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Database: UniProt
Entry: A0A165CDP7_EXIGL
LinkDB: A0A165CDP7_EXIGL
Original site: A0A165CDP7_EXIGL 
ID   A0A165CDP7_EXIGL        Unreviewed;       400 AA.
AC   A0A165CDP7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   08-NOV-2023, entry version 28.
DE   SubName: Full=Acid protease {ECO:0000313|EMBL:KZV82283.1};
GN   ORFNames=EXIGLDRAFT_685027 {ECO:0000313|EMBL:KZV82283.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV82283.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV82283.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV82283.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KV426334; KZV82283.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165CDP7; -.
DR   InParanoid; A0A165CDP7; -.
DR   OrthoDB; 1651995at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KZV82283.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..400
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007855985"
FT   DOMAIN          72..390
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   400 AA;  43156 MW;  A8B03C136B866731 CRC64;
     MVARPFVLVA LFFTLVAAAP PLRTLPLTKR IDHSKVKNIV KSDQARAKGL KNVNKGDGER
     EPVNAFANGI AYVVNVAVGS PAATYSLIVD TGSSNTWIGA DKSYQASNTS FPLDEFVSVS
     YGSGFFEGTA YADQVALSSD LVADYQIIAV ADFSFGFEGY DGILGLGPTI LTNGTVSDFE
     LVDTVVDTLY YDGRIKARVL GAAFAPLNAN GGVGSLAFGA PDPSHYTGLL SYTNVTKAYP
     SSLYFGIDVR FDYGPRTLGY GSGIVDIGTT LILLASDIFE FYANSTGGVY DYYVGLLRLD
     EEQYNKLQPL NLRINGATYE LTANAQILPR TLNVDVGGDP DAYYLIIADL GYPSGFGFDF
     ILGQSFLERF YSVYDSGQNY DNTDSRVGFA QTKYSFSEVN
//
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