(data stored in SCRATCH zone)

SWISSPROT: B6HD84_PENRW

ID   B6HD84_PENRW            Unreviewed;       276 AA.
AC   B6HD84;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 56.
DE   RecName: Full=Proteasome subunit alpha type {ECO:0000256|RuleBase:RU000551};
DE            EC=3.4.25.1 {ECO:0000256|RuleBase:RU000551};
GN   ORFNames=Pc20g01470 {ECO:0000313|EMBL:CAP85476.1}, PCH_Pc20g01470
GN   {ECO:0000313|EMBL:CAP85476.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP85476.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85476.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
CC       specificity. {ECO:0000256|PROSITE-ProRule:PRU00808,
CC       ECO:0000256|RuleBase:RU000551}.
CC   -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
CC       two 19S regulatory subunits. {ECO:0000256|RuleBase:RU000551}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000551}.
CC       Nucleus {ECO:0000256|RuleBase:RU000551}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|SAAS:SAAS00594407}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family.
CC       {ECO:0000256|PROSITE-ProRule:PRU00808,
CC       ECO:0000256|RuleBase:RU000551}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AM920435; CAP85476.1; -; Genomic_DNA.
DR   RefSeq; XP_002562706.1; XM_002562660.1.
DR   STRING; 500485.XP_002562706.1; -.
DR   EnsemblFungi; CAP85476; CAP85476; PCH_Pc20g01470.
DR   GeneID; 8312284; -.
DR   KEGG; pcs:Pc20g01470; -.
DR   eggNOG; KOG0181; Eukaryota.
DR   eggNOG; ENOG410XPQ8; LUCA.
DR   HOGENOM; HOG000091085; -.
DR   KO; K02726; -.
DR   OMA; SGAYFGW; -.
DR   OrthoDB; EOG092C47D8; -.
DR   BioCyc; PCHR:PC20G01470-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c20.
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:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-UniRule.
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   Gene3D; 3.60.20.10; -; 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   InterPro; IPR034644; Proteasome_subunit_alpha2.
DR   PANTHER; PTHR11599:SF89; PTHR11599:SF89; 1.
DR   Pfam; PF00227; Proteasome; 2.
DR   Pfam; PF10584; Proteasome_A_N; 1.
DR   SMART; SM00948; Proteasome_A_N; 1.
DR   SUPFAM; SSF56235; SSF56235; 2.
DR   PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6HD84.
DR   SWISS-2DPAGE; B6HD84.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Cytoplasm {ECO:0000256|PROSITE-ProRule:PRU00808,
KW   ECO:0000256|RuleBase:RU000551};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00808,
KW   ECO:0000256|RuleBase:RU000551};
KW   Nucleus {ECO:0000256|RuleBase:RU000551,
KW   ECO:0000256|SAAS:SAAS00487709};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU00808,
KW   ECO:0000256|RuleBase:RU000551};
KW   Proteasome {ECO:0000256|PROSITE-ProRule:PRU00808,
KW   ECO:0000256|RuleBase:RU000551};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Threonine protease {ECO:0000256|PROSITE-ProRule:PRU00808,
KW   ECO:0000256|RuleBase:RU000551}.
FT   DOMAIN        5     27       PROTEASOME_ALPHA_1. {ECO:0000259|PROSITE:
FT                                PS00388}.
SQ   SEQUENCE   276 AA;  29963 MW;  1D404D9EB14EFAD1 CRC64;
     MADRYSFSLT TFSPSGKLVQ IEYALNAVNQ GVTALGIKAT NGIVLATEKK SSSPLIDPPS
     LSKISLITPD IGMVYAGMGP DYRVLVDKAR KVSHTGYKRI YNEYPPTRIL VQDVARVVQE
     ATQSGGVRPY GVSLLVAGWD EGVEPESEEA KKDDPEEKIS SKTGGIKKGG PSLYQVDPSG
     SYYPWKATAI GKHATSAKTF LEKRYTEGLE LEDAIHIALL TLKETIEGEM NGDTIEIGIV
     GPPADHLLGY EGVEGAQGPR FRKLTKEQIE DYLTNL
//

If you have problems or comments...

PBIL Back to PBIL home page