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Database: UniProt
Entry: A0A093EQE7_TYTAL
LinkDB: A0A093EQE7_TYTAL
Original site: A0A093EQE7_TYTAL 
ID   A0A093EQE7_TYTAL        Unreviewed;       120 AA.
AC   A0A093EQE7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Thioredoxin domain-containing protein 12 {ECO:0000256|ARBA:ARBA00016955};
DE            EC=1.8.4.2 {ECO:0000256|ARBA:ARBA00013094};
DE   Flags: Fragment;
GN   ORFNames=N341_05602 {ECO:0000313|EMBL:KFV42264.1};
OS   Tyto alba (Barn owl).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX   NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV42264.1, ECO:0000313|Proteomes:UP000054190};
RN   [1] {ECO:0000313|EMBL:KFV42264.1, ECO:0000313|Proteomes:UP000054190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV42264.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-disulfide + 2 glutathione = [protein]-dithiol +
CC         glutathione disulfide; Xref=Rhea:RHEA:21064, Rhea:RHEA-COMP:10593,
CC         Rhea:RHEA-COMP:10594, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.8.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00033687};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21066;
CC         Evidence={ECO:0000256|ARBA:ARBA00033687};
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DR   EMBL; KK368334; KFV42264.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093EQE7; -.
DR   Proteomes; UP000054190; Unassembled WGS sequence.
DR   GO; GO:0019153; F:protein-disulfide reductase (glutathione) activity; IEA:UniProtKB-EC.
DR   CDD; cd02959; ERp19; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR037462; ERp19.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR15337; ANTERIOR GRADIENT PROTEIN-RELATED; 1.
DR   PANTHER; PTHR15337:SF10; THIOREDOXIN DOMAIN-CONTAINING PROTEIN 12; 1.
DR   Pfam; PF13899; Thioredoxin_7; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054190};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          1..104
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV42264.1"
FT   NON_TER         120
FT                   /evidence="ECO:0000313|EMBL:KFV42264.1"
SQ   SEQUENCE   120 AA;  13457 MW;  8D51394822F897FB CRC64;
     SGLPLMVIIH KSWCGACKAL KPKFAESKEI SELAHNFVMV NLEDDEEPKD EAFSPDGGYI
     PRILFMDPSG NVHPEIINEK GNPSYKYFYT NADQVVQGMK EAQEKLTGDA FKQKHLGDEL
//
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