CET1_DEBHA
ID CET1_DEBHA Reviewed; 476 AA.
AC Q6BND2;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
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=DEHA2E22726g;
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: 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}.
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DR EMBL; CR382137; CAG88572.2; -; Genomic_DNA.
DR RefSeq; XP_460288.2; XM_460288.1.
DR AlphaFoldDB; Q6BND2; -.
DR SMR; Q6BND2; -.
DR STRING; 4959.XP_460288.2; -.
DR EnsemblFungi; CAG88572; CAG88572; DEHA2E22726g.
DR GeneID; 2903003; -.
DR KEGG; dha:DEHA2E22726g; -.
DR VEuPathDB; FungiDB:DEHA2E22726g; -.
DR eggNOG; ENOG502RZAX; Eukaryota.
DR HOGENOM; CLU_028201_0_0_1; -.
DR InParanoid; Q6BND2; -.
DR OMA; DWVYATI; -.
DR OrthoDB; 1348310at2759; -.
DR Proteomes; UP000000599; Chromosome E.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
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..476
FT /note="mRNA-capping enzyme subunit beta"
FT /id="PRO_0000210115"
FT REGION 1..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 476 AA; 54622 MW; 8FB395B1947EA08A CRC64;
MNVGSILNDE PSPSKKTTND DSGDSVRPDM STYQRHSLVN LLNDPAPNNE LKTKETKKDW
SEDEHSNFRV PVTEPNQQLS PVLRRSSIAD ITNEKDVDIS SSTEHPIEQD KSEKDEDELT
RISKLKSTNK PRRYTEPPIW AQEWIPTSYQ GTANGTPVVN AQESSLSSKR VFDRSSTVNV
DLECSITGVI PPPSVTRTIA EWIYANFTEI PDDQRKYVEL ELKFGTIIDK RAGHRIDINV
STECIFTDNS NTYFDMGVHE VGWNDMCKFL DDLEKSYQDE LRRSPQANSN SPKRKFNILE
SDITDNFYQI TSRNEQPKSI RISKDNLLDP PRYTAINKQR LSSLFIHNPS SMYDLRLSLS
YENPIADNNI DGIIKKNQPT LTRIKKRNSW THRPTVTRFD MTRVLSPRES KNKSGKKIVE
QDQSFEVELE VDTLELFNGF DKFKSGADSI RFEELVEIFV NNARCLNNRV TKLANK
