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Database: UniProt
Entry: A0A139IF24_9PEZI
LinkDB: A0A139IF24_9PEZI
Original site: A0A139IF24_9PEZI 
ID   A0A139IF24_9PEZI        Unreviewed;       447 AA.
AC   A0A139IF24;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
DE   Flags: Fragment;
GN   ORFNames=AC579_9394 {ECO:0000313|EMBL:KXT13166.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT13166.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT13166.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT13166.1,
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:KXT13166.1}.
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DR   EMBL; LFZO01000127; KXT13166.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139IF24; -.
DR   STRING; 113226.A0A139IF24; -.
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; 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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF51; NAPSIN-A; 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   Reference proteome {ECO:0000313|Proteomes:UP000073492}.
FT   DOMAIN          26..357
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          409..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..431
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         447
FT                   /evidence="ECO:0000313|EMBL:KXT13166.1"
SQ   SEQUENCE   447 AA;  47828 MW;  1CF447AA8A5AF835 CRC64;
     MAEAIVPSPF ILQPTFDWFG NDGNWSTFRI NVGSPPQSFQ VLPSTVASEF WVAIPVGCSS
     DPSTGCAASR GVEPFGGVQY QGFQANCSTT WNQQGVFSLG IESALYGPDI TGQYGLDTVS
     FGSVGRSANL TDQAVGGIAS GDFWLGIIGL ATAQSDFGSQ RVSSPLSSMK AQNLTPSASY
     GLSVGAAHRS SAGGIVIGGF DEAAFEPSNI SFAAWAGSAR ALTVSLQNIV VSNPALGTNT
     LFTSPLNMSI DMTISQIWFP ETVCESIAQL CGLTFDDSTD YFTFTIAANS GENQTYNIVL
     PYAAFDQQVG WAKYNNGMAY FPIRRARNDT QYVLGRTFLQ EAYVVDWERG NFTLGQSRHT
     NGVTEGSIVP ILSPEASQKS TLSTGALAGI RLWQLEHVVG ENYGDLKDES HWDEDGVAKE
     LPSRPLKRDA ELPGFDQTPG VELPDFP
//
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