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Database: UniProt
Entry: A0A1I7UY68_9PELO
LinkDB: A0A1I7UY68_9PELO
Original site: A0A1I7UY68_9PELO 
ID   A0A1I7UY68_9PELO        Unreviewed;       253 AA.
AC   A0A1I7UY68;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Proteasome subunit alpha type {ECO:0000256|RuleBase:RU000551};
OS   Caenorhabditis tropicalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold630.g20521.t2};
RN   [1] {ECO:0000313|WBParaSite:Csp11.Scaffold630.g20521.t2}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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       {ECO:0000256|ARBA:ARBA00002000}.
CC   -!- SUBUNIT: The 20S proteasome core is composed of 28 subunits that are
CC       arranged in four stacked rings, resulting in a barrel-shaped structure.
CC       The two end rings are each formed by seven alpha subunits, and the two
CC       central rings are each formed by seven beta subunits.
CC       {ECO:0000256|RuleBase:RU000551}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000551}.
CC       Nucleus {ECO:0000256|RuleBase:RU000551}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00808, ECO:0000256|RuleBase:RU000551}.
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DR   AlphaFoldDB; A0A1I7UY68; -.
DR   STRING; 1561998.A0A1I7UY68; -.
DR   WBParaSite; Csp11.Scaffold630.g20521.t2; Csp11.Scaffold630.g20521.t2; Csp11.Scaffold630.g20521.
DR   Proteomes; UP000095282; Unplaced.
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; IEA:UniProtKB-UniRule.
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 {ECO:0000256|RuleBase:RU000551};
KW   Nucleus {ECO:0000256|RuleBase:RU000551};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|PROSITE-
KW   ProRule:PRU00808}.
FT   DOMAIN          4..26
FT                   /note="Proteasome alpha-type subunits"
FT                   /evidence="ECO:0000259|PROSITE:PS00388"
SQ   SEQUENCE   253 AA;  28234 MW;  093CC069ACBDBFD0 CRC64;
     MNRYDRAITI FSPDGHLFQV EYAQEAVKKG STAVGVRGKD CIVIGVEKKS IPALQDDRTI
     RKIHMIDDHV MLAFAGLSAD ARVLVDRARI ECQSYKLTLE DPVTVAYISR YIANTKQRFT
     QSPGRRPFGI SMLIGGFDHD GTPRLFKTEP SGAYYEYVAN STGRGEKPVR EYLEEHYSEE
     NTVDEATTLK LVVKSLAQVV PPGSQNIEIA VMKKVNDELQ QRVLSTDEIE ALLKVVEAER
     VAAEAEEAAT KKK
//
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