MCE1_KLULA
ID MCE1_KLULA Reviewed; 466 AA.
AC Q6CWR0;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-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=KLLA0B02200g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382122; CAH02022.1; -; Genomic_DNA.
DR RefSeq; XP_451629.1; XM_451629.1.
DR AlphaFoldDB; Q6CWR0; -.
DR SMR; Q6CWR0; -.
DR STRING; 28985.XP_451629.1; -.
DR PRIDE; Q6CWR0; -.
DR EnsemblFungi; CAH02022; CAH02022; KLLA0_B02200g.
DR GeneID; 2897021; -.
DR KEGG; kla:KLLA0_B02200g; -.
DR eggNOG; KOG2386; Eukaryota.
DR HOGENOM; CLU_021710_0_2_1; -.
DR InParanoid; Q6CWR0; -.
DR OMA; KDYYVCE; -.
DR Proteomes; UP000000598; Chromosome B.
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..466
FT /note="mRNA-capping enzyme subunit alpha"
FT /id="PRO_0000210102"
FT REGION 408..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 67
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 466 AA; 53980 MW; 7320E55CA86AA7B9 CRC64;
MDNNRVAPEI PGLRQPGQIT NDIRMLMCKL LNSAKPANTF PGSQPVSFHL ADIEEKLLAQ
DYYVCEKTDG LRALMLIMVN PVTKEQGCFM IDRENNYYMV NGFRFPCLPR ANKKELLETL
QDGTLIDGEL VMQTNPVTKL KELRYLMFDC LAVNGRSLVQ SPTSSRLAHL GKEFFKPYYD
LRSYFPDRCS TFPFKISMKH MNFSYDLAKV AKTLDSLPHV SDGLIFTPVQ AAYHIGGKDS
YLLKWKPEVE NTVDFKLIIE PPVVEDKSLP KSDKNRFYYN YDVKPLFHLY VWQGGNDVNN
RIQDFEQPFT KSDLELLERT YRKFAEIEID DKQWNELKAM EEPLNGRIVE CSKDQESGAW
KLLRFRDDKL NGNHVSVVQK VLESIGDSVS LDDLEQVVDE MRSRWKEREQ GLKNAQKQFN
HQASARSSLS QQHSTEPEQS QDQPKYVDDD DDNWSDDEPD TKRQKI
