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Database: UniProt
Entry: A0A0N5C3J6_STREA
LinkDB: A0A0N5C3J6_STREA
Original site: A0A0N5C3J6_STREA 
ID   A0A0N5C3J6_STREA        Unreviewed;       231 AA.
AC   A0A0N5C3J6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Thioredoxin domain-containing protein {ECO:0000313|WBParaSite:SPAL_0001254100.1};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001254100.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0001254100.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC       hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC       respectively. {ECO:0000256|PIRNR:PIRNR000239}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC       {ECO:0000256|ARBA:ARBA00025719}.
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DR   AlphaFoldDB; A0A0N5C3J6; -.
DR   STRING; 174720.A0A0N5C3J6; -.
DR   WBParaSite; SPAL_0001254100.1; SPAL_0001254100.1; SPAL_0001254100.
DR   Proteomes; UP000046392; Unplaced.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR   CDD; cd03016; PRX_1cys; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR045020; PRX_1cys.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR43503; MCG48959-RELATED; 1.
DR   PANTHER; PTHR43503:SF4; PEROXIREDOXIN-6; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Antioxidant {ECO:0000256|ARBA:ARBA00022862, ECO:0000256|PIRNR:PIRNR000239};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000239};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR000239};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|PIRNR:PIRNR000239}.
FT   DOMAIN          3..175
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        46
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ   SEQUENCE   231 AA;  25745 MW;  BC0B88A30008CF87 CRC64;
     MSLKLGDQFP NFSCATSHGN IEDFHQWLGS SWGILFSHPA DFTPVCTTEL AKAVELAPEF
     EKRDVKMIAL SIDDEESHKK WCHDIITYGK HVGTLKSYNE DSVFPFPIIA DVNRELATKL
     GMLDPEEIGA DGMALTARAV FVIGPQKQLK LSILYPATTG RNFDEILRVI DSLQLTAAQK
     VATPVNWRHG DKCMIIPSLS DVDAELLFGK NIDSIDVPSK KKYLRLTPMP K
//
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