ID V2WPK7_MONRO Unreviewed; 497 AA.
AC V2WPK7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Fad binding domain-containing protein {ECO:0000313|EMBL:ESK83517.1};
GN ORFNames=Moror_4862 {ECO:0000313|EMBL:ESK83517.1};
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:ESK83517.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK83517.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK83517.1,
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 -!- 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:ESK83517.1}.
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DR EMBL; AWSO01001526; ESK83517.1; -; Genomic_DNA.
DR RefSeq; XP_007857180.1; XM_007858989.1.
DR AlphaFoldDB; V2WPK7; -.
DR KEGG; mrr:Moror_4862; -.
DR HOGENOM; CLU_018354_1_0_1; -.
DR OrthoDB; 2463849at2759; -.
DR Proteomes; UP000017559; 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:SF22; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..497
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004711126"
FT DOMAIN 65..236
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 497 AA; 53503 MW; DA25BE89CD608EC3 CRC64;
MSMRTLLGLV LIASHSLLHI DAAPTDPGQA ACSSLVSLLG SELVQSQSGS DFQSSVDTPL
NLINNALVPA CVVYPTNTTH VSAAMSAIYK AKSRYAVLAG GHSAMKGWNN VAGGVLIDFR
DMRQATYDAQ KDTITLQPGI RWVEAVTALA PQGVAPVGGR AAHVGSGFFL GGGISFLSPS
RGWGADNYKE LDVVLVNGTV VTANANNEHK DLFKALKGGG NRFGIVTRYE VEAFHSGTQD
DKRWVGGVIQ YPESSVEAVI KATARYTREV KDPNGTIFSA LVSSVSDSGN ITTIMPVYVF
YQGKELPKSI FGELLSIPHT NISISAMSYA DIVANTFPRE DARGSTYIYG SSALSGKDEK
AFLNVYKTNL KFTKENMNLL NNTSITLTPI PDSQIQFGRQ RGGNAIDAPL TGGYAVVQMA
QTLRAGQVEV PKSVLDGKKK LLDQNKPSAG LPLFLNECDA NQNIFASYGQ YDFLKRTYKK
YDPERFNVRF TDGPKGL
//
