ID A0A172RXS9_9ACTN Unreviewed; 316 AA.
AC A0A172RXS9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=SAMN02910314_01849 {ECO:0000313|EMBL:SEO99312.1};
OS Denitrobacterium detoxificans.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Denitrobacterium.
OX NCBI_TaxID=79604 {ECO:0000313|EMBL:SEO99312.1, ECO:0000313|Proteomes:UP000182975};
RN [1] {ECO:0000313|Proteomes:UP000182975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21843 {ECO:0000313|Proteomes:UP000182975};
RA Varghese N.;
RL Submitted (OCT-2016) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOEC01000016; SEO99312.1; -; Genomic_DNA.
DR RefSeq; WP_066661923.1; NZ_FOEC01000016.1.
DR AlphaFoldDB; A0A172RXS9; -.
DR STRING; 79604.AAY81_04570; -.
DR KEGG; ddt:AAY81_04570; -.
DR PATRIC; fig|79604.3.peg.930; -.
DR OrthoDB; 9800643at2; -.
DR Proteomes; UP000182975; 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:UP000182975};
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..79
FT /note="Release factor glutamine methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF17827"
FT DOMAIN 145..223
FT /note="Methyltransferase small"
FT /evidence="ECO:0000259|Pfam:PF05175"
FT BINDING 173
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT BINDING 220..223
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT BINDING 220
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
SQ SEQUENCE 316 AA; 33934 MW; C8ED51416D6A71A5 CRC64;
MSETWTVKRI LDWISGYLSE RGDENPLLSA QWLVAEALGV SRIQLYADLD RPLSMAERDT
LRDYTRRRGA GEPLQYITGT TDFRFITVRV KPGVLIPRPE TEVLVSEALS ACKPRIAALR
TASVALEGEA EGEEASTPAE PQPFRVVDLC TGSGCIACSI AKEVLQSQVV ATDISDDAIE
LARLNAAELG LSERVDVVQG DLAKGVPAVW NGTVDLVISN PPYIPTAVLG EMSHEVMDYE
PSLALDGGED GLDLYRRIVP AALELLAPGG VLAVELHETC LDEARAIAVE AGFASCRIAV
DLAGRPRVLV ASSPLE
//
