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Database: UniProt
Entry: E8N2Z2_ANATU
LinkDB: E8N2Z2_ANATU
Original site: E8N2Z2_ANATU 
ID   E8N2Z2_ANATU            Unreviewed;       286 AA.
AC   E8N2Z2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE            EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN   Name=cheR {ECO:0000313|EMBL:BAJ65142.1};
GN   OrderedLocusNames=ANT_31160 {ECO:0000313|EMBL:BAJ65142.1};
OS   Anaerolinea thermophila (strain DSM 14523 / JCM 11388 / NBRC 100420 /
OS   UNI-1).
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Anaerolinea.
OX   NCBI_TaxID=926569 {ECO:0000313|EMBL:BAJ65142.1, ECO:0000313|Proteomes:UP000008922};
RN   [1] {ECO:0000313|EMBL:BAJ65142.1, ECO:0000313|Proteomes:UP000008922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14523 / JCM 11388 / NBRC 100420 / UNI-1
RC   {ECO:0000313|Proteomes:UP000008922};
RA   Narita-Yamada S., Kishi E., Watanabe Y., Takasaki K., Ankai A., Oguchi A.,
RA   Fukui S., Takahashi M., Yashiro I., Hosoyama A., Sekiguchi Y., Hanada S.,
RA   Fujita N.;
RT   "Whole genome sequence of Anaerolinea thermophila UNI-1.";
RL   Submitted (DEC-2010) 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};
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DR   EMBL; AP012029; BAJ65142.1; -; Genomic_DNA.
DR   RefSeq; WP_013561483.1; NC_014960.1.
DR   AlphaFoldDB; E8N2Z2; -.
DR   STRING; 926569.ANT_31160; -.
DR   GeneID; 78351355; -.
DR   KEGG; atm:ANT_31160; -.
DR   eggNOG; COG1352; Bacteria.
DR   HOGENOM; CLU_025854_0_1_0; -.
DR   InParanoid; E8N2Z2; -.
DR   OMA; KIWVAGC; -.
DR   OrthoDB; 9816309at2; -.
DR   Proteomes; UP000008922; Chromosome.
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:SF18; CHEMOTAXIS PROTEIN METHYLTRANSFERASE 2; 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:BAJ65142.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008922};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAJ65142.1}.
FT   DOMAIN          4..283
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
SQ   SEQUENCE   286 AA;  33348 MW;  0DEBB92994BC66CF CRC64;
     MASLLGETIT LPEDLFALLS ELIRQHLGLE YPPDKRSILQ DRLYPLLVEE GMDSFFDLYY
     LLKYNGGNET LWKRVQSALA VRETYFWREV DQILAAANYL IPALQAEAPG RTVRVWHAAC
     ASGEEPYSLA MALSENGAVD WERLEIIGTD FDETSLNIAR RGVYGMRSFR VLPAHLREKY
     FTEVQSQHFQ IHEKFLKKVQ FKYLNLMDEA GMQGMQDFDF IFCRNVFIYF DIPSITRTAQ
     HFYEALRNPG YLFLGAAESL LRIPTRFELR ELHRAFVYVK QEKEET
//
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