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Database: UniProt
Entry: F8MXE2_NEUT8
LinkDB: F8MXE2_NEUT8
Original site: F8MXE2_NEUT8 
ID   F8MXE2_NEUT8            Unreviewed;      1030 AA.
AC   F8MXE2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN   ORFNames=NEUTE1DRAFT_131946 {ECO:0000313|EMBL:EGO54413.1};
OS   Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO54413.1};
RN   [1] {ECO:0000313|EMBL:EGO54413.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO54413.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Submitted (APR-2011) 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; GL891307; EGO54413.1; -; Genomic_DNA.
DR   RefSeq; XP_009854372.1; XM_009856070.1.
DR   AlphaFoldDB; F8MXE2; -.
DR   GeneID; 20825594; -.
DR   KEGG; nte:NEUTE1DRAFT131946; -.
DR   VEuPathDB; FungiDB:NEUTE1DRAFT_131946; -.
DR   HOGENOM; CLU_003662_1_0_1; -.
DR   OrthoDB; 5488444at2759; -.
DR   Proteomes; UP000008065; Unassembled WGS sequence.
DR   GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR   CDD; cd06207; CyPoR_like; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 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; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR19384:SF109; SULFITE REDUCTASE [NADPH] FLAVOPROTEIN COMPONENT; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF01558; POR; 1.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   SUPFAM; SSF52922; TK C-terminal 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          643..874
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   1030 AA;  112807 MW;  F000D9293222D6A9 CRC64;
     MPSLSSISGP TYVTSQLLVQ QTAYKLSDKI FSYSPETFDL DVAVKEWAEA NEKNVHGETT
     TVVPLQTRAG AGAFALGYIF SKDFDLAKRH VPQTLLAPSL SLRHLRSSLD QLALLYGVSS
     PFVAHVAAAD YSAEKGLGAD YATALQIAED LGLALVSSSS AYEVQHMSLL ATLLASVLPT
     LHIYDGIRTA RESLRVVDAL GEAHIADVYA KISKEAAALN KRLDTAGKVV ELLKAFNNEL
     GTSYAPFEYH GHEAPETVLV VFGSAEAQLA KQVASALAAE GKKVGTIVVR VYRPFVEEAF
     LEVLPASVRQ IAVLGQVADA AAVEDANVQS ALYSDVLTAV SFTDKLSQAP EVVDVRYAVT
     DAHTPSSIAS IFNKLTSKGE AEPVAFSLTA VEEAQQYVFW DVDNSSAAAS ASAVGRLLET
     EQSNNVYVHQ TYDNLVQGGV VRTDIRVSQK SIEAPYPVES ADVVFVGEEK LLKEIAIVKG
     VKAGGKLIVR LPNFKEDELE KRIPAAAQKE IQEKGIELYV LDSSSSPALE KEAGLLVGVA
     FLRVARADIT KLDSLSADQT ALTEAVNALD QSVRKVEVPA KWAEVENTVA PLVDSVKPNS
     FVAFQKEEEE ETSSLENWQS AAKGFAFKEA YGTQNQLRPD LTVKTYTIKV KENRRLTPTD
     YDRNIFHIEF DLGDSGLTYN IGEALGIHAD NDPEQVLQFI QAYGLNADDL VQVPSREDPA
     VLETRTVYQS LVQNVDILGK PPKRFFEALA QFATDEEEKK KLERLGSKEG ADEFKRLTEE
     DTVTYVDVLD MFKSAHPDFN DLVRIVDPTK RREYSIASAQ AVTPNSVTLM IVVVNWVDTK
     GRTRYGHATR YLSGLAPGST ITASVKPSVM KLPVKDTAPL IMAGLGTGLA PFRAFVQYRA
     MQKAQGKEIG SILLYLGSRH QREEYLYGEE WEAYLDAGVI TLLGAAFSRD QPEKIYIQDR
     MRQTVTDIVK AYIKEEGSFY LCGPTWPVPD VTAVLEEAIA AEAQESSRKV DPRKEIERLK
     EDGRYVLEVY
//
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