ID V4M6W5_EUTSA Unreviewed; 544 AA.
AC V4M6W5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
GN ORFNames=EUTSA_v10022632mg {ECO:0000313|EMBL:ESQ50772.1};
OS Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Eutremeae; Eutrema.
OX NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ50772.1, ECO:0000313|Proteomes:UP000030689};
RN [1] {ECO:0000313|EMBL:ESQ50772.1, ECO:0000313|Proteomes:UP000030689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23518688; DOI=10.3389/fpls.2013.00046;
RA Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., Jenkins J.,
RA Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A.,
RA Mitchell-Olds T., Schumaker K.S., Wang X.;
RT "The Reference Genome of the Halophytic Plant Eutrema salsugineum.";
RL Front. Plant Sci. 4:46-46(2013).
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; KI517392; ESQ50772.1; -; Genomic_DNA.
DR RefSeq; XP_006409319.1; XM_006409256.1.
DR AlphaFoldDB; V4M6W5; -.
DR STRING; 72664.V4M6W5; -.
DR EnsemblPlants; ESQ50772; ESQ50772; EUTSA_v10022632mg.
DR GeneID; 18026326; -.
DR Gramene; ESQ50772; ESQ50772; EUTSA_v10022632mg.
DR KEGG; eus:EUTSA_v10022632mg; -.
DR eggNOG; KOG2730; Eukaryota.
DR OMA; GNQSLDI; -.
DR OrthoDB; 5473515at2759; -.
DR Proteomes; UP000030689; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblPlants.
DR GO; GO:0071164; F:RNA trimethylguanosine synthase activity; IEA:EnsemblPlants.
DR GO; GO:0009452; P:7-methylguanosine RNA capping; IEA:InterPro.
DR GO; GO:0009409; P:response to cold; IEA:EnsemblPlants.
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 Pfam; PF00397; WW; 1.
DR SMART; SM00456; WW; 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:UP000030689}.
FT DOMAIN 183..217
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 160..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 61398 MW; 62259B7564028606 CRC64;
MGRVRSEEEG EAIEALGSLF KLTQIHLWDD GSTDTHLVPL FYEHSDVFPN KSIDDTSNKL
SGIANHRSED MGLIKEMKAL GLPVSFQTNK EWKTRTRGHQ KKGIKFNTLL NEEDYDVASP
LNLVSDYSSD YVIVSEEIDR TCVGNDCVQE SAVEEENHEF GGRDSMLTSE TSDSQRCKVG
NNNDDSDEWK VYWDSFYGRS YFYNIKTQES TWNPPIGMEH LAANSYNTHN LNESATETTE
KPHDDLLGTE PASDLGRVCQ SQYETGALEE VSSLIDRYQE TSIGNQSLDI TPPEEEGAYV
VTSIRKAKKK TRRTRARKIF SSLNTGARRE RVLEEYSDIL GKYWCQRYLL FSRFDEGIKM
DEEGWFSVTP ELIAKHHATR CNEGVVIDCF TGVGGNAIQF ASRSHYVIAI DLDPKKLDLA
KHNAAIYGVA DKIDFVKGDF FDLAHNLKAG TVFLSPPWGG PDYVKASVYD LKTMLRPRDG
DTLFKAAMNI ASTIIMFLPR NVDINQLAEL ALSTSPPWSL EVEKNYLNGK LKAITAYYFR
QDGC
//
