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Database: UniProt
Entry: A0A1Y2CC76_9BASI
LinkDB: A0A1Y2CC76_9BASI
Original site: A0A1Y2CC76_9BASI 
ID   A0A1Y2CC76_9BASI        Unreviewed;       366 AA.
AC   A0A1Y2CC76;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   08-NOV-2023, entry version 19.
DE   RecName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
GN   ORFNames=BCR35DRAFT_297401 {ECO:0000313|EMBL:ORY44650.1};
OS   Leucosporidium creatinivorum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Leucosporidiales; Leucosporidium.
OX   NCBI_TaxID=106004 {ECO:0000313|EMBL:ORY44650.1, ECO:0000313|Proteomes:UP000193467};
RN   [1] {ECO:0000313|EMBL:ORY44650.1, ECO:0000313|Proteomes:UP000193467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=62-1032 {ECO:0000313|EMBL:ORY44650.1,
RC   ECO:0000313|Proteomes:UP000193467};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORY44650.1}.
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DR   EMBL; MCGR01000125; ORY44650.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2CC76; -.
DR   STRING; 106004.A0A1Y2CC76; -.
DR   InParanoid; A0A1Y2CC76; -.
DR   OrthoDB; 5473515at2759; -.
DR   Proteomes; UP000193467; Unassembled WGS sequence.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent 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   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   Methyltransferase {ECO:0000313|EMBL:ORY44650.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193467};
KW   Transferase {ECO:0000313|EMBL:ORY44650.1}.
FT   REGION          29..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..48
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..273
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   366 AA;  40154 MW;  6F2AA66DB8AE6EEC CRC64;
     MRTGRSHRAD AITNSPFVRA LIRPVSSIIP AAPTPQSPPK PQHLIPTQPA PVVQPEGDTK
     KRKRELEDEG EEEQDALKVV VSYSEDNLPP ELNKYWAQRY RLFSLFDEGC QMDLEGWYSV
     TPELIAAQIA ERCRSSVIVD AFCGVGGNAI QFAFTCEKVI ALDISPVRLA CAKRNAEIYG
     VADRITFILG DWLTWSKDYV KRKAAGQVAA EDEVEVVFLS PPWGGIDYQT LGSTPADATA
     TPQSNKLKTI SHPTVPSTPT PALPPPTPSS AAPPSYPLSA LAPLPGDQLF ALARAMTPHV
     AYYLPRNVDI EEVARLPESC PRRTTEGEVV EGVERVEIEE EWMEWKIKAV TAYYGDLAVG
     ATQEAT
//
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