ID   A0A0D0QAZ3_9RHOB        Unreviewed;       179 AA.
AC   A0A0D0QAZ3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Uncharacterized protein SCO1/SenC/PrrC {ECO:0000313|EMBL:KIQ69467.1};
GN   ORFNames=Wenmar_01829 {ECO:0000313|EMBL:KIQ69467.1};
OS   Wenxinia marina DSM 24838.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Wenxinia.
OX   NCBI_TaxID=1123501 {ECO:0000313|EMBL:KIQ69467.1, ECO:0000313|Proteomes:UP000035100};
RN   [1] {ECO:0000313|EMBL:KIQ69467.1, ECO:0000313|Proteomes:UP000035100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24838 {ECO:0000313|EMBL:KIQ69467.1,
RC   ECO:0000313|Proteomes:UP000035100};
RA   Fiebig A., Goeker M., Klenk H.-P.P.;
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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:KIQ69467.1}.
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DR   EMBL; AONG01000009; KIQ69467.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0QAZ3; -.
DR   STRING; 1123501.Wenmar_01829; -.
DR   PATRIC; fig|1123501.6.peg.1927; -.
DR   eggNOG; COG1999; Bacteria.
DR   Proteomes; UP000035100; Unassembled WGS sequence.
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035100}.
FT   DOMAIN          17..179
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         55
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         59
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         145
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        55..59
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   179 AA;  19751 MW;  EEBBBFA92B92C841 CRC64;
     MLGLLWLDYH ADQARVAEEP AFAAAFELTD HRGVVRTEDD FAGRWMLIFF GFANCPDVCP
     TTLAEVAAVM DGLGDDAEEV QPIFISIDPE RDTPQALADF VPLFNERIIG LTGTPGQIAE
     TAEIFPIYFE RIEEASAPDG YTMGHTSHLL LFGPDAGFVD SWPYGTPAEE IIADLRERI
//