(data stored in SCRATCH zone)

SWISSPROT: Q750N9_ASHGO

ID   Q750N9_ASHGO            Unreviewed;       246 AA.
AC   Q750N9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 111.
DE   RecName: Full=Proteasome endopeptidase complex {ECO:0000256|PROSITE-ProRule:PRU00808};
DE            EC=3.4.25.1 {ECO:0000256|PROSITE-ProRule:PRU00808};
GN   ORFNames=AGOS_AGL089W {ECO:0000313|EMBL:AAS54401.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54401.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54401.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of peptide bonds with very broad specificity.;
CC         EC=3.4.25.1; Evidence={ECO:0000256|PROSITE-ProRule:PRU00808};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|SAAS:SAAS00594407}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00808}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016820; AAS54401.1; -; Genomic_DNA.
DR   RefSeq; NP_986577.1; NM_211639.1.
DR   STRING; 33169.AAS54401; -.
DR   MEROPS; T01.971; -.
DR   EnsemblFungi; AAS54401; AAS54401; AGOS_AGL089W.
DR   GeneID; 4622876; -.
DR   KEGG; ago:AGOS_AGL089W; -.
DR   HOGENOM; HOG000091084; -.
DR   InParanoid; Q750N9; -.
DR   KO; K02730; -.
DR   OMA; YGYDMPV; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IBA:GO_Central.
DR   GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR   GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd03754; proteasome_alpha_type_6; 1.
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; IPR034642; Proteasome_subunit_alpha6.
DR   Pfam; PF00227; Proteasome; 1.
DR   Pfam; PF10584; Proteasome_A_N; 1.
DR   SMART; SM00948; Proteasome_A_N; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q750N9.
DR   SWISS-2DPAGE; Q750N9.
KW   Cytoplasm {ECO:0000256|PROSITE-ProRule:PRU00808};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00808};
KW   Nucleus {ECO:0000256|SAAS:SAAS00136223};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU00808};
KW   Proteasome {ECO:0000256|PROSITE-ProRule:PRU00808};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Threonine protease {ECO:0000256|PROSITE-ProRule:PRU00808}.
FT   DOMAIN          6..28
FT                   /note="PROTEASOME_ALPHA_1"
FT                   /evidence="ECO:0000259|PROSITE:PS00388"
SQ   SEQUENCE   246 AA;  27500 MW;  A494DD493C57A722 CRC64;
     MSAAGYDRHI TIFSPEGRLY QVEYAFKATN QTNINSVAIR GKSCTVLVNQ KKVPDKLLEP
     STVTYLFPIA KHIGMCATGP IADARNVAVR CRAMAAEFRY EYGYDMPVHV LAKRFANLSQ
     TYTQRAYMRP LGVVLTFISV DEEEGPSIFK CDPAGYYTGY KATATGPKQQ ELITALEKHF
     KKLQKDRLDE DSWEKVVEFA IGQMINSLGT DFSSKDLEIG VAVAGKFFVL SQDQVEERLV
     AIAEQD
//

If you have problems or comments...

PBIL Back to PBIL home page