CET1_ASHGO
ID CET1_ASHGO Reviewed; 478 AA.
AC Q755F7;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 109.
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=AFL134W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 59 AND 89-90.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53240.2; -; Genomic_DNA.
DR RefSeq; NP_985416.2; NM_210770.2.
DR AlphaFoldDB; Q755F7; -.
DR SMR; Q755F7; -.
DR STRING; 33169.AAS53240; -.
DR EnsemblFungi; AAS53240; AAS53240; AGOS_AFL134W.
DR GeneID; 4621643; -.
DR KEGG; ago:AGOS_AFL134W; -.
DR eggNOG; ENOG502RZAX; Eukaryota.
DR HOGENOM; CLU_037653_0_0_1; -.
DR InParanoid; Q755F7; -.
DR OMA; DWVYATI; -.
DR Proteomes; UP000000591; Chromosome VI.
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 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..478
FT /note="mRNA-capping enzyme subunit beta"
FT /id="PRO_0000210111"
FT REGION 1..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 478 AA; 53963 MW; 8F55B7A9F6D80E2D CRC64;
MSSEKQEGSP RRVLSLSDLV NREDSKDASG NTAGAALKPL SNDEVRRRLA HEDYSSNTAS
QVDDETDTDD GLGEVAFDRA DFRFDFEGQE RSGGRASGEA EAESGGPGHE KATQQPSDAI
ATSPDRESTE PRAMDIFEER ASLESKKNNL RKDLRVLNEI ASTARPGRYK VAPIWAQKWK
PTVRALQNVN SKDLMKIDVS FTQVIPDDDL TKSVQDWVYA TLLSIPPEQR QYVEVEMKFG
ILMDRSSDSQ RVTPPVSSQT VYMEADARMK PDVDERVFVE LNRYVKGISE LTENTGKFNI
IESHNKDEMY RAGINTQRPR FLRMSKDVKT GRVGEFIEKR RISQLLLFSP KDSYDVKISI
NVELPVPEND PPEKYMGQAP LNSRTKERIS YIHNDSCTRI DITKVTNHNK GKRDDAEVTH
EIELELNSQA LLAAFDKIAQ DSKDYATIVR TFLNNGTIIR RKLTSLSYEI FEGGKKVV
