110.1}.
FT   DOMAIN          1..272
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
SQ   SEQUENCE   274 AA;  30655 MW;  C89DBBF39604DF9D CRC64;
     MPLTNQAFDW VCTLVRRESA IVLEKGKEYL VESRLVPLAR AAGAPDVSAY IEGVRVGLDR
     RKQMDIVEAL TTNETSWFRD GAPFTAFSTA VLPDLKQTRG ATRQLRIWSA ACSTGQEAYS
     LAMLLKDSVV AEGWRAEILA TDISNEVLEK GRSGRFSQLE MNRGLPANLL VRHFTRVGTQ
     WQVNDDLKRM VTFQHMNLAL PFRGVGQFDV VFLRNVLIYF DVSTKRDILQ RVRAVLRPGG
     YLFLGGAETT LGVDDGWERT LIGRVSVHRP KNGG
//
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