O43063 (PSB1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable proteasome subunit beta type-1
EC=3.4.25.1

Gene names

Name:	pre3
ORF Names:	SPBC4C3.10c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	226 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity By similarity.
Catalytic activity	Cleavage of peptide bonds with very broad specificity.
Subunit structure	The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel By similarity.
Subcellular location	Cytoplasm. Nucleus Ref.2.
Sequence similarities	Belongs to the peptidase T1B family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Molecular function	Hydrolase Protease Threonine protease
PTM	Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteasomal ubiquitin-dependent protein catabolic process Non-traceable author statement. Source: PomBase regulation of mitotic cell cycle Inferred by curator. Source: PomBase
Cellular_component	cytosol Inferred from direct assay Ref.2. Source: PomBase nucleus Inferred from direct assay Ref.2. Source: PomBase proteasome core complex, beta-subunit complex Inferred from sequence orthology. Source: PomBase
Molecular_function	threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 24	24	Removed in mature form By similarity		PRO_0000026641
	Chain	25 – 226	202	Probable proteasome subunit beta type-1		PRO_0000026642
Sites
	Active site	25	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	O43063 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 88AEEF4B2A87093A	FASTA	226	24,564
	10 20 30 40 50 60 MATTVKDTMN VDINAIKKGE IRMGTTITAL RYKDGVILAA DSRTTMGAYI ANRVTDKLTQ 70 80 90 100 110 120 LTDNIWCCRS GSAADTQTVA DLLKYYLSMY RIQFGHDPSV HTAATLASEM CYQNKNMLSA 130 140 150 160 170 180 GLIVAGYDEK TGGDVYSIPL GGSLHKQPLA IGGSGSAFIY GFCDANFREN MTQEEAVEFL 190 200 210 220 KNAVALAMER DGSSGGTIRM VILNKDGMER KFFAIDTANP IPVFTH

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

[2]

"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAA16832.1.
PIR	T40487.
RefSeq	NP_596295.1. NM_001022216.2.
3D structure databases
ProteinModelPortal	O43063.
SMR	O43063. Positions 16-216.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPBC4C3.10c-1.
Protein family/group databases
MEROPS	T01.010.
Proteomic databases
PaxDb	O43063.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC4C3.10c.1; SPBC4C3.10c.1:pep; SPBC4C3.10c.
GeneID	2540878.
KEGG	spo:SPBC4C3.10c.
Organism-specific databases
PomBase	SPBC4C3.10c.
Phylogenomic databases
eggNOG	COG0638.
HOGENOM	HOG000091079.
KO	K02738.
OMA	NLGTSIM.
OrthoDB	EOG454D82.
Family and domain databases
InterPro	IPR000243. Pept_T1A_subB. IPR016050. Proteasome_bsu_CS. IPR001353. Proteasome_sua/b. IPR023333. Proteasome_suB-type. [Graphical view]
Pfam	PF00227. Proteasome. 1 hit. [Graphical view]
PRINTS	PR00141. PROTEASOME.
PROSITE	PS00854. PROTEASOME_B_1. 1 hit. PS51476. PROTEASOME_B_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20801994.

Entry information

Entry name

PSB1_SCHPO

Accession

Primary (citable) accession number: O43063

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program