ID G3JT75_CORMM Unreviewed; 439 AA.
AC G3JT75;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Aspartic endopeptidase (AP1), putative {ECO:0000313|EMBL:EGX88222.1};
GN ORFNames=CCM_08265 {ECO:0000313|EMBL:EGX88222.1};
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:EGX88222.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX88222.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX88222.1,
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; JH126405; EGX88222.1; -; Genomic_DNA.
DR RefSeq; XP_006673467.1; XM_006673404.1.
DR AlphaFoldDB; G3JT75; -.
DR SMR; G3JT75; -.
DR MEROPS; A01.080; -.
DR GeneID; 18170273; -.
DR KEGG; cmt:CCM_08265; -.
DR VEuPathDB; FungiDB:CCM_08265; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_2_1; -.
DR InParanoid; G3JT75; -.
DR OMA; WYGGVQS; -.
DR OrthoDB; 2900143at2759; -.
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 CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
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; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001610}.
FT DOMAIN 106..423
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 124
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 323
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 439 AA; 47120 MW; CDD7F0AB370D9D35 CRC64;
MEAFFQAQAK FQASPGLTKV RAKPNQNYKR HGTKSYVYLL NRFGFEPTKP GPYRRVSHLQ
QRGLAQSHVA VGGRAAVTSR LAKTLDAAGT QTGEVTAEDQ QNDSEYLCEV SIGTPPQKVL
LDFDTGSSDL WIFSTELSKA TQKGHTIFNP SKSSTFKKLP GQTWQISYGD GSSASGDCGS
DNVTIGGLTI EGQTVELASK LAAQFAQGTG DGLLGLAFPA INTVKKNGQP APAQTPVANM
MTQGDIPKQS QLFTSAFYSE RDADGPQSFY TFGYVDEALV KASGKDIAWT KIDSSEGFWM
FPSASVSIAG KKLALDGNTA IADTGTTLAL VSDEVCDALY KAIPGAKYDA QQQGYVFPLT
TKPEDLPAFE VAAEDLAFAQ ADDKNWYGGV QSRGSNPFDI LGDAFLKSVY AIWDQGNQRF
GAVPKIEKTQ NLTAKAQSQ
//
