Reviewed, UniProtKB/Swiss-Prot Q9P6Q6 (CET1_SCHPO)

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:	pct1
ORF Names:	SPAC644.04

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	303 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end. Ref.2
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. Ref.2
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
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	mRNA capping Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mRNA cap methyltransferase complex Inferred from electronic annotation. Source: InterPro
Molecular function	polynucleotide 5'-phosphatase activity Inferred from electronic annotation. Source: EC protein homodimerization activity Ref.2 Inferred from direct assay. Source: GeneDB_SPombe
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
cdk9	Q96WV9	1	EBI-443547,EBI-443557

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 303	303	mRNA-capping enzyme subunit beta		PRO_0000210117

Sequences

	Sequence		Length	Mass (Da)
	Q9P6Q6-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 51A5A112CE927AED	FASTA	303	35,444
	10 20 30 40 50 60 MDLKGLLHEE NELPSIEKRK IDENAVEHDK VERKRTKSVA VPKIEMNFLN KPIVPDTTKV 70 80 90 100 110 120 ISNFLTHYLI TEPVEHVEIE AKLGTLIDLE TQNRFEFPVM NETILNPEFN LRTRFESDMT 130 140 150 160 170 180 ASEHKYLNEF LNQAFRDSQK PGRLPFAYKH TKQVDLFYET EDNSRDKIRV SKNQSDNQVL 190 200 210 220 230 240 ACVKKRRVAD LFLYCPNDAF DIRISISDEL PVSMPSGNQQ PSLTRLKDRV GYVHQEIKID 250 260 270 280 290 300 LTKTTQNDPV YDTTERHELE VEFGNIADLR DRAQKAKDGM EAPLFRRVQL FMDNVRILRR EHS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	"Homodimeric quaternary structure is required for the in vivo function and thermal stability of Saccharomyces cerevisiae and Schizosaccharomyces pombe RNA triphosphatases." Hausmann S., Pei Y., Shuman S. J. Biol. Chem. 278:30487-30496(2003) [PubMed: 12788946] [Abstract] Cited for: FUNCTION, SUBUNIT.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB90131.1.
RefSeq	NP_593872.1.
3D structure databases
SMR	Q9P6Q6. Positions 31-303.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9P6Q6. 2 interactions.
STRING	Q9P6Q6.
Genome annotation databases
GeneID	2543671.
GenomeReviews	Gene locus pct1 in contig CU329670_GR.
KEGG	spo:SPAC644.04.
NMPDR	fig|4896.1.peg.3842.
Organism-specific databases
GeneDB_Spombe	SPAC644.04.
Phylogenomic databases
eggNOG	fuNOG08284.
OrthoDB	EOG9N5XD0.
PhylomeDB	Q9P6Q6.
Enzyme and pathway databases
BRENDA	3.1.3.33. 653.
Gene expression databases
ArrayExpress	Q9P6Q6.
Family and domain databases
InterPro	IPR004206. mRNA_capping_enz_bsu. [Graphical view]
Gene3D	G3DSA:3.20.100.10. mRNA_capping_enz_bsu. 1 hit.
Pfam	PF02940. mRNA_triPase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CET1_SCHPO

Accession

Primary (citable) accession number: Q9P6Q6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	October 1, 2000
Last modified:	January 19, 2010
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)