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
//