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Database: UniProt
Entry: A0A165L4D3_EXIGL
LinkDB: A0A165L4D3_EXIGL
Original site: A0A165L4D3_EXIGL 
ID   A0A165L4D3_EXIGL        Unreviewed;       415 AA.
AC   A0A165L4D3;
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:KZV97330.1};
GN   ORFNames=EXIGLDRAFT_608140 {ECO:0000313|EMBL:KZV97330.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV97330.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV97330.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV97330.1,
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; KV425931; KZV97330.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165L4D3; -.
DR   InParanoid; A0A165L4D3; -.
DR   OrthoDB; 656651at2759; -.
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; 2.
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:KZV97330.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..415
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007861535"
FT   DOMAIN          91..404
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        109
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   415 AA;  43152 MW;  F88DCB299C0B6F3C CRC64;
     MLSTSFLSLV LFAALGLGVA GLSIHELANS TETSSIRAPI RKLVRHEKLK DLVVHDQAHA
     KALVHRGTGG KSLSEDAQVA GAAIANLVTT YIASMNVGSP ATTYDVIVDT GSSNTWVGSG
     TPFRFTRTTR NLSESMFVQY GSGFVVGFEV IDQVSFGGPL TIPNQEIGVA TASQGFAGVD
     GIVGLGPTDL TEGTVQGQDT IPTVTDNLFA LGIIPAPVIS VSFAPTNLTF DVNGELVFGG
     VDTSKFIGTL SVFRITSSSP ANAFFGIDAS FSFGGTTILP LSPGIVDTGT TLILLATQAF
     SAYTKRSGAV PDGATGLLRL TPAQFAALPS LNVIVGGVTF TLTPDAQRWP QQLNTAIGGS
     TSFVYLIVNT LGSPEGQGLD FILGQFFLER FYSVFDSTGF VGLAPTVFTN ATVNN
//
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