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O93803 (CET1_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
mRNA-capping enzyme subunit beta

EC=3.1.3.33
Alternative name(s):
Polynucleotide 5'-triphosphatase
mRNA 5'-triphosphatase
Short name=TPase
Gene names
Name:CET1
ORF Names:CaO19.10140, CaO19.2609
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.

Catalytic activity

A 5'-phosphopolynucleotide + H2O = a polynucleotide + phosphate.

Cofactor

Divalent ions By similarity.

Subunit structure

The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an RNA 5'-triphosphatase.

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the fungal TPase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 520520mRNA-capping enzyme subunit beta
PRO_0000210112

Regions

Compositional bias92 – 954Poly-Ser

Natural variations

Natural variant121P → S in strain: IFO 1060.

Sequences

Sequence LengthMass (Da)Tools
O93803 [UniParc].

Last modified September 13, 2005. Version 2.
Checksum: 5C0690F5476C9DEC

FASTA52058,801
        10         20         30         40         50         60 
MNVGSILNDD PPSSGNANGN DDNTKIIKSP TAYHKPSVHE RHSITSMLND TPSDSTPTKK 

        70         80         90        100        110        120 
PEPTISPEFR KPSISSLTSP SVAHKPPPLP PSSSSVGSSE HSSARSSPAI TKRNSIANII 

       130        140        150        160        170        180 
DAYEEPATKT EKKAELNSPK INQSTPVPKL EEHENDTNKV EKVVDSAPEP KPKKEPQPVF 

       190        200        210        220        230        240 
DDQDDDLTKI KKLKQSKKPR RYETPPIWAQ RWVPPNRQKE ETNVDDGNEA ITRLSEKPVF 

       250        260        270        280        290        300 
DYTTTRSVDL ECSITGMIPP SSITRKIAEW VYANFSNVEE KSKRNVELEL KFGKIIDKRS 

       310        320        330        340        350        360 
GNRIDLNVVT ECIFTDHSSV FFDMQVEEVA WKEITKFLDE LEKSFQEGKK GRKFKTLESD 

       370        380        390        400        410        420 
NTDSFYQLGR KGEHPKRIRV TKDNLLSPPR LVAIQKERVA DLYIHNPGSL FDLRLSMSLE 

       430        440        450        460        470        480 
IPVPQGNIES IITKNKPEMV REKKRISYTH PPTITKFDLT RVIGNKTEDK YEVELEAGVM 

       490        500        510        520 
EIFAAIDKIQ KGVDNLRLEE LIEVFLNNAR TLNNRLNKIC 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of the Candida albicans gene for mRNA 5'-triphosphatase: association of mRNA 5'-triphosphatase and mRNA 5'-guanylyltransferase activities is essential for the function of mRNA 5'-capping enzyme in vivo."
Yamada-Okabe T., Mio T., Matsui M., Kashima Y., Arisawa M., Yamada-Okabe H.
FEBS Lett. 435:49-54(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 10259 / CBS 5796 / DSM 5817 / JCM 2078 / NBRC 1060.
[2]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB016242 Genomic DNA. Translation: BAA33965.1.
AACQ01000044 Genomic DNA. Translation: EAK99345.1.
AACQ01000043 Genomic DNA. Translation: EAK99443.1.
RefSeqXP_718274.1. XM_713181.1.
XP_718369.1. XM_713276.1.

3D structure databases

ProteinModelPortalO93803.
ModBaseSearch...

Protein-protein interaction databases

STRING5476.CAL0003365.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3639986.
3640140.
KEGGcal:CaO19.10140.
cal:CaO19.2609.

Organism-specific databases

CGDCAL0003365. CET1.

Phylogenomic databases

eggNOGNOG84753.
KOK01098.

Family and domain databases

Gene3D3.20.100.10. 1 hit.
InterProIPR023577. CYTH-like_domain.
IPR004206. mRNA_capping_enz_bsu_dom.
[Graphical view]
PfamPF02940. mRNA_triPase. 1 hit.
[Graphical view]
SUPFAMSSF55154. mRNA_capping_enz_bsu. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCET1_CANAL
AccessionPrimary (citable) accession number: O93803
Secondary accession number(s): Q5A957
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 13, 2005
Last modified: April 3, 2013
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Candida albicans

Candida albicans: entries and gene names

SIMILARITY comments

Index of protein domains and families