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Database: UniProt
Entry: A0A1V0GYB5_9RHOB
LinkDB: A0A1V0GYB5_9RHOB
Original site: A0A1V0GYB5_9RHOB 
ID   A0A1V0GYB5_9RHOB        Unreviewed;       204 AA.
AC   A0A1V0GYB5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=SCO family protein {ECO:0000313|EMBL:ARC38808.1};
GN   ORFNames=A6J80_21110 {ECO:0000313|EMBL:ARC38808.1};
OS   Paracoccus yeei.
OG   Plasmid unnamed4 {ECO:0000313|EMBL:ARC38808.1,
OG   ECO:0000313|Proteomes:UP000191257}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=147645 {ECO:0000313|EMBL:ARC38808.1, ECO:0000313|Proteomes:UP000191257};
RN   [1] {ECO:0000313|Proteomes:UP000191257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_252 {ECO:0000313|Proteomes:UP000191257};
RC   PLASMID=Plasmid unnamed4 {ECO:0000313|Proteomes:UP000191257};
RA   Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA   Sadzewicz L., Sengamalay N., Ott S., Godinez A., Nagaraj S., Nadendla S.,
RA   Geyer C., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (MAR-2017) 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; CP020444; ARC38808.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V0GYB5; -.
DR   KEGG; pye:A6J80_21110; -.
DR   Proteomes; UP000191257; Plasmid unnamed4.
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   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.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Plasmid {ECO:0000313|EMBL:ARC38808.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191257}.
FT   BINDING         81
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         85
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         169
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        81..85
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   204 AA;  22814 MW;  386B183152F4A1AB CRC64;
     MRRRKLILGG AGLLGAFGFT LGLGAWRSGD LRRLTDVRET ESGRPDLSRM VWRLIDDQGN
     PVVPQDWLSQ ASMVFFGFTW CPDVCPTTLM DIADWLEGLG QDADRIRVAM ITVDPERDSP
     EILAEYLSNF DIRIRGLTGS ADAVAEAAEA FDVTYTRLPR DDGDYTMNHT SGVFVFRPSG
     ELASTIDFHE ERRFAVPKIR RAIG
//
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