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Database: UniProt
Entry: G4VMQ5_SCHMA
LinkDB: G4VMQ5_SCHMA
Original site: G4VMQ5_SCHMA 
ID   G4VMQ5_SCHMA            Unreviewed;       430 AA.
AC   G4VMQ5;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183 {ECO:0000313|Proteomes:UP000008854, ECO:0000313|WBParaSite:Smp_010800.1};
RN   [1] {ECO:0000313|Proteomes:UP000008854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Puerto Rican {ECO:0000313|Proteomes:UP000008854};
RX   PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA   Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA   De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA   Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA   Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA   Zerlotini A., Dunne D.W., Berriman M.;
RT   "A systematically improved high quality genome and transcriptome of the
RT   human blood fluke Schistosoma mansoni.";
RL   PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
RN   [2] {ECO:0000313|WBParaSite:Smp_010800.1}
RP   IDENTIFICATION.
RC   STRAIN=Puerto Rican {ECO:0000313|WBParaSite:Smp_010800.1};
RG   WormBaseParasite;
RL   Submitted (DEC-2018) 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   RefSeq; XP_018653541.1; XM_018798617.1.
DR   AlphaFoldDB; G4VMQ5; -.
DR   STRING; 6183.G4VMQ5; -.
DR   EnsemblMetazoa; Smp_010800.1; Smp_010800.1; Smp_010800.
DR   GeneID; 8353570; -.
DR   KEGG; smm:Smp_010800; -.
DR   WBParaSite; Smp_010800.1; Smp_010800.1; Smp_010800.
DR   CTD; 8353570; -.
DR   eggNOG; KOG2730; Eukaryota.
DR   HOGENOM; CLU_638296_0_0_1; -.
DR   InParanoid; G4VMQ5; -.
DR   OrthoDB; 5473515at2759; -.
DR   PhylomeDB; G4VMQ5; -.
DR   Proteomes; UP000008854; Unassembled WGS sequence.
DR   ExpressionAtlas; G4VMQ5; baseline.
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   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; 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008854}.
FT   REGION          14..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   430 AA;  48403 MW;  DEBC5B8E23060892 CRC64;
     MFALHSRDVI DSLSDVSSSD DEDEITKSKV SSPDDEIAVP SQRFAPVSLT EVLRKRNKVA
     RVLYSSSKIL PKYWKRRYDL FERFDEGVQL DEESWYSITP EAIACHQAKT CSCDLLVDAF
     AGVGGNTIQF ARTCRLVLAI ENCFPRLLML QINAQIYGVL SNIMLVCGDV EKILSSLRIV
     LFSSTSSTID DDTNMPNSEN QYGSDNLEAT FICSPEKNQS TLLSGNNEQS VDFLSETSIN
     VEDNISKSNF NSSERHSSSP SSLLANTETT LEVNPELNGN ETLEKPTNST FNSLIDIIFM
     SPPWGGPDYI GKVFPPGSTS WNQRKRRHWL YDLKEMEPIK NLEDIPFLNK ALNISRHVCN
     KILIYLPRNS SIGQLIQMSW PLGNCEYIAD CCSCKQYLNV HIETYCLRGR QLALGLYLGS
     FPCFEENIIV
//
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