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Database: UniProt
Entry: A0A0A2WJ97_9GAMM
LinkDB: A0A0A2WJ97_9GAMM
Original site: A0A0A2WJ97_9GAMM 
ID   A0A0A2WJ97_9GAMM        Unreviewed;       192 AA.
AC   A0A0A2WJ97;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=SCO1/SenC family protein {ECO:0000313|EMBL:KGQ18792.1};
GN   ORFNames=LF41_325 {ECO:0000313|EMBL:KGQ18792.1};
OS   Lysobacter dokdonensis DS-58.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1300345 {ECO:0000313|EMBL:KGQ18792.1, ECO:0000313|Proteomes:UP000030518};
RN   [1] {ECO:0000313|EMBL:KGQ18792.1, ECO:0000313|Proteomes:UP000030518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-58 {ECO:0000313|EMBL:KGQ18792.1,
RC   ECO:0000313|Proteomes:UP000030518};
RA   Kim J.F., Kwak M.-J.;
RT   "Genome sequences of Lysobacter dokdonensis DS-58.";
RL   Submitted (SEP-2014) 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:KGQ18792.1}.
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DR   EMBL; JRKJ01000016; KGQ18792.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2WJ97; -.
DR   STRING; 1300345.LF41_325; -.
DR   PATRIC; fig|1300345.3.peg.2000; -.
DR   eggNOG; COG1999; Bacteria.
DR   OrthoDB; 6335573at2; -.
DR   Proteomes; UP000030518; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030518};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..192
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001996757"
FT   DOMAIN          28..192
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         68
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         72
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        68..72
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   192 AA;  20862 MW;  8701891AF4A06F64 CRC64;
     MKWLRSMTAC LALLVASSGA AETGKTGSRP ADSVYQLSMP LTDARGKTQD WRALEGKPRI
     VAMFYTSCPY MCPLIVESAK AVEHALPPAQ RGRVGVVLIS LDPARDTPAV LRETATKRKI
     DATRWLLAAP APADVRKIAG VLDVRYRRLA DGNFNHTSVL ILLDARGRIV ARTEQIGPKP
     DADFVSAVRA QL
//
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