ID   A0A139ITF0_9PEZI        Unreviewed;       512 AA.
AC   A0A139ITF0;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=AC579_4593 {ECO:0000313|EMBL:KXT18029.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT18029.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT18029.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT18029.1,
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 oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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:KXT18029.1}.
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DR   EMBL; LFZO01000011; KXT18029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139ITF0; -.
DR   STRING; 113226.A0A139ITF0; -.
DR   Proteomes; UP000073492; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR   PANTHER; PTHR42973:SF54; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..512
FT                   /note="FAD-binding PCMH-type domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007297712"
FT   DOMAIN          68..241
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   512 AA;  56890 MW;  A8CF78D6C6D37FF3 CRC64;
     MIKNIALVAS FLSTCLAYSI HRPEGFDDPQ PNTSCCAMLS AALGSKISYP SDLTYNDSLT
     SYWSDRETDV KPKCIVRPNL DQDVSQAVRL LASNKHCKFA IRGGGHLGWP EAANIQDGIT
     FDLSSLDSVS VSQDKTITTV GGGAYWNQVY SYLDTMNLNC AGGRYATVGV GGLTLGGGIS
     FFSPRVGWVA DTVESFDVVL GNGQLEEGVS STKYPDLFRA LKGGSNNFGI VTSLKLKTWS
     GGPFLTGTVE YDISHTPELS QAFLKTVGTK KENWDPYAAF LQQYYFVKDP STNGTTSTRI
     DNILAYTQPF PKDDSTPNFL KPLQNAAPSK RIDLGVQHLS EFLTKFQDKD STKPRQVLSN
     LSFRQDESNF MEKLISLFES TTKLLFRKMS HMYLVLVFQP IHPVFTSRGN NSLGFDPEEE
     VPLVNLCIQT SWAGAEFDDL VVSTIREAIE KANELAKEYG VDSDWLYLNY SEEWQDPIPG
     YGEEVEILRM VSREYDPEGV FQRQVPGGFK LW
//