ID A0A1S3IK56_LINUN Unreviewed; 249 AA.
AC A0A1S3IK56;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
GN Name=LOC106165078 {ECO:0000313|RefSeq:XP_013398625.1};
GN Synonyms=LOC106177883 {ECO:0000313|RefSeq:XP_013416254.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013398625.1};
RN [1] {ECO:0000313|RefSeq:XP_013398625.1, ECO:0000313|RefSeq:XP_013416254.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013398625.1,
RC ECO:0000313|RefSeq:XP_013416254.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000280};
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
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DR RefSeq; XP_013398625.1; XM_013543171.2.
DR RefSeq; XP_013416254.1; XM_013560800.1.
DR STRING; 7574.A0A1S3IK56; -.
DR EnsemblMetazoa; XM_013543171.2; XP_013398625.1; LOC106165078.
DR EnsemblMetazoa; XM_013560800.1; XP_013416254.1; LOC106177883.
DR GeneID; 106165078; -.
DR GeneID; 106177883; -.
DR KEGG; lak:106165078; -.
DR KEGG; lak:106177883; -.
DR OrthoDB; 47465at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR CDD; cd03015; PRX_Typ2cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681:SF171; AT16346P-RELATED; 1.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT DOMAIN 56..214
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 37..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 249 AA; 27560 MW; 105C98FDADB4A11A CRC64;
MSEAIFVEVR RGGYMTVGKT LDGKEPEPKV AVTHEVVERT PSSSQSANMT STKEGLRIGK
PAPNFSGTAV IDGDFKTVKL DDYRGKYLVF FFYPLDFTFV CPTEIIAFSD RSEEFRSIGC
EVVACSTDSH FSHLAWVNTP RKKGGLGQMK IPLLADKTME IAKAYGVLKE EDGVTFRGLF
IIDGQGILRQ VTVNDLPVGR SVDETLRLVQ AFQFTDKHGE VCPAGWRPGA DTMKPDPKGS
QTYFEKTNK
//
