ID A0A0M3I8N3_ASCLU Unreviewed; 508 AA.
AC A0A0M3I8N3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=cytochrome-b5 reductase {ECO:0000256|ARBA:ARBA00012011};
DE EC=1.6.2.2 {ECO:0000256|ARBA:ARBA00012011};
OS Ascaris lumbricoides (Giant roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0001372401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ALUE_0001372401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000256|ARBA:ARBA00006105}.
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DR AlphaFoldDB; A0A0M3I8N3; -.
DR WBParaSite; ALUE_0001372401-mRNA-1; ALUE_0001372401-mRNA-1; ALUE_0001372401.
DR Proteomes; UP000036681; Unplaced.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd06183; cyt_b5_reduct_like; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 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; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR46237:SF1; CYTOCHROME B5 REDUCTASE 4; 1.
DR PANTHER; PTHR46237; CYTOCHROME B5 REDUCTASE 4 FAMILY MEMBER; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 53..129
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 269..371
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 508 AA; 57577 MW; 10C3A09F2C268BDC CRC64;
MNQEDIMKMP PKLKMPASTR SQGGRLKVAL QPGRGIMDWV QLTSGKQLAS QQLPFVTDEE
LRKHNSADDC WILLDNKVYD VTEYLTFHPG GVEQLMKAAG CDGTNLFHKY HSWINYETML
SSCFVGYFKG DRSQLPQPTE SWFDDDSDEW LAMEVERQRE ETAAKLAQLN IRIVDTSKGR
LYLSCDEWSN LKPENVCVDV VRNSVRVLIK PFDGTPLELH WKRIPKVLTS GMFTVLVDSS
MIKIQFETTV NMGIFSSLDL LSVDEEPPER SRECTITEIR QVARNIYLYE MSLPPSSYFS
VPIGHHVYLT INKDGGSLLR SYTPVLVDGN ARKISFFIKI YEDGIFSSEL HKLETGAILK
ISNPIGTIDF LSACAPYVVA IAAGTGITPM LRLLAARNDD SNTYTTLLAI NATPEDRLEK
TFYQYCGLKL GKDRVTFYHF ENDDHELNFR MMSTFLAEMG PKILEKREED GIADCYRILI
CGPTSFVESA KRLVTITSPE LESSVHIF
//
