ID A0A0M4EW60_DROBS Unreviewed; 476 AA.
AC A0A0M4EW60;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=CG14882 {ECO:0000313|EMBL:ALC47717.1};
GN ORFNames=Dbus_chr3Rg2467 {ECO:0000313|EMBL:ALC47717.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC47717.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC47717.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC47717.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP012526; ALC47717.1; -; Genomic_DNA.
DR RefSeq; XP_017847918.1; XM_017992429.1.
DR RefSeq; XP_017847919.1; XM_017992430.1.
DR AlphaFoldDB; A0A0M4EW60; -.
DR SMR; A0A0M4EW60; -.
DR STRING; 30019.A0A0M4EW60; -.
DR GeneID; 108603532; -.
DR OMA; WLYVGAK; -.
DR OrthoDB; 276396at2759; -.
DR Proteomes; UP000494163; Chromosome 3r sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000494163}.
FT DOMAIN 70..319
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 476 AA; 52863 MW; D19E4CF6E83FE579 CRC64;
MVNTEMTSPS VDTIDIGEYT LKEYVPAKAF ESNLKITFTD ANEQDIVKPL PGGQLNCGPT
LKFPFALEGY LPTCVTIQEA NELVTADENT HTKRVLELIL DISALGTLDY MPGDTVGILP
KNAKTVVEQL LQRLELSEQA DSICRVDLSL HCAKKNAKVP GHIPATTTPR EIFTHCLSLN
AVPQKQFLSA LAKYTSNINE REFLASLSSK HGAAHYHTLI LEQGLCLQDL LELCPSCKPT
LALLVEHLPR LLPRPYSIAN SPLECSKHQL SIIFSIRAPK PGVTTSMLDA LIAQHKQKEH
QKPVELNIYP RMHNAFRYTE EHFTGNQILI AVGTGVAPFL GFLAHKAQNH ELATGLTWLY
MGAKTPQAIP KLDKLFEWHE TGLIQCLNIC TSRDSTEGGP KYVHELLEED AETLVNFLLD
PKTVLYVCAD GAKISKSISQ SLSSCLQQAL ELNETEAAQE IQEMRTKGKY REDLWI
//