ID G3J685_CORMM Unreviewed; 555 AA.
AC G3J685;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=Penicillopepsin {ECO:0000313|EMBL:EGX96984.1};
GN ORFNames=CCM_01643 {ECO:0000313|EMBL:EGX96984.1};
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:EGX96984.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX96984.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX96984.1,
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, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; JH126399; EGX96984.1; -; Genomic_DNA.
DR RefSeq; XP_006666861.1; XM_006666798.1.
DR AlphaFoldDB; G3J685; -.
DR GeneID; 18163673; -.
DR KEGG; cmt:CCM_01643; -.
DR VEuPathDB; FungiDB:CCM_01643; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_0_1; -.
DR InParanoid; G3J685; -.
DR OMA; AYMARIK; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000001610; 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:SF23; ASPARTIC ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G15950)-RELATED; 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}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000001610};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..555
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003445928"
FT DOMAIN 240..552
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 95..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..121
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..205
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 256
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 443
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 555 AA; 57745 MW; ABDD4F59AFD18AA8 CRC64;
MYTKALPALL LVLELTSFAT AAPYLEKRSF KVERFQNEGY TGRNGPRALA KAYRKYSIPL
PDGLVDALEK QDTEMLARRR TKWYSPVAGA APAVAVEQVS EKKVGDDEED DDEEEDAGDE
QVEEKSIAGD LLGGLLGGGA GKGNPAQGAE NGNKPQGAGK GEGAGGNKGG KGEGKGAGGK
NPNFNPTPTP SSSPSPSPSP SPSPNNGDPN ADAMAALARA RKGNQTGLVP TIPEPNDVEY
LSEVKIGGQP VTLDFDTGSS DLWVFNTQLP GQQTQGRQVY DPTRSNTFKP MPGAEFAIRY
GDGSGATGNV GTDVVEIGGA VVPAQAVELA TQVTDTFVQD ANNGGLVGLA FGSINAVKPQ
KQKTFFENIM PSLQEPLFTA DLRAGKPGAY EFGRIDRSKF TGEMAWIPAN TTAGFWQFST
GSFAVGDGPV QPASRPGGQA IADTGTTLLL ADPAIVQGYY SQVPGAANDR QAGGVVVPCR
AQLPDLHLDI GGAYMARIKG ADINFAPVDK TNTTCFGGLQ ASPQGGLGIY GDILFKSQFV
AFNGGNNSLG MANHA
//