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Database: UniProt
Entry: A0A196SMU2_BLAHN
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ID   A0A196SMU2_BLAHN        Unreviewed;       434 AA.
AC   A0A196SMU2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
GN   ORFNames=AV274_0715 {ECO:0000313|EMBL:OAO17576.1};
OS   Blastocystis sp. subtype 1 (strain ATCC 50177 / NandII).
OC   Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC   Blastocystis.
OX   NCBI_TaxID=478820 {ECO:0000313|EMBL:OAO17576.1, ECO:0000313|Proteomes:UP000078348};
RN   [1] {ECO:0000313|EMBL:OAO17576.1, ECO:0000313|Proteomes:UP000078348}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50177 / NandII {ECO:0000313|Proteomes:UP000078348};
RA   Gentekaki E., Curtis B., Stairs C., Eme L., Herman E., Klimes V.,
RA   Arias M.C., Elias M., Hilliou F., Klute M., Malik S.-B., Pightling A.,
RA   Rachubinski R., Salas D., Schlacht A., Suga H., Archibald J., Ball S.G.,
RA   Clark G., Dacks J., Van Der Giezen M., Tsaousis A., Roger A.;
RT   "Nuclear genome of Blastocystis sp. subtype 1 NandII.";
RL   Submitted (MAY-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:OAO17576.1}.
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DR   EMBL; LXWW01000025; OAO17576.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A196SMU2; -.
DR   STRING; 478820.A0A196SMU2; -.
DR   OrthoDB; 5473515at2759; -.
DR   Proteomes; UP000078348; Unassembled WGS sequence.
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   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:UP000078348}.
FT   REGION          51..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          89..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   434 AA;  48676 MW;  18A1A4CB7D2D6360 CRC64;
     MELVDAFCHS QFYRFEESCS TVDTDTSPTV RHTINFMPYR HLYKELEAQY CDPGESSEEP
     STNEMSAEEQ NSHRSAVIDA MIARMEQGLP AEFGTKRRTS KPHKANRSQK EKKLTAIPHT
     AFQNEMYIQA LINKEWVPCV VLDMEVPNET SEGYQYSYLV QPLQSISNAS ETIHLTPDDV
     SFLSPEQEAR LFQASFSTQP HQPLIQLLVT ETAARTPKSS LPPSVRKYYW QRYRLFSRWD
     DGIQFDEEGL FSVTPEALAL HTAVRCACDV VVDAFAGIGG NTIQLARTCR RVVAIDTCLE
     RLKMLQHNSA LYGVAHRIDA VCADCRTVLP ALKADVVVLA PPWGGVNYSK KEVFRLEDLP
     AGLDGTALFA MARTVTRNVV MLLPRNVDRR QVAELGEEGE VVELVEGMVD GVVKMVIAYF
     GDLAASPQTL NMLM
//
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