ID V2WK83_MONRO Unreviewed; 411 AA.
AC V2WK83;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Fad binding domain-containing protein {ECO:0000313|EMBL:ESK87238.1};
GN ORFNames=Moror_5826 {ECO:0000313|EMBL:ESK87238.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK87238.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK87238.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK87238.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK87238.1}.
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DR EMBL; AWSO01000819; ESK87238.1; -; Genomic_DNA.
DR RefSeq; XP_007853469.1; XM_007855278.1.
DR AlphaFoldDB; V2WK83; -.
DR KEGG; mrr:Moror_5826; -.
DR HOGENOM; CLU_009665_3_2_1; -.
DR OrthoDB; 5491711at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
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; PTHR47178:SF3; FAD-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47178; MONOOXYGENASE, FAD-BINDING; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 302..341
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 411 AA; 46315 MW; 22699539BF1976DE CRC64;
MDKNRVLIIG GGPSGLLTAH ILNKLSIPYT LFEQDSDISS RAPDWDFGIH WTQSSLPACL
PRHITYEKLK AAQVDPGLDP AKDDFLPVFN LSTGEEMHRI NMPFVMRLRR SQFMKLLREG
LGDVRYGKRL SAINTDYDHV VTATFTDGTI EHGTLLIGTD GAQSVVRNFL FSSDPAKAAL
KPSRIVSRTV ITTLPPHAVD NIRALDKRMS IGHHPGGIFA WFGSHECPPN VPSSKWKYTL
MMSRKEPLHI PADQGGPGVL ERAKGIARIR FCEPFRSIWE AVPEGAQVWC NRLSSWPTEE
WDNRNGRVTL VGDAAHPMLP HRGQGLNSAI QDVARLSECL RFHYHPNPNP DRKVLGPFKK
ALDVYEKELW KRGRDAVIMS DENAEAVHDW ERLRMSPLWR FGIRPVDDLC A
//
