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Database: UniProt
Entry: A0A0F5K563_9BURK
LinkDB: A0A0F5K563_9BURK
Original site: A0A0F5K563_9BURK 
ID   A0A0F5K563_9BURK        Unreviewed;       201 AA.
AC   A0A0F5K563;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN   ORFNames=WM40_01210 {ECO:0000313|EMBL:KKB65266.1};
OS   Robbsia andropogonis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Robbsia.
OX   NCBI_TaxID=28092 {ECO:0000313|EMBL:KKB65266.1, ECO:0000313|Proteomes:UP000033618};
RN   [1] {ECO:0000313|EMBL:KKB65266.1, ECO:0000313|Proteomes:UP000033618}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICMP2807 {ECO:0000313|EMBL:KKB65266.1,
RC   ECO:0000313|Proteomes:UP000033618};
RA   Lopes-Santos L., Castro D.B., Ottoboni L.M., Park D., Weirc B.S.,
RA   Destefano S.A.;
RT   "Draft Genome Sequence of Burkholderia andropogonis type strain ICMP2807,
RT   isolated from Sorghum bicolor.";
RL   Submitted (MAR-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:KKB65266.1}.
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DR   EMBL; LAQU01000001; KKB65266.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F5K563; -.
DR   STRING; 28092.WM40_01210; -.
DR   PATRIC; fig|28092.6.peg.269; -.
DR   Proteomes; UP000033618; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033618}.
FT   DOMAIN          21..198
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         59
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         63
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        59..63
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   201 AA;  21472 MW;  8B5718F3497358DA CRC64;
     MSAALGGCGK RGADFANLDI TGSRDFDPRF SLADSHGTLR TIADWHGKVV VLLFGYAQCP
     DVCPTSLAEL ARAKERLGAD GNRLQVVFLT VDPDRDTPAI LTEYVRAFDA GFVALRPETD
     AAVQQLAKQF HIYVAKTPAT SAAGASMSQP GAGHYGIAHT AASFVFDPEG RLRLYAKDGE
     GVDRWVHDAR LLLAPERTGA A
//
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