ID G2YS10_BOTF4 Unreviewed; 437 AA.
AC G2YS10;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Similar to FAD binding domain containing protein {ECO:0000313|EMBL:CCD54408.1};
GN ORFNames=BofuT4_P124560.1 {ECO:0000313|EMBL:CCD54408.1};
OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD54408.1, ECO:0000313|Proteomes:UP000008177};
RN [1] {ECO:0000313|Proteomes:UP000008177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; FQ790351; CCD54408.1; -; Genomic_DNA.
DR AlphaFoldDB; G2YS10; -.
DR STRING; 999810.G2YS10; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_018354_1_1_1; -.
DR InParanoid; G2YS10; -.
DR Proteomes; UP000008177; Unplaced contigs.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008177};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..437
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003440923"
FT DOMAIN 1..168
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 437 AA; 47145 MW; 0D091A67DA347435 CRC64;
MLLLRVALVT ITLGFTRAAS SSECCQFSVK GGGHTPFPGA ASINDGVTID LAKLNTISVD
KNANIAYVGS GLKWGQIYEY LEPKNMMVAG GRDSLVGIGG LIVGGGYSWF APQKGFVADT
VINFELVVGN GSIINVNATS NSDLFVGLKG GGNNFGIVTR YDMETFPFDK LWGGIMVYPA
STAKAQINFF TNFTNHISDD PKANFLNIWS YKQVSGTQSI FNVIDYVAPV VAPAIYSDAL
AIPDLVSSTM RITNVSSLTD ELSGTSTLDS RYIFVTTTFS NSAEMYETAV NISNKHLEPF
KNTTGLVWSI LFQPIPLIVS EHSVAAGGNI MGVDRSKDNL TLFLVYVTWL EASDDQKLTD
AAYATVEEIN AATDDLGVTN PFVYLNYAGK TQNPLAGYGE KNTEKMRALS KKYDPRGTFQ
KLVKGGFKIP GVETVID
//