ID C5LM56_PERM5 Unreviewed; 228 AA.
AC C5LM56;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Peroxidoxin 2, putative {ECO:0000313|EMBL:EER02187.1};
GN ORFNames=Pmar_PMAR008969 {ECO:0000313|EMBL:EER02187.1},
GN Pmar_PMAR010894 {ECO:0000313|EMBL:EEQ99631.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EER02187.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 {ECO:0000313|EMBL:EER02187.1}, and ATCC 50983 / TXsc
RC {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) 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.
CC {ECO:0000256|PIRNR:PIRNR000239}.
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DR EMBL; GG685476; EEQ99631.1; -; Genomic_DNA.
DR EMBL; GG683392; EER02187.1; -; Genomic_DNA.
DR RefSeq; XP_002766914.1; XM_002766868.1.
DR RefSeq; XP_002769469.1; XM_002769423.1.
DR EnsemblProtists; EEQ99631; EEQ99631; Pmar_PMAR010894.
DR EnsemblProtists; EER02187; EER02187; Pmar_PMAR008969.
DR GeneID; 9051472; -.
DR GeneID; 9055091; -.
DR OMA; HGPMNIP; -.
DR OrthoDB; 103042at2759; -.
DR Proteomes; UP000007800; Unassembled WGS sequence.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
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; 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|PIRNR:PIRNR000239};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000239}; Peroxidase {ECO:0000256|PIRNR:PIRNR000239};
KW Redox-active center {ECO:0000256|PIRNR:PIRNR000239};
KW Reference proteome {ECO:0000313|Proteomes:UP000007800}.
FT DOMAIN 6..173
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 52
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 228 AA; 25664 MW; 6527FDBFC5CF6581 CRC64;
MPEFKQKLGA EFPNFDCKTT KGDFKFHEFL DSDPKKPYTI LFSHPKDFTP VCTTELGKLE
KNKDEFTKRG VKLIGISCDS VPDHHAWSKD VLAYQNMPGD DLSYPIIADP DREIVSMLGM
LDPNEKDAAG VPLPARALFV IGPDHKLKLS IVYPATTGRN YDELIRTLDS LHLTADFSLA
TPVDWKQGER VIVAPNVATE EAQKRFKNLE IKDLPSGKPY LRYVDAPE
//
