ID A0A3B5Y798_WHEAT Unreviewed; 426 AA.
AC A0A3B5Y798;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS1A02G432300.1};
RN [1] {ECO:0000313|EnsemblPlants:TraesCS1A02G432300.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS1A02G432300.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS1A02G432300.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A3B5Y798; -.
DR SMR; A0A3B5Y798; -.
DR STRING; 4565.A0A3B5Y798; -.
DR PaxDb; 4565-Traes_1AL_B31B6EA0E-2; -.
DR EnsemblPlants; TraesCS1A02G432300.1; TraesCS1A02G432300.1; TraesCS1A02G432300.
DR Gramene; TraesCAD_scaffold_056304_01G000100.1; TraesCAD_scaffold_056304_01G000100.1; TraesCAD_scaffold_056304_01G000100.
DR Gramene; TraesCS1A02G432300.1; TraesCS1A02G432300.1; TraesCS1A02G432300.
DR Gramene; TraesCS1A03G1051200.1; TraesCS1A03G1051200.1.CDS; TraesCS1A03G1051200.
DR Gramene; TraesPAR_scaffold_064760_01G000100.1; TraesPAR_scaffold_064760_01G000100.1; TraesPAR_scaffold_064760_01G000100.
DR OMA; GWRSICS; -.
DR Proteomes; UP000019116; Chromosome 1A.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0071164; F:RNA trimethylguanosine synthase activity; IBA:GO_Central.
DR GO; GO:0036261; P:7-methylguanosine cap hypermethylation; IBA:GO_Central.
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: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:UP000019116}.
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..47
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 426 AA; 47756 MW; CEBA68E97491306B CRC64;
MAATVTTKLR EPGRDVDGEL SDVPAVRPDP GLGPPLDRAP THEPVPTAMP PAAESSSMRK
LGKLFRLTEV HLWDDFYVKT EDCDATETTD CTGSQTTETR NKGAKTTDED HSFVEDMELA
SRMADQTGDD THLNEQRHQL IYNDALSLSD IPDKELIYIS VIATIDEAQH DKNMQNDSPM
TEVLEMNQEG TTNKNKKRIS FPWQGWRSIC SFLLYLPFMY WNQRYSLFSL FDSGIKMDEE
GWFSVTPEPI AKHHASRVGA GILIDCFAGV GGNTIQFATK CKHVVAVDID PQKIGYAQHN
ATIYGVNDHI DFIVGDFINI APHLKGETVF MSPPWGGPDY AKVDVYDMKT MLKPCDGYHL
FKLATAIASR VVMFLPRNSD LEQLADMCLS VDPPWAVEVE KNFLNGKLKT ITAYFEEHVS
TDVEHQ
//
