ID   A0A1I2JIH0_9BACT        Unreviewed;       207 AA.
AC   A0A1I2JIH0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Protein SCO1/2 {ECO:0000313|EMBL:SFF53643.1};
GN   ORFNames=SAMN04488541_10513 {ECO:0000313|EMBL:SFF53643.1};
OS   Thermoflexibacter ruber.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Thermoflexibacteraceae;
OC   Thermoflexibacter.
OX   NCBI_TaxID=1003 {ECO:0000313|EMBL:SFF53643.1, ECO:0000313|Proteomes:UP000199513};
RN   [1] {ECO:0000313|EMBL:SFF53643.1, ECO:0000313|Proteomes:UP000199513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GEY, DSM 9560 {ECO:0000313|Proteomes:UP000199513};
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}.
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; FONY01000051; SFF53643.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2JIH0; -.
DR   STRING; 1003.SAMN04488541_10513; -.
DR   Proteomes; UP000199513; 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; 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; 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:UP000199513}.
FT   DOMAIN          39..201
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         77
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         81
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        77..81
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   207 AA;  23840 MW;  2877C26023ECA06A CRC64;
     MTILAVPTFI ILFLHSFGEN KFEIPVMNPS SPDCQSNVLD SVHRIPPFKF ISQDGKEVTE
     KDFEGKVYIV DFFFTRCPDI CPTMTSELVR VQEAFKDFPD VRILSHSVDP LYDSVAILKE
     YAQKFKANTQ IWTFVTGDKG AIYNMARCGY FISARENTSP ISVDFVHSDK VVLIDKEKRI
     RGYYSGTNRK EIDRLITEVQ ILLQEYK
//