ID A0A1F3P063_9BACT Unreviewed; 292 AA.
AC A0A1F3P063;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=peptide chain release factor N(5)-glutamine methyltransferase {ECO:0000256|ARBA:ARBA00012771};
DE EC=2.1.1.297 {ECO:0000256|ARBA:ARBA00012771};
GN ORFNames=A3G23_08070 {ECO:0000313|EMBL:OFY70744.1};
OS Bacteroidetes bacterium RIFCSPLOWO2_12_FULL_37_12.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797365 {ECO:0000313|EMBL:OFY70744.1, ECO:0000313|Proteomes:UP000176497};
RN [1] {ECO:0000313|EMBL:OFY70744.1, ECO:0000313|Proteomes:UP000176497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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};
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:OFY70744.1}.
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DR EMBL; MEPC01000023; OFY70744.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3P063; -.
DR STRING; 1797365.A3G23_08070; -.
DR Proteomes; UP000176497; Unassembled WGS sequence.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:UniProt.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
DR GO; GO:0102559; F:protein-(glutamine-N5) methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
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 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 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:OFY70744.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OFY70744.1}.
FT DOMAIN 24..70
FT /note="Release factor glutamine methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF17827"
FT DOMAIN 99..193
FT /note="Methyltransferase small"
FT /evidence="ECO:0000259|Pfam:PF05175"
SQ SEQUENCE 292 AA; 34009 MW; 2178F281BBED1F0C CRC64;
MHHEFLEKLR DIYPEREIKS IFFIVLKSVL NFSNIEYIFH KHESIDANKL PEIKTIINRL
KKNEPIQYIL RQTEFCGISL FVNKHALIPR QETEELVEMI IKDVQEKRNR VNILDIGTGS
GCIAIALKKK LPKSHVTAVD ISRQALKVAI KNSHLLKSRI LFKRVDILKK NHPLYKQKFH
IIVSNPPYVL SSQKKDMHKN VLEYEPEKAL FAPDKDPIIF YHKILEFSKK HLATEGSIFF
EINPMLKNEI IDKANSLGFK QLRVVKDMNG KERFIIILKE KGNRVLGRGI GV
//
