ID   PSA1_TRYBB              Reviewed;         266 AA.
AC   Q9GU37;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   22-FEB-2023, entry version 72.
DE   RecName: Full=Proteasome subunit alpha type-1;
DE   AltName: Full=20SPA1;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=427;
RX   PubMed=11309374; DOI=10.1074/jbc.m008342200;
RA   Huang L., Jacob R.J., Pegg S.C.H., Baldwin M.A., Wang C.C.,
RA   Burlingame A.L., Babbitt P.C.;
RT   "Functional assignment of the 20 S proteasome from Trypanosoma brucei using
RT   mass spectrometry and new bioinformatics approaches.";
RL   J. Biol. Chem. 276:28327-28339(2001).
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; AF198386; AAG28527.1; -; mRNA.
DR   AlphaFoldDB; Q9GU37; -.
DR   SMR; Q9GU37; -.
DR   BRENDA; 3.4.25.1; 6519.
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; cd03754; proteasome_alpha_type_6; 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   InterPro; IPR034642; Proteasome_subunit_alpha6.
DR   PANTHER; PTHR11599:SF11; PROTEASOME SUBUNIT ALPHA TYPE-6; 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   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Proteasome.
FT   CHAIN           1..266
FT                   /note="Proteasome subunit alpha type-1"
FT                   /id="PRO_0000124069"
SQ   SEQUENCE   266 AA;  29336 MW;  6B226FCDC0124B4B CRC64;
     MSRAGFDKYI TVFSPEGSLY QVEYAFKAVT YAGLLTVAIR CKDAVLVFTQ HSVPDKLMRP
     ETITSLYNVN DNTGVCITGR APDGKALVQK ARNEASEYKY RYGMPMLVSV LAKPWQDMAQ
     VRTQQAGMRL MGTIMTFVGM EQNDEDGAWI PQIYCVDPAG GAAVHACAVG KKQIEACAFL
     EKKQKNAPFH TLSQKEAAMI ALAALQSALG ESLRASGVEV GRCTADDHHF LRVSDREVKK
     WLTPLAKPGY RAAYVLVRHT FHVVNP
//