MCE1_CANGA
ID MCE1_CANGA Reviewed; 449 AA.
AC Q6FQ31;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=CAGL0I09570g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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}.
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DR EMBL; CR380955; CAG60600.1; -; Genomic_DNA.
DR RefSeq; XP_447663.1; XM_447663.1.
DR AlphaFoldDB; Q6FQ31; -.
DR SMR; Q6FQ31; -.
DR STRING; 5478.XP_447663.1; -.
DR EnsemblFungi; CAG60600; CAG60600; CAGL0I09570g.
DR GeneID; 2888936; -.
DR KEGG; cgr:CAGL0I09570g; -.
DR CGD; CAL0132534; CAGL0I09570g.
DR VEuPathDB; FungiDB:CAGL0I09570g; -.
DR eggNOG; KOG2386; Eukaryota.
DR HOGENOM; CLU_021710_0_2_1; -.
DR InParanoid; Q6FQ31; -.
DR OMA; KDYYVCE; -.
DR Proteomes; UP000002428; Chromosome I.
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; IEA:UniProtKB-EC.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
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..449
FT /note="mRNA-capping enzyme subunit alpha"
FT /id="PRO_0000210100"
FT REGION 405..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 66
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 449 AA; 51664 MW; 5537EF3CF6F56E7D CRC64;
MDARISPEIP GIIQPGNVTQ DLKMLVCKLL NSPKPSKTFP GSQPVSFQHS DIRDKLVAQD
YYVCEKTDGL RVLMLVVVNP ITGEQGCFMI DRENNYYLVN GFHFPRLPQK KKEELLETSQ
NGTLIDGELV IQKNPMTKLQ ELRYLMFDCL AINGRSLVQS PTSSRLAHLG KEFYKPYYDL
RSIYPDKCAT FPFKLSMKHM DFSYSLVKVA NSLDKLPHLS DGLIFTPVRT PYAVGGKDSL
LLKWKPEQEN SVDFKLILEI PMTEDNSVAK KDPRRWYYNY DAKPTFALYV WQGGSDVNTK
LQNFEQPFDK REMQVLEKTY KRFAELSISD EQWQELKNLE EPLNGRIVEC TKDPETGSWT
MLRFRDDKLN GNHTSVVQKV LESISDSVTI DDLAESVPEI KSAWDERKNG AYQHHSSSFS
ESRQQPKAEP VAEKKQTEPK YVDDDDWSD
