ID   YCF42_TRICV             Reviewed;         204 AA.
AC   P49537;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Putative peroxiredoxin ycf42;
DE            EC=1.11.1.-;
DE   AltName: Full=Thioredoxin peroxidase;
GN   Name=ycf42;
OS   Trieres chinensis (Marine centric diatom) (Odontella sinensis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta; Mediophyceae;
OC   Biddulphiophycidae; Eupodiscales; Parodontellaceae; Trieres.
OX   NCBI_TaxID=1514140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kowallik K.V., Stoebe B., Schaffran I., Kroth-Pancic P., Freier U.;
RT   "The chloroplast genome of a chlorophyll a+c-containing alga, Odontella
RT   sinensis.";
RL   Plant Mol. Biol. Rep. 13:336-342(1995).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + a hydroperoxide = [protein]-disulfide + an
CC         alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC         COMP:10594, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:35924, ChEBI:CHEBI:50058;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
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 typical 2-Cys
CC       peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC       intersubunit disulfide (By similarity). Ycf42 lacks the peroxidatic
CC       cysteine residue and is therefore probably not active as a peroxidase
CC       (Probable). {ECO:0000250|UniProtKB:Q06830, ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; Z67753; CAA91672.1; -; Genomic_DNA.
DR   PIR; S78299; S78299.
DR   AlphaFoldDB; P49537; -.
DR   SMR; P49537; -.
DR   PeroxiBase; 11135; Osin2CysPrx.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:RHEA.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Antioxidant; Chloroplast; Oxidoreductase; Peroxidase; Plastid;
KW   Redox-active center.
FT   CHAIN           1..204
FT                   /note="Putative peroxiredoxin ycf42"
FT                   /id="PRO_0000135146"
FT   DOMAIN          5..163
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   204 AA;  23519 MW;  2B7B0509AFE1C555 CRC64;
     MTNFPKIGKT PPNFLTIGVY KKRLGKIRLS DYRGKKYVIL FFYPANFTAI SPTELMLLSD
     RISEFRKLST QILAISVDSP FSHLQYLLCN REEGGLEDLN YPLVSDLTQT ITRDYQVLTD
     EGLAFPGLFI IDKEGIIQYY TVNNLLCGRN INELLRILES IQYVKENPGY ACPVNWNFGD
     QVFYSHPLKS KIYFKDLYSP KKSS