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
//