(data stored in ACNUC7421 zone)

SWISSPROT: Q75BX8_ASHGO

ID   Q75BX8_ASHGO            Unreviewed;       393 AA.
AC   Q75BX8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 100.
DE   SubName: Full=ACR143Wp {ECO:0000313|EMBL:AAS51369.1};
GN   ORFNames=AGOS_ACR143W {ECO:0000313|EMBL:AAS51369.1};
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:AAS51369.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51369.1, 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 A1 family.
CC       {ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS01079896}.
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DR   EMBL; AE016816; AAS51369.1; -; Genomic_DNA.
DR   RefSeq; NP_983545.1; NM_208898.1.
DR   STRING; 33169.AAS51369; -.
DR   MEROPS; A01.053; -.
DR   EnsemblFungi; AAS51369; AAS51369; AGOS_ACR143W.
DR   GeneID; 4619677; -.
DR   KEGG; ago:AGOS_ACR143W; -.
DR   HOGENOM; HOG000197681; -.
DR   InParanoid; Q75BX8; -.
DR   OMA; GVECANL; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0030163; P:protein catabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IBA:GO_Central.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR13683; PTHR13683; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75BX8.
DR   SWISS-2DPAGE; Q75BX8.
KW   Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..393
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004285419"
FT   DOMAIN          83..390
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   393 AA;  42882 MW;  5CF84C41B67C9EF8 CRC64;
     MKLQLLSLLV LLVPSISAEN GVFYAQVYRD GVDVVSNPEL ISRHVEAVAA RHELSRRTVE
     DEELQVGGGK FSANVYNFEN FQYSVDITLG TPAQNFRVAL DTGSSLLWIP SDRCTSQICR
     TRNRYRSGAS STFKATDKTL RLQYVKGDAK ARVSYDTLYF AGAKIENQGF GEAEAIGDDF
     SGARFDGIIG IGYPSIGYGI KPPINTLIDS GGLKDPMFGI YISNAQNRNS PVGEIVLGGY
     NTQKFKGDIK WLPVLRKAFW ETDLSAFKVG NFALDVQGLT AVFDTGSSFI IMPEDTYTDF
     VSQFPGASHD DGTDYVDCST VNSGPDLTLD FGGVALKLSA RDYVMQLGRN TCILAVSGNS
     RVTGEVILGD TFLRRYYTIY NFGDNTIGVA SAV
//

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