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Database: UniProt
Entry: A0A0M3IE58_ASCLU
LinkDB: A0A0M3IE58_ASCLU
Original site: A0A0M3IE58_ASCLU 
ID   A0A0M3IE58_ASCLU        Unreviewed;       138 AA.
AC   A0A0M3IE58;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=protein-disulfide reductase {ECO:0000256|ARBA:ARBA00012612};
DE            EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
OS   Ascaris lumbricoides (Giant roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0001635901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ALUE_0001635901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) +
CC         NADH; Xref=Rhea:RHEA:18749, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC         COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00000696};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + H(+) +
CC         NADPH; Xref=Rhea:RHEA:18753, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC         COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00001346};
CC   -!- SIMILARITY: Belongs to the nucleoredoxin family.
CC       {ECO:0000256|ARBA:ARBA00025782}.
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DR   AlphaFoldDB; A0A0M3IE58; -.
DR   WBParaSite; ALUE_0001635901-mRNA-1; ALUE_0001635901-mRNA-1; ALUE_0001635901.
DR   Proteomes; UP000036681; Unplaced.
DR   CDD; cd02964; TryX_like_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR13871; THIOREDOXIN; 1.
DR   PANTHER; PTHR13871:SF7; THIOREDOXIN DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13905; Thioredoxin_8; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
FT   DOMAIN          1..138
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   138 AA;  15597 MW;  6E4409496FED2876 CRC64;
     LPIHLFIFAW SVRQFVIFQG KVVALYFSAH WCPPCRQFTP VLKDFYEELE GEGFEIVFVS
     FDRSESDLEE YMQEAHGDWY FIPFGSNEIQ ELAKKFDVSG IPALVVIKSN GDVITKNGRA
     DVSSRSPAQA LGAWKAAA
//
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