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PRMC_BRADU
ID   PRMC_BRADU              Reviewed;         297 AA.
AC   Q89XT8;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Release factor glutamine methyltransferase {ECO:0000255|HAMAP-Rule:MF_02126};
DE            Short=RF MTase {ECO:0000255|HAMAP-Rule:MF_02126};
DE            EC=2.1.1.297 {ECO:0000255|HAMAP-Rule:MF_02126};
DE   AltName: Full=N5-glutamine methyltransferase PrmC {ECO:0000255|HAMAP-Rule:MF_02126};
DE   AltName: Full=Protein-(glutamine-N5) MTase PrmC {ECO:0000255|HAMAP-Rule:MF_02126};
DE   AltName: Full=Protein-glutamine N-methyltransferase PrmC {ECO:0000255|HAMAP-Rule:MF_02126};
GN   Name=prmC {ECO:0000255|HAMAP-Rule:MF_02126}; Synonyms=hemK;
GN   OrderedLocusNames=blr0219;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
CC   -!- FUNCTION: Methylates the class 1 translation termination release
CC       factors RF1/PrfA and RF2/PrfB on the glutamine residue of the
CC       universally conserved GGQ motif. {ECO:0000255|HAMAP-Rule:MF_02126}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-
CC         methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release
CC         factor] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42896, Rhea:RHEA-
CC         COMP:10271, Rhea:RHEA-COMP:10272, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:61891; EC=2.1.1.297; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02126};
CC   -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC       family. PrmC subfamily. {ECO:0000255|HAMAP-Rule:MF_02126}.
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DR   EMBL; BA000040; BAC45484.1; -; Genomic_DNA.
DR   RefSeq; NP_766859.1; NC_004463.1.
DR   RefSeq; WP_011083051.1; NC_004463.1.
DR   AlphaFoldDB; Q89XT8; -.
DR   SMR; Q89XT8; -.
DR   STRING; 224911.27348466; -.
DR   EnsemblBacteria; BAC45484; BAC45484; BAC45484.
DR   GeneID; 64020081; -.
DR   KEGG; bja:blr0219; -.
DR   PATRIC; fig|224911.5.peg.213; -.
DR   eggNOG; COG2890; Bacteria.
DR   HOGENOM; CLU_018398_3_1_5; -.
DR   InParanoid; Q89XT8; -.
DR   OMA; FDARYWE; -.
DR   PhylomeDB; Q89XT8; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0102559; F:protein-(glutamine-N5) methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0018364; P:peptidyl-glutamine methylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_02126; RF_methyltr_PrmC; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR004556; HemK-like.
DR   InterPro; IPR040758; PrmC_N.
DR   InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   Pfam; PF05175; MTS; 1.
DR   Pfam; PF17827; PrmC_N; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00536; hemK_fam; 1.
DR   TIGRFAMs; TIGR03534; RF_mod_PrmC; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..297
FT                   /note="Release factor glutamine methyltransferase"
FT                   /id="PRO_0000414505"
FT   BINDING         134..138
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT   BINDING         157
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT   BINDING         200..203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT   BINDING         200
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
SQ   SEQUENCE   297 AA;  31485 MW;  EF8192AFF2ABAEB4 CRC64;
     MTPRVSDPFT GQSIESARRT LAARLRSAQL EEAELDARIL LGAALGLDLT GLIAQAARLL
     TEAEASRIAQ HAQRRIAGEP VARILGTREF WGLPFRLSDA TLVPRPDTET VVERALELFR
     EQKATQQPRI ADIGTGSGAI LLALLHDIPG AFGVGTDLSL NALETARGNA VTLGLADRSA
     FVACSYLAAL RGPFDLIVSN PPYIPSAEIP KLSLEVREHD PHLALDGGND GYDAYRALIP
     QAAERLAPGG ALIVEAGQGQ ARNIETLLTA AALVVDRPPK ADLAGIPRAV SARKMPP
 
 
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