ID W9H874_9PROT Unreviewed; 301 AA.
AC W9H874;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=N825_30175 {ECO:0000313|EMBL:EWY40961.1};
OS Skermanella stibiiresistens SB22.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Skermanella.
OX NCBI_TaxID=1385369 {ECO:0000313|EMBL:EWY40961.1, ECO:0000313|Proteomes:UP000019486};
RN [1] {ECO:0000313|EMBL:EWY40961.1, ECO:0000313|Proteomes:UP000019486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB22 {ECO:0000313|EMBL:EWY40961.1,
RC ECO:0000313|Proteomes:UP000019486};
RA Zhu W., Wang G.;
RT "The genome sequence of Skermanella stibiiresistens.";
RL Submitted (AUG-2013) 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; Evidence={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: 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:EWY40961.1}.
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DR EMBL; AVFL01000005; EWY40961.1; -; Genomic_DNA.
DR AlphaFoldDB; W9H874; -.
DR STRING; 1385369.N825_30175; -.
DR PATRIC; fig|1385369.3.peg.1675; -.
DR OrthoDB; 9800643at2; -.
DR Proteomes; UP000019486; Unassembled WGS sequence.
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:0019538; P:protein 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; IPR004556; HemK-like.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR040758; PrmC_N.
DR InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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; PF13847; Methyltransf_31; 1.
DR Pfam; PF17827; PrmC_N; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_02126}; Reference proteome {ECO:0000313|Proteomes:UP000019486};
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 24..94
FT /note="Release factor glutamine methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF17827"
FT DOMAIN 133..260
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140..144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT BINDING 192
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT BINDING 206..209
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT BINDING 206
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
SQ SEQUENCE 301 AA; 31595 MW; 8A3D738024D09CA3 CRC64;
MTGAPPEGTV EIPPELGGTP TLREVTRHGE RLLRDAGVDT PDLDARLLTG AALGMTRQHM
LIHATARLNQ PQVARVLGFI ARRVAREPVS RILGRREFWS LDFTLSAATL DPRPDSETVV
EEALAGVADK RAPLSVLDLG TGTGCLLLAV LSELPAAMGL GVDQSTEAVA TATANARRLG
LGPRARFAVG DWMTGLEDRF DIVMSNPPYI PDAEITTLSP EVTGFDPRAA LAGGADGLDA
YRAITAGLGG VLKPGGRIIF EVGFGQSHDV AALLEAAGLS QIGFRKDLAG IERVVFGHLG
A
//