ID A0A3B5Z5I2_WHEAT Unreviewed; 413 AA.
AC A0A3B5Z5I2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
GN ORFNames=CFC21_009417 {ECO:0000313|EMBL:KAF6992429.1};
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:TraesCS1B02G467900.1};
RN [1] {ECO:0000313|EMBL:KAF6992429.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF6992429.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS1B02G467900.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS1B02G467900.1};
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 [3] {ECO:0000313|EnsemblPlants:TraesCS1B02G467900.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF6992429.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF6992429.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) 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}.
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DR EMBL; CM022212; KAF6992429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B5Z5I2; -.
DR SMR; A0A3B5Z5I2; -.
DR STRING; 4565.A0A3B5Z5I2; -.
DR PaxDb; 4565-Traes_1AL_39EE1BA6E-1; -.
DR EnsemblPlants; TraesCS1B02G467900.1; TraesCS1B02G467900.1; TraesCS1B02G467900.
DR Gramene; TraesCAD_scaffold_211220_01G000100.1; TraesCAD_scaffold_211220_01G000100.1; TraesCAD_scaffold_211220_01G000100.
DR Gramene; TraesCLE_scaffold_021251_01G000500.1; TraesCLE_scaffold_021251_01G000500.1; TraesCLE_scaffold_021251_01G000500.
DR Gramene; TraesCS1B02G467900.1; TraesCS1B02G467900.1; TraesCS1B02G467900.
DR Gramene; TraesCS1B03G1249700.1; TraesCS1B03G1249700.1.CDS; TraesCS1B03G1249700.
DR OMA; LEMDWHR; -.
DR OrthoDB; 5473515at2759; -.
DR Proteomes; UP000019116; Chromosome 1B.
DR Proteomes; UP000815260; Chromosome 1B.
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..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 45946 MW; 513327414CE54A26 CRC64;
MVATVTKKLQ EPRRDVDGEL SNVPAVGLEP GSLNAGPTRE SVPTVVMPPA AAEYSSMRKL
GKLFKLTEVH LWDDFYVKTG DCDATETTGC TGSQTTENRN KVAKTTDADH SFVEDMELAS
RMADQTGDDT HLDEQRHELI YNETLSLSDI PDKELTYISV IATIDEAQHD KNMQNDSPMT
EVLEMNQEVH SCPDMANMST DIARYWNQRY SLFSLFDSGI KTDEEGWFSV TPELIAKHHA
SRVGAGILID CFAGIGGNTI QFATKCKHVV AVDVDPQKIG YAQHNATIYG VNDHIDFIVG
DFINIAPHLK GETVFMSPPW GGPDYAEVDV YDIKTMLKPC DGYHLFKLAM AIASRVVMFL
PRNCDLDQLA DMCLSVDPPW AVEVEKNFLN GKLKTITAYF EEHVSVDVEV EHQ
//
