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Database: UniProt
Entry: V2XYL2_MONRO
LinkDB: V2XYL2_MONRO
Original site: V2XYL2_MONRO 
ID   V2XYL2_MONRO            Unreviewed;       491 AA.
AC   V2XYL2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   28-JUN-2023, entry version 32.
DE   SubName: Full=Putative fad dependent oxidoreductase {ECO:0000313|EMBL:ESK84494.1};
GN   ORFNames=Moror_6174 {ECO:0000313|EMBL:ESK84494.1};
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:ESK84494.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK84494.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK84494.1,
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:ESK84494.1}.
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DR   EMBL; AWSO01001292; ESK84494.1; -; Genomic_DNA.
DR   RefSeq; XP_007856207.1; XM_007858016.1.
DR   AlphaFoldDB; V2XYL2; -.
DR   KEGG; mrr:Moror_6174; -.
DR   HOGENOM; CLU_018354_1_0_1; -.
DR   OrthoDB; 1820950at2759; -.
DR   Proteomes; UP000017559; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.20; -; 1.
DR   InterPro; IPR012951; BBE.
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-RELATED; 1.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..491
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004712398"
FT   DOMAIN          57..229
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   491 AA;  52573 MW;  8B80B3C235EFE755 CRC64;
     MKGSKLLAAI TLSLNAGFGY GTSIAACNAL HSALPGRVSF PGSKAYVNDN QHYTQGSSQN
     STCSVEPASV DEVAIILQVV TNGITRSPFA VKGGGHTGNF GFSSTTGVQI SMSRFNQVEY
     DANTSTVKIG SGQIWENVYA QLASSGVSVV GGRVPGVGVG GLSLGGGYSF HSDQRGLTVD
     TIISHDLVLP NGTFVTVTNE TDSDLFFALK GGFNNFGIVT SFTMRAFPQT DVWIARITYP
     MNASDAVNQA IVKFTANNTD FKASTQPVYG AFGTSENDSI ITSSLFYDGP TPPSGLFDEY
     FNIPGAAPNI SGAISYPDAI TTLTAALASL NPPRTARHTV PIYHYTVGIL NEMKSQFERI
     IAETKASNRS FIALVISPEP FARPNVQSTD SAYPHPPGRF VCPSVLEVHW EDPAYDQFFV
     NAIAEAQQAI QAQAIKEGES FPNDILYSNY APGNTPLELI YGDNLSRLRE VKRRVDPENV
     MYLTGGFKIE P
//
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