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Database: UniProt
Entry: A0A182YU36_BIOGL
LinkDB: A0A182YU36_BIOGL
Original site: A0A182YU36_BIOGL 
ID   A0A182YU36_BIOGL        Unreviewed;        98 AA.
AC   A0A182YU36;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Peroxiredoxin {ECO:0000313|EnsemblMetazoa:BGLB000181-PA};
GN   Name=106057061 {ECO:0000313|EnsemblMetazoa:BGLB000181-PA};
OS   Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Planorbidae; Biomphalaria.
OX   NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB000181-PA, ECO:0000313|Proteomes:UP000076420};
RN   [1] {ECO:0000313|EnsemblMetazoa:BGLB000181-PA}
RP   IDENTIFICATION.
RC   STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB000181-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC       hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC       respectively. Plays a role in cell protection against oxidative stress
CC       by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC       signaling events. {ECO:0000256|ARBA:ARBA00003330}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010505}.
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DR   AlphaFoldDB; A0A182YU36; -.
DR   EnsemblMetazoa; BGLB000181-RA; BGLB000181-PA; BGLB000181.
DR   VEuPathDB; VectorBase:BGLB000181; -.
DR   Proteomes; UP000076420; Unassembled WGS sequence.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR037944; PRX5-like.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR10430; PEROXIREDOXIN; 1.
DR   PANTHER; PTHR10430:SF16; PEROXIREDOXIN-5, MITOCHONDRIAL; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
FT   DOMAIN          1..76
FT                   /note="Redoxin"
FT                   /evidence="ECO:0000259|Pfam:PF08534"
SQ   SEQUENCE   98 AA;  10719 MW;  9B1BB4CDA97A673F CRC64;
     MISCVSVNDP FVMDAWGKST HADGKIRMLA DPRGEFTIAL GMDLDCKQIL GGIRSQKYSL
     VIEDGKIQSI NVDPEHTGLA CLLCIKNMRA SDSPVPKR
//
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