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Q9SXU1

- PSA7_CICAR

UniProt

Q9SXU1 - PSA7_CICAR

Protein

Proteasome subunit alpha type-7

Gene

PAD1

Organism
Cicer arietinum (Chickpea) (Garbanzo)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      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-7 (EC:3.4.25.1)
    Alternative name(s):
    20S proteasome alpha subunit D
    20S proteasome subunit alpha-4
    Gene namesi
    Name:PAD1
    OrganismiCicer arietinum (Chickpea) (Garbanzo)
    Taxonomic identifieri3827 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeCicereaeCicer

    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 – 249249Proteasome subunit alpha type-7PRO_0000124161Add
    BLAST

    Proteomic databases

    PRIDEiQ9SXU1.
    ProMEXiQ9SXU1.

    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

    ProteinModelPortaliQ9SXU1.
    SMRiQ9SXU1. Positions 4-231.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    KOiK02731.

    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.

    Q9SXU1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARYDRAITV FSPDGHLFQV EYALEAVRKG NAAVGVRGTD NVVLGVEKKS    50
    TAKLQDTRSV RKIVNLDDHI ALACAGLKAD ARVLINRARV ECQSHRLTVE 100
    DPVTVEYITR YIAGLQQKYT QSGGVRPFGL STLIVGFDPY TGSPSLYQTD 150
    PSGTFSAWKA NATGRNSNSI REFLEKNFKE TSGQETVKLA IRALLEVVES 200
    GGKNIEVAVM TKENGLRQLE EAEIDAIVAE IEAEKAAAEA AKKAPPKDT 249
    Length:249
    Mass (Da):27,097
    Last modified:May 1, 2000 - v1
    Checksum:iB598A14A7A00D7F1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB025000 mRNA. Translation: BAA76428.1.
    RefSeqiNP_001265921.1. NM_001278992.1.

    Genome annotation databases

    GeneIDi101498666.
    KEGGicam:101498666.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB025000 mRNA. Translation: BAA76428.1 .
    RefSeqi NP_001265921.1. NM_001278992.1.

    3D structure databases

    ProteinModelPortali Q9SXU1.
    SMRi Q9SXU1. Positions 4-231.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q9SXU1.
    ProMEXi Q9SXU1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 101498666.
    KEGGi cam:101498666.

    Phylogenomic databases

    KOi K02731.

    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. "Genes expressed in Ascochyta rabiei-inoculated chickpea plants and elicited cell cultures as detected by differential cDNA-hybridization."
      Ichinose Y., Tiemann K., Schwenger-Erger C., Toyoda K., Hein F., Hanselle T., Cornels H., Barz W.
      Z. Naturforsch. C 55:44-54(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: ILC3279.
      Tissue: Leaf.

    Entry informationi

    Entry nameiPSA7_CICAR
    AccessioniPrimary (citable) accession number: Q9SXU1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 8, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 70 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    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