ID A0A1R1X773_9FUNG Unreviewed; 884 AA.
AC A0A1R1X773;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=NADPH--hemoprotein reductase {ECO:0000256|ARBA:ARBA00023797};
DE EC=1.6.2.4 {ECO:0000256|ARBA:ARBA00023797};
GN ORFNames=AYI70_g10314 {ECO:0000313|EMBL:OMJ10462.1}, AYI70_g11977
GN {ECO:0000313|EMBL:OMJ07767.1}, AYI70_g5390
GN {ECO:0000313|EMBL:OMJ18367.1};
OS Smittium culicis.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133412 {ECO:0000313|EMBL:OMJ10462.1, ECO:0000313|Proteomes:UP000187283};
RN [1] {ECO:0000313|EMBL:OMJ10462.1, ECO:0000313|Proteomes:UP000187283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSMNP {ECO:0000313|EMBL:OMJ10462.1,
RC ECO:0000313|Proteomes:UP000187283};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-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:OMJ10462.1}.
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DR EMBL; LSSN01005973; OMJ07767.1; -; Genomic_DNA.
DR EMBL; LSSN01004992; OMJ10462.1; -; Genomic_DNA.
DR EMBL; LSSN01001772; OMJ18367.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R1X773; -.
DR STRING; 133412.A0A1R1X773; -.
DR Proteomes; UP000187283; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF17; NADPH--CYTOCHROME P450 REDUCTASE; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000187283};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 73..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 201..376
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 439..723
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 159..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 884 AA; 98622 MW; 5526035EF68F34D8 CRC64;
MTIEDSKHNA STTINQETDS TTYRFGSFEP ISEDSISPVS ETFNNPLLNL VSTTFSSAYS
IFKAFLSGQK SFYLFSVAVV YIFFSFFTDL SLLLASFITS KSKVSPLKSP SQKSNMKSNS
NGFSIFNLDR KDLIIMTTMV VGASTFIFRK LILNSSKAAE NKNADPQPQP ELEPETQAES
APVTDLDRSI PDVMKLKNKN IAIFYGSQTG TAEDLANRLS RSLQNDFGAL PFVIDPEDFD
VESLSRIPSN YHIILVLSTT GEGEPTDNMV KWYKKLIPAE DHLNADFSSL KLPNFQVPED
LEVSSDYVFD KDLPLKNLHF SAFGLGNTTY ENFNVHVKQV SKRLVSLGAQ LIGPLGLGDD
DDDVDHDFSK WKDAAAPLIA QKIDSSSAAS SDKSFISDWI VSEVTDAKEY DSSKFNTLRS
STTENESQLH PSQIKVDNRN PWGSVVCAAK QLCHPENERQ TAHVEFDISD SDISYTTGDH
VAVWPINSDI HVDALIQLLN VNKDQVVKAV PNPESTNSNP FQYSYSTYEG ILTHYMDVTS
PISQDNLKQV LLPNVSSQPG KEFIDKLIND KSFYSSNVTT PTTTPAELLQ ELVSIETKSN
VPADLKFVLS FDVLLSLLPR LSPRFYSISS SSKESPNSIS TTVVALQYMS TKNQNRYGVA
SNYLNAIVDA TTKKSIITKE TISSLTKFDP PYHTLEKIVT DSLFKKADIR VPIFVRKSVF
KLPSDPSIPI VMVGPGTGLA PFRAFIRERA FMINTNNEKV GPTVLFFGNR YESKDYLYKE
ELESTFETLS KSSSESKLFT AFSRDTDQKV YVQNRILENS ELVYKLLFEM NGYFYICGDG
SRMAVDVAKA LLDVAKAHNK SDSSPTDLVE SLKKTGRYQE DIWF
//
