ID A0A222VV67_9PSEU Unreviewed; 287 AA.
AC A0A222VV67;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 ORFNames=DES30_106382 {ECO:0000313|EMBL:PWV75764.1},
GN SAMN05421630_10759 {ECO:0000313|EMBL:SDD26761.1};
OS Prauserella marina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Prauserella.
OX NCBI_TaxID=530584 {ECO:0000313|EMBL:SDD26761.1, ECO:0000313|Proteomes:UP000199494};
RN [1] {ECO:0000313|EMBL:SDD26761.1, ECO:0000313|Proteomes:UP000199494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5506 {ECO:0000313|EMBL:SDD26761.1,
RC ECO:0000313|Proteomes:UP000199494};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PWV75764.1, ECO:0000313|Proteomes:UP000246674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45268 {ECO:0000313|EMBL:PWV75764.1,
RC ECO:0000313|Proteomes:UP000246674};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; QGTN01000006; PWV75764.1; -; Genomic_DNA.
DR EMBL; FMZE01000007; SDD26761.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222VV67; -.
DR STRING; 530584.SAMN05421630_10759; -.
DR KEGG; pmad:BAY61_25520; -.
DR OrthoDB; 9800643at2; -.
DR Proteomes; UP000199494; Unassembled WGS sequence.
DR Proteomes; UP000246674; 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:UP000199494};
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 10..76
FT /note="Release factor glutamine methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF17827"
FT DOMAIN 113..198
FT /note="Methyltransferase small"
FT /evidence="ECO:0000259|Pfam:PF05175"
FT BINDING 144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT BINDING 194..197
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT BINDING 194
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
SQ SEQUENCE 287 AA; 30857 MW; EDA1C4D4FE1C0535 CRC64;
MKRQPLRLAI LEATRILDQA GVASPRNDAE LIVAHVLGVE RGRLPLIPLV DPAVIEAIGQ
LVAQRAKRIP LQHLTGWAAM GDITVAVGQG VFVPRPETEL LLEWGLKLLR GREYPVVVDL
CTGSGVLALA FANARQDAVV YALDNDPHAL AWARHNADAR VEVGDTAIRL YSGDVADHTV
FAELDGLVDL VVCNPPYVPE GTEVPPEVAG YDPPRAVFAS GHGLDVIRHV VTTAARLLRP
GGGLAIEHDD THGRVVPGLL ESRRVLRDVV GHTDLTGRPR FVTALRG
//
