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Database: UniProt
Entry: C9QEF0_VIBOR
LinkDB: C9QEF0_VIBOR
Original site: C9QEF0_VIBOR 
ID   C9QEF0_VIBOR            Unreviewed;       196 AA.
AC   C9QEF0;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Cytochrome oxidase biogenesis protein Sco1/SenC/PrrC copper metallochaperone {ECO:0000313|EMBL:EGU54028.1};
GN   ORFNames=VIOR3934_19415 {ECO:0000313|EMBL:EGU54028.1};
OS   Vibrio orientalis CIP 102891 = ATCC 33934.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio; Vibrio oreintalis group.
OX   NCBI_TaxID=675816 {ECO:0000313|EMBL:EGU54028.1, ECO:0000313|Proteomes:UP000002817};
RN   [1] {ECO:0000313|EMBL:EGU54028.1, ECO:0000313|Proteomes:UP000002817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 102891 / ATCC 33934 {ECO:0000313|Proteomes:UP000002817};
RX   PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA   Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA   McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT   "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT   Scleritoderma cyanea.";
RL   Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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:EGU54028.1}.
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DR   EMBL; AFWH01000001; EGU54028.1; -; Genomic_DNA.
DR   RefSeq; WP_004412326.1; NZ_AFWH01000001.1.
DR   AlphaFoldDB; C9QEF0; -.
DR   STRING; 675816.VIA_001583; -.
DR   PATRIC; fig|675816.5.peg.108; -.
DR   eggNOG; COG1999; Bacteria.
DR   OrthoDB; 9790194at2; -.
DR   Proteomes; UP000002817; 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; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   PANTHER; PTHR12151:SF27; PUTATIVE-RELATED; 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}.
FT   DOMAIN          26..194
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   BINDING         159
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   196 AA;  21868 MW;  61D42815B05CAE3D CRC64;
     MSKNWSLILV AAFALGFGLK SYLDLQNETS PATEDSSVTL FGENNQAVSL FDPNDERVRV
     VYFGFTRCPD VCPTSLAMLA GALNQIDQPI KDQFRPIFIS LDPERDAAAD SYKYAQYFHP
     MIEGLSAPLD VTTPLAHKYG VIFRKTELEN SELKYTLDHS SYFYFLKPDG TLITKVPHTL
     TPAPLVEAFK TITSKG
//
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