ID   A0A011NKY1_9PROT        Unreviewed;       196 AA.
AC   A0A011NKY1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=SCO1/SenC {ECO:0000313|EMBL:EXI65050.1};
DE   Flags: Precursor;
GN   ORFNames=AW08_03503 {ECO:0000313|EMBL:EXI65050.1};
OS   Candidatus Accumulibacter adjunctus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=1454001 {ECO:0000313|EMBL:EXI65050.1, ECO:0000313|Proteomes:UP000020218};
RN   [1] {ECO:0000313|EMBL:EXI65050.1, ECO:0000313|Proteomes:UP000020218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-12 {ECO:0000313|Proteomes:UP000020218};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-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:EXI65050.1}.
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DR   EMBL; JFAX01000029; EXI65050.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A011NKY1; -.
DR   STRING; 1454001.AW08_03503; -.
DR   PATRIC; fig|1454001.3.peg.3541; -.
DR   Proteomes; UP000020218; 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; PS51257; PROKAR_LIPOPROTEIN; 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:UP000020218};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..196
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001462345"
FT   DOMAIN          18..194
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         70
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         74
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        70..74
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   196 AA;  21214 MW;  ED06CF64F6D33ED9 CRC64;
     MKTFPSLASL VLLLNLMLVA CSGPPAFKST DITGVDWGKE LALTDHTGQP RRLADFKGKA
     VIVFFGYTQC PDVCPTTLLS MRETVARLGS DAGRVQVLFV TLDPARDTQQ LLAEYVTAFN
     PGFIGLRGDE AATAAAAREF KVFYVRQPGS TPDSYSIDHS TGSYVFDPQG RLRLLVRHGE
     APDHVAADLK LLLAGK
//