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
//