(data stored in SCRATCH zone)

SWISSPROT: Q751N3_ASHGO

ID   Q751N3_ASHGO            Unreviewed;       306 AA.
AC   Q751N3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 110.
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_AGL336W {ECO:0000313|EMBL:AAS54155.1};
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:AAS54155.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54155.1, 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}.
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DR   EMBL; AE016820; AAS54155.1; -; Genomic_DNA.
DR   RefSeq; NP_986331.1; NM_211393.1.
DR   STRING; 33169.AAS54155; -.
DR   EnsemblFungi; AAS54155; AAS54155; AGOS_AGL336W.
DR   GeneID; 4622624; -.
DR   KEGG; ago:AGOS_AGL336W; -.
DR   HOGENOM; HOG000091080; -.
DR   InParanoid; Q751N3; -.
DR   KO; K02725; -.
DR   OMA; TQEMVAC; -.
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:0034515; C:proteasome storage granule; IEA:EnsemblFungi.
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   Gene3D; 3.60.20.10; -; 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; PTHR11599:SF12; 1.
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; Q751N3.
DR   SWISS-2DPAGE; Q751N3.
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          79..101
FT                   /note="PROTEASOME_ALPHA_1"
FT                   /evidence="ECO:0000259|PROSITE:PS00388"
SQ   SEQUENCE   306 AA;  33585 MW;  C06C3B0895AF9277 CRC64;
     MRHLGRLQYA TEPPINRGDG IIYIPFHEYQ ISVSNDNTRA TSRGRVANTA PVQLTSTSKE
     GGVHEQLGHC ELVMFRNNYD GDTVTFSPTG RLFQVEYALE AIKQGSATVG LRSNKYVVLV
     ALKRNADELS SYQKKIIKCD DHMGLSLAGL APDARVLSNF LRQQCNYSQL VYARDLSVVK
     AGQLLSDKAQ KNTQSYGGRP YGVGLLLAGY DNSGAHLLEF QPSGNTLELY GAAIGARSQG
     AKTYLERVME EYLEIEDADA LIKHGVEALK HSLKDETLST KNLSIAIVGK DMPFTLYDGE
     AVAAYL
//

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