ID   PSA1_TRYCR              Reviewed;         265 AA.
AC   P92188; P90643;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Proteasome subunit alpha type-1;
DE   AltName: Full=Proteasome 29 kDa subunit;
DE   AltName: Full=TCPR29;
OS   Trypanosoma cruzi.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=5693;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tulahuen;
RA   Lima B.D., Batista J.A.N., Bartholomeu D.C., Vainstein M.H., de Sa C.;
RT   "T. cruzi 29 kDa proteasome subunit class II mRNA.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DM28;
RA   Bartholomeu D.C., Batista J.A.N., Lima B.D., Vainstein M.H., Sa Martins C.;
RT   "The 29 kDa subunit genomic sequence of Trypanosoma cruzi proteasome.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
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; U73850; AAB48403.1; -; Genomic_DNA.
DR   EMBL; U73851; AAB48404.1; -; mRNA.
DR   EMBL; U75302; AAB48405.1; -; mRNA.
DR   AlphaFoldDB; P92188; -.
DR   SMR; P92188; -.
DR   VEuPathDB; TriTrypDB:BCY84_10829; -.
DR   VEuPathDB; TriTrypDB:C3747_40g158; -.
DR   VEuPathDB; TriTrypDB:C4B63_48g135; -.
DR   VEuPathDB; TriTrypDB:Tc_MARK_3684; -.
DR   VEuPathDB; TriTrypDB:TcBrA4_0016650; -.
DR   VEuPathDB; TriTrypDB:TcCL_ESM02198; -.
DR   VEuPathDB; TriTrypDB:TcCLB.506167.40; -.
DR   VEuPathDB; TriTrypDB:TcCLB.506327.10; -.
DR   VEuPathDB; TriTrypDB:TcCLB.507785.20; -.
DR   VEuPathDB; TriTrypDB:TCDM_03196; -.
DR   VEuPathDB; TriTrypDB:TcG_04821; -.
DR   VEuPathDB; TriTrypDB:TCSYLVIO_004937; -.
DR   VEuPathDB; TriTrypDB:TcYC6_0125780; -.
DR   OMA; NTQVYGK; -.
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:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd03749; proteasome_alpha_type_1; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR035144; Proteasome_alpha1.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   PANTHER; PTHR11599:SF12; PTHR11599:SF12; 1.
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   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Proteasome.
FT   CHAIN           1..265
FT                   /note="Proteasome subunit alpha type-1"
FT                   /id="PRO_0000124071"
FT   REGION          237..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..265
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        38
FT                   /note="A -> T (in Ref. 2; AAB48403)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   265 AA;  29335 MW;  730E0EC27994AA2A CRC64;
     MFKNQYDTNT TTWSPTGRLF QVEYANEAVN NGSAAVGAKN KDFVVLTALK RSPVAQFSSY
     QEKVFKLDDH VGMAIAGLVA DGRMLARFVR TECMNYRYMH DSDNPLPLIA EIVGEKYQRH
     IQFAGKRPFG VGLLIAGYDS TGPHLYHTVP SGDVFDFKAT AMGLRSQAAR TYLEKHFESF
     PDCGLDELIM HALKALAAAT SGGAELNIKN TTIAIVGKGT PFMVLTEEAA RKYLDGFKMR
     PEDIPPAPEA EEEETLQERS LDVEE