GenomeNet

Database: UniProt
Entry: A0A166UCL4_9PEZI
LinkDB: A0A166UCL4_9PEZI
Original site: A0A166UCL4_9PEZI 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system