ID A0A135TL96_9PEZI Unreviewed; 399 AA.
AC A0A135TL96;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 27.
DE SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:KXH48877.1};
GN ORFNames=CSAL01_09006 {ECO:0000313|EMBL:KXH48877.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH48877.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH48877.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH48877.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
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:KXH48877.1}.
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DR EMBL; JFFI01001940; KXH48877.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135TL96; -.
DR STRING; 1209931.A0A135TL96; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000070121; 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 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; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
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, ECO:0000313|EMBL:KXH48877.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070121};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..399
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007803801"
FT DOMAIN 85..395
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 103
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 287
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 116..121
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 399 AA; 43570 MW; 7CA90E52B72DC973 CRC64;
MKSTLLTAAV LLGAAQAEVH KLKLKKVPIE EQLNSVPIEH QVRQLGQKYM GARPDSHADA
MFNQKPFTST GEHPVPVSNF MNAQYFSEIE IGTPPQTFKV VLDTGSSNLW VPSQQCGSIA
CYLHSKYDSS SSSTYKSNGS EFEIHYGSGS LTGFVSQDDV SIGDLKIKKQ DFAEATSEPG
LAFAFGRFDG ILGLGYDTIS VNKIVPPFYN LVNQKAIDEP VFAFYLGDTN EEGDESEATF
GGIDDSHYEG KITYIPLRRK AYWEVDLDAI TLGDETADLE GHGAILDTGT SLNVLPSALA
ELLNKEIGAK KGYNGQYSVE CSKRDELPDI TFTLSGYNFS ISAYDYVLEV SGSCISTFQG
MDFPEPVGPL VILGDAFLRR WYSVYDLGKN AVGLAKAKK
//