ID   A0A1Q4FCN3_9SPHI        Unreviewed;       235 AA.
AC   A0A1Q4FCN3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=SCO family protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BGP14_06195 {ECO:0000313|EMBL:OJY90988.1};
OS   Sphingobacteriales bacterium 44-15.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895837 {ECO:0000313|EMBL:OJY90988.1, ECO:0000313|Proteomes:UP000186250};
RN   [1] {ECO:0000313|EMBL:OJY90988.1, ECO:0000313|Proteomes:UP000186250}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=44-15 {ECO:0000313|EMBL:OJY90988.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJY90988.1}.
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DR   EMBL; MKWG01000007; OJY90988.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q4FCN3; -.
DR   STRING; 1895837.BGP14_06195; -.
DR   Proteomes; UP000186250; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Pfam; PF02630; SCO1-SenC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        203..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         51
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         55
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         138
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        51..55
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   235 AA;  26211 MW;  BE955EE417D6A088 CRC64;
     MLSGFNLPNE KNFLAQKAAN IRVFDATGKT FELYSLLGKK PLIISPVYTR CHSLCGVISN
     GVQTAINELG TLGQDFTMVS FSFDSSDRQI NLAAYESRWK MDGVNWKTIS ASGKDIQRLL
     SSIGYEYDYD PATKEFNHPS ILIVLTPGGR ISRFIYGVNP SKKDIKLAVI EAMAEKIRPG
     LFKGFYLRCF GYDPALKTYK PDWRFIISTS AGLLMISLVS GLFIKSFIIS KNQDG
//