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Reviewed, UniProtKB/Swiss-Prot O94579 (PSA2_SCHPO)

Last modified November 3, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable proteasome subunit alpha type-2
    EC=3.4.25.1
Gene names
ORF Names: SPCC1442.06
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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 By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the peptidase T1A family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
Proteasome
   Molecular functionHydrolase
Protease
Threonine protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_SPombe

nucleus

Inferred from direct assay. Source: GeneDB_SPombe

proteasome core complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionthreonine-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 245245Probable proteasome subunit alpha type-2
PRO_0000124089

Sequences

Sequence LengthMass (Da)Tools
O94579-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: CFCCA93537D2464A

FASTA24526,404
        10         20         30         40         50         60 
MTDKYAFSLT TFSPNGKLVQ IEYALNAVNA GVTSVGIKAT DGVVLATEKK PTSELAIGAS 

        70         80         90        100        110        120 
LEKVCAITPD IGMVYSGMGP DFRVLVDKSR KVAQTTYKKI YNEYPPTKIL VQEIASVMQE 

       130        140        150        160        170        180 
STQSGGVRPF GVSLLVAGMD EKGPSLYQVD PSGTYFAWKA TAIGKSSTAA KTFLEKRYND 

       190        200        210        220        230        240 
ELELDDAVHT AILALKETFE GELTEDNIEI AVVSTKPTDS GIVGVPGGHF CRLSQSEIRD 


YLDQV 

« Hide

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. expand/collapse author list , 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.

Cross-references

Sequence databases

CU329672 Genomic DNA. Translation: CAA21440.1.
PIRT40971.
RefSeqNP_588320.1.

3D structure databases

HSSPHSSP built from PDB template 1RYP based on UniProtKB P23639.
ModBaseSearch...

Protein-protein interaction databases

STRINGO94579.

Protein family/group databases

MEROPST01.972.

Genome annotation databases

GeneID2539026.
KEGGspo:SPCC1442.06.
NMPDRfig|4896.1.peg.658.

Organism-specific databases

GeneDB_SpombeSPCC1442.06.

Phylogenomic databases

OMAHIALLTL.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-000243-MON.
BRENDA3.4.25.1. 653.

Gene expression databases

ArrayExpressO94579.

Family and domain databases

InterProIPR000426. Proteasome_asu_CS.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
PROSITEPS00388. PROTEASOME_A. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePSA2_SCHPO
AccessionPrimary (citable) accession number: O94579
Entry history
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: May 1, 1999
Last modified: November 3, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents