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Q9GU37

- PSA1_TRYBB

UniProt

Q9GU37 - PSA1_TRYBB

Protein

Proteasome subunit alpha type-1

Gene
N/A
Organism
Trypanosoma brucei brucei
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    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

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-1 (EC:3.4.25.1)
    Alternative name(s):
    20SPA1
    OrganismiTrypanosoma brucei brucei
    Taxonomic identifieri5702 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

    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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 266266Proteasome subunit alpha type-1PRO_0000124069Add
    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

    ProteinModelPortaliQ9GU37.
    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.

    Q9GU37-1 [UniParc]FASTAAdd to Basket

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    MSRAGFDKYI TVFSPEGSLY QVEYAFKAVT YAGLLTVAIR CKDAVLVFTQ    50
    HSVPDKLMRP ETITSLYNVN DNTGVCITGR APDGKALVQK ARNEASEYKY 100
    RYGMPMLVSV LAKPWQDMAQ VRTQQAGMRL MGTIMTFVGM EQNDEDGAWI 150
    PQIYCVDPAG GAAVHACAVG KKQIEACAFL EKKQKNAPFH TLSQKEAAMI 200
    ALAALQSALG ESLRASGVEV GRCTADDHHF LRVSDREVKK WLTPLAKPGY 250
    RAAYVLVRHT FHVVNP 266
    Length:266
    Mass (Da):29,336
    Last modified:March 1, 2001 - v1
    Checksum:i6B226FCDC0124B4B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF198386 mRNA. Translation: AAG28527.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF198386 mRNA. Translation: AAG28527.1 .

    3D structure databases

    ProteinModelPortali Q9GU37.
    ModBasei Search...
    MobiDBi Search...

    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 nameiPSA1_TRYBB
    AccessioniPrimary (citable) accession number: Q9GU37
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 51 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