ID   A0A0D7A7L8_9AGAR        Unreviewed;       415 AA.
AC   A0A0D7A7L8;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Acid protease {ECO:0000313|EMBL:KIY46755.1};
GN   ORFNames=FISHEDRAFT_46699 {ECO:0000313|EMBL:KIY46755.1};
OS   Fistulina hepatica ATCC 64428.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX   NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY46755.1, ECO:0000313|Proteomes:UP000054144};
RN   [1] {ECO:0000313|EMBL:KIY46755.1, ECO:0000313|Proteomes:UP000054144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY46755.1,
RC   ECO:0000313|Proteomes:UP000054144};
RX   PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA   Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA   Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA   LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA   Hibbett D.S.;
RT   "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT   genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL   Fungal Genet. Biol. 76:78-92(2015).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KN882024; KIY46755.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D7A7L8; -.
DR   OrthoDB; 656651at2759; -.
DR   Proteomes; UP000054144; 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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KIY46755.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054144}.
FT   DOMAIN          70..405
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        88
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   415 AA;  44052 MW;  B3E73CB04D79E555 CRC64;
     MSSNVVIRSL PFATSLVKRH AKDILARDRA RAQKLLAGLS PHGPRATRQA NSIEASDVES
     VDVTNAAVTY TMTVGVGSPA TDYTLLIDTG SSNTWIGADK SYEPTETATR TGNYFFVAYG
     SGVALGRQYL DQVTLGSNLV IEDQSIGVSI MARGFSGVDG ILGIGPVGLT AGMLPMHADV
     YQRTDKVYGT GTVTDTDAVP TVTDNLYSQG TIPTESIGIF YQPSTSSEEL AGGELSFGGP
     DSELYSSAIT YVPITSTSPA SNYWGIDQTL MYGDSTTLLS STAGIVDTGT TLLMIASDAF
     EAYKEATGAT LDETTGLLTV TEEQYATMES MYFTIGDTTF EFTANAQIWP RALNSTLGGD
     DDTIYLITAD LGSDSGQGLD FINGFAFLQR FYSVFDTTNS RVGIACTEYT QATTN
//