ID A0A166UCL4_9PEZI Unreviewed; 483 AA.
AC A0A166UCL4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 31.
DE SubName: Full=Endothiapepsin {ECO:0000313|EMBL:KZL73242.1};
GN ORFNames=CT0861_11547 {ECO:0000313|EMBL:KZL73242.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL73242.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL73242.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL73242.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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:KZL73242.1}.
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DR EMBL; LFIV01000047; KZL73242.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166UCL4; -.
DR STRING; 708197.A0A166UCL4; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000076552; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..483
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007880513"
FT DOMAIN 160..479
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 92..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 367
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 403..442
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 483 AA; 50148 MW; 9FA6935D847AEAE0 CRC64;
MRFANSAAVA AFVPFVFHLV DAAPSKIEIA TLGGAAFRIE QVPNPDFYYG SRRGPIALAR
AYSKFGQQIP DDLLSLIDQI LEDLGLLNGG KGVHKGGKGK GKGKGKGKGG KGGGNAGAGG
SKGNGTTTTP GGGGGDKGNG TKTPPNGEVA AIPAEFDSQY LCPVQIGTPP QTLNLNFDTG
SSDLWVFSSE TPVTQVVGQT IYNINASSSA KALQGASWSI SYGDGSSSRG NVYMDTVTIG
GVTVENQAVE SANQVSASFS RNKNQSGLVG LAFGKINTVQ PAKQKTFFEN AMNNLATPLF
TANLKKAAVL LAGNYNFGFL DPTEFTGEIT FVPANTTAGF WQFTAQGFAV GSNGSAPTSA
PHEAIADTGT TLMLLPDAIV SAYYQRIASA KFDSTNGGFV FNCKDQIPSF TVDLGTYQAV
VPGEFMKFAP VDGETIETST TCFGGIQSAA ALPFAIYGDV FLKSQYVVFH GGNNELGFAN
KPL
//