ID   A0A1H1L0N5_9FLAO        Unreviewed;       206 AA.
AC   A0A1H1L0N5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Protein SCO1/2 {ECO:0000313|EMBL:SDR68093.1};
GN   ORFNames=SAMN04487764_0218 {ECO:0000313|EMBL:SDR68093.1};
OS   Gillisia sp. Hel1_33_143.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Gillisia.
OX   NCBI_TaxID=1336796 {ECO:0000313|EMBL:SDR68093.1, ECO:0000313|Proteomes:UP000199552};
RN   [1] {ECO:0000313|EMBL:SDR68093.1, ECO:0000313|Proteomes:UP000199552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hel1_33_143 {ECO:0000313|EMBL:SDR68093.1,
RC   ECO:0000313|Proteomes:UP000199552};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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DR   EMBL; LT629737; SDR68093.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1L0N5; -.
DR   STRING; 1336796.SAMN04487764_0218; -.
DR   Proteomes; UP000199552; Chromosome i.
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; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   PANTHER; PTHR12151:SF25; SCO1 PROTEIN HOMOLOG; 1.
DR   Pfam; PF02630; SCO1-SenC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000199552}.
FT   DOMAIN          40..204
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         78
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         82
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         167
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        78..82
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   206 AA;  23477 MW;  D007264C8446780D CRC64;
     MTVKFQLILL IIMGLLTSCE DQNRHLPILG NKEVANNEED TIYHSIPYFS FIDQDSLTIT
     SNTFTDKIYV ADFFFTSCPT ICPIMKNQMQ RVYEKFKGNK NVAFLSHSID PSHDSVPVLK
     TYAEDLDINN GQWHFVTGNR EEIFAIAENH YMVSAQEDPS APGGAIHSGA FILIDKQKRI
     RGYYDGTNTE EVDKLIEDIP ILLNNY
//