ID A0A368EYY3_ANCCA Unreviewed; 354 AA.
AC A0A368EYY3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Oxidoreductase NAD-binding domain protein {ECO:0000313|EMBL:RCN23989.1};
GN ORFNames=ANCCAN_30322 {ECO:0000313|EMBL:RCN23989.1};
OS Ancylostoma caninum (Dog hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN23989.1, ECO:0000313|Proteomes:UP000252519};
RN [1] {ECO:0000313|EMBL:RCN23989.1, ECO:0000313|Proteomes:UP000252519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Baltimore {ECO:0000313|EMBL:RCN23989.1,
RC ECO:0000313|Proteomes:UP000252519};
RA Mitreva M.;
RT "Draft genome of the hookworm Ancylostoma caninum.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:RCN23989.1}.
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; JOJR01024486; RCN23989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368EYY3; -.
DR STRING; 29170.A0A368EYY3; -.
DR Proteomes; UP000252519; Unassembled WGS 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 InterPro; IPR003097; CysJ-like_FAD-binding.
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.
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:UP000252519}.
FT DOMAIN 14..159
FT /note="Sulfite reductase [NADPH] flavoprotein alpha-
FT component-like FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF00667"
FT DOMAIN 198..316
FT /note="Oxidoreductase FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF00175"
SQ SEQUENCE 354 AA; 40035 MW; 697E9A2802AC4D38 CRC64;
MGMLAIADQV CTVSVNPSTE KINPTIPAHV PPKSSLRHLF TYCLDIRRTP GRPILRALAE
GAQNEQEKRR LLELTSAQGF TEFNDFVRQP GLSLADILFA FPSVRPSPDR LIELLPRLIP
RSYSASSCRG RRVRFIYSVM HFTAENGRRY ARNGLATDWL LGLKVGDMIK IMHKETARFR
LPPPSLPSSD AARMPLLMVG PGTGVAVFLA FCQHLLNIKL NNPENCLDVP RYLYFGCRNL
EKDSLYLDEL KSYVREGILT ELILCESRVD GDRPKRVQDA LKQRISQVCD FIFNSGSDVP
SRVFICGDAK GMSKDVFQCF HDIIKEGTGR SDEEARAYMV EMQKADRYVE DVWS
//