ID V2XY32_MONRO Unreviewed; 407 AA.
AC V2XY32;
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 protease {ECO:0000313|EMBL:ESK97450.1};
GN ORFNames=Moror_17629 {ECO:0000313|EMBL:ESK97450.1};
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:ESK97450.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK97450.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK97450.1,
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}.
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:ESK97450.1}.
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DR EMBL; AWSO01000025; ESK97450.1; -; Genomic_DNA.
DR RefSeq; XP_007843202.1; XM_007845011.1.
DR AlphaFoldDB; V2XY32; -.
DR STRING; 1381753.V2XY32; -.
DR KEGG; mrr:Moror_17629; -.
DR HOGENOM; CLU_013253_1_4_1; -.
DR OrthoDB; 4946at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
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; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF1; ASPARTYL PROTEINASE; 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; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000313|EMBL:ESK97450.1};
KW Protease {ECO:0000313|EMBL:ESK97450.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..407
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004712910"
FT DOMAIN 97..404
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 63..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 115
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 294
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 128..132
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 407 AA; 42719 MW; 847BCF6F5FE4677D CRC64;
MRSLITALAL LQVALGLSIP TRVGNRIPLN KRSTLVDENG VVNIDTLKRQ LLRAQSKVQR
GVSAFEKNTG TAHPQAKKLS TRDTGNDPLQ DIDQVLWSGT ISVGTPAKEF TVDFDTGSSD
LFLPGASCTV NCAGHEVFDT DASSTAEDQD KTFMLRFGDG STSEGEVFHD TVTVAGLTAT
EQAVGAATQY SNGFAVDQFP PDGLMGMAFP EISDFEENPV FQTLVAQGVT TEPVFAFKLS
TSGSELTVGG TDDSLFSGQL TNTPVTTRGF WQVELEAVSV DGNAVVNGLS SIIDTGTTLI
LGDDRSVAAF YAAIPGSKDA SQTAGPGFFT VPCDSIPEVS LTFGGRAFSV SPDTFNLGLL
SRGSNDCVGG IAGGSPVEFW VVGDVFLQNV YTVFDVGNTQ VGFADLA
//
