MCE1_DEBHA
ID MCE1_DEBHA Reviewed; 458 AA.
AC Q6BT58;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 96.
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=DEHA2D03322g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382136; CAG86747.2; -; Genomic_DNA.
DR RefSeq; XP_458612.2; XM_458612.1.
DR AlphaFoldDB; Q6BT58; -.
DR SMR; Q6BT58; -.
DR STRING; 4959.XP_458612.2; -.
DR PRIDE; Q6BT58; -.
DR EnsemblFungi; CAG86747; CAG86747; DEHA2D03322g.
DR GeneID; 2901066; -.
DR KEGG; dha:DEHA2D03322g; -.
DR eggNOG; KOG2386; Eukaryota.
DR HOGENOM; CLU_021710_0_2_1; -.
DR InParanoid; Q6BT58; -.
DR OMA; KDYYVCE; -.
DR OrthoDB; 1544021at2759; -.
DR Proteomes; UP000000599; Chromosome D.
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; IEA:UniProtKB-EC.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
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..458
FT /note="mRNA-capping enzyme subunit alpha"
FT /id="PRO_0000210101"
FT REGION 387..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..449
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 458 AA; 53123 MW; CC0BB8061AF0739A CRC64;
MIQLEERDMP EIPGTILDRN ETQELRLMVA DLLGRRNPSF PGAQPISFER YHLNDTLMNK
DYYVCEKSDG LRCLLFIINH PERGEGVFLI TRENDYYYIP NIHFPLTNNE EKGKTYHHGT
LLDGELVLET KNVPEPVLRF CIFDALAING KDITKRHLPK RLGYITEQVM KPFDNFKRKN
PEIVNAPDFP FKVSFKLMTS SYHADDVLSK MDQLFHESDG LIFTCAETPY VFGTDSTLLK
WKPAHENTVD YKMEMIFKKF QDPDLDPRDP DSTYTDYDSK PELIKLRVWK GGADYEDFTK
LSLENEDWEK LKNLRQPLQG RIVECRKKLS DPGFWEMLRF RNDKSNGNHI SVVDKILHSI
QDGVSEEELI EACPKIGKAW KKRIYEKSQG SRSSYSETGR SHPEPNREDE PASKRTKIDM
EEPEPNGFGG STTNHQNASK QNSGEFQDIP TYEDSDDE
