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Database: UniProt
Entry: A7EE76_SCLS1
LinkDB: A7EE76_SCLS1
Original site: A7EE76_SCLS1 
ID   A7EE76_SCLS1            Unreviewed;       571 AA.
AC   A7EE76;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=SS1G_03616 {ECO:0000313|EMBL:EDO01142.1};
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079 {ECO:0000313|EMBL:EDO01142.1, ECO:0000313|Proteomes:UP000001312};
RN   [1] {ECO:0000313|Proteomes:UP000001312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   EMBL; CH476624; EDO01142.1; -; Genomic_DNA.
DR   RefSeq; XP_001595527.1; XM_001595477.1.
DR   AlphaFoldDB; A7EE76; -.
DR   EnsemblFungi; EDO01142; EDO01142; SS1G_03616.
DR   GeneID; 5491881; -.
DR   KEGG; ssl:SS1G_03616; -.
DR   VEuPathDB; FungiDB:sscle_07g055330; -.
DR   eggNOG; ENOG502QUMR; Eukaryota.
DR   HOGENOM; CLU_040056_0_0_1; -.
DR   InParanoid; A7EE76; -.
DR   OMA; YAQWVNL; -.
DR   OrthoDB; 1951464at2759; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 2.
DR   Gene3D; 3.40.462.20; -; 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:SF39; 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:UP000001312}.
FT   DOMAIN          51..231
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   571 AA;  64783 MW;  2A67E055F51A8A33 CRC64;
     MATGEFTAKE IAIQDLENLV NTLGFSNCFK KGKGFYENEV TQYATSSYEY VRTLPALILK
     PRNKQDIATI LEYATKRKIG VSVRTGGHQY SGASSCTAPN IQMDLSETFK GPDDRTLLRK
     QGRLHTSVSW SLKEFTDFCA ENRIFAPHGQ CIAVHLGGHV QTGGYGQLGR SFGLLADHVL
     EIDIVDYEGI PRRLVHDSPN EAERDLFNAI LGGSPGNFGV VTHFTIKVHK DEDYEGSIGM
     KCLYPYSRDR AEKLLDLVAK MSDGLDSEGN EMVLARNYDV CLNVVSSGNE FAALFPGKAK
     SLRDFYNNHD DLPNIDPNLP QYPKLIYVWA QWVKLKDTDV FDEKLWFDKL SDGCIDSISI
     NHKELMSYPM SYMTGSWWIL DAVREYPYPY IKSTRMSDKT DLSKSGWPKW LAQRIDKIVA
     PENNGLFVCA QIQPFGGPES KTVKNANNGT SYSWRNSTIT CTLDCFYNFK HDKKQEAEQW
     QKENEEGAIG ENGVFSTKDM RPLWGSFGEY DFSKIWDAYH DSQEKYDKLR RLRKIHDPTG
     VFTPNTFCVP REGEDTKDLL AERVKQQALL S
//
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