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Q9NDA2

- PSA7_TRYBB

UniProt

Q9NDA2 - PSA7_TRYBB

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Protein

Proteasome subunit alpha type-7

Gene

PSA4

Organism
Trypanosoma brucei brucei
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

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

MEROPSiT01.978.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-7 (EC:3.4.25.1)
Alternative name(s):
20S proteasome subunit alpha-4
Gene namesi
Name:PSA4
OrganismiTrypanosoma brucei brucei
Taxonomic identifieri5702 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
  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-7PRO_0000124158Add
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

Structurei

3D structure databases

ProteinModelPortaliQ9NDA2.
SMRiQ9NDA2. Positions 2-239.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

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.

Q9NDA2 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSYDRAITVF SPDGHLFQVE YAQEAVRKGL CAVGVKGKDS IIFAVEKKSV
60 70 80 90 100
QKLQDSRTTR KIYKLDEHIY LASAGLSADA RVVVNHAQLE CQRFRLSYED
110 120 130 140 150
AIDVDLLVRY VARVQQRSTQ SSGSRPYGVS TIIGGFNENG QPQLWKTEPS
160 170 180 190 200
GTSSAWNAAA IGRNDKVVLE FMEKNYQDGM TRDRCVHFAI KALLEAVESG
210 220 230 240
SKNIELLVLE RGKAAYMSDT ELHRFVVEVE KEREEEAARR RRLAEED
Length:247
Mass (Da):27,865
Last modified:October 1, 2000 - v1
Checksum:iB2C522510C068670
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF169652 mRNA. Translation: AAF89684.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF169652 mRNA. Translation: AAF89684.1 .

3D structure databases

ProteinModelPortali Q9NDA2.
SMRi Q9NDA2. Positions 2-239.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi T01.978.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view ]
SMARTi SM00948. Proteasome_A_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Functional assignment of the 20 S proteasome from Trypanosoma brucei using mass spectrometry and new bioinformatics approaches."
    Huang L., Jacob R.J., Pegg S.C.H., Baldwin M.A., Wang C.C., Burlingame A.L., Babbitt P.C.
    J. Biol. Chem. 276:28327-28339(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 427.

Entry informationi

Entry nameiPSA7_TRYBB
AccessioniPrimary (citable) accession number: Q9NDA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: October 1, 2000
Last modified: October 29, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3