ID A0A026W5P8_OOCBI Unreviewed; 278 AA.
AC A0A026W5P8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 22-FEB-2023, entry version 43.
DE RecName: Full=Proteasome subunit alpha type {ECO:0000256|RuleBase:RU000551};
GN ORFNames=DMN91_012603 {ECO:0000313|EMBL:RLU14716.1}, X777_10564
GN {ECO:0000313|EMBL:EZA50936.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA50936.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA50936.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
RN [2] {ECO:0000313|EMBL:RLU14716.1, ECO:0000313|Proteomes:UP000279307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Clonal line C1 {ECO:0000313|EMBL:RLU14716.1};
RX PubMed=30249741; DOI=10.1101/gr.237123.118;
RA McKenzie S.K., Kronauer D.J.C.;
RT "The genomic architecture and molecular evolution of ant odorant
RT receptors.";
RL Genome Res. 28:1757-1765(2018).
RN [3] {ECO:0000313|EMBL:RLU14716.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Clonal line C1 {ECO:0000313|EMBL:RLU14716.1};
RA Mckenzie S.K., Kronauer D.J.C.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KK107429; EZA50936.1; -; Genomic_DNA.
DR EMBL; QOIP01000014; RLU14716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026W5P8; -.
DR STRING; 2015173.A0A026W5P8; -.
DR EnsemblMetazoa; XM_011345901.1; XP_011344203.1; LOC105283274.
DR OMA; NTQVYGK; -.
DR OrthoDB; 166567at2759; -.
DR Proteomes; UP000053097; Unassembled WGS sequence.
DR Proteomes; UP000279307; Chromosome 14.
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; cd03749; proteasome_alpha_type_1; 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; IPR035144; Proteasome_alpha1.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR PANTHER; PTHR11599:SF12; PROTEASOME SUBUNIT ALPHA TYPE-1; 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}; Reference proteome {ECO:0000313|Proteomes:UP000053097}.
FT DOMAIN 6..28
FT /note="Proteasome alpha-type subunits"
FT /evidence="ECO:0000259|PROSITE:PS00388"
FT REGION 236..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 278 AA; 30937 MW; C8700B9C38043391 CRC64;
MFRNQYDSDV TVWSPQGRLH QVEYAMEAVK LGSATVGLKN KTHAVLIALK RASSELSAHQ
KKIIPIDKHM GISISGLTAD ARILSRYMRT ECLNYKYAHD DTLPVSRLIS SLGNKMQTCT
QRYDRRPYGV GLLVAGYDDQ GPHIYQTCPS ANYFDCKAMA IGSRSQSART YLEKHLNEFL
SSDLNDLVKH GLRALRDTLP NEVDLSVKNV SIAVVGKDHD FTILDETETA TYLTQIEGDD
KRGRPSEPAV QDDSRPPQDP PADEGPQDPQ VAIAMETD
//
