ID A0A091D3D3_FUKDA Unreviewed; 356 AA.
AC A0A091D3D3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Nucleoredoxin {ECO:0000256|ARBA:ARBA00026178};
DE EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
GN ORFNames=H920_13045 {ECO:0000313|EMBL:KFO25537.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO25537.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO25537.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO25537.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KN123351; KFO25537.1; -; Genomic_DNA.
DR RefSeq; XP_010640711.1; XM_010642409.1.
DR AlphaFoldDB; A0A091D3D3; -.
DR STRING; 885580.ENSFDAP00000004881; -.
DR GeneID; 104875041; -.
DR CTD; 64359; -.
DR eggNOG; KOG2501; Eukaryota.
DR OrthoDB; 1201562at2759; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR CDD; cd03071; PDI_b'_NRX; 1.
DR CDD; cd03009; TryX_like_TryX_NRX; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR InterPro; IPR041861; NRX_PDI_b.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR045870; TryX_NRX_thioredoxin_dom.
DR PANTHER; PTHR46472; NUCLEOREDOXIN; 1.
DR PANTHER; PTHR46472:SF1; NUCLEOREDOXIN; 1.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR Pfam; PF13905; Thioredoxin_8; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT DOMAIN 88..235
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 356 AA; 39934 MW; 6C8C434C5D8B3B84 CRC64;
MNLSVQTSSL KKVCSEPRAA LAQKCFVSPL EARGVGPTPF ELKLWNKYRI SNIPSLIFLD
ATTGKVVCRN GLLVIRDDPE GLEFPWGPKP FREVIAGPLL RNNGQSLDSS SLEGSHVGVY
FSAHWCPPCR SLTRVLVESY RKIKEAGQKF EIIFVSADRS EESFKQYFSE MPWLAVPYTD
EARRSRLNRL YGIQGIPTLI VLDPQGEVIT RQGRVEVLND EDCREFPWHP KPVLELSDSN
AVQLNEGPCL VLFVDSEDDG ESEAAKQLIQ PIAEKIIAKY KAKEEEAPLL FFVAGEDDMT
DSLRDYTNLP EAAPLLTILD MSARAKYVMD VEEITPAIVE AFVNDFLAEK LKPEPI
//
