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Database: UniProt
Entry: A0A139ICG7_9PEZI
LinkDB: A0A139ICG7_9PEZI
Original site: A0A139ICG7_9PEZI 
ID   A0A139ICG7_9PEZI        Unreviewed;       644 AA.
AC   A0A139ICG7;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=AC579_5649 {ECO:0000313|EMBL:KXT12296.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT12296.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT12296.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT12296.1,
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   -!- 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:KXT12296.1}.
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DR   EMBL; LFZO01000157; KXT12296.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139ICG7; -.
DR   STRING; 113226.A0A139ICG7; -.
DR   Proteomes; UP000073492; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   Pfam; PF00026; Asp; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        411..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          21..389
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          509..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..558
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..644
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   644 AA;  69113 MW;  90C8665EB940A203 CRC64;
     MVGPVSVQPY NQWLGNDGNW STIQVQIGTP PHLVNLLPAT SVSTIWPIDS QGCLISSDPT
     LISDPVNCPE LRGGLFSSAS VNDSSFQAVA ASNGDGYLYL PFSKSQQSQG YNGTAIVGTD
     TVVLTLKSGT PKLSGQTVAS NLDVLPYLGM FGLTGYASHV NSTSQADTTK APLQALKDGG
     TTSAYSYGYT AGRYYTAEPE LLSLTFGGYD ANRGAVTEDK AISATFGDDW QRDLVVVITG
     INIGGASVEG LDGGIHNVFI DSLIPEIWLP ESTCQAFERA FNLVWNETLQ YYLVNSSQHD
     QMLEDGKTVT FTLAGNKTEG APTVDIEMPY NAFDQALQYP LAGIEDASTS YRYFPLKRAS
     GSGQYTLGRT FLQEAYLTAD YGNSRFYVSK AKPLDGTALD LRCIGCKKSG LSTGAIVGIA
     VAAAVVGLMI AAFFFWRWKK KRDIRKLLAE LQVTSRASIG GTTIQDDDPH NVEFFKATIP
     AEEEVKPELD GSAAVPAGFV QYGRHELASN GSVRRTSQQS GLSRGTISPI SGRMPSHARN
     LSYGSSDGQP SPSAGDSPSL GQGVWGVSPH GSPDPEMREV RHHSGGQWYF ELPANPRSPQ
     SQRPALDVIQ STNAAPAEPP EVRADPRSPV VPESESRFRE DLRE
//
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