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Protein

Proteasome subunit alpha type-7-1

Gene

Pros28.1

Organism
Drosophila virilis (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Protein family/group databases

MEROPSiT01.973.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-7-1 (EC:3.4.25.1)
Alternative name(s):
Proteasome 28 kDa subunit 1
Gene namesi
Name:Pros28.1
OrganismiDrosophila virilis (Fruit fly)
Taxonomic identifieri7244 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophila

Organism-specific databases

FlyBaseiFBgn0025405. Dvir\Pros28.1.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
  3. proteasome core complex, alpha-subunit complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 247247Proteasome subunit alpha type-7-1PRO_0000124156Add
BLAST

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

STRINGi7244.FBpp0232921.

Structurei

3D structure databases

ProteinModelPortaliO16811.
SMRiO16811. Positions 5-229.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
OrthoDBiEOG71VSTG.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O16811-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSRYDRAVT IFSPDGRLLQ VEYAQEAVRK GSTAVGVRGG NCVVLGVEKK
60 70 80 90 100
SVAKLQEDRT VRKICVLDHV VMAFAGLTDA RILINRAQVE CQSHRLNVED
110 120 130 140 150
PVTLEYITRY IAQLKQKYTQ SNGRRPFGIS CLIGGFDADG SPYLFQTEPS
160 170 180 190 200
GIFYEYKANA TGCSAKTVRE FFEKQYREEE VSTERGAVKL AIRALLEVAQ
210 220 230 240
SGQHNLEVAI MENGKPLKML DRKVILEYLD IIEKEKEEEL EKKKQKK
Length:247
Mass (Da):27,914
Last modified:January 1, 1998 - v1
Checksum:i8D31FA5DEA7269D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017649 Genomic DNA. Translation: AAC34196.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017649 Genomic DNA. Translation: AAC34196.1.

3D structure databases

ProteinModelPortaliO16811.
SMRiO16811. Positions 5-229.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7244.FBpp0232921.

Protein family/group databases

MEROPSiT01.973.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

FlyBaseiFBgn0025405. Dvir\Pros28.1.

Phylogenomic databases

eggNOGiCOG0638.
OrthoDBiEOG71VSTG.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Evolutionary conservation of a testes-specific proteasome subunit gene in Drosophila."
    Belote J.M., Miller M., Smyth K.A.
    Gene 215:93-100(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiPSA71_DROVI
AccessioniPrimary (citable) accession number: O16811
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: January 1, 1998
Last modified: January 7, 2015
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.