ID A0A168FS50_CORDF Unreviewed; 486 AA.
AC A0A168FS50;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 30.
DE SubName: Full=Candidapepsin-4 {ECO:0000313|EMBL:OAA75553.1};
GN ORFNames=LEL_07541 {ECO:0000313|EMBL:OAA75553.1};
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:OAA75553.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA75553.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA75553.1,
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:OAA75553.1}.
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DR EMBL; AZHF01000005; OAA75553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168FS50; -.
DR STRING; 1081108.A0A168FS50; -.
DR OrthoDB; 615305at2759; -.
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; cd05474; SAP_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; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033876; SAP-like.
DR PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 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|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..486
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007896993"
FT DOMAIN 59..424
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 77
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 273
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 486 AA; 51367 MW; 27AFA52B46E59315 CRC64;
MHDILALSAL LGLASAGTVS VDIHKQINAE LYDALKIHRR TGDPIVDLQA INNVTGGGYY
ADLGIGTPKQ VLTFHLDTGS SDTWVNQKGN NFCRYGSPEL QLPPSCLKQF DPDASSTFET
TIRGGFKISY LDGSQSSGDY FNDTVTIGDM TITQQQLGLA KKSSSATGLM GLGMSVGVAA
KKEYPTIIDN LVSQGYIDTA AFSLYLDSVT ESHGTFLFGG VDTKKYIGDL ATLPLVADDI
HGSDNVTSYA VDLTGFSVDG VSLPSLKTKA ILDTGATLVL LPGRVVTPIY TKLGVVSVTG
IATPFIDCSG STKKDGKDNL AKTKFNFEFN GKTISVPLKE MIVNSFDDHQ DIFKSPLLKS
QFKDFGKVCM FGIANADDYK TQEPDPLGSS GGSSNEPEYA LLGDTFLRSA YVVYDLARQE
VAIAQSYPKS NETNIVTLKA NSTIPSIKGM DAPAEDTAAS AAGLVRAPST AAAAALAVVA
AAVFAM
//