(data stored in SCRATCH zone)

SWISSPROT: Q75BX7_ASHGO

ID   Q75BX7_ASHGO            Unreviewed;       408 AA.
AC   Q75BX7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 99.
DE   SubName: Full=ACR144Wp {ECO:0000313|EMBL:AAS51370.1};
GN   ORFNames=AGOS_ACR144W {ECO:0000313|EMBL:AAS51370.1};
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:AAS51370.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51370.1, 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}.
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; AE016816; AAS51370.1; -; Genomic_DNA.
DR   RefSeq; NP_983546.1; NM_208899.1.
DR   STRING; 33169.AAS51370; -.
DR   MEROPS; A01.018; -.
DR   EnsemblFungi; AAS51370; AAS51370; AGOS_ACR144W.
DR   GeneID; 4619678; -.
DR   KEGG; ago:AGOS_ACR144W; -.
DR   HOGENOM; HOG000197681; -.
DR   InParanoid; Q75BX7; -.
DR   KO; K01381; -.
DR   OMA; LGKYYTE; -.
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; Q75BX7.
DR   SWISS-2DPAGE; Q75BX7.
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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..408
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004286714"
FT   DOMAIN          93..405
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   408 AA;  44484 MW;  2778232ACA3F4AA9 CRC64;
     MRFQTLLPLA ALLAPSFANA EGGVYKATLH KQSFDITPEE LSMKQRAASV GQKYLNALSK
     VVSDPSIQNE YNLFAKNNDG HVSELANLAN NIYAADVTIG TPPQDFRVVV DTGSSTLWVP
     GKECRAMACR LHKRYDHDRS STYKENGTLT GVTYGSGSIM GYVSEDTFRI SDLEIPGQQF
     TETTDEPGSV FVFAAFDGIL GLAYPSLGYG VTPPFQQLME KKLVKEPVFG MYLDDMKTGE
     GNGQLVLGGY DETKFKGEIA WLPVRRQAYW EVVFDSVTVG DDNIPLENYG AAIDSGTSLI
     TFPSELFNQF ISKLSGVTKD RQGNVYVDCA NKQTAPPLTF GFGGHKFSIS GEDYIISVPG
     QSARCMPAIV QLDIDSAGKV AIIGDVFLRR YYSIYDFGNN AVGLATAV
//

If you have problems or comments...

PBIL Back to PBIL home page