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Database: UniProt
Entry: A0A0W4ZPW9_PNEJ7
LinkDB: A0A0W4ZPW9_PNEJ7
Original site: A0A0W4ZPW9_PNEJ7 
ID   A0A0W4ZPW9_PNEJ7        Unreviewed;       242 AA.
AC   A0A0W4ZPW9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
GN   ORFNames=T551_01701 {ECO:0000313|EMBL:KTW30418.1};
OS   Pneumocystis jirovecii (strain RU7) (Human pneumocystis pneumonia agent).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Pneumocystomycetes; Pneumocystaceae; Pneumocystis.
OX   NCBI_TaxID=1408657 {ECO:0000313|EMBL:KTW30418.1, ECO:0000313|Proteomes:UP000053447};
RN   [1] {ECO:0000313|Proteomes:UP000053447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RU7 {ECO:0000313|Proteomes:UP000053447};
RX   PubMed=26899007; DOI=10.1038/ncomms10740;
RA   Ma L., Chen Z., Huang D.W., Kutty G., Ishihara M., Wang H., Abouelleil A.,
RA   Bishop L., Davey E., Deng R., Deng X., Fan L., Fantoni G., Fitzgerald M.,
RA   Gogineni E., Goldberg J.M., Handley G., Hu X., Huber C., Jiao X., Jones K.,
RA   Levin J.Z., Liu Y., Macdonald P., Melnikov A., Raley C., Sassi M.,
RA   Sherman B.T., Song X., Sykes S., Tran B., Walsh L., Xia Y., Yang J.,
RA   Young S., Zeng Q., Zheng X., Stephens R., Nusbaum C., Birren B.W.,
RA   Azadi P., Lempicki R.A., Cuomo C.A., Kovacs J.A.;
RT   "Genome analysis of three Pneumocystis species reveals adaptation
RT   mechanisms to life exclusively in mammalian hosts.";
RL   Nat. Commun. 7:10740-10740(2016).
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:KTW30418.1}.
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DR   EMBL; LFWA01000007; KTW30418.1; -; Genomic_DNA.
DR   RefSeq; XP_018229709.1; XM_018373964.1.
DR   AlphaFoldDB; A0A0W4ZPW9; -.
DR   STRING; 1408657.A0A0W4ZPW9; -.
DR   GeneID; 28940219; -.
DR   VEuPathDB; FungiDB:T551_01701; -.
DR   eggNOG; KOG2730; Eukaryota.
DR   OrthoDB; 5473515at2759; -.
DR   Proteomes; UP000053447; 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; 2.
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:UP000053447}.
SQ   SEQUENCE   242 AA;  27706 MW;  305205A60F561A1D CRC64;
     MKKQIQKLQE LKQEEINIGA SIKYDKYGES YIAIGKTIVR HSRSNFPSKL HKYWGQRYRL
     FKHFDKGIWL DEESWYSVTP EPLGRQIATH LSKLYKDNFV LIDGFCGAGG NAIQFALIEK
     IAVIAIDYDP VKLICAKHNA RIYNGDVIFL SPPWGGPSYQ NTEVFNIETM QPYPASLLFR
     AANYMVNNSN KIVMYLPRTS SLASITKLID YPHKVEAHYL KTSGKIKAIC CYFGPLVKQL
     KT
//
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