GenomeNet

Database: UniProt
Entry: A0A2K3L9Z4_TRIPR
LinkDB: A0A2K3L9Z4_TRIPR
Original site: A0A2K3L9Z4_TRIPR 
ID   A0A2K3L9Z4_TRIPR        Unreviewed;       538 AA.
AC   A0A2K3L9Z4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=protein-disulfide reductase {ECO:0000256|ARBA:ARBA00012612};
DE            EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
DE   Flags: Fragment;
GN   ORFNames=L195_g031277 {ECO:0000313|EMBL:PNX75343.1};
OS   Trifolium pratense (Red clover).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX   NCBI_TaxID=57577 {ECO:0000313|EMBL:PNX75343.1, ECO:0000313|Proteomes:UP000236291};
RN   [1] {ECO:0000313|EMBL:PNX75343.1, ECO:0000313|Proteomes:UP000236291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:PNX75343.1};
RX   PubMed=24500806; DOI=10.3732/ajb.1300340;
RA   Istvanek J., Jaros M., Krenek A., Repkova J.;
RT   "Genome assembly and annotation for red clover (Trifolium pratense;
RT   Fabaceae).";
RL   Am. J. Bot. 101:327-337(2014).
RN   [2] {ECO:0000313|EMBL:PNX75343.1, ECO:0000313|Proteomes:UP000236291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:PNX75343.1};
RX   PubMed=28382043; DOI=10.3389/fpls.2017.00367;
RA   Istvanek J., Dluhosova J., Dluhos P., Patkova L., Nedelnik J., Repkova J.;
RT   "Gene Classification and Mining of Molecular Markers Useful in Red Clover
RT   (Trifolium pratense) Breeding.";
RL   Front. Plant Sci. 8:367-367(2017).
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}.
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:PNX75343.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ASHM01028901; PNX75343.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K3L9Z4; -.
DR   Proteomes; UP000236291; Unassembled WGS sequence.
DR   ExpressionAtlas; A0A2K3L9Z4; baseline.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR   CDD; cd03009; TryX_like_TryX_NRX; 2.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR004146; DC1.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR045870; TryX_NRX_thioredoxin_dom.
DR   PANTHER; PTHR13871; THIOREDOXIN; 1.
DR   PANTHER; PTHR13871:SF96; THIOREDOXIN DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF03107; C1_2; 1.
DR   Pfam; PF13905; Thioredoxin_8; 3.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 3.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000236291}.
FT   DOMAIN          1..134
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          288..451
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PNX75343.1"
SQ   SEQUENCE   538 AA;  60728 MW;  0856A56EB2A0C27F CRC64;
     VGIDSLKGKK IGFYFSASWC GPCQRFTPIL AEVYNELSPN GDFEVVFVSA DEDEEAFKNY
     FSKMPWLAIP FSDTETRNSL DELFHVNGIP HLALLHETGK VITEDGVDII RDYGAEGYPF
     TSERVQELKD QEEEAKRNQS LRSLLVSRSR DFVISSDGNK IPISELEGKT VGLYFCATSY
     RSCALFTQKL KDVYKKLKEK GENIEVVFIP LDDEEESLKK ELESLPWLSL PIKDKTCAKL
     IQYFELSELP TLVIIGPDGK TLHPNVAEAI EDHGIDAYPF TPEKFVELDE IAKAKEATQT
     LESVLVSGGQ DFVIKNGGEK IPVSELEGKT VLLYFSAHWC PPCRAFLPKL IDAYHKIKAQ
     DKDTLEVVFL SSDRDQDSFD EFFAGMPWLA LPFGDSRKEI LSRKFKVSGI PMLVAIGPSG
     RTVTKEARDL IGLYGADAYP FTEERIKEIE AKNDDIAKGW PEKVTHETHE HELVLSRRRI
     YYCDDCNKEG HIWSYFCEEC DFDLHPNCAL GDKGSVNSKE EEKPNDGWVC DGDVCTKA
//
DBGET integrated database retrieval system