O93803 (CET1_CANAL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	CaO19.2609, CaO19.10140

Organism

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

Taxonomic identifier

237561 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	mRNA capping mRNA processing
Cellular component	Nucleus
Molecular function	Hydrolase
Gene Ontology (GO)
Biological process	cellular response to drug Inferred from mutant phenotype. Source: CGD mRNA capping Inferred from direct assay Ref.1. Source: CGD
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATPase activity Inferred from direct assay. Source: CGD polynucleotide 5'-phosphatase activity Inferred from direct assay Ref.1. Source: CGD transferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 520	520	mRNA-capping enzyme subunit beta		PRO_0000210112
Regions
	Compositional bias	92 – 95	4	Poly-Ser
Natural variations
	Natural variant	12	1	P → S in strain: IFO 1060.

Sequences

	Sequence		Length	Mass (Da)
	O93803 [UniParc]. Last modified September 13, 2005. Version 2. Checksum: 5C0690F5476C9DEC	FASTA	520	58,801
	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

References

	« Hide 'large scale' referencesShow '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: 9755857] [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: 15123810] [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.
RefSeq	XP_718274.1. XM_713181.1. XP_718369.1. XM_713276.1.
3D structure databases
ProteinModelPortal	O93803.
ModBase	Search...
Protein-protein interaction databases
STRING	O93803.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3639986. 3640140.
KEGG	cal:CaO19.10140. cal:CaO19.2609.
Organism-specific databases
CGD	CAL0003365. CET1.
Phylogenomic databases
PhylomeDB	O93803.
Family and domain databases
InterPro	IPR023577. CYTH-like_domain. IPR004206. mRNA_capping_enz_bsu_dom. [Graphical view]
Gene3D	G3DSA:3.20.100.10. mRNA_capping_enz_bsu. 1 hit.
KO	K01098.
Pfam	PF02940. mRNA_triPase. 1 hit. [Graphical view]
SUPFAM	SSF55154. mRNA_capping_enz_bsu. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CET1_CANAL

Accession

Primary (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:	January 25, 2012
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program