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Entry: A0A2S7QFG5_9HELO
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ID   A0A2S7QFG5_9HELO        Unreviewed;       255 AA.
AC   A0A2S7QFG5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   08-NOV-2023, entry version 16.
DE   RecName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
GN   ORFNames=CJF32_00008580 {ECO:0000313|EMBL:PQE25287.1};
OS   Rutstroemia sp. NJR-2017a WRK4.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Rutstroemiaceae; Rutstroemia.
OX   NCBI_TaxID=2070412 {ECO:0000313|EMBL:PQE25287.1, ECO:0000313|Proteomes:UP000238813};
RN   [1] {ECO:0000313|EMBL:PQE25287.1, ECO:0000313|Proteomes:UP000238813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJR-2017a WRK4 {ECO:0000313|EMBL:PQE25287.1,
RC   ECO:0000313|Proteomes:UP000238813};
RA   Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(2),N(7)-dimethyl 5'-triphosphoguanosine)-
CC         ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end
CC         (N(2),N(2),N(7)-trimethyl 5'-triphosphoguanosine)-(ribonucleoside) in
CC         mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67624,
CC         Rhea:RHEA-COMP:17171, Rhea:RHEA-COMP:17315, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:167623,
CC         ChEBI:CHEBI:172880; Evidence={ECO:0000256|ARBA:ARBA00024488};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67625;
CC         Evidence={ECO:0000256|ARBA:ARBA00024488};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC         in mRNA + S-adenosyl-L-methionine = a 5'-end (N(2),N(7)-dimethyl 5'-
CC         triphosphoguanosine)-ribonucleoside in mRNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:67620, Rhea:RHEA-COMP:17167, Rhea:RHEA-
CC         COMP:17315, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:156461, ChEBI:CHEBI:172880;
CC         Evidence={ECO:0000256|ARBA:ARBA00024618};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67621;
CC         Evidence={ECO:0000256|ARBA:ARBA00024618};
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       Trimethylguanosine synthase family. {ECO:0000256|ARBA:ARBA00025783}.
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:PQE25287.1}.
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DR   EMBL; NJPR01000075; PQE25287.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S7QFG5; -.
DR   STRING; 2070412.A0A2S7QFG5; -.
DR   InParanoid; A0A2S7QFG5; -.
DR   OrthoDB; 5473515at2759; -.
DR   Proteomes; UP000238813; Unassembled WGS sequence.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009452; P:7-methylguanosine RNA capping; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR019012; RNA_cap_Gua-N2-MeTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR14741; S-ADENOSYLMETHIONINE-DEPENDENT METHYLTRANSFERASE RELATED; 1.
DR   PANTHER; PTHR14741:SF32; TRIMETHYLGUANOSINE SYNTHASE; 1.
DR   Pfam; PF09445; Methyltransf_15; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000238813}.
SQ   SEQUENCE   255 AA;  28069 MW;  FA6D5237C5DFE098 CRC64;
     MVVDSSNANG DSEMTGLIAN GSQVFPLDEN CTHYTALNQI PWDLQKYWQQ RYHVFSLYDE
     GIYMTDDAWF GVTPEPVANQ IASDYAKLIS PAKTTIIDIF AGAGGNSIAF ALTNRWAHVI
     AIEKDPSVIA CAQNNAYVYG VGDQITWVNG DCFEYLAAHS SSINPKETVI FASPPWGGPG
     YTSENIFDLS TMYPYSVQHI HEACKTMDTA LYLPRTSDLR QIAKLVPDGK KVEVVQYCME
     GASKALVAYI PATEP
//
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