ID A0A139I2U0_9PEZI Unreviewed; 842 AA.
AC A0A139I2U0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=NADPH--hemoprotein reductase {ECO:0000256|ARBA:ARBA00023797};
DE EC=1.6.2.4 {ECO:0000256|ARBA:ARBA00023797};
DE Flags: Fragment;
GN ORFNames=AC579_73 {ECO:0000313|EMBL:KXT08999.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT08999.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT08999.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT08999.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) 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:KXT08999.1}.
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DR EMBL; LFZO01000386; KXT08996.1; -; Genomic_DNA.
DR EMBL; LFZO01000386; KXT08997.1; -; Genomic_DNA.
DR EMBL; LFZO01000386; KXT08999.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139I2U0; -.
DR Proteomes; UP000073492; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06204; CYPOR; 1.
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; 2.
DR HAMAP; MF_03212; NCPR; 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; IPR023208; P450R.
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 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW Steroid biosynthesis {ECO:0000256|ARBA:ARBA00022955};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 213..367
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 423..685
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KXT08999.1"
SQ SEQUENCE 842 AA; 93381 MW; 4889744968D9B054 CRC64;
IIVEVFVVFR CLKYTAYSSR PFLAVSDPFS LTQPPAATFS AALELTLHFS AESCRSATPI
PYIVDALHSP AGSSSFPCAV IHRYILFGPL GCEFAAGLAP CPFRCSKSSP VQSARAVRTD
GQSSSSFSSH ASSHAHALPE NALSPSTIMA SLDTLDIVVL VVLLLGTVAY FTKGTYWAVQ
KDPYASANAN GHAAKAGKTR NILEKMEESG KNCVVFYGSQ TGTAEDYASR LAKEGSSRFG
LKTMTADLEE YDYENLDQWP EDKIAFFVLA TYGEGEPTDN AVEFYEFIHG DEPSFSEKSA
DEQPLSNMKY VAFGLGNNTY EHYNSMVREV DKSLTKLGAQ RIGAAGQGDD GAGTMEEDFL
AWKEPMWAAL AEAMQLEERE AVYEPNYEVT EQPEMSAESD TVYLGEPNKN HLEGHSKGPY
NAHNPYIAPI AESYELFHDK SRNCLHMEID ISASNLSYTT GDHIAIWPNN AGKEVDRLLE
VCDLSDKRNT VIKVKGLDAT AKVPFPTPTT YDTVFRYQLE ICAPVSRQFV GTLAQFSPSD
EIKEKMTKIG SDKDVFADEV AKKNFNIAQF LQYAGNGQKW PKIPFSLFIE GLNKIQPRYY
SISSSSLVQK HKVAITAVVE SVEVPGAPHI VKGVTTNYLL SLMLKQHGEA NPDPHGLNYA
ITGPRNKYDG CHVPVHIRHS NFKLPSDPSK PIIMVGPGTG VAPFRGFVQE RAQQAKNGEK
VGKTILFFGC RNRTEDFIYE KEWEQWTEDM GGAFELVCAF SRETEKKVYV QHRLKERAEE
INKLLEQKAY FYVCGDAANM AREVNEILAM IISEQRGVDK KKGEDIVKSM RAANQYQEDV
WS
//
