ID   V2Y4M7_MONRO            Unreviewed;       456 AA.
AC   V2Y4M7;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Aspartic peptidase a1 {ECO:0000313|EMBL:ESK86594.1};
GN   ORFNames=Moror_9738 {ECO:0000313|EMBL:ESK86594.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK86594.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK86594.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK86594.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA   Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(2014).
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:ESK86594.1}.
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DR   EMBL; AWSO01000914; ESK86594.1; -; Genomic_DNA.
DR   RefSeq; XP_007854080.1; XM_007855889.1.
DR   AlphaFoldDB; V2Y4M7; -.
DR   MEROPS; A01.077; -.
DR   KEGG; mrr:Moror_9738; -.
DR   HOGENOM; CLU_013253_1_1_1; -.
DR   OrthoDB; 4946at2759; -.
DR   Proteomes; UP000017559; 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; cd05471; pepsin_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; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF51; 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..456
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004712565"
FT   DOMAIN          125..439
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        332
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        366..399
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   456 AA;  50687 MW;  6496454D21C137B7 CRC64;
     MRILHLSILS TSTLFLTAIA DPLPLHSPGF TAPLKHVWDL SRRSEVDISY RKRVEHGRRR
     LALAVGQPNP KKYFNRIDIP NMKGIQVDIK DSDGEKKTLL AASEAEEEDG YHSTRLEIES
     IDIGYICKTF IGTPLREFNM LVDSGSADFW VPREGCLSES GKKCAHKTLG PNTSNTFRSS
     NDFFFISYGS GDVLGFMGND TLSIADLQLK EYRFGTVTME SDYIALPEVS WDGIMGFGKP
     KISREPNTQP LLLALYNAGL IPFPIVSFKI PRFLDHEEGE MTLGALNPAR FKLDTVVTLQ
     STGTNGFWEV RVDKFGVNGA EMFSNEKVAI LDTGTTLIIV PPEDAELIHA FIPGSTFDGE
     EYRIPCNSSN HISVWFGGKE FDIDSRDMAM DLDEGKSECY SGIAPGDIGM GEGVWLMGDT
     LLKNVYMSLN MDTDEVTLAK LMQDTSRPCY FQVACE
//