ID A0A135SN03_9PEZI Unreviewed; 478 AA.
AC A0A135SN03;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 30.
DE SubName: Full=Endothiapepsin {ECO:0000313|EMBL:KXH37255.1};
GN ORFNames=CNYM01_13087 {ECO:0000313|EMBL:KXH37255.1};
OS Colletotrichum nymphaeae SA-01.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH37255.1, ECO:0000313|Proteomes:UP000070054};
RN [1] {ECO:0000313|EMBL:KXH37255.1, ECO:0000313|Proteomes:UP000070054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-01 {ECO:0000313|EMBL:KXH37255.1,
RC ECO:0000313|Proteomes:UP000070054};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:KXH37255.1}.
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DR EMBL; JEMN01001448; KXH37255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135SN03; -.
DR Proteomes; UP000070054; 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};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454}.
FT DOMAIN 158..474
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 88..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 362
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 398..437
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 478 AA; 49402 MW; BFDB59B83E135AE5 CRC64;
MRFTKPAAVA AFVPFASHLV DAAPRKLEIS TLGGAAFRIE QAPNPDFYYG NRRGPIALAR
AYSKFGQQIP DDLLGLIDQI LGELGLLNGG KGNGGRKGGK GGGKGKGKGG KGGNAGAGGS
KGNGTTTTPG GGGNKGNGTK TPPGGEVAAI PAEFDSQYLC PVQIGTPPQT IPLNFDTGSS
DLWVFSSETP ITQVAGQTVY NINASTSAKV LQGASWSISY GDGSSSQGNV FMDTVTIGGV
TVESQAVESA TQVSSSFSRN KNQSGLVGLA FGNINTVTPA KQKTFFENAM NNLAMPLFTA
NLKKAAAGNY NFGFLDSTEY TGDITFVPAN TTQGFWQFTA QGFAVGSNGS APTSAPHAAI
ADTGTTLMLL PDAIVSAYYQ RIASAKYDAT NGGFVFNCKD TIPSFTVDMG KYQAVVPGDF
MKFAPVDGQT VETSTTCFGG IQSSAGLPFA IYGDVFLKSQ FVVFHGGNKE LGFANKPL
//
