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Database: UniProt
Entry: B2W2I9_PYRTR
LinkDB: B2W2I9_PYRTR
Original site: B2W2I9_PYRTR 
ID   B2W2I9_PYRTR            Unreviewed;       480 AA.
AC   B2W2I9;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   SubName: Full=Candidapepsin-4 {ECO:0000313|EMBL:EDU46475.1};
GN   ORFNames=PTRG_03637 {ECO:0000313|EMBL:EDU46475.1};
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU46475.1, ECO:0000313|Proteomes:UP000001471};
RN   [1] {ECO:0000313|Proteomes:UP000001471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; DS231617; EDU46475.1; -; Genomic_DNA.
DR   RefSeq; XP_001933970.1; XM_001933935.1.
DR   AlphaFoldDB; B2W2I9; -.
DR   STRING; 426418.B2W2I9; -.
DR   EnsemblFungi; EDU46475; EDU46475; PTRG_03637.
DR   GeneID; 6341868; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_9_3_1; -.
DR   InParanoid; B2W2I9; -.
DR   OMA; CNVTLGT; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000001471; 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};
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:UP000001471};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..480
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002784448"
FT   DOMAIN          67..389
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        85
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        315..353
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   480 AA;  50127 MW;  C45AAA904D2C6F55 CRC64;
     MKYTTILVLV AQLAASAAAL KLVPRENPAV VRLDTQRRNV INPIAHDQLR RRQSVVQQTL
     DNLETLYFAN ASMGTPPQNF RLHIDTGSSD LWVNSANSNL CAQGGNQCGQ SGIYNANDSS
     TYKYVNSVFN ISYVDGSGAS GDYATDTFRI GGTTVRNLQF GIGYVSSSPE GILGIGYTIN
     EVAVGRAGLQ PYPNLPQKLV DDKTIKTNAY SLWLNDLDAS TGSILFGGVD TDKFSGELQT
     LPIIPDRGEF AEFIIALTGM GMNGKNGSLF ENDNVPVLLD SGSSLMYLPD AVVRSLYSTF
     NARYDSSQGA AFVDCKLADQ QGSVDFNFSG VMISVPINEL VIVAAVSRGQ PVCILGIAPA
     GNSVSVLGDT FLRSAYVVYD LANNEISLAQ TNFNATTENV QEIQSGTGGV PNAKAVAGAI
     STAAVGTGGP RVNGPSVTGG AGGSISSSTG AAVPYATMNP WVSGAAALAG AGIMVGFNGF
//
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