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Database: UniProt
Entry: A0A163DA79_DIDRA
LinkDB: A0A163DA79_DIDRA
Original site: A0A163DA79_DIDRA 
ID   A0A163DA79_DIDRA        Unreviewed;       443 AA.
AC   A0A163DA79;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KZM23024.1};
GN   ORFNames=ST47_g5618 {ECO:0000313|EMBL:KZM23024.1};
OS   Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS   rabiei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX   NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM23024.1, ECO:0000313|Proteomes:UP000076837};
RN   [1] {ECO:0000313|EMBL:KZM23024.1, ECO:0000313|Proteomes:UP000076837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ArDII {ECO:0000313|EMBL:KZM23024.1,
RC   ECO:0000313|Proteomes:UP000076837};
RX   PubMed=27091329; DOI=10.1038/srep24638;
RA   Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT   "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT   Ascochyta rabiei provides insight into the necrotrophic effector
RT   repertoire.";
RL   Sci. Rep. 6:24638-24638(2016).
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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:KZM23024.1}.
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DR   EMBL; JYNV01000200; KZM23024.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A163DA79; -.
DR   STRING; 5454.A0A163DA79; -.
DR   Proteomes; UP000076837; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR46720; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01460)-RELATED; 1.
DR   PANTHER; PTHR46720:SF3; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01460)-RELATED; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT   DOMAIN          9..362
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   443 AA;  48309 MW;  2310CCC957AFA9E1 CRC64;
     MADQQSGIAI VGAGVGGLAF AIGLTRHSIP FTIYESAPAF STVGAGVGLG PNALRAMDLI
     DKRFRDMYMD VATGNLNPEK KHVMMEAMRM EEGLGQGESW WGHGEWGAPY FERTGAHRKD
     LLDIMTSLID KDAVRFNSTV VDIEQSNDQV ALTFADGRVA GHAAVIDCGG IRGLARRIVL
     ADHFPEAVEP QYTHKYVYRT VVSTEDATEM LGELATDAKM FVSRDANLST YPISKGKQVN
     VVAFKRDPHP WQHARGTLEV DRKSMLEDFG GIGMDKRLSR LLEHVAPIRW PIFDHPTTPT
     YHSGLLCLLG DAAHASTPHQ GAGAGQALED ALILTVALSK LHSTLPLSLL ATPSPARTAA
     FTAAFTAYDE VRRPRAQRQV ATARECGELY NLRDPKTGDA MGVEEVLGEL RGRFEWLWSH
     DLEGGVGGVE DRVRVLLREG GVL
//
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