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
//