ID J3LPI8_ORYBR Unreviewed; 685 AA.
AC J3LPI8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
GN Name=102708232 {ECO:0000313|EnsemblPlants:OB03G29640.1};
OS Oryza brachyantha (malo sina).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB03G29640.1};
RN [1] {ECO:0000313|EnsemblPlants:OB03G29640.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB03G29640.1};
RX PubMed=23481403;
RA Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA Chen M.;
RT "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT Oryza genome evolution.";
RL Nat. Commun. 4:1595-1595(2013).
RN [2] {ECO:0000313|EnsemblPlants:OB03G29640.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2013) 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}.
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 RefSeq; XP_006651475.1; XM_006651412.2.
DR AlphaFoldDB; J3LPI8; -.
DR STRING; 4533.J3LPI8; -.
DR EnsemblPlants; OB03G29640.1; OB03G29640.1; OB03G29640.
DR GeneID; 102708232; -.
DR Gramene; OB03G29640.1; OB03G29640.1; OB03G29640.
DR KEGG; obr:102708232; -.
DR eggNOG; KOG2730; Eukaryota.
DR HOGENOM; CLU_024358_0_0_1; -.
DR OMA; PRNIDQN; -.
DR OrthoDB; 5473515at2759; -.
DR Proteomes; UP000006038; Chromosome 3.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000006038}.
FT DOMAIN 315..343
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 45..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 685 AA; 76148 MW; D4905A0AF84BAECF CRC64;
MPGDAEDLSP AVRKLGRHFR LTEVHIWDDW YADGADVSHR SWRSVDTDSA GCQTDKIQNK
PAKQTDEGHS FVEDLELVNL MGSLGLPVSF RTSKEKKNTP NKVKKNGRKV SYEAENTLIY
DDSRTCTGTK EIESISQLMV LVEQTNLCSS SRTAAGYNEI CKGDVEEMDK DILCANEQEE
SGCGDLCSAK VLSGSKAENN CEHETSQFHA NMSNPVKADS PVRQNQTAGV VVQLNKEMLG
PNSVDNESSI SSAEICLKGG LSTIKDQLSG ETPSTSPDIN GLDHETCLSS AEPCPIDNNP
TQNSDSSFYF EYGDWRVLWD PFYSRYYFYN ILTQESTWYP PHGLEDFASH SSTYVPEGLN
ELGSQNKSIP AQEHDQAGGD KHLDGQGQDC YSELSNLSDI LDEERIDQCM VTFTNEAYHT
DSIQSDSSMS EISEMKLEVA RIKKKKRVRR SKSYHLCQDL AGNISNDIAK YWTQRYSLFS
LFDSGIKMDE EGWFSVTPEL IAKHHASRVG ASIVIDCFTG VGGNAIHFAT KCKHVIAIDI
DPQKIDCAQH NATVYGVNDH IDFITGDFIH MSPHLKGETA FMSPPWGGPD YAKVDVYDIT
MLKPCDGYSL FKLGTSIASR VVMFLPRNID QNQLADMCLS VDPPWAVEVE KNFLNGKLKA
ITAYFEQQDG SDASDTNPPN PEYHT
//