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Database: UniProt
Entry: A0A498IG11_MALDO
LinkDB: A0A498IG11_MALDO
Original site: A0A498IG11_MALDO 
ID   A0A498IG11_MALDO        Unreviewed;       227 AA.
AC   A0A498IG11;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DVH24_004988 {ECO:0000313|EMBL:RXH81074.1};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH81074.1, ECO:0000313|Proteomes:UP000290289};
RN   [1] {ECO:0000313|EMBL:RXH81074.1, ECO:0000313|Proteomes:UP000290289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC   TISSUE=Young leaf {ECO:0000313|EMBL:RXH81074.1};
RA   Hu J.;
RT   "A high-quality apple genome assembly.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RXH81074.1}.
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DR   EMBL; RDQH01000338; RXH81074.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498IG11; -.
DR   STRING; 3750.A0A498IG11; -.
DR   Proteomes; UP000290289; Chromosome 12.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0097237; P:cellular response to toxic substance; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR039648; DHPH_N.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR48105:SF26; NADPH-DEPENDENT THIOREDOXIN REDUCTASE 3; 1.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290289}.
FT   DOMAIN          48..91
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00070"
FT   DOMAIN          136..225
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00085"
SQ   SEQUENCE   227 AA;  25590 MW;  EDCCA01A7B19DFB4 CRC64;
     MSKVHLRLYM KDSEPKIQDE TSKERMLRGI SACAICDGAS PLFKGQVLAV VGGGDTATEE
     ALYLKKYARH IHLLVRRDQL RASRAMQDRL DHEWRQAVTA AGSGCIAALS VERYLVGKDL
     IIEFHQYALR KLYHESPRLI CVLYTAPTCG PCRTLKPILG TVSSVVQFFV VQVIDEFDHN
     VHFVEIEIEE DPEVVEATGI MGTPCVQFFK NKEMIRTVSG VKMKSEY
//
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