ID D8F493_9DELT Unreviewed; 299 AA.
AC D8F493;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Release factor glutamine methyltransferase {ECO:0000256|HAMAP-Rule:MF_02126};
DE Short=RF MTase {ECO:0000256|HAMAP-Rule:MF_02126};
DE EC=2.1.1.297 {ECO:0000256|HAMAP-Rule:MF_02126};
DE AltName: Full=N5-glutamine methyltransferase PrmC {ECO:0000256|HAMAP-Rule:MF_02126};
DE AltName: Full=Protein-(glutamine-N5) MTase PrmC {ECO:0000256|HAMAP-Rule:MF_02126};
DE AltName: Full=Protein-glutamine N-methyltransferase PrmC {ECO:0000256|HAMAP-Rule:MF_02126};
GN Name=prmC {ECO:0000256|HAMAP-Rule:MF_02126,
GN ECO:0000313|EMBL:EFK09478.1};
GN ORFNames=NPH_3143 {ECO:0000313|EMBL:EFK09478.1};
OS delta proteobacterium NaphS2.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=88274 {ECO:0000313|EMBL:EFK09478.1, ECO:0000313|Proteomes:UP000003834};
RN [1] {ECO:0000313|EMBL:EFK09478.1, ECO:0000313|Proteomes:UP000003834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NaphS2 {ECO:0000313|EMBL:EFK09478.1,
RC ECO:0000313|Proteomes:UP000003834};
RX PubMed=21124915; DOI=10.1371/journal.pone.0014072;
RA Didonato R.J., Young N.D., Butler J.E., Chin K.J., Hixson K.K., Mouser P.,
RA Lipton M.S., Deboy R., Methe B.A.;
RT "Genome Sequence of the Deltaproteobacterial Strain NaphS2 and Analysis of
RT Differential Gene Expression during Anaerobic Growth on Naphthalene.";
RL PLoS ONE 5:E14072-E14072(2010).
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:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00000932, ECO:0000256|HAMAP-
CC Rule:MF_02126};
CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC family. PrmC subfamily. {ECO:0000256|HAMAP-Rule:MF_02126}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02126}.
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:EFK09478.1}.
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DR EMBL; ADZZ01000282; EFK09478.1; -; Genomic_DNA.
DR AlphaFoldDB; D8F493; -.
DR OrthoDB; 9800643at2; -.
DR Proteomes; UP000003834; Unassembled WGS sequence.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 NCBIfam; TIGR00536; hemK_fam; 1.
DR NCBIfam; TIGR03534; RF_mod_PrmC; 1.
DR PANTHER; PTHR18895; HEMK METHYLTRANSFERASE; 1.
DR PANTHER; PTHR18895:SF74; MTRF1L RELEASE FACTOR GLUTAMINE METHYLTRANSFERASE; 1.
DR Pfam; PF05175; MTS; 1.
DR Pfam; PF17827; PrmC_N; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_02126}; Reference proteome {ECO:0000313|Proteomes:UP000003834};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_02126};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02126}.
FT DOMAIN 11..80
FT /note="Release factor glutamine methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF17827"
FT DOMAIN 112..206
FT /note="Methyltransferase small"
FT /evidence="ECO:0000259|Pfam:PF05175"
FT BINDING 129..133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT BINDING 152
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT BINDING 198..201
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT BINDING 198
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
SQ SEQUENCE 299 AA; 33549 MW; EAEDCDFDA1B0B69F CRC64;
MTPKAWCIKT LLETATDYLA GKGIENARLN AEVLLAYQLQ VQRISLYLNF EQPLTEKEVS
GFRRLIKRRL EHEPLQYITG KQEFWSLSFQ VNPHVLIPRP ETEILVEQAM DLATALTEEG
TQLRFLDLGT GSGVIAVAMA KQIPESLVFA TDISGKALDV ARANAQAHGV SSSITFIQGD
LFEPLMLEKP AFHLIASNPP YVCTHEISGL QSEIALYEPR AALDGGKDGM DYLKEIIKQA
PRFLLPGGWL LLEMSPFQVE KALFALAETD VYQNTKPVQD YSHHQRVIKA QLRQEIQPY
//
