ID   MCE1_ASHGO              Reviewed;         463 AA.
AC   Q755D0;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=AFL107W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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}.
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DR   EMBL; AE016819; AAS53267.1; -; Genomic_DNA.
DR   RefSeq; NP_985443.1; NM_210797.1.
DR   AlphaFoldDB; Q755D0; -.
DR   SMR; Q755D0; -.
DR   STRING; 33169.AAS53267; -.
DR   EnsemblFungi; AAS53267; AAS53267; AGOS_AFL107W.
DR   GeneID; 4621670; -.
DR   KEGG; ago:AGOS_AFL107W; -.
DR   eggNOG; KOG2386; Eukaryota.
DR   HOGENOM; CLU_021710_0_2_1; -.
DR   InParanoid; Q755D0; -.
DR   OMA; KDYYVCE; -.
DR   Proteomes; UP000000591; Chromosome VI.
DR   GO; GO:0031533; C:mRNA cap methyltransferase complex; IEA:EnsemblFungi.
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:0006370; P:7-methylguanosine mRNA capping; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0008033; P:tRNA processing; IEA:EnsemblFungi.
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..463
FT                   /note="mRNA-capping enzyme subunit alpha"
FT                   /id="PRO_0000210098"
FT   REGION          404..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        66
FT                   /note="N6-GMP-lysine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   463 AA;  53647 MW;  9CE70B191A391159 CRC64;
     MDSRDAPEVP GIRQPANVTT DLKMIICKLL NSPKPAKTFP GSQPVSFQHV DIEEKLLAQD
     YYVCEKTDGL RALMLIIMNP VTKEQGCFLI DRENNYYLLN GFRFPRLPRA NRKELLETLQ
     DGTLVDGELV VQTNPATRLR ELRYLMFDCL AINGRALVQS PTSSRLAHLG KEFYKPYYDL
     RAYYPDRCAT FPFKLSMKHM NFSFDLDRVA GSLDKLPHVS DGLIFTAVDT PYTVGGKDST
     LLKWKPEQEN TVDFKMILEI PVVEDDTLPK KDRNRFYYNF DVKPSFHLYI WQGGPDVNTR
     LHDFEQPFSK KELEILHRTY KVFAELQISD EQWAKMKALE QPLNGRIVEC AKDQETGEWK
     FLRFRDDKLN GNHVSVVQKV LESISDSVKL EDLEHMIPRI KARWEERKSK KRTHSSISGP
     MLPPVAETKA PREATQSRYI DDEDWSDEAD DDDEDSLKRA RIE