ID A0A0Q3HF73_BRADI Unreviewed; 636 AA.
AC A0A0Q3HF73;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
GN Name=100828859 {ECO:0000313|EnsemblPlants:KQK21384};
GN ORFNames=BRADI_1g60460v3 {ECO:0000313|EMBL:KQK21384.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQK21384.1};
RN [1] {ECO:0000313|EMBL:KQK21384.1, ECO:0000313|EnsemblPlants:KQK21384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK21384.1,
RC ECO:0000313|EnsemblPlants:KQK21384};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQK21384.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK21384.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK21384}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK21384};
RG EnsemblPlants;
RL Submitted (AUG-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 EMBL; CM000880; KQK21384.1; -; Genomic_DNA.
DR EMBL; CM000880; PNT77279.1; -; Genomic_DNA.
DR RefSeq; XP_014752982.1; XM_014897496.1.
DR AlphaFoldDB; A0A0Q3HF73; -.
DR EnsemblPlants; KQK21384; KQK21384; BRADI_1g60460v3.
DR EnsemblPlants; PNT77279; PNT77279; BRADI_1g60460v3.
DR Gramene; KQK21384; KQK21384; BRADI_1g60460v3.
DR Gramene; PNT77279; PNT77279; BRADI_1g60460v3.
DR Proteomes; UP000008810; Chromosome 1.
DR ExpressionAtlas; A0A0Q3HF73; baseline.
DR GO; GO:0008168; F: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 CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 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 InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_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.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000008810}.
FT DOMAIN 303..331
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
SQ SEQUENCE 636 AA; 70435 MW; 8066294C981F7995 CRC64;
MPAAAESSAI RKLGQLFKLS EVHLWDDSYV TGASETQDWY AAETGCPGSQ IAKTRNRAAK
QTDEDPSFVE DMELVSLMGS LGLPVSFSTR KEKKNIAIKG KHQGRQAPCE ELNTSTVDDA
RTCENTEELE GAQELMGCME HTNSGISSMT AVGYNEVYHA DADKMLGEDM VYVEKSGFVT
ACSVEKIPRD EAHNECEPND NTSNLVESSS PVQENQAAGS VVQLNKVMLG QNSVTNESMM
SCTDDCQRGK SSVREDQISW ETPSVSHDND VDCEVCPCPA EPSPVNNHVE KSASDFNYEH
GDWKVLWDQF YSQYYFFNIM TQVSTWYPPQ GLEDFASYCS TYPSQGLDEP SLQYTSTSVQ
EHNKSSTKCD KSSGLVCWAD NTMDNYISEA DRHVVQYEAH MSSCDNGGTT FDQAGVGRHL
NHQVHDLYSD APNLSDVPDE ESMCLSAITT IDEAQHDESE QNGSLVTEAL EVSQEVTTTK
NKKRVRRSQS YRSCQDLADN ISTDIAKYWN QRYSLFSLFD SGIKMDEEGW FSVTPEPIAK
HHASRVSAGI VIDCFTGVGG NTIQFATKCK HVVAVDIDPQ KICCAQHNAT VYGVNDHIDF
VVGDFIHISP HLKVWPALST SNDCCYFVVI QCPKSS
//
