ID A0A078ISB3_BRANA Unreviewed; 465 AA.
AC A0A078ISB3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
GN Name=BnaCnng25810D {ECO:0000313|EMBL:CDY53955.1};
GN ORFNames=GSBRNA2T00011803001 {ECO:0000313|EMBL:CDY53955.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY53955.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY53955.1, ECO:0000313|Proteomes:UP000028999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LK033256; CDY53955.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078ISB3; -.
DR STRING; 3708.A0A078ISB3; -.
DR PaxDb; 3708-A0A078ISB3; -.
DR EnsemblPlants; CDY53955; CDY53955; GSBRNA2T00011803001.
DR Gramene; CDY53955; CDY53955; GSBRNA2T00011803001.
DR Proteomes; UP000028999; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000028999};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 434..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 174..202
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 220..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 465 AA; 52187 MW; 18AE1041AE6D926D CRC64;
MGMVGSEVEE ESASIKALGS LFKLTQIHLW EDGSTDTCLV PLFHEHNRFE DMGLIQEMKA
LGLPVAFQTN KEWKNRTKSI PQKKRIKDRS DQVNVDVASP QSLLVSDCSP HHAIGGDEEV
DGSSVENDCV QISAVEQNDE VACLGDGDRD SLLTSEATDS RSYELGDEHG SSEWKVYWDS
FYGRNYFYNV MTQESTWQPP LGMEHLAYSH ETHNLNEFPT EKQPDDLLRN LPADDVPPEQ
SDDLGGVCQS QHETKTLEEV SSLIDTYQET SIGNQLLDVT TLEEEGNGTS VVKTIKKAKK
KTRRSRAKKI FSCSNTAGVP DEYSDVLGKY WCQRYLLFSR FDESIKMDEE GWFSVTPEAI
AKHHASRGSG GVVIDCFTGV GGNAIQFASR SHYVIAIDLD PKKLDLAKHN AAVYGVADKI
DFVKGDFFDL AHNLKVFFLQ LVSFFFWWIV IKKGIPIWIL SMIGF
//
