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
//