Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q60177

- PSA_METJA

UniProt

Q60177 - PSA_METJA

Protein

Proteasome subunit alpha

Gene

psmA

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.jannaschii proteasome is able to cleave oligopeptides after Glu, Asp, Tyr, Phe, Trp, slightly after Arg, but not after Ala. Thus, displays caspase-like and chymotrypsin-like activities and low level of trypsin-like activity.1 PublicationUniRule annotation

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.1 PublicationUniRule annotation

    Enzyme regulationi

    The formation of the proteasomal ATPase PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers opening of the gate for substrate entry. Interconversion between the open-gate and close-gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity.UniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. proteasomal protein catabolic process Source: UniProtKB
    2. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alphaUniRule annotation (EC:3.4.25.1UniRule annotation)
    Alternative name(s):
    20S proteasome alpha subunitUniRule annotation
    Proteasome core protein PsmAUniRule annotation
    Gene namesi
    Name:psmAUniRule annotation
    Ordered Locus Names:MJ0591
    OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
    Taxonomic identifieri243232 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
    ProteomesiUP000000805: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. proteasome core complex, alpha-subunit complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 261261Proteasome subunit alphaPRO_0000124174Add
    BLAST

    Interactioni

    Subunit structurei

    The 20S proteasome core is composed of 14 alpha and 14 beta subunits that assemble into four stacked heptameric rings, resulting in a barrel-shaped structure. The two inner rings, each composed of seven catalytic beta subunits, are sandwiched by two outer rings, each composed of seven alpha subunits. The catalytic chamber with the active sites is on the inside of the barrel. Has a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is capped at one or both ends by the proteasome regulatory ATPase, PAN.2 PublicationsUniRule annotation

    Protein-protein interaction databases

    STRINGi243232.MJ0591.

    Structurei

    Secondary structure

    1
    261
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi23 – 3311
    Beta strandi48 – 525
    Turni62 – 643
    Beta strandi68 – 725
    Beta strandi75 – 806
    Helixi84 – 907
    Helixi93 – 10210
    Helixi110 – 12314
    Beta strandi136 – 1405
    Beta strandi149 – 1524
    Beta strandi159 – 1635
    Turni171 – 1766
    Helixi177 – 1804
    Helixi192 – 20110
    Beta strandi202 – 2043
    Beta strandi209 – 2168
    Turni217 – 2204
    Beta strandi221 – 2244
    Turni227 – 2304
    Helixi231 – 2333
    Turni234 – 2396
    Beta strandi240 – 2423

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3H4PX-ray4.10A/B/C/D/E/F/G/H/I/J/K/L/M/N1-261[»]
    ProteinModelPortaliQ60177.
    SMRiQ60177. Positions 5-247.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ60177.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    KOiK03432.
    OMAiFQVNYAR.
    PhylomeDBiQ60177.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    HAMAPiMF_00289_A. Proteasome_A_A.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR019982. Proteasome_asu_arc.
    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.
    TIGRFAMsiTIGR03633. arc_protsome_A. 1 hit.
    PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
    PS51475. PROTEASOME_ALPHA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q60177-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQMVPPSAYD RAITVFSPEG RLYQVEYARE AVRRGTTAIG IACKDGVVLA    50
    VDRRITSKLV KIRSIEKIFQ IDDHVAAATS GLVADARVLI DRARLEAQIY 100
    RLTYGEEISI EMLAKKICDI KQAYTQHGGV RPFGVSLLIA GIDKNEARLF 150
    ETDPSGALIE YKATAIGSGR PVVMELLEKE YRDDITLDEG LELAITALTK 200
    ANEDIKPENV DVCIITVKDA QFKKIPVEEI KKLIEKVKKK LNEENKKEEE 250
    NREETKEKQE E 261
    Length:261
    Mass (Da):29,321
    Last modified:November 1, 1997 - v1
    Checksum:i93FC7DF277E01AD8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L77117 Genomic DNA. Translation: AAB98581.1.
    PIRiG64373.
    RefSeqiNP_247571.1. NC_000909.1.
    WP_010870095.1. NC_000909.1.

    Genome annotation databases

    EnsemblBacteriaiAAB98581; AAB98581; MJ_0591.
    GeneIDi1451456.
    KEGGimja:MJ_0591.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L77117 Genomic DNA. Translation: AAB98581.1 .
    PIRi G64373.
    RefSeqi NP_247571.1. NC_000909.1.
    WP_010870095.1. NC_000909.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3H4P X-ray 4.10 A/B/C/D/E/F/G/H/I/J/K/L/M/N 1-261 [» ]
    ProteinModelPortali Q60177.
    SMRi Q60177. Positions 5-247.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243232.MJ0591.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAB98581 ; AAB98581 ; MJ_0591 .
    GeneIDi 1451456.
    KEGGi mja:MJ_0591.

    Phylogenomic databases

    eggNOGi COG0638.
    KOi K03432.
    OMAi FQVNYAR.
    PhylomeDBi Q60177.

    Miscellaneous databases

    EvolutionaryTracei Q60177.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    HAMAPi MF_00289_A. Proteasome_A_A.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR019982. Proteasome_asu_arc.
    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.
    TIGRFAMsi TIGR03633. arc_protsome_A. 1 hit.
    PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
    PS51475. PROTEASOME_ALPHA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
    2. "Biochemical and physical properties of the Methanococcus jannaschii 20S proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the eucaryal 26S proteasome."
      Wilson H.L., Ou M.S., Aldrich H.C., Maupin-Furlow J.
      J. Bacteriol. 182:1680-1692(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH PAN.
    3. "Structural insights into the regulatory particle of the proteasome from Methanocaldococcus jannaschii."
      Zhang F., Hu M., Tian G., Zhang P., Finley D., Jeffrey P.D., Shi Y.
      Mol. Cell 34:473-484(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT, GATED STRUCTURE, SUBUNIT.

    Entry informationi

    Entry nameiPSA_METJA
    AccessioniPrimary (citable) accession number: Q60177
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 102 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Methanococcus jannaschii
      Methanococcus jannaschii: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3