ID A0A168GGJ2_CORDF Unreviewed; 411 AA.
AC A0A168GGJ2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 28.
DE SubName: Full=Endothiapepsin {ECO:0000313|EMBL:OAA76461.1};
GN ORFNames=LEL_06145 {ECO:0000313|EMBL:OAA76461.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA76461.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA76461.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA76461.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAA76461.1}.
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DR EMBL; AZHF01000004; OAA76461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168GGJ2; -.
DR STRING; 1081108.A0A168GGJ2; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000076881; 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:SF2; ASPERGILLOPEPSIN-1-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; 1.
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:UP000076881};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..411
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007897157"
FT DOMAIN 98..408
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 116
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 301
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 411 AA; 43681 MW; 5B4D25F3218284D8 CRC64;
MKTAGTFVAL AAAAGTAAAA PSEGTGLKFS IPAHKNPIQR NPIADAHYAL RKFATPETIE
KIEADLLARR EAVLLGQRDE NTTVGANPHG QDGVDTSYLC EVSIGTPPQK LMLDFDTGSS
DLWVFSTDTQ TSETNGQTLY KPAKSSSSKL LQGFKWAIGY GDKSNSKGVV YQDVVKIGTA
SVNNQAVESA TDVSSQFTND SGSSGLLGLA YDKGNTVKPT QQKTWFSNIK SRLAQPLFTA
RLKHQEVGSY NFGYIDQSQY TGDISYTPAF TDALGHRLFN ATGYAVADAE LNDRVITGTA
DTGTSIVYLP TDVASDYWSN VDGAQKQQVA EGQYLWVFDC NTSLPTFSFG VGSGRITIHS
DNINFASEQG SCIGGLGGID GALAIFGDVA MKSGFVVYDD GNNQLGWAEG A
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