ID   A0A0B7I0T8_9FLAO        Unreviewed;       199 AA.
AC   A0A0B7I0T8;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=BsSco {ECO:0000313|EMBL:CEN43368.1};
GN   ORFNames=CCAND38_100032 {ECO:0000313|EMBL:CEN43368.1}, CCAND93_220024
GN   {ECO:0000313|EMBL:CEN52185.1};
OS   Capnocytophaga canis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=1848903 {ECO:0000313|EMBL:CEN43368.1, ECO:0000313|Proteomes:UP000045051};
RN   [1] {ECO:0000313|Proteomes:UP000038200, ECO:0000313|Proteomes:UP000045051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CcD38 {ECO:0000313|EMBL:CEN43368.1,
RC   ECO:0000313|Proteomes:UP000045051}, and CcD93
RC   {ECO:0000313|EMBL:CEN52185.1, ECO:0000313|Proteomes:UP000038200};
RA   MANFREDI Pablo;
RL   Submitted (JAN-2015) 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; CDOI01000002; CEN43368.1; -; Genomic_DNA.
DR   EMBL; CDOL01000135; CEN52185.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B7I0T8; -.
DR   STRING; 1848903.CCAND38_100032; -.
DR   Proteomes; UP000038200; Unassembled WGS sequence.
DR   Proteomes; UP000045051; 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; 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:UP000045051};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..199
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007763034"
FT   DOMAIN          26..199
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         64
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         68
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         152
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        64..68
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   199 AA;  22338 MW;  C23375A45297AD44 CRC64;
     MKMRGIYALF LLLGMIACQT KEKPEIVTIG KAPSFTFTNQ NNQTINNETY AGMVYVVDFF
     FTDCPTICPV MTNNMVKIQN ELKDKNVGFA SFSINPEEDT PEVLKAYAQK KGATSANWHF
     LTGEVDAIYD LSNKGFNLHV EEVAGDIHRF EHSGLFALID QHGNIVSRKG KDGKPIIYYN
     GLNDSQVKML IEDIKSLIE
//