ID A0A0D2D8C0_9EURO Unreviewed; 439 AA.
AC A0A0D2D8C0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN ORFNames=PV07_03545 {ECO:0000313|EMBL:KIW31959.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW31959.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW31959.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW31959.1,
RC ECO:0000313|Proteomes:UP000054466};
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 Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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DR EMBL; KN847041; KIW31959.1; -; Genomic_DNA.
DR RefSeq; XP_016252175.1; XM_016390273.1.
DR AlphaFoldDB; A0A0D2D8C0; -.
DR STRING; 569365.A0A0D2D8C0; -.
DR GeneID; 27342739; -.
DR VEuPathDB; FungiDB:PV07_03545; -.
DR HOGENOM; CLU_009665_19_3_1; -.
DR OrthoDB; 981595at2759; -.
DR Proteomes; UP000054466; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR PANTHER; PTHR13789:SF147; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G01950)-RELATED; 1.
DR Pfam; PF01494; FAD_binding_3; 2.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054466}.
FT DOMAIN 5..172
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 297..359
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 439 AA; 48332 MW; 0D58B0325D29D299 CRC64;
MASLQIIIIG TGIAGLATAI SLSQKTKHNI LILESSPILT EAGAGIQCSA AASRILSNWG
LRKQFEAVAT CPDFTEIRRY EDNELIGLIF ANVKNYSTRL RGFPHWLVHR VDYQKILAEA
AATSGVKIEF GQKVMAIDVE QVKVILEGGR SLHADLIIGA DGIHSRTRAS IPGLKDVVPQ
RTENYCYRAL VPREEMLKNP VTATLIDNQS QQAWAGQFKH IIAYPIAKGR FYNLVMTIPD
LGDAPLGKYN EPGDVVEMRQ VFKDFNDTVQ AVLDAVDSCA KWVLAELPPL PTWSSPDGRV
ILVGDACHAM APHAASGAAT SLEDAEVLGL CVATCNGLAD LPRAAKDYEH LRKARCERIQ
EISRENATTF ALPDGPMQQA RDRIWIAQKA MLEKQLQEDS PLIVPAEDMT QQFPHPALVQ
WLVGHDIIEE AKRYLASRE
//
