ID Q0V2F9_PHANO Unreviewed; 487 AA.
AC Q0V2F9;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 24-JAN-2024, entry version 98.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=SNOG_01805 {ECO:0000313|EMBL:EAT91454.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT91454.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; CH445326; EAT91454.2; -; Genomic_DNA.
DR RefSeq; XP_001792431.1; XM_001792379.1.
DR AlphaFoldDB; Q0V2F9; -.
DR EnsemblFungi; SNOT_01805; SNOT_01805; SNOG_01805.
DR GeneID; 5969276; -.
DR KEGG; pno:SNOG_01805; -.
DR VEuPathDB; FungiDB:JI435_018050; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_3_1; -.
DR InParanoid; Q0V2F9; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
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:UP000001055};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 79..401
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 97
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 292
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 327..365
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 487 AA; 50590 MW; BA25DABF431609CD CRC64;
MMKLQTSTAM RGSAIDNKRQ THSATANGSC HACAPPLAAR SHEVIGVILS NAGVSGRCSQ
PGATRSTVQQ TLDNLETLYY ANASLGTPPQ QFRLHIDTGS SDLWVNAKNS PLCQQGGNQC
GESGMYHAND SSTYKYVNGV FNISYVDGSG ASGDYATDDF RFGGQTVEDL QFGIGYESTS
PEGILGIGYT INEVAVGRGG LDPYPNLPQK LVDDGKITTN AYSLWLNDLD ASTGSILFGG
VDTDKFHGTL QTLPIIPERG EYAEFIIALT GMGQNGQNTS IFANQNVPVL LDSGSSLMYL
PDAVARQLYQ KYNARFDQAQ GAAYVDCDLA NQQGSLDFVF SGVHISVPLN ELVVVAAVSR
GQPICLLGVG PAGNSVAVLG DTFLRSAYVV YDLANNEISL AQTNFNATTE NIQEIQKGSD
GVPNATGVPD AVSTAAVGTG GPRVNGPSVT GGLGGSTGAA MPAATANPWL GGAAVIGAGA
LLGFNGF
//
