ID   G3JNS1_CORMM            Unreviewed;       492 AA.
AC   G3JNS1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Peptidase aspartic, catalytic {ECO:0000313|EMBL:EGX89911.1};
GN   ORFNames=CCM_08164 {ECO:0000313|EMBL:EGX89911.1};
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:EGX89911.1, ECO:0000313|Proteomes:UP000001610};
RN   [1] {ECO:0000313|EMBL:EGX89911.1, ECO:0000313|Proteomes:UP000001610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM01 {ECO:0000313|EMBL:EGX89911.1,
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; JH126404; EGX89911.1; -; Genomic_DNA.
DR   RefSeq; XP_006673366.1; XM_006673303.1.
DR   AlphaFoldDB; G3JNS1; -.
DR   GeneID; 18170173; -.
DR   KEGG; cmt:CCM_08164; -.
DR   VEuPathDB; FungiDB:CCM_08164; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_478239_0_0_1; -.
DR   InParanoid; G3JNS1; -.
DR   OMA; QIGLMET; -.
DR   OrthoDB; 1767283at2759; -.
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:InterPro.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47965:SF109; ASPARTIC PROTEINASE 3-RELATED; 1.
DR   PANTHER; PTHR47965; ASPARTYL PROTEASE-RELATED; 1.
DR   Pfam; PF00026; Asp; 2.
DR   SUPFAM; SSF50630; Acid proteases; 2.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022750};
KW   Protease {ECO:0000256|ARBA:ARBA00022750};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001610}.
FT   DOMAIN          38..475
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          248..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..336
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   492 AA;  51516 MW;  2BE0140BA451A24D CRC64;
     MKHLPLLLLA GEAATAQPRV FQNLVQHFES AEMGPFIPFV ELGFGAAPAL QPITGIFDTG
     SSDTIVPEAG SEVCQQARQQ CTAPAPVVLG QFDPAAAAAA GDFRRLDGQR FNATFGGGDQ
     YDGDYIKTSV VLGQDGQGRV AGAQVALASH SEPRTELPQV PVFGLGSDPE RGIGEAKMKD
     AGVTKGQAYS VVLNPTPLGN GSVFFGGIDR AKFEGELNEV PLAKNKRGEL PEFVVKMSSV
     ALVPGARDAA NNGSARRDAD GGSRRAKRMS WKRGVGARRL GTAKNTYGPQ GAARREVGER
     RLAMRNKRSD GYHKKNRNGD KKNGNGNSNN GSNACNGSKN EINLGLDPRD GFILMDTGGV
     EMALPAHVVS ALAQALGTSF SEDDGLGPVP CGQLEGDAAL IMRFQDDAVE TRVPLAHMRL
     SAALADPALT SDGLCQLVVR AVADGGGEGT SVATLPFFAA VYTVFDLDGN RLFFAPAKGD
     PGAPAAQLEE FP
//