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Database: UniProt
Entry: T5AEN7_OPHSC
LinkDB: T5AEN7_OPHSC
Original site: T5AEN7_OPHSC 
ID   T5AEN7_OPHSC            Unreviewed;       413 AA.
AC   T5AEN7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   22-FEB-2023, entry version 38.
DE   SubName: Full=Endothiapepsin-like protein {ECO:0000313|EMBL:EQL03925.1};
GN   ORFNames=OCS_00368 {ECO:0000313|EMBL:EQL03925.1};
OS   Ophiocordyceps sinensis (strain Co18 / CGMCC 3.14243) (Yarsagumba
OS   caterpillar fungus) (Hirsutella sinensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=911162 {ECO:0000313|EMBL:EQL03925.1, ECO:0000313|Proteomes:UP000019374};
RN   [1] {ECO:0000313|EMBL:EQL03925.1, ECO:0000313|Proteomes:UP000019374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Co18 / CGMCC 3.14243 {ECO:0000313|Proteomes:UP000019374};
RC   TISSUE=Fruit-body {ECO:0000313|EMBL:EQL03925.1};
RX   DOI=10.1007/s11434-013-5929-5;
RA   Hu X., Zhang Y., Xiao G., Zheng P., Xia Y., Zhang X., St Leger R.J.,
RA   Liu X., Wang C.;
RT   "Genome survey uncovers the secrets of sex and lifestyle in caterpillar
RT   fungus.";
RL   Chin. Sci. Bull. 58:2846-2854(2013).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KE652187; EQL03925.1; -; Genomic_DNA.
DR   AlphaFoldDB; T5AEN7; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_0_3_1; -.
DR   Proteomes; UP000019374; 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; cd06097; Aspergillopepsin_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; IPR034163; Aspergillopepsin-like_cat_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966:SF1; ASPARTYL PROTEINASE; 1.
DR   PANTHER; PTHR47966; 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   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019374};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..413
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004596791"
FT   DOMAIN          86..406
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        104
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        292
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        329..368
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   413 AA;  45141 MW;  00D8AEC7CA1B8D4E CRC64;
     MQTVGLLFVL LAALSAALAV PLESPGGSFA LIVAKRNGEK RDFYHDLAAS HRKWGTATPG
     EAVQMLALAK GESQVKVQPM AQDMVYLAEA EIGTPPQKIK LALDTGSSDV WVQSTDTRYR
     VNRHGPWPAR YSPNASTSAH QVDKAAWNII YADASSAIGV VYRDTIRIGD LEVKDAPIES
     AAMISDAFEM ETGFSGIMGL AKQLNNSIAP PEPTFLSLLR RQLKTPVFSV DLRRNASSRF
     DFGHIDESLA SDNITWLQSN PANPHWSVDL ELTSWTGNET VWLYHKFEAI VDTGTSLMFI
     PDILASMYWD QVPGVQTAPL AHASYRFPCA ISDKLPDVLF KLPGTEHVLT IPGRYLNYGP
     TGQDPTMCWG GMQGSGQLGN TTILGDAMLK ALFVAFDMEK GRIGFANKKL HDV
//
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