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Database: UniProt
Entry: A0A1I5TQM3_9RHOB
LinkDB: A0A1I5TQM3_9RHOB
Original site: A0A1I5TQM3_9RHOB 
ID   A0A1I5TQM3_9RHOB        Unreviewed;       227 AA.
AC   A0A1I5TQM3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Protein SCO1/2 {ECO:0000313|EMBL:SFP85191.1};
GN   ORFNames=SAMN04488047_11469 {ECO:0000313|EMBL:SFP85191.1};
OS   Tranquillimonas alkanivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Tranquillimonas.
OX   NCBI_TaxID=441119 {ECO:0000313|EMBL:SFP85191.1, ECO:0000313|Proteomes:UP000199356};
RN   [1] {ECO:0000313|EMBL:SFP85191.1, ECO:0000313|Proteomes:UP000199356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19547 {ECO:0000313|EMBL:SFP85191.1,
RC   ECO:0000313|Proteomes:UP000199356};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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DR   EMBL; FOXA01000014; SFP85191.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5TQM3; -.
DR   STRING; 441119.SAMN04488047_11469; -.
DR   Proteomes; UP000199356; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199356};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        33..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         101
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         105
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         191
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        101..105
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   227 AA;  24860 MW;  42B756D86354F9FC CRC64;
     MLNLKQVEVV DAPTSRSLKR RATNTTMTSS VKIPWVLAVA AALALGWGLL WAGYFSESPG
     DTEGEAPFYA DFDLTAHTGM FMTEEDFAGQ WKLIFFGFAN CPDVCPTTLS EVAAVMDGLG
     PDKEKVQPLF ITVDPERDTP EVLANFVPRF DAGIIGLTGT PEQTARTAEN FYIYYEKVEE
     AAAPGDYTMG HSSQLFLFGP DGGYVTSWQY GTPAEEILAD LRERISS
//
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