CET1_CANAL
ID CET1_CANAL Reviewed; 520 AA.
AC O93803; A0A1D8PS47; Q5A957;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 127.
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=CAALFM_CR02090CA;
GN ORFNames=CaO19.10140, CaO19.2609;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10259 / CBS 5796 / DSM 5817 / JCM 2078 / NBRC 1060;
RX PubMed=9755857; DOI=10.1016/s0014-5793(98)01037-0;
RA Yamada-Okabe T., Mio T., Matsui M., Kashima Y., Arisawa M.,
RA Yamada-Okabe H.;
RT "Isolation and characterization of the Candida albicans gene for mRNA 5'-
RT triphosphatase: association of mRNA 5'-triphosphatase and mRNA 5'-
RT guanylyltransferase activities is essential for the function of mRNA 5'-
RT capping enzyme in vivo.";
RL FEBS Lett. 435:49-54(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; AB016242; BAA33965.1; -; Genomic_DNA.
DR EMBL; CP017630; AOW30959.1; -; Genomic_DNA.
DR RefSeq; XP_718274.1; XM_713181.1.
DR AlphaFoldDB; O93803; -.
DR SMR; O93803; -.
DR BioGRID; 1223080; 1.
DR STRING; 237561.O93803; -.
DR PRIDE; O93803; -.
DR GeneID; 3640140; -.
DR KEGG; cal:CAALFM_CR02090CA; -.
DR CGD; CAL0000199068; CET1.
DR VEuPathDB; FungiDB:CR_02090C_A; -.
DR eggNOG; ENOG502RZAX; Eukaryota.
DR HOGENOM; CLU_028201_0_0_1; -.
DR InParanoid; O93803; -.
DR OMA; DWVYATI; -.
DR OrthoDB; 1348310at2759; -.
DR BRENDA; 3.6.1.74; 1096.
DR PRO; PR:O93803; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0031533; C:mRNA cap methyltransferase complex; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:CGD.
DR GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IDA:CGD.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IDA:CGD.
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..520
FT /note="mRNA-capping enzyme subunit beta"
FT /id="PRO_0000210112"
FT REGION 1..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 12
FT /note="P -> S (in strain: IFO 1060)"
SQ SEQUENCE 520 AA; 58801 MW; 5C0690F5476C9DEC CRC64;
MNVGSILNDD PPSSGNANGN DDNTKIIKSP TAYHKPSVHE RHSITSMLND TPSDSTPTKK
PEPTISPEFR KPSISSLTSP SVAHKPPPLP PSSSSVGSSE HSSARSSPAI TKRNSIANII
DAYEEPATKT EKKAELNSPK INQSTPVPKL EEHENDTNKV EKVVDSAPEP KPKKEPQPVF
DDQDDDLTKI KKLKQSKKPR RYETPPIWAQ RWVPPNRQKE ETNVDDGNEA ITRLSEKPVF
DYTTTRSVDL ECSITGMIPP SSITRKIAEW VYANFSNVEE KSKRNVELEL KFGKIIDKRS
GNRIDLNVVT ECIFTDHSSV FFDMQVEEVA WKEITKFLDE LEKSFQEGKK GRKFKTLESD
NTDSFYQLGR KGEHPKRIRV TKDNLLSPPR LVAIQKERVA DLYIHNPGSL FDLRLSMSLE
IPVPQGNIES IITKNKPEMV REKKRISYTH PPTITKFDLT RVIGNKTEDK YEVELEAGVM
EIFAAIDKIQ KGVDNLRLEE LIEVFLNNAR TLNNRLNKIC
