ID   PSA5_ENTHI              Reviewed;         247 AA.
AC   Q94561;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Proteasome subunit alpha type-5;
OS   Entamoeba histolytica.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=5759;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 30459 / HM-1:IMSS;
RX   PubMed=9041528; DOI=10.1016/s0166-6851(96)02770-3;
RA   Ramos M.A., Stock R.P., Sanchez-Lopez R., Olvera F., Lizardi P.M.,
RA   Alagon A.;
RT   "The Entamoeba histolytica proteasome alpha-subunit gene.";
RL   Mol. Biochem. Parasitol. 84:131-135(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RC   STRAIN=ATCC 30459 / HM-1:IMSS;
RX   PubMed=9274882; DOI=10.1016/s0166-6851(97)00096-0;
RA   Ramos M.A., Mercado G.C., Salgado L.M., Sanchez-Lopez R., Stock R.P.,
RA   Lizardi P.M., Alagon A.;
RT   "Entamoeba histolytica contains a gene encoding a homologue to the 54 kDa
RT   subunit of the signal recognition particle.";
RL   Mol. Biochem. Parasitol. 88:225-235(1997).
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   -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC       19S regulatory subunits. The 20S proteasome core is composed of 28
CC       subunits that are arranged in four stacked rings, resulting in a
CC       barrel-shaped structure. The two end rings are each formed by seven
CC       alpha subunits, and the two central rings are each formed by seven beta
CC       subunits. The catalytic chamber with the active sites is on the inside
CC       of the barrel (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
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DR   EMBL; AF386797; AAL50554.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q94561; -.
DR   SMR; Q94561; -.
DR   STRING; 5759.rna_EHI_004760-1; -.
DR   VEuPathDB; AmoebaDB:EHI5A_060070; -.
DR   VEuPathDB; AmoebaDB:EHI7A_067390; -.
DR   VEuPathDB; AmoebaDB:EHI8A_068220; -.
DR   VEuPathDB; AmoebaDB:EHI_004760; -.
DR   VEuPathDB; AmoebaDB:KM1_112080; -.
DR   eggNOG; KOG0176; Eukaryota.
DR   OMA; FQVEYAR; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProt.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd03753; proteasome_alpha_type_5; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR033812; Proteasome_alpha_type_5.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   Pfam; PF00227; Proteasome; 1.
DR   Pfam; PF10584; Proteasome_A_N; 1.
DR   SMART; SM00948; Proteasome_A_N; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Proteasome.
FT   CHAIN           1..247
FT                   /note="Proteasome subunit alpha type-5"
FT                   /id="PRO_0000124122"
SQ   SEQUENCE   247 AA;  27247 MW;  B39C01D3D56161BF CRC64;
     MFMTKNENDH GVNTFSSEGR LFQVEYATEA MKLGSTVIGI QTKEGVVLAV EKRISSPLML
     GSSIEKIIEI DDHIGAAVSG LTADARTLID NARLEAQNHR FMYDEPINVE VVAQAISDLS
     LRFGEGSRKK KVMSRPFGVA LLIAGVDETG PRLFQTDPSG MFIEFYAKAT GAGTEAAQSI
     LHEKYNKSMT LREAEILALS TLKQVMEEKL NSKNVEVALV TVEKKKFEIM DTAFIENLIG
     EIKEELI