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Database: UniProt
Entry: H9B9L9_EIMTE
LinkDB: H9B9L9_EIMTE
Original site: H9B9L9_EIMTE 
ID   H9B9L9_EIMTE            Unreviewed;       382 AA.
AC   H9B9L9;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000259|Pfam:PF07992};
OS   Eimeria tenella (Coccidian parasite).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=5802 {ECO:0000313|EMBL:AET50679.1};
RN   [1] {ECO:0000313|EMBL:AET50679.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Houghton {ECO:0000313|EMBL:AET50679.1};
RX   PubMed=22244352; DOI=10.1186/1471-2164-13-21;
RA   Amiruddin N., Lee X.W., Blake D.P., Suzuki Y., Tay Y.L., Lim L.S.,
RA   Tomley F.M., Watanabe J., Sugimoto C., Wan K.L.;
RT   "Characterisation of full-length cDNA sequences provides insights into the
RT   Eimeria tenella transcriptome.";
RL   BMC Genomics 13:21-21(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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DR   EMBL; JN987456; AET50679.1; -; mRNA.
DR   AlphaFoldDB; H9B9L9; -.
DR   VEuPathDB; ToxoDB:ETH2_1319100; -.
DR   VEuPathDB; ToxoDB:ETH_00028950; -.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   PANTHER; PTHR22912:SF217; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT   DOMAIN          36..355
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   382 AA;  40813 MW;  C81690368956CA3D CRC64;
     MQLHRLAARP LTVPTVHVSA LFRRTHQRSF SSQSEYDVVV IGGGPGGYVA AIKAAQLGLK
     TACVEKRGAL GGTCLNVGCI PSKALLNMSH KYKEASSDFS RFGIRVSDVS VDISSMQDYK
     DKIVSGLTQG IEGLFKRNKV DYLNGTGRLA GPHAVQVQPI DAGNPQMLMA KNVILATGSE
     PAPLAGGALE VDEETIVSST GALALPRVPK HLVVVGGGVI GLELGSVWRN LGAEVTVVEF
     CDKIIPALDA EIGRAFQKLL ERQGIKFMFG TKVVGSQKAD GGVTLSLENV KSGDASEVQC
     DVVLVAVGRR PYTKDLGLEE LGINLDNRGR VVVNEQMQVP NYPNIMAIGD LIQGVRKTSI
     QMFHVYKRTL LTPPSFQAQP DA
//
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