ID   REHY_SYNRU              Reviewed;         218 AA.
AC   P52574;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Probable 1-Cys peroxiredoxin;
DE            EC=1.11.1.24 {ECO:0000250|UniProtKB:P30041};
DE   AltName: Full=Rehydrin;
DE   AltName: Full=Thioredoxin peroxidase;
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000305};
OS   Syntrichia ruralis (Great hairy screw-moss) (Tortula ruralis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Dicranidae; Pottiales; Pottiaceae; Syntrichia.
OX   NCBI_TaxID=38588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RA   Oliver M.J., Scott H.B. II;
RT   "Desiccation-tolerance and gene expression: analysis of a recovery clone,
RT   Tr288, and its implications in mRNA storage during drying.";
RL   J. Exp. Bot. 45:577-583(1994).
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC       hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC       respectively. Seems to contribute to the inhibition of germination
CC       during stress (By similarity). Associated with the rehydration events
CC       involved in the recovery of the desiccation-tolerant moss (Ref.1).
CC       {ECO:0000250|UniProtKB:P30041, ECO:0000269|Ref.1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC         disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC         ChEBI:CHEBI:50058; EC=1.11.1.24;
CC         Evidence={ECO:0000250|UniProtKB:P30041};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O04005}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O04005}.
CC   -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC       residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC       attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC       cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC       cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC       bridge. The disulfide is subsequently reduced by an appropriate
CC       electron donor to complete the catalytic cycle. In this 1-Cys
CC       peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide
CC       with a cysteine from another protein or with a small thiol molecule.
CC       {ECO:0000250|UniProtKB:O35244}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U40818; AAA83758.1; -; mRNA.
DR   AlphaFoldDB; P52574; -.
DR   SMR; P52574; -.
DR   PeroxiBase; 4418; Tru1CysPrx.
DR   PRIDE; P52574; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR   CDD; cd03016; PRX_1cys; 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   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Antioxidant; Cytoplasm; Nucleus; Oxidoreductase; Peroxidase;
KW   Redox-active center.
FT   CHAIN           1..218
FT                   /note="Probable 1-Cys peroxiredoxin"
FT                   /id="PRO_0000135111"
FT   DOMAIN          5..166
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        47
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P30041"
SQ   SEQUENCE   218 AA;  24085 MW;  0903049D8CC12743 CRC64;
     MGGGWALGDL VPDIQADSTM GHIKVRDYCK DGWTIIFSHP GDYPPVCTTE LGKIAAYNPE
     FEKRGVKLLG LSTDTVEDHQ GWIKDIESYT PDAPVLYPIL ADPDRKITVA LNMMDPDEKD
     ANGKPLASRA LHIIGPDCRL KLSLLYPGTT GRNFDEVLRV LDSLQLASKH KIATPANWQK
     GEPVVISPSV SDEKAKQMFP QGWETVNLPK ALRMTFVD