ID   A0A1V8SFM9_9PEZI        Unreviewed;       627 AA.
AC   A0A1V8SFM9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   13-SEP-2023, entry version 25.
DE   RecName: Full=NADPH-dependent FMN and FAD-containing oxidoreductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B0A48_16240 {ECO:0000313|EMBL:OQN97936.1};
OS   Rachicladosporium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQN97936.1, ECO:0000313|Proteomes:UP000192596};
RN   [1] {ECO:0000313|Proteomes:UP000192596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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:OQN97936.1}.
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DR   EMBL; NAJO01000049; OQN97936.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8SFM9; -.
DR   STRING; 1507870.A0A1V8SFM9; -.
DR   InParanoid; A0A1V8SFM9; -.
DR   OrthoDB; 276396at2759; -.
DR   Proteomes; UP000192596; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.360; -; 1.
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; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
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:SF10; NADPH-DEPENDENT DIFLAVIN OXIDOREDUCTASE 1; 1.
DR   PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192596}.
FT   DOMAIN          1..124
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          207..484
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          179..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   627 AA;  70469 MW;  D30EBE18AF021828 CRC64;
     MAERLRFDTT VLDLDSIQMR DLLKYSMVIF AVSTAGQGEM PQNARSFWKT LLSGALKPGV
     LRRLRFTSFG IGDSSYLRYN VAHRMLCGRL AQLGASLFCE RGEGNEQHPE GHSAGFREWL
     VPLKDAVLSA FPLPESLEPL ADDDFIQPKW MLAGRAIIED QSPPISAEVN GTGHHVKDNV
     EDGVDHEHPA GPHEREAGPS KCLFPVSDSY SAFIDSNKRA TSGTHFQDVR LLDLRLDREY
     KHGPGAVAVV YPKNFPTDVN DFIDLMQWQS CADHPLDVVA TGELAGQVGS PSPLRHLDLA
     GTTCTIRWLL ENVLDIMSIP RRSFFANLAY FAGTGTEDEV YQRDRLLELA NPELIDELWD
     YTTRPKRTIL EVMMDFTTIK IPWEYALSVL PIMRGRQFSI ASGGKYMQDE IGRTRVQLLV
     AIADPPSPII KYRRRYGICT RYITTLQAGQ QINIGMQQGY LDVQPKEVEV PVIMIGPGTG
     LAPMRSMIHQ RRAWAEGLDL KPAGSRLAGD LLFFGCRSSD ADDFFREEWE PLVRDEGLQV
     YTAYSRDKTP PKQYVQDLLR ANSVQVYRTL VELNGKVYLS GSSGAMPKGV REALLEVLEK
     EGPMTRTDAE VYLDGMEKQG RYKQETW
//