ID   A0A1Z9AFI3_9GAMM        Unreviewed;       210 AA.
AC   A0A1Z9AFI3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN   ORFNames=CBC55_12435 {ECO:0000313|EMBL:OUV19225.1};
OS   Gammaproteobacteria bacterium TMED95.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1986771 {ECO:0000313|EMBL:OUV19225.1, ECO:0000313|Proteomes:UP000195745};
RN   [1] {ECO:0000313|EMBL:OUV19225.1, ECO:0000313|Proteomes:UP000195745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMED95 {ECO:0000313|EMBL:OUV19225.1};
RA   Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT   "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT   for marine microbiology.";
RL   Submitted (MAY-2017) 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:OUV19225.1}.
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DR   EMBL; NHEW01000037; OUV19225.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z9AFI3; -.
DR   Proteomes; UP000195745; 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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          52..210
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         90
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         94
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         177
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        90..94
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   210 AA;  22921 MW;  4F65035ED8F60045 CRC64;
     MPSETQKAGI RKTLTLLLGF IALMVGVIMA NYLYRDVSMT PEQAAKIGFI RFETPRPIQL
     SELVLANGEP IKADYFLGNW NLLYFGFTAC PDICPTTLAL LNQASEQYQG EQPSIHLVSV
     DPEQDTPKQL ARYLAGFNPA FNGLTGSHEA ITRFATQVNV AFGKIPGAEP GTYTVDHTGS
     IVVIDPQGRY AGFIKAPHQT AQLMQVFAGL
//