ID A0A0D2JQ25_9EURO Unreviewed; 637 AA.
AC A0A0D2JQ25;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=Z520_11638 {ECO:0000313|EMBL:KIX92609.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX92609.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIX92609.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX92609.1,
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 -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:60344; EC=1.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00036596};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; KN848102; KIX92609.1; -; Genomic_DNA.
DR RefSeq; XP_016626732.1; XM_016782126.1.
DR AlphaFoldDB; A0A0D2JQ25; -.
DR STRING; 1442371.A0A0D2JQ25; -.
DR GeneID; 27717384; -.
DR VEuPathDB; FungiDB:Z520_11638; -.
DR OrthoDB; 9164at2759; -.
DR Proteomes; UP000053411; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19384:SF84; METHIONINE SYNTHASE REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053411}.
FT DOMAIN 216..488
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 70257 MW; CFF81E3CBB799F9A CRC64;
MSATMASGHP LPLTAHSHPD NPVPEEPMTS RKLSISASQL STVPSSSYSD SASSVDTEPT
TPTTENLSDV PFDDLNGQPS QNPQGKKRRA STLLVSQDSE DARLFLGERG ASTAMIQKAC
CGGGCCMLQE LRTKRPRPGQ TPLKIPQNPA YQSLKINLGH LSLDSELSGI VEVPPKTVSF
ESLSSSPSRT YAEPQRQQKP EVLKHPPNFV TPHPPYEVFS APLFHARELT KPGAEKRTYH
FDIDVTDYPK ESGDVDFVVG GAIGVCAPNP PDMVDQIFDL LGVPSFVRDK PILLKTTTGR
WPTIWGEEEA RELVTTRREL LTWCSDIQSY PPTKGLFRLL AEHAEDENEK IILMYLSSAQ
GQAAFCDLRT GPYITLPQLL SSFPSSRPPL DHILSVLNQL MPRFYSLSQD PTISCQRDGT
QCRRLIEIAV TVHEADDYAT GKRTGVGSGF LERLAKQVIQ AEQEGKNPRD LDLRVPMFRG
LMANPLAREF VTDGPMLLIG AGVGIAPFRG FVHRRLKSAN CANKVWVLQG VRDSLLDELY
SGDWGVHEDK VKKVVQSRRG QGRYVQEEVR AQADLVWFII NAVDGRIFVC GSSKGMGEGV
EAALIDVAMA KGKLNRDEAQ SFWDEKKSSG QYIAETW
//
