NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 10259 / CBS 5796 / IFO 1060 / JCM 2078;
DOI=10.1016/S0014-5793(98)01037-0; PubMed=9755857 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada-Okabe T., Mio T., Matsui M., Kashima Y., Arisawa M., Yamada-Okabe H.;
"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.";
FEBS Lett. 435:49-54(1998).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC5314;
DOI=10.1073/pnas.0401648101; PubMed=15123810 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The diploid genome sequence of Candida albicans.";
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).

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: 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).
SIMILARITY: Belongs to the fungal TPase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB016242; BAA33965.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AACQ01000044; EAK99345.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AACQ01000043; EAK99443.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_718274.1; -.
XP_718369.1; -.

3D structure databases

HSSP

O13297; 1D8I. [HSSP ENTRY / PDB]

ModBase

O93803.

Organism-specific databases

CGD

CAL0003365; CET1.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from InterPro).
GO:0004651;	Molecular function: polynucleotide 5'-phosphatase activity (inferred from electronic annotation from InterPro).
GO:0006370;	Biological process: mRNA capping (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR004206; mRNA_triPase.
Graphical view of domain structure.

Pfam

PF02940; mRNA_triPase; 1.
Pfam graphical view of domain structure.

Genome annotation databases

GeneID

3639986; -.
3640140; -.

KEGG

cal:CaO19.10140; -.
cal:CaO19.2609; -.

Other

ProtoNet

O93803.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Hydrolase; mRNA capping; mRNA processing; Nucleus.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 520`	`520`	`mRNA-capping enzyme subunit beta.`	`PRO_0000210112`
`COMPBIAS`	`92 95`	`4`	`Poly-Ser.`
`VARIANT`	`12 12`	`1`	`P -> S (in strain: IFO 1060).`

Sequence information

Length: 520 AA [This is the length of the unprocessed precursor]

Molecular weight: 58801 Da [This is the MW of the unprocessed precursor]

CRC64: 5C0690F5476C9DEC [This is a checksum on the sequence]

        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

O93803 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools