ID   PSA71_DROVI             Reviewed;         247 AA.
AC   O16811;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   24-JAN-2024, entry version 115.
DE   RecName: Full=Proteasome subunit alpha type-7-1;
DE   AltName: Full=Proteasome 28 kDa subunit 1;
GN   Name=Pros28.1;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9666090; DOI=10.1016/s0378-1119(98)00256-x;
RA   Belote J.M., Miller M., Smyth K.A.;
RT   "Evolutionary conservation of a testes-specific proteasome subunit gene in
RT   Drosophila.";
RL   Gene 215:93-100(1998).
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; AF017649; AAC34196.1; -; Genomic_DNA.
DR   AlphaFoldDB; O16811; -.
DR   SMR; O16811; -.
DR   MEROPS; T01.973; -.
DR   eggNOG; KOG0183; Eukaryota.
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; cd03755; proteasome_alpha_type_7; 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:SF15; PROTEASOME SUBUNIT ALPHA TYPE-7-1-RELATED; 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; Nucleus; Proteasome.
FT   CHAIN           1..247
FT                   /note="Proteasome subunit alpha type-7-1"
FT                   /id="PRO_0000124156"
SQ   SEQUENCE   247 AA;  27914 MW;  8D31FA5DEA7269D7 CRC64;
     MSSRYDRAVT IFSPDGRLLQ VEYAQEAVRK GSTAVGVRGG NCVVLGVEKK SVAKLQEDRT
     VRKICVLDHV VMAFAGLTDA RILINRAQVE CQSHRLNVED PVTLEYITRY IAQLKQKYTQ
     SNGRRPFGIS CLIGGFDADG SPYLFQTEPS GIFYEYKANA TGCSAKTVRE FFEKQYREEE
     VSTERGAVKL AIRALLEVAQ SGQHNLEVAI MENGKPLKML DRKVILEYLD IIEKEKEEEL
     EKKKQKK
//