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Database: UniProt
Entry: A0A2C6K8E6_9APIC
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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
//
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