ID A0A165D3Y2_EXIGL Unreviewed; 329 AA.
AC A0A165D3Y2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:KZV83731.1};
DE Flags: Fragment;
GN ORFNames=EXIGLDRAFT_582786 {ECO:0000313|EMBL:KZV83731.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV83731.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV83731.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV83731.1,
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; KV426257; KZV83731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165D3Y2; -.
DR STRING; 1314781.A0A165D3Y2; -.
DR InParanoid; A0A165D3Y2; -.
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:SF74; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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:KZV83731.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 1..319
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZV83731.1"
FT NON_TER 329
FT /evidence="ECO:0000313|EMBL:KZV83731.1"
SQ SEQUENCE 329 AA; 35156 MW; 0BA1A87ADD2192A0 CRC64;
YVVNVAIGSP ASTYSLIVDT GSSNTWIGAD KSFHETNTSI LVSDSVAVSY GSGFFEGAAF
VDQVALSDDL VAYPQIIGVA GFSFGFAGYD GILGLGPPIL TNGTVSNFEL VDTVVDVLYY
EGHIQARVLG AALAPLNANG GVGSLAFGAP DPSQYTGLLS YTNVTKAYPS SLYFGIDLRF
DYGPRTIGYG SGIVDVGTTL ILLASDIYEA YANSTGGVYD YSVGLLRLDE EEYNRLQPLN
LRINGATYEL TSNAQILPRT LNVDVGGDED AYYLIVADLG YPSGFGLDFI LGQCFLERFY
SVYDSGQNYD NTDSRVGFAE TKYSFSETN
//