ID   A0A124IIL8_9SPHN        Unreviewed;       207 AA.
AC   A0A124IIL8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Electron transporter {ECO:0000313|EMBL:KUO56870.1};
GN   ORFNames=APF82_00195 {ECO:0000313|EMBL:KUO56870.1};
OS   Sphingomonadales bacterium BRH_c42.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales.
OX   NCBI_TaxID=1734407 {ECO:0000313|EMBL:KUO56870.1, ECO:0000313|Proteomes:UP000054281};
RN   [1] {ECO:0000313|EMBL:KUO56870.1, ECO:0000313|Proteomes:UP000054281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c42 {ECO:0000313|EMBL:KUO56870.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) 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:KUO56870.1}.
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; LOEX01000021; KUO56870.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A124IIL8; -.
DR   Proteomes; UP000054281; 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:SF5; AT19154P; 1.
DR   PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 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}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..207
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007174431"
FT   DOMAIN          41..207
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         79
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         83
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        79..83
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   207 AA;  22038 MW;  BCAF66D8E36E93CF CRC64;
     MNYRAMPSPK QKSNFVVFAA LSLALAACDG AATAPPQDPP LAGADIGGPF ELVDQHGKTV
     RWEDFAGKYR MVYFGFTYCP DICPTDVGRM VHGLGRLEKL EPEKAAKVVP IFISVDPERD
     TPAVVGEFAA AFSDKLIGLT GTPEQVKAAA DAFRVYYSRG EDTPGGGYLV DHSAVVYLFG
     PQGEPLATLP VDKGADAVAA ELAKWVS
//