PRMC_BURPS
ID PRMC_BURPS Reviewed; 285 AA.
AC Q63QE9;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=BPSL3074;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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; BX571965; CAH37085.1; -; Genomic_DNA.
DR RefSeq; WP_004527812.1; NZ_CP009538.1.
DR RefSeq; YP_109669.1; NC_006350.1.
DR AlphaFoldDB; Q63QE9; -.
DR SMR; Q63QE9; -.
DR STRING; 272560.BPSL3074; -.
DR EnsemblBacteria; CAH37085; CAH37085; BPSL3074.
DR KEGG; bps:BPSL3074; -.
DR PATRIC; fig|272560.51.peg.2180; -.
DR eggNOG; COG2890; Bacteria.
DR OMA; FDARYWE; -.
DR Proteomes; UP000000605; Chromosome 1.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0018364; P:peptidyl-glutamine methylation; IEA:UniProtKB-UniRule.
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..285
FT /note="Release factor glutamine methyltransferase"
FT /id="PRO_0000414506"
FT BINDING 119..123
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT BINDING 142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT BINDING 175
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT BINDING 191..194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT BINDING 191
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
SQ SEQUENCE 285 AA; 30250 MW; 0F3239D23E5AC886 CRC64;
MNTTKPSPAT AAELLRASPL DALDARILLA HALGWSRTQL ITRADEPLDA AARARYLALQ
ARRAAGEPIA QLTGAREFFG LEFDITPDVL IPRPETELLV ETALDAIDGI ASPCVLDLGT
GSGAIAVSIA SERPDARVWA LERSVAALDV ARRNARKLLD PARAGGPLRF LESDWYAALD
PGLRFHVVVS NPPYIARHDP HLAEGDLRFE PRGALTDEND GLAAIRTIVA GAHAFVAPGG
ALWLEHGYDQ AAAVRTLLDA AGFADVESRA DLASIERASG GRLPG
