ID   U6GZG2_9EIME            Unreviewed;       579 AA.
AC   U6GZG2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Thioredoxin, putative {ECO:0000313|EMBL:CDI85701.1};
GN   ORFNames=EPH_0016720 {ECO:0000313|EMBL:CDI85701.1};
OS   Eimeria praecox.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=51316 {ECO:0000313|EMBL:CDI85701.1};
RN   [1] {ECO:0000313|EMBL:CDI85701.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDI85701.1};
RA   Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA   Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA   Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA   Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA   Tomley F., Pain A.;
RT   "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDI85701.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDI85701.1};
RA   Aslett M.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000256|ARBA:ARBA00006347}.
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DR   EMBL; HG694175; CDI85701.1; -; Genomic_DNA.
DR   AlphaFoldDB; U6GZG2; -.
DR   EnsemblProtists; CDI85701; CDI85701; EPH_0016720.
DR   VEuPathDB; ToxoDB:EPH_0016720; -.
DR   OrthoDB; 5399045at2759; -.
DR   CDD; cd02961; PDI_a_family; 1.
DR   CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR   PANTHER; PTHR18929:SF132; PROTEIN DISULFIDE-ISOMERASE A3; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   3: Inferred from homology;
FT   DOMAIN          24..165
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          394..549
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          381..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   579 AA;  64256 MW;  7317E1C65FB7E531 CRC64;
     MAAHRGVVSA SDAEEGVQAD RRVYSEEQKA RAAADQKTVM DSGPVSLSDA TYNDFMAAHP
     LALVMFYAPW CYWSRSALPE LEAAAKLLSH HVPPVVSAKV DCTENEDLCN QEYIREYPTI
     RLYIEGVGHL YEGRRYRSHI LHWVDLKVDR DKQLVSAAHL DELISTSNSD GKSSSSEDGH
     VVVVAAFPPN YSRGGFQAVA RAFGEEVLFG DTSDPELTTR LIDKHVLPRL PEKERSSSEV
     SRQLKPPFVV VFAPHKDEPG VHIYKGPVGE VKELRAFVRQ WLFPVVSLFD AESIGSSFFS
     DSRPKLLLLL DSSKQDGRLK EVESANPTDP LLAAFRAVAE KNRVSVAAAV SGNSKNYEKQ
     LLNLLGIEDE SLPQVRIMQV SRNPDGPQHP AKKFRPSSPL PSVDQGREAL EEMMNAFVSG
     VLSHSVPPYF RSETPPDTPE PRGRVRTLVA STFATEVRKE PNVLVEFYAP WCGFCRKMEP
     AYKELAMRVA GVSGLLIARI DATRNEVDGV AVAGYPTLYL YRKGDKEPLL YAGDRSTRDM
     LKWLSLRVRG TSPFDPEELM SRDIGNSNDK AAASVLEEL
//