ID A0A1R3I8P6_COCAP Unreviewed; 669 AA.
AC A0A1R3I8P6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
GN ORFNames=CCACVL1_14012 {ECO:0000313|EMBL:OMO78928.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO78928.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO78928.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO78928.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMO78928.1}.
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; AWWV01010507; OMO78928.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3I8P6; -.
DR STRING; 210143.A0A1R3I8P6; -.
DR EnsemblPlants; OMO78928; OMO78928; CCACVL1_14012.
DR Gramene; OMO78928; OMO78928; CCACVL1_14012.
DR OMA; GYFLFNT; -.
DR OrthoDB; 5473515at2759; -.
DR Proteomes; UP000188268; 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 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 PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000313|EMBL:OMO78928.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Transferase {ECO:0000313|EMBL:OMO78928.1}.
FT DOMAIN 273..301
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
SQ SEQUENCE 669 AA; 74247 MW; 691119D4C9023C3C CRC64;
MLSYAGTMVL GRLDNLLGYG KVKTLSDSST LPEDMELAEE MNALGLPLSF HTNKDTRSEM
ARSKKKSVRR KHRHEDTEEL LEFSTVSEME IVSPPTFHDN SSSSFCSMSM LGQSESSYHD
IAVAVNESQD PDCKQEDSAS LARTSYGSVM EQNGDGISDL VTNDGSDYDI ARVSGTIFKE
DEDIAVNSSS LGAGVLLECC VMEPDLDLCK NEPDRSLMEN ECCECSSGAH CNEKSEKLCY
DNGPEQLPVS ELYSTNSDVL DCDDNDHTYF GDWNVYWDSF YMRNYFYNVK TQVSTWDPPP
GMENLVLDTH NDKPNQMTTE SLQISVHESR LEEILSDELS NGTGLTAASS LTMPSISKSL
EQAGEYCEIS GSCDGEVTLG LISDAQGIVD SMIKISTGTI SDDDDDDIPL ETVTSAKDQV
DTLLVAPTKK GKKKTRRRAQ GKLSRDNEEL QFQGMFEEHS AIIGKYWCQR YLLFSRFDEG
IKMDEEGWFS VTPELIARHH ASRCGNGIVV DAFTGAGGNA IQFAQRSSHV IAIDIDPKKI
EYAYHNAAVY GVNDRIDFVM GDFFVLAPKL KADTVFLSPP WGGPDYTKVE IYDLKTMLRP
CDGYFLFNVA KKIACRIVMF LPRNVDVNQL AELSLSSEPP WSVEVEKNFL NGKLKAITAY
FTETAVSGQ
//
