PSA1_TRYBB
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 25-MAY-2022, entry version 70.
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; -; 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 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..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