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Database: UniProt
Entry: A0A154WFZ9_9PROT
LinkDB: A0A154WFZ9_9PROT
Original site: A0A154WFZ9_9PROT 
ID   A0A154WFZ9_9PROT        Unreviewed;       202 AA.
AC   A0A154WFZ9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Electron transport protein SCO1/SenC {ECO:0000313|EMBL:KZD12395.1};
GN   ORFNames=AUP43_16490 {ECO:0000313|EMBL:KZD12395.1};
OS   Oceanibaculum pacificum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Oceanibaculaceae; Oceanibaculum.
OX   NCBI_TaxID=580166 {ECO:0000313|EMBL:KZD12395.1, ECO:0000313|Proteomes:UP000076400};
RN   [1] {ECO:0000313|EMBL:KZD12395.1, ECO:0000313|Proteomes:UP000076400}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCCC 1A02656 {ECO:0000313|EMBL:KZD12395.1,
RC   ECO:0000313|Proteomes:UP000076400};
RA   Lu L., Lai Q., Shao Z., Qian P.;
RT   "Genome sequence of Oceanibaculum pacificum MCCC 1A02656.";
RL   Submitted (DEC-2015) 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:KZD12395.1}.
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DR   EMBL; LPXN01000027; KZD12395.1; -; Genomic_DNA.
DR   RefSeq; WP_067552402.1; NZ_LPXN01000027.1.
DR   AlphaFoldDB; A0A154WFZ9; -.
DR   STRING; 580166.AUP43_16490; -.
DR   OrthoDB; 9790194at2; -.
DR   Proteomes; UP000076400; 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:UP000076400}.
FT   DOMAIN          43..202
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
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         168
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   202 AA;  22123 MW;  D951CB0299717076 CRC64;
     MIRRRFLLGV AGLAGLLAAT LFAGWWQVDG PGARTPRLSI AGGPPPLAQA EMTLTDHEGR
     RTSPASWVGR PTLLFFGFTY CPDVCPTTLS DITGWLEALG GEARDINVAF VTVDPERDTA
     EAMADYVDMF HPAIVGYTGA PDEIRKTADF FGAFYKKVET ESGYMMNHTA TVFLFDAAGN
     FRSTIDYHEA REIAVPKIRK VL
//
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