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Database: UniProt
Entry: G3JJU4_CORMM
LinkDB: G3JJU4_CORMM
Original site: G3JJU4_CORMM 
ID   G3JJU4_CORMM            Unreviewed;       464 AA.
AC   G3JJU4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Candidapepsin-4 {ECO:0000313|EMBL:EGX92128.1};
GN   ORFNames=CCM_06288 {ECO:0000313|EMBL:EGX92128.1};
OS   Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX   NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX92128.1, ECO:0000313|Proteomes:UP000001610};
RN   [1] {ECO:0000313|EMBL:EGX92128.1, ECO:0000313|Proteomes:UP000001610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM01 {ECO:0000313|EMBL:EGX92128.1,
RC   ECO:0000313|Proteomes:UP000001610};
RX   PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA   Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA   Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT   "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT   valued traditional Chinese medicine.";
RL   Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; JH126402; EGX92128.1; -; Genomic_DNA.
DR   RefSeq; XP_006671492.1; XM_006671429.1.
DR   AlphaFoldDB; G3JJU4; -.
DR   GeneID; 18168303; -.
DR   KEGG; cmt:CCM_06288; -.
DR   VEuPathDB; FungiDB:CCM_06288; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_030513_0_0_1; -.
DR   InParanoid; G3JJU4; -.
DR   OMA; PAELWIG; -.
DR   OrthoDB; 2550277at2759; -.
DR   Proteomes; UP000001610; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
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; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001610};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..464
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003446261"
FT   DOMAIN          75..401
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        93
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        293
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        326..363
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   464 AA;  48588 MW;  8D48970FDD47EA4A CRC64;
     MSLSAALLCL LASQAVAAPA GGQDAAPVVQ DGIFQLPVFT VSAEEELAAS AGTTKRQVSA
     GLDNVKFGAR PAVALGTTIM VGTPPQKVIL EPDTGSSQLW VPGSHAAQPR VGDESVYFDR
     DASTSLKDLK KPSAASYGDK EWVLMNMVND NVAIGGKSMD KLNFGIGNMT SPHTTLGRLV
     GVMGLLPPSK ANKDVDFVPQ KLLDKKLVKT RAFSMGLRKK GQGLLTFGGY DTSKFSGSLE
     KLPLQLTKSR HSNRGGSYVV SVKSLSFTAS KGGSSETVLD DQSIKKPLTI GIDSGSPALA
     LKSTLLTIIQ DKLQGKLTGG LLQVGCDVVD ANAQLDFNMS DSTTISVPLS DMVIKKIDND
     KNCLLAIQAN DQVPAELWIG GHFLRRSLVV YDPDDSCIYV ARGADCGTSL VAIDGKMPAA
     AVKGKCSEEA VVAEKPDAGA AASIAALTPD QLSALLDPRI DVEE
//
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