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Database: UniProt
Entry: A0A165D3Y2_EXIGL
LinkDB: A0A165D3Y2_EXIGL
Original site: A0A165D3Y2_EXIGL 
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
//
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