ID   A0A1N7K9H6_9RHOB        Unreviewed;       252 AA.
AC   A0A1N7K9H6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Protein SCO1/2 {ECO:0000313|EMBL:SIS58229.1};
GN   ORFNames=SAMN05421795_101733 {ECO:0000313|EMBL:SIS58229.1};
OS   Phaeovulum vinaykumarii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Phaeovulum.
OX   NCBI_TaxID=407234 {ECO:0000313|EMBL:SIS58229.1, ECO:0000313|Proteomes:UP000186098};
RN   [1] {ECO:0000313|Proteomes:UP000186098}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18714 {ECO:0000313|Proteomes:UP000186098};
RA   Varghese N., Submissions S.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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; FTOM01000001; SIS58229.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1N7K9H6; -.
DR   STRING; 407234.SAMN05421795_101733; -.
DR   Proteomes; UP000186098; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000186098}.
FT   BINDING         114
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         118
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         202
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        114..118
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   252 AA;  27383 MW;  ECF96FFD2A15DF3F CRC64;
     MSLFCALGID SPCQLRNQFT DAAHGRQIRV GGAEVPIPAR QAAIAAAVVA IAGLGVAGYA
     VMRPAPDMFA QCRVDGRPAP IGGPFTLTDE TGRKVTDRDV ITGPTLLYFG YTFCPDVCPM
     DNMRNALAVM ALEDSGRMVT PVFISVDSGR DTPETLRQFT DVMHPRMIGL TGTPEQVKAA
     SKAYRTFYQI RDPEDEYYLI DHSTQTYLVF PELGFVENFD RDVEAEDMAA RVACFVDAWT
     ASQAAKTAPA GQ
//