(data stored in ACNUC7421 zone)

SWISSPROT: Q75CA0_ASHGO

ID   Q75CA0_ASHGO            Unreviewed;       541 AA.
AC   Q75CA0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 122.
DE   SubName: Full=ACR012Cp {ECO:0000313|EMBL:AAS51239.1};
GN   ORFNames=AGOS_ACR012C {ECO:0000313|EMBL:AAS51239.1};
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:AAS51239.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51239.1, 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   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|RuleBase:RU003355, ECO:0000256|SAAS:SAAS01201832}.
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DR   EMBL; AE016816; AAS51239.1; -; Genomic_DNA.
DR   RefSeq; NP_983415.1; NM_208768.1.
DR   STRING; 33169.AAS51239; -.
DR   EnsemblFungi; AAS51239; AAS51239; AGOS_ACR012C.
DR   GeneID; 4619540; -.
DR   KEGG; ago:AGOS_ACR012C; -.
DR   HOGENOM; HOG000199176; -.
DR   InParanoid; Q75CA0; -.
DR   KO; K01336; -.
DR   OMA; WIGSKHA; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005773; C:vacuole; IEA:GOC.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0009267; P:cellular response to starvation; IEA:EnsemblFungi.
DR   GO; GO:0000425; P:pexophagy; IEA:EnsemblFungi.
DR   GO; GO:0007039; P:protein catabolic process in the vacuole; IEA:EnsemblFungi.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:EnsemblFungi.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 3.30.70.80; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75CA0.
DR   SWISS-2DPAGE; Q75CA0.
KW   Hydrolase {ECO:0000256|RuleBase:RU003355, ECO:0000256|SAAS:SAAS01077244};
KW   Protease {ECO:0000256|RuleBase:RU003355, ECO:0000256|SAAS:SAAS01201830};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Serine protease {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS01201831}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..541
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004286542"
FT   DOMAIN          74..174
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          214..435
FT                   /note="Peptidase_S8"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
SQ   SEQUENCE   541 AA;  58464 MW;  E5A5D0B12C7B406C CRC64;
     MKLQRAVWPA VALTTAQALL ILPQAEDELV VAEAHRGQLV QWMARENQER KAQGAEQQSP
     LFRVDDVTRA IPHKYIVVFR EGVSDEEAAF HMELVEAAHA ESVARLDEQH AFFRSTRGEN
     NEFGIAATRA EGGIEGEFAL GEQLRGYVGY FTEDMVGLLR SNPHVHFVEE DSMVFASDFT
     TQNGAPWGLA RVSHREKLNS GSFNKYLYDD NSGEGVTSYV IDTGINIDHV DFEDRALWGK
     TIPNNDADYD GNGHGTHCAG TIASKTYGVA KKANVVAVKV LRSNGTGSMS DVLRGVEYAV
     KAHRKAAEKA DKGFKGSTAN MSLGGGRSQA LDLAVDAAVD AGIHFAVAAG NENQDACNTS
     PAASQKAITV GASTLADDRA YFSNWGRCVD LFAPGMNILS TYIGSDTAVA TLSGTSMASP
     HVAGLLTYFL SLQPDGDSEF RNKQTISPEV LKKKVIDFGT KDALSSLPAR TANVLIYNGG
     GADLSDFWGN KPKKVSGPKF TYADDEEAMG SDLDRLIHEL ESSTDAMFSG FRTILDRMNI
     I
//

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