ID J4C430_THEOR Unreviewed; 573 AA.
AC J4C430;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=thioredoxin-disulfide reductase {ECO:0000256|ARBA:ARBA00012610};
DE EC=1.8.1.9 {ECO:0000256|ARBA:ARBA00012610};
GN ORFNames=TOT_030000733 {ECO:0000313|EMBL:BAM41471.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM41471.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM41471.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM41471.1,
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 -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003691}.
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DR EMBL; AP011948; BAM41471.1; -; Genomic_DNA.
DR RefSeq; XP_009691772.1; XM_009693477.1.
DR AlphaFoldDB; J4C430; -.
DR STRING; 869250.J4C430; -.
DR EnsemblProtists; BAM41471; BAM41471; TOT_030000733.
DR GeneID; 20715888; -.
DR KEGG; tot:TOT_030000733; -.
DR VEuPathDB; PiroplasmaDB:TOT_030000733; -.
DR eggNOG; KOG4716; Eukaryota.
DR OrthoDB; 5473641at2759; -.
DR Proteomes; UP000003786; Chromosome 3.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR046952; GSHR/TRXR-like.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR NCBIfam; TIGR01438; TGR; 1.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF8; THIOREDOXIN REDUCTASE 1; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000003786}.
FT DOMAIN 84..411
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 431..549
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT REGION 59..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 573 AA; 63088 MW; 281C1DF8865C7898 CRC64;
MFGSRRLIST TVPRIFLSSY LILRQRDLTP PVYCISSINS SISQNSRFNS TLGFVSGPNS
DFMDGSSKEE ESDHKRENKM SEHYDLVVLG AGPGGMSAAK EAATLGKKTL LFDFVNPSPR
GTTWGVGGTC VNVGCIPKKL MHYAGTLRSA NADRYNYGLT DKLEDGPVDW ARLVKNVQNH
VKMLNFTYRV SVNMPNLTYV NAYATLKDSK TVEYKLNGET KTATGDKILI AVGERPYVPQ
DVEGAKENAI TSDDLFSLPK APGKTLVVGG SYVALESAGF LASLGYDVNV SVRSILLRGF
DRQCVDKVQE LMEASGVKFL FQKTPKKIEK SDERYKVTFG DGSVDYYDTV MYATGRMPLD
DIKNYKSLGL EFDNSYNLVT HNEKTNLDNV YAVGDILSNK PKLAPVAIKA GELLAQRLFN
NSTVQMKYED VPVCVYTPFE YSSCGLTEEE AIKRYGEDGI EVYLKEYSNL EVSAAHRVNK
KTDDDLDFPL TCLTKVICLK DDTIVGLHFV GPNAGEIMQG FSVLLLLKAK KKDLDRVVGI
HPTDAESFMD LTVTKSSKQS WIAKGGCAGG KCG
//
