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Database: UniProt
Entry: A0A0D2K021_9EURO
LinkDB: A0A0D2K021_9EURO
Original site: A0A0D2K021_9EURO 
ID   A0A0D2K021_9EURO        Unreviewed;       541 AA.
AC   A0A0D2K021;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=Z520_08007 {ECO:0000313|EMBL:KIX96229.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX96229.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIX96229.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX96229.1,
RC   ECO:0000313|Proteomes:UP000053411};
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 Fonsecaea multimorphosa CBS 102226.";
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   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   EMBL; KN848078; KIX96229.1; -; Genomic_DNA.
DR   RefSeq; XP_016630352.1; XM_016778504.1.
DR   AlphaFoldDB; A0A0D2K021; -.
DR   STRING; 1442371.A0A0D2K021; -.
DR   GeneID; 27713753; -.
DR   VEuPathDB; FungiDB:Z520_08007; -.
DR   OrthoDB; 1094055at2759; -.
DR   Proteomes; UP000053411; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.30.465.10; -; 2.
DR   Gene3D; 3.40.462.20; -; 2.
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:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..541
FT                   /note="FAD-binding PCMH-type domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002245801"
FT   DOMAIN          72..242
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   541 AA;  58702 MW;  F44BEC71233D2DC5 CRC64;
     MLFVTRGGMS WKALFTCVLA LLSSTVIAAP GSNFKALQQC VNGALAGGGN VEKRVQSPAN
     ATWDDAYIGA IIKPETPAMI AFAESFTEVG ALMGCANTTG YQAVPRSGRH HFEGWSALNG
     SLVIDVSSLD YIKVSSDLSN ATIGAGANLG QIYTELSVVN KTFLGGICPT VALGGYLGVG
     GYSLQHRALG IAVDQVLSFK AILASGELVT VSPTSYPDLW FAARGGGQYA FIVEATVKIL
     TLPRSAMVVG FYNNSDTRYE VARKWLDWAP TAPKELTTQL NVYSNRTHLI GWYLGGSPEQ
     LRTALNSSGL LDVADGVVSI DGNCSTANSR MYWQDPSTRC TDDASAYKAF LKVYNTESIN
     LTPIQPAFRL DNTPALPSEP VAEPWPRFGV ISKTYFTQKS RPITNDTLKE LINSSASLGE
     EAGFWGEWTS FGIANPTTTS AFPWLKEAQA LLRIEMNSPK NVTQYNQNRA WLLNFEKFFR
     PRVGNASYAG YVDADISINP LTAFYGNNTC RLISIKQKYD PNNFFRNPFS VPTQVPKGIS
     C
//
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