ID A0A1G2DDJ1_9BACT Unreviewed; 251 AA.
AC A0A1G2DDJ1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=A2942_03230 {ECO:0000313|EMBL:OGZ11603.1};
OS Candidatus Lloydbacteria bacterium RIFCSPLOWO2_01_FULL_50_20.
OC Bacteria; Candidatus Lloydbacteria.
OX NCBI_TaxID=1798665 {ECO:0000313|EMBL:OGZ11603.1, ECO:0000313|Proteomes:UP000178534};
RN [1] {ECO:0000313|EMBL:OGZ11603.1, ECO:0000313|Proteomes:UP000178534}
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:OGZ11603.1}.
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DR EMBL; MHLP01000035; OGZ11603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2DDJ1; -.
DR STRING; 1798665.A2942_03230; -.
DR Proteomes; UP000178534; 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: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; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004556; HemK-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR NCBIfam; TIGR00536; hemK_fam; 1.
DR PANTHER; PTHR18895; HEMK METHYLTRANSFERASE; 1.
DR PANTHER; PTHR18895:SF74; MTRF1L RELEASE FACTOR GLUTAMINE METHYLTRANSFERASE; 1.
DR Pfam; PF05175; MTS; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
FT DOMAIN 80..195
FT /note="Methyltransferase small"
FT /evidence="ECO:0000259|Pfam:PF05175"
SQ SEQUENCE 251 AA; 28262 MW; F4293A3E9787A6AA CRC64;
MNKETRWLLR EKYHGVETPE FQEDVERLNG GLPLAYVIGW VDFLGCRIDL SAKPLIPRPE
TEFWVEQAIA EVASCQLLVA RKKNPIKILD LFSGSGCIGI ALLKHLPNAT VDFGEKDPKL
CQQIKKNIAL NNIDASQTCI VQTDTFSNIT ETYDYIFANP PYIDSARKET AENSVILHEP
HGALFADEGG LSFIIKLINE SAPYLKPRGV MYIEFGENQK EAITLIANAA GWKSEFHKDQ
FSKWRMAKCV S
//