ID B6DTG4_BODSA Unreviewed; 142 AA.
AC B6DTG4;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Tryparedoxin {ECO:0000313|EMBL:ACI16006.1, ECO:0000313|EMBL:CUG90309.1};
GN ORFNames=BSAL_26065 {ECO:0000313|EMBL:CUG90309.1};
OS Bodo saltans (Flagellated protozoan).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Eubodonida; Bodonidae; Bodo.
OX NCBI_TaxID=75058 {ECO:0000313|EMBL:ACI16006.1};
RN [1] {ECO:0000313|EMBL:ACI16006.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Lake Konstanz {ECO:0000313|EMBL:ACI16006.1};
RA Jackson A.P., Quail M.A., Berriman M.;
RT "Insights into the genome sequence of a free-living kinetoplastid: Bodo
RT saltans (Kinetoplastida: Euglenozoa).";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CUG90309.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Konstanz {ECO:0000313|EMBL:CUG90309.1};
RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000051952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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; FJ168553; ACI16006.1; -; Genomic_DNA.
DR EMBL; CYKH01001813; CUG90309.1; -; Genomic_DNA.
DR VEuPathDB; TriTrypDB:BSAL_26065; -.
DR OMA; TDDYKHE; -.
DR OrthoDB; 3073590at2759; -.
DR Proteomes; UP000051952; Unassembled WGS sequence.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR CDD; cd03009; TryX_like_TryX_NRX; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
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; PTHR46472; NUCLEOREDOXIN; 1.
DR PANTHER; PTHR46472:SF1; NUCLEOREDOXIN; 1.
DR Pfam; PF13905; Thioredoxin_8; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000051952}.
FT DOMAIN 1..142
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 142 AA; 15925 MW; 9DBB3ECBCDDB9418 CRC64;
MSGIAKVLGL EAVKNKAGEL ALSSLAGKTV FLYFSASWCP PCRGFTPQLG AFYDKFAKDK
NFEVVFVSWD EEEDDFNGYY EKMQWATLPF DEAKSKELTQ TFNVESIPTL IGIDADSGEI
VTRSARTMVV KDPEGEKFPW KE
//
