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Database: UniProt
Entry: A0A0D1YCQ2_9PEZI
LinkDB: A0A0D1YCQ2_9PEZI
Original site: A0A0D1YCQ2_9PEZI 
ID   A0A0D1YCQ2_9PEZI        Unreviewed;       521 AA.
AC   A0A0D1YCQ2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIV98451.1};
GN   ORFNames=PV09_09736 {ECO:0000313|EMBL:KIV98451.1};
OS   Verruconis gallopava.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX   NCBI_TaxID=253628 {ECO:0000313|EMBL:KIV98451.1, ECO:0000313|Proteomes:UP000053259};
RN   [1] {ECO:0000313|EMBL:KIV98451.1, ECO:0000313|Proteomes:UP000053259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 43764 {ECO:0000313|EMBL:KIV98451.1,
RC   ECO:0000313|Proteomes:UP000053259};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004721}.
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00010139}.
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DR   EMBL; KN847681; KIV98451.1; -; Genomic_DNA.
DR   RefSeq; XP_016208321.1; XM_016363853.1.
DR   AlphaFoldDB; A0A0D1YCQ2; -.
DR   GeneID; 27317709; -.
DR   VEuPathDB; FungiDB:PV09_09736; -.
DR   HOGENOM; CLU_006937_8_2_1; -.
DR   OrthoDB; 2785305at2759; -.
DR   Proteomes; UP000053259; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR43098:SF2; FAD-BINDING MONOOXYGENASE AUSB-RELATED; 1.
DR   PANTHER; PTHR43098; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053259}.
SQ   SEQUENCE   521 AA;  58505 MW;  FC2200CA7C4F13F7 CRC64;
     MCDVEGYIYM PLLEETGYMP KHKYSYGPEL RGHAERIADM WNLRSRTIFR QHTQSMEWDN
     SKAEWIVHTQ FTTRDRKDLD QTIRAKYVLL GGGQLTHPKV PIVKGLDRFD RHMFHTSRWD
     YEYTGGTSED NKPAMDKLKD KVVAIIGTGA TAVQTVPELA KYAKHLYVVQ RTPSSVDIRG
     QRETDSTWWK EMTSQKGWWR ARNANYADIL GQKNPPPKDN LVADQWTIGN PSYCTAWGYD
     GVLAPEEVPK YVHDLHVQDV PRAERIRQRV EETVKDRATA EKLKHWYPTW CKRPCFHDEY
     LPAFNRPNVT LVDTDGHGVD SFTETGFIVA GKEYAVDCLV LSTGYKTRGP APTARFDVRI
     TGRDGIDMGK AFDDEVSTLH GLMRAGFPNL FFSGIAQASL SGNVVYNADV FARHVAYILS
     TAQQRHGAGA LIESTQLAEQ AWGDLVATYS VGLAGMGGCT PSYLNSEGGL DKMMQTAPPE
     ALAKIVRSGL WGRGVNHYMM TLDDWKNEGR LNGLSIAAAA A
//
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