ID A0A2C6K8E6_9APIC Unreviewed; 86 AA.
AC A0A2C6K8E6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:PHJ17570.1};
DE Flags: Fragment;
GN ORFNames=CSUI_008608 {ECO:0000313|EMBL:PHJ17570.1};
OS Cystoisospora suis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Cystoisospora.
OX NCBI_TaxID=483139 {ECO:0000313|EMBL:PHJ17570.1, ECO:0000313|Proteomes:UP000221165};
RN [1] {ECO:0000313|EMBL:PHJ17570.1, ECO:0000313|Proteomes:UP000221165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wien I {ECO:0000313|EMBL:PHJ17570.1,
RC ECO:0000313|Proteomes:UP000221165};
RX PubMed=28161402; DOI=10.1016/j.ijpara.2016.11.007;
RA Palmieri N., Shrestha A., Ruttkowski B., Beck T., Vogl C., Tomley F.,
RA Blake D.P., Joachim A.;
RT "The genome of the protozoan parasite Cystoisospora suis and a reverse
RT vaccinology approach to identify vaccine candidates.";
RL Int. J. Parasitol. 47:189-202(2017).
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 -!- 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:PHJ17570.1}.
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DR EMBL; MIGC01004872; PHJ17570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C6K8E6; -.
DR VEuPathDB; ToxoDB:CSUI_008608; -.
DR OrthoDB; 5473641at2759; -.
DR Proteomes; UP000221165; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase 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; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR046952; GSHR/TRXR-like.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF2; GLUTATHIONE REDUCTASE; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000221165}.
FT DOMAIN 38..84
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PHJ17570.1"
FT NON_TER 86
FT /evidence="ECO:0000313|EMBL:PHJ17570.1"
SQ SEQUENCE 86 AA; 9564 MW; 944334812A035B8B CRC64;
AKYGKEDLEI YLFQFSPLFY SCVHRQKAAS SRKSAEDVDL TPPCLVKMIC VKSEEERVVG
LHFIGPSAGE IMQGFALSIR LGAKKV
//