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
//