ID   A0A446BFI0_9PEZI        Unreviewed;       616 AA.
AC   A0A446BFI0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   22-FEB-2023, entry version 13.
DE   SubName: Full=207a95d4-ec4c-4407-97e6-f4519bbca4ef {ECO:0000313|EMBL:SPQ21272.1};
GN   ORFNames=TT172_LOCUS3691 {ECO:0000313|EMBL:SPQ21272.1};
OS   Thermothielavioides terrestris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides.
OX   NCBI_TaxID=2587410 {ECO:0000313|EMBL:SPQ21272.1, ECO:0000313|Proteomes:UP000289323};
RN   [1] {ECO:0000313|EMBL:SPQ21272.1, ECO:0000313|Proteomes:UP000289323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Huttner S., Dainat J.;
RL   Submitted (APR-2018) 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; OUUZ01000008; SPQ21272.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A446BFI0; -.
DR   Proteomes; UP000289323; Unassembled WGS sequence.
DR   GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC.
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}.
FT   DOMAIN          198..471
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          11..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          142..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   616 AA;  68670 MW;  93F23B2F4A9C8C8C CRC64;
     MSTQIDLLLA THSAASIPEE PQPGPSAAPS LTYSDSSDEH EPEEPRQPEL RRRRASTRLI
     AQSPADVQRI TGETTTQLIR RCCGGGCCLG LGRPEQQDVD FEQIEFPDND AYRSLCLKID
     RVPATLTNVC DVPEQTVFLQ PLRRPSSIPS PTDSAASLDA DGETSAVGDV EKTLHNLSLE
     APDTRIQPPL FVQPHPPHHV FAARIHSARE LTRPGAEKRT FHFDLDVTNY PEGEDVDFKV
     GGAIGVTAPN EASMVEEVLD LLLVPRFLRD KPVLLRTTKG RWPTVWGDDQ ARELVTTRRD
     LLTWCSDIQS YPPTKPLLRV LAEHATDANE RKVLLYLCSA EGQGVFCDFR TGPHVSLVQL
     LHAFPSAKPP LDLLLSVLQP LMPRFYSLSN DPHESFLTRD GKQHRLIEIA VTVHETADWR
     SGRRTGVGSG FFQRQALAFL DAQRRGEKDP EFYIPMFKGL MANPLAKQFV SDGPMLLIGA
     GVGIAPFRGF VQRRLKTANC ANKVWVLQGI RDSLLDELYS GEWGAHEDEV KRVVESRRGE
     GRYVQEEVRA QADLVWYIIN SVDGRVFVCG SSKGMGEGVE QALVDVAMAK GNLEREEAQQ
     FWNLKREAGQ YITETW
//