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Database: UniProt
Entry: A0A1B9YZJ7_9BRAD
LinkDB: A0A1B9YZJ7_9BRAD
Original site: A0A1B9YZJ7_9BRAD 
ID   A0A1B9YZJ7_9BRAD        Unreviewed;       208 AA.
AC   A0A1B9YZJ7;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Electron transporter SenC {ECO:0000313|EMBL:OCK60160.1};
GN   ORFNames=LMTR3_19225 {ECO:0000313|EMBL:OCK60160.1};
OS   Bradyrhizobium sp. LMTR 3.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=189873 {ECO:0000313|EMBL:OCK60160.1, ECO:0000313|Proteomes:UP000093220};
RN   [1] {ECO:0000313|EMBL:OCK60160.1, ECO:0000313|Proteomes:UP000093220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMTR 3 {ECO:0000313|EMBL:OCK60160.1,
RC   ECO:0000313|Proteomes:UP000093220};
RA   Ormeno-Orrillo E., Duran D., Rey L., Ruiz Argueso T., Imperial J.,
RA   Martinez E.;
RL   Submitted (JUL-2016) 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:OCK60160.1}.
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DR   EMBL; MAXC01000012; OCK60160.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B9YZJ7; -.
DR   STRING; 189873.LMTR3_19225; -.
DR   Proteomes; UP000093220; 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:UP000093220}.
FT   BINDING         80
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         84
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        80..84
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   208 AA;  22760 MW;  CA8043003278F972 CRC64;
     MATRRRLLGL TAGLLLAGRG WSSRAQSSEG TSAARLMDDL MWNRGPIGGP FALIDHTGKP
     RTDEDFRGKL LLIYFGYSYC PDVCPTDLQQ IGLAIDGLGA GAEAVQPIFI TLDPERDTAA
     HLAGYVPLFH PRLIGLTGSA EQIRRVALAF KVYYAKYPPD SPDYVIDHSS FVYLVDEAGK
     YIGFLPSGTA ADRITETITL HLSDRTKR
//
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