ID H0X788_OTOGA Unreviewed; 853 AA.
AC H0X788;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
GN Name=TGS1 {ECO:0000313|Ensembl:ENSOGAP00000011264.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000011264.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000011264.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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 EMBL; AAQR03104796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03104797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03104798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03104799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03104800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03104801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0X788; -.
DR STRING; 30611.ENSOGAP00000011264; -.
DR Ensembl; ENSOGAT00000012577.2; ENSOGAP00000011264.2; ENSOGAG00000012572.2.
DR eggNOG; KOG2730; Eukaryota.
DR GeneTree; ENSGT00390000018056; -.
DR HOGENOM; CLU_016892_0_0_1; -.
DR InParanoid; H0X788; -.
DR OMA; GWETYWA; -.
DR TreeFam; TF313065; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0071164; F:RNA trimethylguanosine synthase activity; IEA:Ensembl.
DR GO; GO:0009452; P:7-methylguanosine RNA capping; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 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 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005225}.
FT REGION 58..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 853 AA; 96016 MW; 074B0D28BEA31D6C CRC64;
MCCEKWSRVA EMLLFIEDRG EECKILCLCS RAFVEDRKLC NLGLKGYYVK CSGNNTGDSA
AEEEEGGQSQ GAAESCDSKG LDESELDSEA ELMRSMGLPL QFGGIAAHKN FEVSMNTRNK
VKRKKKKKKL QTKYLNEIMQ ESWRKYEEDD ILDSDDPSSV EQYENTRACK LQSKKDIETE
NLPVENTLLP KLEITEKWEK YWNEYGGGLL WQSWQEKHPD QTLSAEPWNF PDTKEEWEQH
YSQLYWYYLE QFQYWEAQGW TFDGSQGCDT DICASKTEVE SKKDENCTKV DLVSFPSSPV
MVENDSSDAS DKDHNEILDG ISSITLNAEE IEQGHLDSSV SCAGSQQHSD VVSSRIECPA
SGQSEPSNSR TKDNHLPGNS STDHPAQESQ ESSGANTSRD RPHTTCVDGE ESDDDPPEHK
PAKLKRSHEL DIDEIPDPDF DDSGSLLGFK HGSGQKYGGI PNFSHRQVRY LEKNVKRKSK
YLDMRKQIKM KNKHIFFTEE SEKPFFKKSK ALSKVEKFLM WVNEPVDEEA SQESFSHDNV
EDTCTSGNSE EQDVSVKKGG DPLETSNPEP ERCQATSSAG ELETEINEGA SLGAAVPEEK
DCVTRDPAAS LQTAEGRKKK KEKKNRRVNG LPPEIASVPE LVKYWAQRYR LFSRFDDGIK
LDREGWFSVT PEKIAEHIAG RISQSFKCDV IVDAFCGVGG NTIQFALTGK RVIAIDIDPV
KIDLARNNAE VYGVADKIEF ICGDFLLLAS CLKADVVFLS PPWGGPDYAT AKTFDIRTMM
SPDGYPFFEI FRLSQKITNN IIYFLPRNAD VDQVASLAGP GGQVEIEQNF LNNKLKTITA
YFGDLIRRPA SET
//
