ID   A0A1H6J6B6_9FLAO        Unreviewed;       223 AA.
AC   A0A1H6J6B6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Protein SCO1/2 {ECO:0000313|EMBL:SEH54482.1};
GN   ORFNames=SAMN02927937_00111 {ECO:0000313|EMBL:SEH54482.1};
OS   Paenimyroides aquimaris.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Paenimyroides.
OX   NCBI_TaxID=1159016 {ECO:0000313|EMBL:SEH54482.1, ECO:0000313|Proteomes:UP000199634};
RN   [1] {ECO:0000313|EMBL:SEH54482.1, ECO:0000313|Proteomes:UP000199634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10825 {ECO:0000313|EMBL:SEH54482.1,
RC   ECO:0000313|Proteomes:UP000199634};
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; FNXE01000001; SEH54482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6J6B6; -.
DR   STRING; 1159016.SAMN02927937_00111; -.
DR   OrthoDB; 9811998at2; -.
DR   Proteomes; UP000199634; 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   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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199634};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          48..218
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         86
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         90
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         174
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        86..90
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   223 AA;  25554 MW;  B11573ACF902FF67 CRC64;
     MKKNNSYIWI SLIILVFGIY AVPKIVDRFK NASVVENDRL NVANRKELKV IGKAPAFSFT
     NQNNETITNA DYEGKVYLVE FFFSNCPTIC PIMNENMVKL QNEFQMNANF GIVSITIDPE
     NDTPEHLKKH AEFLGVTMKN WNFLTGTEDA VFDLSKKFNL YVGKNDDAPG GFEHSGLFAL
     IDKKGNIRSR NMENMDYPMF YYDGTTDEGV QMLKEDIKQL IKE
//