ID A0A0D3FJG8_9ORYZ Unreviewed; 690 AA.
AC A0A0D3FJG8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART03G20430.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART03G20430.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART03G20430.1};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART03G20430.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) 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 AlphaFoldDB; A0A0D3FJG8; -.
DR STRING; 65489.A0A0D3FJG8; -.
DR PaxDb; 65489-OBART03G20430-1; -.
DR EnsemblPlants; OBART03G20430.1; OBART03G20430.1; OBART03G20430.
DR Gramene; OBART03G20430.1; OBART03G20430.1; OBART03G20430.
DR eggNOG; KOG2730; Eukaryota.
DR HOGENOM; CLU_024358_0_0_1; -.
DR Proteomes; UP000026960; 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:UP000026960}.
FT DOMAIN 314..342
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 264..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 690 AA; 77126 MW; B949CABC7FBD2096 CRC64;
MPGDAEDLPP AITKLGRHFR LTEAHIWDGW YAAGADVSHR SWRSDDIDSG GCCQTDKVQN
KPTKQTDEGD LFVEDLELSN LMGSLGLPVS FSTSKEKKNA PNKVKKNGRR VSYEAANTLI
DDDSRTCTGT KETESIVQLM ACVEQTNPCS SSRITVGYNE VCQGDIEKMD KDIVYANEQE
ESGDLCSSKV LSSSKAEDNY EHETCQFHAN MNNPVKADSP VRENETAEVV LQLNKEMLGQ
NSVDNESRFS SAEICMEGGL STIKDQLSGE TPSTSHDNKD VDHETCQSSA EPSPVDNNPA
QKSDSSFYFE YGDWRVLWDP FYSRYYFYNI LTQESTWYPP HGLEDFASHS NTCIPEDQDE
FGSQNKSTPA QEHDQAGGDK HLDEQGQACY SELSNLSDIP DGERINQCMV TFTDEARHTD
NIHHQNDSSM SEISEMNQEI GRTKKKKRVR RSKSYHSCQD LAGNISNDIA KYWAQRYSLF
SLFDSGIKMD EEGWFSVTPE LIAKHHASRV GAGIVIDCFT GVGGNAIHFA NKCRHVIAID
IDPQKIDCAQ HNATVYGVHD HIDFIRGDFI HVAPRLKGET VFMSPPWGGP DYAKVDVYDI
KTMLKPCDGY SLFKLGTSIA SRVVMFLPRN IDQNQLADMC LSVDPPWAVE VEKNFLNGKL
KAITAYFEQQ DGSDVQDASD TNPQNPEYHA
//
