ID   CET1_CANAL              Reviewed;         520 AA.
AC   O93803; Q5A957;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   16-JUN-2009, entry version 47.
DE   RecName: Full=mRNA-capping enzyme subunit beta;
DE            EC=3.1.3.33;
DE   AltName: Full=Polynucleotide 5'-triphosphatase;
DE   AltName: Full=mRNA 5'-triphosphatase;
DE            Short=TPase;
GN   Name=CET1; ORFNames=CaO19.2609, CaO19.10140;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10259 / CBS 5796 / IFO 1060 / JCM 2078;
RX   MEDLINE=98427288; 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
RT   5'-triphosphatase: association of mRNA 5'-triphosphatase and mRNA 5'-
RT   guanylyltransferase activities is essential for the function of mRNA
RT   5'-capping enzyme in vivo.";
RL   FEBS Lett. 435:49-54(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
RA   Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
RA   Davis R.W., Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
CC   -!- FUNCTION: First step of mRNA capping. Converts the 5'-triphosphate
CC       end of a nascent mRNA chain into a diphosphate end.
CC   -!- CATALYTIC ACTIVITY: A 5'-phosphopolynucleotide + H(2)O = a
CC       polynucleotide + phosphate.
CC   -!- COFACTOR: Divalent ions (By similarity).
CC   -!- SUBUNIT: The mRNA-capping enzyme is composed of two separate
CC       chains alpha and beta, respectively a mRNA guanylyltransferase and
CC       an RNA 5'-triphosphatase.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the fungal TPase family.
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DR   EMBL; AB016242; BAA33965.1; -; Genomic_DNA.
DR   EMBL; AACQ01000044; EAK99345.1; -; Genomic_DNA.
DR   EMBL; AACQ01000043; EAK99443.1; -; Genomic_DNA.
DR   RefSeq; XP_718274.1; -.
DR   RefSeq; XP_718369.1; -.
DR   HSSP; O13297; 1D8I.
DR   GeneID; 3639986; -.
DR   GeneID; 3640140; -.
DR   KEGG; cal:CaO19.10140; -.
DR   KEGG; cal:CaO19.2609; -.
DR   CGD; CAL0003365; CET1.
DR   OMA; O93803; ECIFTDH.
DR   BRENDA; 3.1.3.33; 1124.
DR   GO; GO:0031533; C:mRNA capping enzyme complex; IEA:InterPro.
DR   GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IEA:InterPro.
DR   GO; GO:0006370; P:mRNA capping; IEA:UniProtKB-KW.
DR   InterPro; IPR004206; mRNA_capping_enz_bsu.
DR   Gene3D; G3DSA:3.20.100.10; mRNA_capping_enz_bsu; 1.
DR   Pfam; PF02940; mRNA_triPase; 1.
PE   3: Inferred from homology;
KW   Hydrolase; mRNA capping; mRNA processing; Nucleus.
FT   CHAIN         1    520       mRNA-capping enzyme subunit beta.
FT                                /FTId=PRO_0000210112.
FT   COMPBIAS     92     95       Poly-Ser.
FT   VARIANT      12     12       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
//