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Database: UniProt
Entry: W1NH10_AMBTC
LinkDB: W1NH10_AMBTC
Original site: W1NH10_AMBTC 
ID   W1NH10_AMBTC            Unreviewed;       251 AA.
AC   W1NH10;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Proteasome subunit alpha type {ECO:0000256|RuleBase:RU000551};
GN   ORFNames=AMTR_s00010p00259960 {ECO:0000313|EMBL:ERM94455.1};
OS   Amborella trichopoda.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333 {ECO:0000313|EMBL:ERM94455.1, ECO:0000313|Proteomes:UP000017836};
RN   [1] {ECO:0000313|Proteomes:UP000017836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24357323;
RG   Amborella Genome Project;
RT   "The Amborella genome and the evolution of flowering plants.";
RL   Science 342:1241089-1241089(2013).
CC   -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which
CC       is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC       Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC       pH. The proteasome has an ATP-dependent proteolytic activity.
CC       {ECO:0000256|ARBA:ARBA00002000}.
CC   -!- SUBUNIT: The 20S proteasome core is composed of 28 subunits that are
CC       arranged in four stacked rings, resulting in a barrel-shaped structure.
CC       The two end rings are each formed by seven alpha subunits, and the two
CC       central rings are each formed by seven beta subunits.
CC       {ECO:0000256|RuleBase:RU000551}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000551}.
CC       Nucleus {ECO:0000256|RuleBase:RU000551}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00808, ECO:0000256|RuleBase:RU000551}.
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DR   EMBL; KI397513; ERM94455.1; -; Genomic_DNA.
DR   RefSeq; XP_006827218.1; XM_006827155.2.
DR   AlphaFoldDB; W1NH10; -.
DR   STRING; 13333.W1NH10; -.
DR   EnsemblPlants; ERM94455; ERM94455; AMTR_s00010p00259960.
DR   GeneID; 18422202; -.
DR   Gramene; ERM94455; ERM94455; AMTR_s00010p00259960.
DR   KEGG; atr:18422202; -.
DR   eggNOG; KOG0178; Eukaryota.
DR   HOGENOM; CLU_035750_4_3_1; -.
DR   OMA; RECFKVV; -.
DR   OrthoDB; 166567at2759; -.
DR   Proteomes; UP000017836; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IBA:GO_Central.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd03752; proteasome_alpha_type_4; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   PANTHER; PTHR11599:SF13; PROTEASOME SUBUNIT ALPHA TYPE-4; 1.
DR   PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   Pfam; PF10584; Proteasome_A_N; 1.
DR   SMART; SM00948; Proteasome_A_N; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU000551};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000551};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|PROSITE-
KW   ProRule:PRU00808}; Reference proteome {ECO:0000313|Proteomes:UP000017836}.
FT   DOMAIN          5..27
FT                   /note="Proteasome alpha-type subunits"
FT                   /evidence="ECO:0000259|PROSITE:PS00388"
SQ   SEQUENCE   251 AA;  27561 MW;  4205B5497B08903A CRC64;
     MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGN AGTAIGILST DGVVLVGEKK VTSKLLQTSK
     STEKMYKIDD HLACAVAGIM SDANILINTA RVQAQRYTYA YQEPMPVEQL VQSLCDTKQG
     YTQFGGLRPF GVSFLFAGWD KNFGFQLYMS DPSGNYGGWK AAAIGANNQA AQSMLKQEYK
     DEINTEEAVQ LALKVLSKTM DSTSLTSEKL ELAKIYLPSP SGEVKYQVCS ADSLENYLVR
     FGVTQPPADA S
//
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