ID   A0A1V6T9R0_9EURO        Unreviewed;       642 AA.
AC   A0A1V6T9R0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN   ORFNames=PENSTE_c009G03537 {ECO:0000313|EMBL:OQE23085.1};
OS   Penicillium steckii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE23085.1, ECO:0000313|Proteomes:UP000191285};
RN   [1] {ECO:0000313|Proteomes:UP000191285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQE23085.1}.
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DR   EMBL; MLKD01000009; OQE23085.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6T9R0; -.
DR   STRING; 303698.A0A1V6T9R0; -.
DR   OrthoDB; 9164at2759; -.
DR   Proteomes; UP000191285; 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:UP000191285}.
FT   DOMAIN          224..481
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   642 AA;  70277 MW;  5581169EBFCD37D6 CRC64;
     MVHAVESVMP SANVASTGAR SRKGTFQDIP VSSTSHPDNP IPEEPRGVRS LSITDFNFNG
     SPASQGTESS GSDSPATPLT PPDLQTLQVS DDNDNKPAGR SRRASTILIS QNSDDMRRVL
     ENVGTSGTQK IESMCCGGGC CRGRPLQPLD GPISGFNSIT APDNDAFESL GLNVDLLTLD
     SDLSNLAPLP EKTVSFSPAP AYTANFELGP SDHPPRFVQP HPPYEVYRAP LHHTRELTKG
     GAEKRTYHFD IDVTDYPAES GMVDFVVGGA IGVCPKNKDE EVEDILNLLG VPKSMRDKKV
     LMRTTKGRWP TIWGDDKPRE LITSRREVLS WCSDIQSYAP TKALFRTLAE YAYEQNEKKI
     LEYLSSAQGQ GAFCELRTSS HISLSQLLHA FPSSQPPLDH LLSVLNTLMP RFYSLSQDPM
     ISCQFKGTEC RRLVEVAVTV ADSDDWRGGT RTGVGSGYLE SLARKAIAAE ARGEKLDIHI
     PMFRGLMANP LATKFASDGP MLLIGAGVGI APFRGFVQRR LQSANCANKV WVLQGVRDSL
     LDELYSGEWG VHEDKVRTVV QSRRGESRYV QEEVRHQADL VWYVINALDG RVFVCGSGKG
     MGEGVEAALV EVAMAKGNLN SEEATLFWQR KKEAGQYIAE TW
//