CET1_YARLI
ID CET1_YARLI Reviewed; 386 AA.
AC Q6C2H4;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=mRNA-capping enzyme subunit beta;
DE EC=3.6.1.74 {ECO:0000250|UniProtKB:O13297};
DE AltName: Full=mRNA 5'-phosphatase;
DE AltName: Full=mRNA 5'-triphosphate monophosphatase;
GN Name=CET1; OrderedLocusNames=YALI0F07865g;
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: First step of mRNA capping. Converts the 5'-triphosphate end
CC of a nascent mRNA chain into a diphosphate end.
CC {ECO:0000250|UniProtKB:O13297}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end
CC diphospho-ribonucleoside in mRNA + H(+) + phosphate;
CC Xref=Rhea:RHEA:67004, Rhea:RHEA-COMP:17164, Rhea:RHEA-COMP:17165,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167618; EC=3.6.1.74;
CC Evidence={ECO:0000250|UniProtKB:O13297};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67005;
CC Evidence={ECO:0000250|UniProtKB:O13297};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O13297};
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:O13297}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the fungal TPase 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; CR382132; CAG77945.1; -; Genomic_DNA.
DR RefSeq; XP_505138.1; XM_505138.1.
DR AlphaFoldDB; Q6C2H4; -.
DR SMR; Q6C2H4; -.
DR STRING; 4952.CAG77945; -.
DR EnsemblFungi; CAG77945; CAG77945; YALI0_F07865g.
DR GeneID; 2908374; -.
DR KEGG; yli:YALI0F07865g; -.
DR VEuPathDB; FungiDB:YALI0_F07865g; -.
DR HOGENOM; CLU_028201_0_0_1; -.
DR InParanoid; Q6C2H4; -.
DR OMA; HHMIMTR; -.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0031533; C:mRNA cap methyltransferase complex; IBA:GO_Central.
DR GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IBA:GO_Central.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IBA:GO_Central.
DR GO; GO:0098507; P:polynucleotide 5' dephosphorylation; IBA:GO_Central.
DR CDD; cd07470; CYTH-like_mRNA_RTPase; 1.
DR Gene3D; 3.20.100.10; -; 1.
DR InterPro; IPR040343; Cet1/Ctl1.
DR InterPro; IPR033469; CYTH-like_dom_sf.
DR InterPro; IPR004206; mRNA_triPase_Cet1.
DR InterPro; IPR037009; mRNA_triPase_Cet1_sf.
DR PANTHER; PTHR28118; PTHR28118; 1.
DR Pfam; PF02940; mRNA_triPase; 1.
DR SUPFAM; SSF55154; SSF55154; 1.
PE 3: Inferred from homology;
KW Hydrolase; mRNA capping; mRNA processing; Nucleus; Reference proteome.
FT CHAIN 1..386
FT /note="mRNA-capping enzyme subunit beta"
FT /id="PRO_0000210118"
FT REGION 1..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 386 AA; 43288 MW; 09186169A060433C CRC64;
MDIGKMINDD NGSDSRRTSV KSLLNSPPTG LPSSDDRPDS KASSTSDLAQ QLTNEMESGE
DDDDEDAAAA VNHKPRRYSR PPIWATKWQG TGRHAERDHR PPPHRQDRRD PRMERQSGGS
RALPASSTTT ITGCPPSISG IKPFESVTRT VTSWLHAHLS TMSPEQLQTV ELEAKIGTIQ
HKKAGADRAR LDLPIVTEAV VNQQYVQAQC SFSSQLPESL LEEAKRILDA ADPKFIKSTE
HTIHRDEIYE GQQDKGNLRI TRDDVTGRQV AKIRKKAIAH IMIHCPTDPF DIRLSLATES
PTDDVPQGVC RTRRKDRISY LYDGFRADLT KVSGSSMSSE LEMEADSHKL IGYFTDRNDP
HNMDKVEELL QILLDSMRYV NRRLKA
