ID   A0A1G9X1L9_9BACT        Unreviewed;       212 AA.
AC   A0A1G9X1L9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Protein SCO1/2 {ECO:0000313|EMBL:SDM90441.1};
GN   ORFNames=SAMN04488090_4517 {ECO:0000313|EMBL:SDM90441.1};
OS   Siphonobacter aquaeclarae.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC   Siphonobacter.
OX   NCBI_TaxID=563176 {ECO:0000313|EMBL:SDM90441.1, ECO:0000313|Proteomes:UP000198901};
RN   [1] {ECO:0000313|EMBL:SDM90441.1, ECO:0000313|Proteomes:UP000198901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21668 {ECO:0000313|EMBL:SDM90441.1,
RC   ECO:0000313|Proteomes:UP000198901};
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; FNGS01000010; SDM90441.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9X1L9; -.
DR   STRING; 563176.SAMN04488090_4517; -.
DR   OrthoDB; 9811998at2; -.
DR   Proteomes; UP000198901; 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:UP000198901}.
FT   DOMAIN          44..209
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         82
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         86
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         172
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        82..86
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   212 AA;  23659 MW;  90BC406C41A48A9A CRC64;
     MKWFSFAALL LLLAACQQEQ GRLPILGPRG GIKTRVIDGK MVTDSVYHEI PDFAFVDQDG
     DTVRSADFRG KIYVADFFFT TCPTICPKMT GEMKKLYEKF KGNPDVLFLS HSIDPKRDSV
     GRLNEYATDL GVAGQKQWRF ITGDRKAIFD IGQNAYFVTA KEDSAEPGGI LHSGAFVLID
     PEMHIRGIYD GTKDEVVAEV SEAIALLRKE KK
//