CET1_CANGA
ID CET1_CANGA Reviewed; 602 AA.
AC Q6FUZ2;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 103.
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=CAGL0E06050g;
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: 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; CR380951; CAG58871.1; -; Genomic_DNA.
DR RefSeq; XP_445952.1; XM_445952.1.
DR AlphaFoldDB; Q6FUZ2; -.
DR SMR; Q6FUZ2; -.
DR STRING; 5478.XP_445952.1; -.
DR EnsemblFungi; CAG58871; CAG58871; CAGL0E06050g.
DR GeneID; 2887417; -.
DR KEGG; cgr:CAGL0E06050g; -.
DR CGD; CAL0128976; CAGL0E06050g.
DR VEuPathDB; FungiDB:CAGL0E06050g; -.
DR eggNOG; ENOG502RZAX; Eukaryota.
DR HOGENOM; CLU_037653_0_0_1; -.
DR InParanoid; Q6FUZ2; -.
DR OMA; FHESTAT; -.
DR Proteomes; UP000002428; Chromosome E.
DR GO; GO:0031533; C:mRNA cap methyltransferase complex; IEA:EnsemblFungi.
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 GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:EnsemblFungi.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
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..602
FT /note="mRNA-capping enzyme subunit beta"
FT /id="PRO_0000210113"
FT REGION 1..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 276
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 602 AA; 68350 MW; A58C2F3412D70C4F CRC64;
MSEHHSKRAL SLDDLVNHDE NDKSKLQKLA DNESSVRSDD NRPGAIENIV NGNNSNSDLN
SNGVIEEDTD TDDDVGGEFT FDNGITFDYD KQDRFSPEKK RIQARKKDTS KTTPSISNES
PSNSKESSVP VDPLSSNISA TDRKDSSEEK PDLTGPELVK EPDTNEYKRP SIQSITNAED
TTYNDHKAAG MEKTSNKHSL PNILSDSIDE TVTEEHKPKT ETEQTITEYQ QENKQKDNVN
ESNSEETHDI KNDNMNQVEK IFQEKTSTLS KKNSVKKDLE LLNEISASSK PNKYKNTPIW
AQKWKPTVKA LQNIDTNDFK IDNSILDIIP DDDLTKSVQD WVYATLYSID PDLRPFIELE
MKFGVLLESK SPDRVNPPVS SQAVYTDMDA HLTPNVDETV FKELSKYIQS LSEITENAGK
FNVIEAQTKD AVYRVGTSTQ RPRFLRMSSD VKTGRIGAFI EKRHISQLLI YSPKDSYDVK
LSINLELPVP ENDPPEKYQH QTPVSERTKE RVSYIHNDSC TRFDITKVQN HNKGIKSNDV
EITHEIELEI NTPALIKAFD NIMTDSKEYA TLIRTFLNNG TIVRRKLSSL SYEIFEGQKK
IQ