ID   PRMC_BIFLO              Reviewed;         294 AA.
AC   Q8G3P4;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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}; OrderedLocusNames=BL1713;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(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; AE014295; AAN25497.1; -; Genomic_DNA.
DR   RefSeq; NP_696861.1; NC_004307.2.
DR   RefSeq; WP_007055663.1; NC_004307.2.
DR   AlphaFoldDB; Q8G3P4; -.
DR   SMR; Q8G3P4; -.
DR   STRING; 206672.BL1713; -.
DR   EnsemblBacteria; AAN25497; AAN25497; BL1713.
DR   KEGG; blo:BL1713; -.
DR   PATRIC; fig|206672.9.peg.1766; -.
DR   HOGENOM; CLU_018398_4_0_11; -.
DR   OMA; FDARYWE; -.
DR   PhylomeDB; Q8G3P4; -.
DR   Proteomes; UP000000439; 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; 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   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..294
FT                   /note="Release factor glutamine methyltransferase"
FT                   /id="PRO_0000414502"
FT   BINDING         148
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT   BINDING         201..204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT   BINDING         201
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
SQ   SEQUENCE   294 AA;  32022 MW;  2CC4A7D270DAD4D9 CRC64;
     MLITDIINQA SSQLREAGIE TPEHDAKLLL AEAAGVELRD VDRALLMGEE LGTTGQLAVF
     RAMLDRRAKR EPLQYITGHA PFRYLDLKVG PGVFIPRPET ETVVQAGLDW LTKNGMIHPC
     VVDLCAGSGA IGLSVVSEVP GSQVWAVELS PNTAEWTRRN LSETAKKYPS IASNYHLEIA
     DATSFATLAQ LDGTVDIVIT NPPYVPQTDI PEQPEVRDWD PELALYGGSM DGTLIPERII
     ERACRLLKPG GVLVMEHDVT QGDRLVAFAR ATGFAAASTG QDWTGRDRYL FAVS