ID J4D9P2_THEOR Unreviewed; 613 AA.
AC J4D9P2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=NADPH--hemoprotein reductase {ECO:0000256|ARBA:ARBA00023797};
DE EC=1.6.2.4 {ECO:0000256|ARBA:ARBA00023797};
GN ORFNames=TOT_030000772 {ECO:0000313|EMBL:BAM41510.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM41510.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM41510.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM41510.1,
RC ECO:0000313|Proteomes:UP000003786};
RX PubMed=22951932;
RA Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT "Comparative genome analysis of three eukaryotic parasites with differing
RT abilities to transform leukocytes reveals key mediators of Theileria-
RT induced leukocyte transformation.";
RL MBio 3:e00204-e00212(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; AP011948; BAM41510.1; -; Genomic_DNA.
DR RefSeq; XP_009691811.1; XM_009693516.1.
DR AlphaFoldDB; J4D9P2; -.
DR STRING; 869250.J4D9P2; -.
DR EnsemblProtists; BAM41510; BAM41510; TOT_030000772.
DR GeneID; 20715923; -.
DR KEGG; tot:TOT_030000772; -.
DR VEuPathDB; PiroplasmaDB:TOT_030000772; -.
DR eggNOG; KOG1158; Eukaryota.
DR OrthoDB; 101479at2759; -.
DR Proteomes; UP000003786; Chromosome 3.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.360; -; 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; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
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:SF17; NADPH--CYTOCHROME P450 REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000003786}.
FT DOMAIN 24..169
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 229..492
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 613 AA; 70858 MW; B87E354F3970976B CRC64;
MNVELAGGLI NLGLGFYKKP LKKCKIYYAS QTGTAERYSR TLAQKLLKVT NICEESPANL
QDYVEEDFTR EDAVIVFLVA THYDGLFPDD TGRFVKYIRR LVRNEVRLDN LKYCVFGLGS
SDYEYYNEAA KNMQKSLKEL GAEEFTPIYL CDELNGVGRE FERWLDQLFK GLCRLYNIEY
ASLNLKSLKE HDYFKSWRYL CDLELRFVNI SLESNFEPVP NDIICKQQYQ GVEVKVKENV
NLIPNADQSV HHIVFDYDGE YSVSDTAYLL YRNPRHICSM SISLYGKYPE LLLDLSKEIT
FVPRYGNVRE KVTFSPPFPI PTTIKDSLEL YCDLTSLPSD DEIMKFCCFL KDKKDVERIT
KLVRNEKIMK QIREEVKMTL HEFMMLFFPN VKFNLSGFLQ LVPKQKPKPY TISSRPKTGE
LTVTVKLIEY NLHSLKTFYN VNVKRELFNE SIAYNELIKR RIYKGNCSRY LCEMKEGQKI
KLFVRTSLFA SVNMNAPMLL IANGTGIAAF RGIWHSLKNT CNNTGASSMT SSDKSTSSAS
SSSNEVTMML GFRTTNHVLY KEELEQLSQQ ENVRILYAFS REQDKIYVQE LVKNNLELIR
GVLDRGGTIC ICG
//
