ID U3IEK4_ANAPP Unreviewed; 888 AA.
AC U3IEK4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 2.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
GN Name=TGS1 {ECO:0000313|Ensembl:ENSAPLP00000005676.2};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000005676.2, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000005676.2, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000005676.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; U3IEK4; -.
DR STRING; 8840.ENSAPLP00000005676; -.
DR Ensembl; ENSAPLT00000006307.2; ENSAPLP00000005676.2; ENSAPLG00000006073.2.
DR GeneTree; ENSGT00390000018056; -.
DR HOGENOM; CLU_016892_0_0_1; -.
DR Proteomes; UP000016666; Chromosome 2.
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:UP000016666}.
FT REGION 122..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..137
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 888 AA; 99157 MW; FC1C38F3A7B4AF5B CRC64;
MVQEPRGVLV AGLLLRAGAA GGIVCLCSRA FVEDRKLYKL GLKGFYVKDD NGSTGEEQAS
EEENRCPNVA FRVDSNHALD LEEIELDSEA ELMKSMGLPL HFGGQSAHRD FVATEKYRKR
SNMKIMKKKK KKKELQQKHR DKMGQECQDQ ANGDHKQSIS DDPAPATEQS EKSKTEIVSE
GNHGSSETLA NEALPGELKE KWEKYWSEYG EGLLWQSWLE KHKEASSLEV LTASEPWNSP
DTKEEWEQHY SELYWYYWEQ FQYWTSQGWT TESSHNDSME VHGVTQEADL SGEKDLISLE
AECSEVLSLE LSPSHTRGEE TLTSSAEPHN EIISGICNLN LNLDEVEQSS APPAVTHEDP
QEHGSSNSES QCLCASSQKE PCDGGTRKRS ASCENKSINQ SGSQGSCNSC SSNDKEQLLL
PDRNEDEEEE PPENRVAKVK RSHELDVDEN PVEDPEETCS ILGFKCGTGQ KYGGIPDFTH
RSVQYLEKKA KLKSRFLDMR KPRKSKNTHI FFTEEPETSS QKNKTLKKVE EFLKQVNTPV
EEATSQKASP QDKVEGSSTS SDSEDQDSVT TTRSVRFSIQ NPEPLPSSVG GGEPGTSKPE
EEVKVITANS ADGQGTRKTE CGSGRVLVPM DIPDYLREET EDVSPVVDEK NTTKKKEKRR
KRKNKIALGS IPAEIAADPE LVKYWAQRYR LFSRFDEGIK LDREGWFSVT PEKIAEHIAV
RVAQAFNCDT VVDAFCGVGG NAIQFALTSK RVIAIDIDPE KLSLARSNAE VYGVADKIEF
MCGDFMVLAA DLKADVVFLS PPWGGPDYAT AEIFDIQTMI CPDGFEIFRL SKKITNNIVY
FLPRNADINQ IASLAGPGGK VEIEQNFLNN KLKTITAYFG DLIRRDLT
//
