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Database: UniProt
Entry: A0A2P6RV92_ROSCH
LinkDB: A0A2P6RV92_ROSCH
Original site: A0A2P6RV92_ROSCH 
ID   A0A2P6RV92_ROSCH        Unreviewed;       251 AA.
AC   A0A2P6RV92;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
GN   ORFNames=RchiOBHm_Chr2g0132081 {ECO:0000313|EMBL:PRQ50336.1};
OS   Rosa chinensis (China rose).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC   Rosa.
OX   NCBI_TaxID=74649 {ECO:0000313|EMBL:PRQ50336.1, ECO:0000313|Proteomes:UP000238479};
RN   [1] {ECO:0000313|EMBL:PRQ50336.1, ECO:0000313|Proteomes:UP000238479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Old Blush {ECO:0000313|Proteomes:UP000238479};
RA   Bendahmane M.;
RT   "The Rosa genome provides new insights in the design of modern roses.";
RL   Nat. Genet. 0:0-0(2018).
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:PRQ50336.1}.
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DR   EMBL; PDCK01000040; PRQ50336.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P6RV92; -.
DR   STRING; 74649.A0A2P6RV92; -.
DR   EnsemblPlants; PRQ50336; PRQ50336; RchiOBHm_Chr2g0132081.
DR   Gramene; PRQ50336; PRQ50336; RchiOBHm_Chr2g0132081.
DR   OMA; KALCIYY; -.
DR   OrthoDB; 5473515at2759; -.
DR   Proteomes; UP000238479; Chromosome 2.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071164; F:RNA trimethylguanosine synthase activity; IEA:RHEA.
DR   GO; GO:0009452; P:7-methylguanosine RNA capping; 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:SF41; 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   Acyltransferase {ECO:0000313|EMBL:PRQ50336.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000238479};
KW   Transferase {ECO:0000313|EMBL:PRQ50336.1}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   251 AA;  28487 MW;  E4B1FB4C6B2D474D CRC64;
     MKTKKSSKQR RTRRSKRSKL LQLPTQTHET RRVIEEGVSP LVEKYWFQRY DLFSRYDEGI
     KLDEQGWYSV TPEQIAIRQA KRCENATVVI DCFAGVGGNA IQFASMCYHV VAIEIDPLKV
     NMAINNARIY GVEDYIDFIV GDFFQLAPSL KGDIVFLSPP WGGPSYRRVK KFTLDLLEPK
     DGYAIFQAAQ AITPNIIMFL PRNVDLLQVE ELCWLSSPPL EFEIEENYVQ GNLKGVTVYF
     GGAAASQCGP S
//
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