ID   MCE1_YARLI              Reviewed;         391 AA.
AC   Q6C783;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=mRNA-capping enzyme subunit alpha;
DE   AltName: Full=GTP--RNA guanylyltransferase;
DE            Short=GTase;
DE   AltName: Full=mRNA guanylyltransferase;
DE            EC=2.7.7.50 {ECO:0000250|UniProtKB:Q01159};
GN   Name=CEG1; OrderedLocusNames=YALI0E02904g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Second step of mRNA capping. Transfer of the GMP moiety of
CC       GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction
CC       intermediate. {ECO:0000250|UniProtKB:Q01159}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC         end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC         Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC         Evidence={ECO:0000250|UniProtKB:Q01159};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013;
CC         Evidence={ECO:0000250|UniProtKB:Q01159};
CC   -!- SUBUNIT: Heterodimer. The mRNA-capping enzyme is composed of two
CC       separate chains alpha and beta, respectively a mRNA guanylyltransferase
CC       and an mRNA 5'-triphosphate monophosphatase.
CC       {ECO:0000250|UniProtKB:Q01159}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic GTase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382131; CAG79058.1; -; Genomic_DNA.
DR   RefSeq; XP_503479.1; XM_503479.1.
DR   AlphaFoldDB; Q6C783; -.
DR   SMR; Q6C783; -.
DR   STRING; 4952.CAG79058; -.
DR   EnsemblFungi; CAG79058; CAG79058; YALI0_E02904g.
DR   GeneID; 2912122; -.
DR   KEGG; yli:YALI0E02904g; -.
DR   VEuPathDB; FungiDB:YALI0_E02904g; -.
DR   HOGENOM; CLU_021710_0_2_1; -.
DR   InParanoid; Q6C783; -.
DR   OMA; KDYYVCE; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0031533; C:mRNA cap methyltransferase complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004484; F:mRNA guanylyltransferase activity; IBA:GO_Central.
DR   GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; IEA:EnsemblFungi.
DR   GO; GO:0006370; P:7-methylguanosine mRNA capping; IBA:GO_Central.
DR   CDD; cd07895; Adenylation_mRNA_capping; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR001339; mRNA_cap_enzyme_adenylation.
DR   InterPro; IPR017075; mRNA_cap_enzyme_alpha.
DR   InterPro; IPR013846; mRNA_cap_enzyme_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF03919; mRNA_cap_C; 1.
DR   Pfam; PF01331; mRNA_cap_enzyme; 1.
DR   PIRSF; PIRSF036959; mRNA_cap_alpha; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
PE   3: Inferred from homology;
KW   GTP-binding; mRNA capping; mRNA processing; Nucleotide-binding;
KW   Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
FT   CHAIN           1..391
FT                   /note="mRNA-capping enzyme subunit alpha"
FT                   /id="PRO_0000210105"
FT   REGION          363..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        63
FT                   /note="N6-GMP-lysine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   391 AA;  45531 MW;  69B7E0EA6957D9C3 CRC64;
     MSGIVPEIPG EQAPPDAAHQ LKVDVARLLQ KPKLNFPGAQ PVSFARKHIE EELFKRDYYV
     CEKSDGLRCL MYVTWENNPD TGPQQVTYLI TRNNEFFFIP MVHFPSNDGK PLQDTIVDGE
     LVLTKAEPRS LHFLMFDCLA CNKILLTGRP LDKRLGYLNA AISHPLKEYL HKNPEVARDF
     PFSVRVKDMQ FAYNVMNVFA SFPHLPHITD GLIFTCRDHP YVSGTDERIL KWKKQDENSV
     DFLMTMKFPI FEDTNGESWT DYDAKPEITL LVWTGRDGSR PYGELYLTDE EWDNLKALEE
     PLEERVVECI KDDKKRWRYL RFRDDKTNAN YITTVEKVID SIDDPVSEKN LLDAAPKIKE
     LWKERNRRPR DEDRKRVGGD DHDHGAKRAR Q