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Database: UniProt
Entry: A0A0D2HKP7_9EURO
LinkDB: A0A0D2HKP7_9EURO
Original site: A0A0D2HKP7_9EURO 
ID   A0A0D2HKP7_9EURO        Unreviewed;       603 AA.
AC   A0A0D2HKP7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=Z520_02554 {ECO:0000313|EMBL:KIY02416.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY02416.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIY02416.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY02416.1,
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};
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DR   EMBL; KN848064; KIY02416.1; -; Genomic_DNA.
DR   RefSeq; XP_016636538.1; XM_016773068.1.
DR   AlphaFoldDB; A0A0D2HKP7; -.
DR   STRING; 1442371.A0A0D2HKP7; -.
DR   GeneID; 27708300; -.
DR   VEuPathDB; FungiDB:Z520_02554; -.
DR   OrthoDB; 1664005at2759; -.
DR   Proteomes; UP000053411; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748:SF116; D-LACTATE DEHYDROGENASE (CYTOCHROME) (AFU_ORTHOLOGUE AFUA_7G02560); 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053411}.
FT   DOMAIN          177..354
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          114..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   603 AA;  66049 MW;  6DB6AE4E399C56DF CRC64;
     MKSIARLSRP VGSLLRCAER ERSCFAPWAA RSFHNSHTKL EEQSKGDAKE NLSFRGQLYQ
     STADRLKRER ASEEQYIKAA SSRGGGAGGR TLSLSFVILS VAAAAYYLGK RGERPLDASS
     TTPLPRAQPP QHDTRTSNLQ AAWVDFAQIV GKDNVSTVPD DLEAHSGSEF SSYTTKPNER
     PFAIVYPATT EEVSKIMKVC HERKIPVTAL SGGTSLEGHF APTRGGICID MARMDKILEL
     RTQDLDIVVQ PALGWEDLNE ELKGHGMFFP PDPGPGAKIG GMVGTGCSGT NAYRYGTMRD
     WVVSLTVVLA DGTIIKTRRR PRKSSAGYNL TQMFIGSEGT LGIVTEATLK ITVLPKSQSV
     AVATFPTIHS AAECVARVVG EGIQLAGMEI LDDVQMRCIN KSGMTSRPWQ EAPTLFFKFA
     GTPEGVKEQI KIIRNIAKGT KNQSFEFAKN DDEAAELWSA RKEALWSVMA MRKNNSDHVW
     TTDVAVPISR LADIIQETHD DVASSGLIGG ICGHVGDGNF HTILLYNDTE KKTAEDLVHR
     MIRRAIAMEG TVTGEHGVGL KKREYLREEL GEETVDAMRK LKQAFDPLGL LNCDKIVQIE
     QGH
//
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