ID A0A139HVV9_9PEZI Unreviewed; 451 AA.
AC A0A139HVV9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 28-JUN-2023, entry version 31.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=AC579_6721 {ECO:0000313|EMBL:KXT06557.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT06557.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT06557.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT06557.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KXT06557.1}.
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DR EMBL; LFZO01000551; KXT06557.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139HVV9; -.
DR STRING; 113226.A0A139HVV9; -.
DR Proteomes; UP000073492; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05474; SAP_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..451
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007297023"
FT DOMAIN 80..393
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 26..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 98
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 275
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 310..349
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 451 AA; 49228 MW; 22044E1D067123EA CRC64;
MNTHTISVAI ATILLLGSAE AINLKQKSTS DTSPKVVHQK VHKHHHIDNP AERDRRRFVH
KRQAENGAVN VPLSNELFLY YMEMTVGTPP QEFQVHVDTG SSDLWLNYAG SDYCESRSDP
CITGTYSAND SSTYEYVNSL FTIQYVDGSE SAGDYQFGVG YDSSTPDGIL GIGYAANEVQ
VAYGGKTYAN LPVSLRDQKY INTLAYSFWL NDLMAEEGEL LFGGVDTAKY TGDLVSLPII
AEKGVYREFT VELTAVGLSG DAEEFSGTTT EIHLDTGASL SYLPDDTTRA IWDRLDAQYL
EEYGVAIADC SLAATDDTID FRFSDDLTIQ VSMREMVIPL PTGLGFDVCF VGVLPAARSP
LSTSDRQYLI LGDTFLRSAY VVYDLENNEI SMAQTLFNTT DSNVVEIANG TDMPSGTGSD
SDEQESGGSS PRSSSIALLL MMVVGTMVFL N
//