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Database: UniProt
Entry: A0A0K0DXU0_STRER
LinkDB: A0A0K0DXU0_STRER
Original site: A0A0K0DXU0_STRER 
ID   A0A0K0DXU0_STRER        Unreviewed;       283 AA.
AC   A0A0K0DXU0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Thioredoxin domain-containing protein {ECO:0000313|WBParaSite:SSTP_0000205500.1};
OS   Strongyloides stercoralis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=6248 {ECO:0000313|Proteomes:UP000035681, ECO:0000313|WBParaSite:SSTP_0000205500.1};
RN   [1] {ECO:0000313|Proteomes:UP000035681}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SSTP_0000205500.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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DR   AlphaFoldDB; A0A0K0DXU0; -.
DR   STRING; 6248.A0A0K0DXU0; -.
DR   WBParaSite; SSTP_0000205500.1; SSTP_0000205500.1; SSTP_0000205500.
DR   Proteomes; UP000035681; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02968; SCO; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR003782; SCO1/SenC.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR12151:SF5; AT19154P; 1.
DR   PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   Pfam; PF02630; SCO1-SenC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR603782-1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        73..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          114..280
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         149
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         153
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         240
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        149..153
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   283 AA;  32959 MW;  05652C377F15F17D CRC64;
     MLSRVIRLKP FFKQSNYCLA SFCSKKGDLK VNIDVKKLKE EIKNLNNDGN VRPDFMNFKQ
     QQVKKTRERS YIFNWKSVLA TFGIGSILLL VLTYMRQQKL NEEEKRRKVM AGKARIGGEW
     ELINTEGKLE GSKDLLGNWV LTYFGFTHCP DICPDEIEKM ISVINQLNEN NPEIPIIPVF
     ISVDPDRDTP ERVKIYCNEF SPKLRGYTGT TEQVKKVTKT FRIYHSQGPK TAEDDYIVDH
     TVIMYLIDPN GEFHDYYGQN KTDKEIADII RLKVLKYELA KKK
//
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