CET1_KLULA
ID CET1_KLULA Reviewed; 556 AA.
AC Q6CT22;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=KLLA0C16049g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382123; CAH01768.1; -; Genomic_DNA.
DR RefSeq; XP_452917.1; XM_452917.1.
DR AlphaFoldDB; Q6CT22; -.
DR SMR; Q6CT22; -.
DR STRING; 28985.XP_452917.1; -.
DR PRIDE; Q6CT22; -.
DR EnsemblFungi; CAH01768; CAH01768; KLLA0_C16049g.
DR GeneID; 2892078; -.
DR KEGG; kla:KLLA0_C16049g; -.
DR eggNOG; ENOG502RZAX; Eukaryota.
DR HOGENOM; CLU_037653_0_0_1; -.
DR InParanoid; Q6CT22; -.
DR OMA; DWVYATI; -.
DR Proteomes; UP000000598; Chromosome C.
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..556
FT /note="mRNA-capping enzyme subunit beta"
FT /id="PRO_0000210116"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 556 AA; 62743 MW; 64BD4598D3E67D45 CRC64;
MKPSRGLSLT DLVNHDDAPP LNNGDNNVKQ EEVQAENLAT NPASVLAPGP VIVDTLPPVE
APVSTSDTGN TSHTGAAPQT AVTAESDETD TDDEPGEIVF ENTKFRFDDE EQQPQKDKLV
KGTSSEKKDK QVNAATKEIQ LDSKPVKEQS PKTKDEGDIP VEDADKADNK VETQKKENGI
KQEVEPVEQD GKKSVEPAKQ SKEDSKKEKD IFQQKTSNAS VKNNIKKDLK ILSELSSSSL
PKRYNVPPIW ARKWKPTVKA LQAIDSSNLK LDDSILGFIP EDDLTKSVQD WIYATLIAVE
PELRQFIEVE MKYGLIIDPS TSNRVNPPVS SQCVFTDLDS TMKPDVDERV FDEFNRYIKN
LSELNENMGK FNIIDSHASD LSYRVRTHTE RPKFLRMTRD VNTGRIAQFI EKRKISQILL
YSPKDSYDTK ISISLELPVP ENDPPEKYKN HTPTGHRLKK RTSYIHNDSC TRFDITRVEN
KPIRVNNKNE KEPESDTTYE VELEINTPAL LNAFDNIQHD SKEYAAIVRT FLNNGTIVRR
KLSSLSYDIY KGSNKL
