ID Q2USF0_ASPOR Unreviewed; 279 AA.
AC Q2USF0;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 22-FEB-2023, entry version 103.
DE RecName: Full=Proteasome subunit alpha type {ECO:0000256|RuleBase:RU000551};
GN ORFNames=AO090005000451 {ECO:0000313|EMBL:BAE55515.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE55515.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE55515.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. {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; AP007151; BAE55515.1; -; Genomic_DNA.
DR RefSeq; XP_001817517.1; XM_001817465.2.
DR AlphaFoldDB; Q2USF0; -.
DR STRING; 510516.Q2USF0; -.
DR MEROPS; T01.A11; -.
DR EnsemblFungi; BAE55515; BAE55515; AO090005000451.
DR GeneID; 5989462; -.
DR KEGG; aor:AO090005000451; -.
DR VEuPathDB; FungiDB:AO090005000451; -.
DR HOGENOM; CLU_035750_4_1_1; -.
DR OMA; YQEQIPT; -.
DR OrthoDB; 166567at2759; -.
DR Proteomes; UP000006564; Chromosome 1.
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:0034515; C:proteasome storage granule; IEA:EnsemblFungi.
DR GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IEA:EnsemblFungi.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR CDD; cd03750; proteasome_alpha_type_2; 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:SF16; PROTEASOME SUBUNIT ALPHA TYPE-2; 1.
DR PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1.
DR Pfam; PF00227; Proteasome; 2.
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:UP000006564}.
FT DOMAIN 5..27
FT /note="Proteasome alpha-type subunits"
FT /evidence="ECO:0000259|PROSITE:PS00388"
FT REGION 143..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 279 AA; 30174 MW; 45B775639BC4DD07 CRC64;
MADRYSFSLT TFSPSGKLVQ IEYALNAVNQ GVTALGIKAT NGIVLATEKK SSSPLIDPPS
LSKVSLITPD IGMVYAGMGP DYRVLVDKAR KVSHTGYKRI YNEYPPTRIL VQDVARVVQE
ATQSGGVRPY GVSLLIAGWD EGVEPESEEA QKGDNEDEPK KATGKTGGIL KGGPSLYQVD
PSGSYYPWKA TAIGKHATSA KTFLEKRYTE GLELEDAIHI ALLTLKETIE GEMNGDTIEI
GIVGPPADHL LGFEGVEGAQ GPRFRKLTKE EIEDYLTNL
//
