ID   A0A1I3UU20_9SPHN        Unreviewed;       193 AA.
AC   A0A1I3UU20;
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:SFJ85361.1};
GN   ORFNames=SAMN03159338_2558 {ECO:0000313|EMBL:SFJ85361.1};
OS   Sphingomonas sp. NFR04.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1566283 {ECO:0000313|EMBL:SFJ85361.1, ECO:0000313|Proteomes:UP000198602};
RN   [1] {ECO:0000313|EMBL:SFJ85361.1, ECO:0000313|Proteomes:UP000198602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NFR04 {ECO:0000313|EMBL:SFJ85361.1,
RC   ECO:0000313|Proteomes:UP000198602};
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; FORV01000003; SFJ85361.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3UU20; -.
DR   STRING; 1566283.SAMN03159338_2558; -.
DR   OrthoDB; 9790194at2; -.
DR   Proteomes; UP000198602; 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..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..193
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011687525"
FT   DOMAIN          29..193
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         67
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         71
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         158
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        67..71
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   193 AA;  20699 MW;  E1006FBB85CAA51E CRC64;
     MNWMFRALIA SAMLALAACG TGSTEAPPLA GARIGGPFTL TDQNGKTVTD ADFAGKYRIV
     YFGYTYCPDV CPTDLTKIGA ALRTLDKQGP GTAQKIVPLF ITVDPERDGP AQLKQYVGNF
     HPRLVGLTGS PQAIAQVAKE YAVAYMKQPT PSGYLMGHTE VAYLMGPDGK PITSLPLEKD
     PPAIVAELEH WVR
//