ID   A0A9Y1YSP0_CHISP        Unreviewed;       223 AA.
AC   A0A9Y1YSP0;
DT   08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2023, sequence version 1.
DT   02-OCT-2024, entry version 5.
DE   SubName: Full=Peroxiredoxin 6 {ECO:0000313|EMBL:WIR74294.1};
DE            EC=1.11.1.24 {ECO:0000313|EMBL:WIR74294.1};
GN   Name=Prx6 {ECO:0000313|EMBL:WIR74294.1};
OS   Chilo suppressalis (Asiatic rice borer moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea;
OC   Crambidae; Crambinae; Chilo.
OX   NCBI_TaxID=168631 {ECO:0000313|EMBL:WIR74294.1};
RN   [1] {ECO:0000313|EMBL:WIR74294.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=37282754;
RA   Mo W., Li Q., He X., Lu Z., Xu H., Zheng X., Guo J., Lu Y., Wang S.;
RT   "Identification and characterization of Prx5 and Prx6 in Chilo suppressalis
RT   in response to environmental stress.";
RL   Insect Biochem. 0:0-0(2023).
RN   [2] {ECO:0000313|EMBL:WIR74294.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Lu Y.;
RL   Submitted (JAN-2023) to the EMBL/GenBank/DDBJ databases.
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   EMBL; OQ230772; WIR74294.1; -; mRNA.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:TreeGrafter.
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   2: Evidence at transcript level;
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          2..166
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        44
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ   SEQUENCE   223 AA;  25145 MW;  864B42042214CB63 CRC64;
     MPLLGEEFPD FTANTTEGEI NFHEWVGKSW AILFSHPSDF TPVCTTELAR ILNLLPEFNK
     RNVKVIGLSC DTVSSHKEWC KDIKHYAGFN EDEKFPYPII EDKDRKVATL LGMVDKDELD
     TSGMPLTARA VFIIDANKKF RLSFLYPATT GRNFDEILRV IDSLQLTDKA KVATPVDWKM
     GDDCMVLPTL PEDQLSKVFP QGVTTVPVPS GKNYLKKTTC PKV
//