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Database: UniProt
Entry: W0DYZ2_9GAMM
LinkDB: W0DYZ2_9GAMM
Original site: W0DYZ2_9GAMM 
ID   W0DYZ2_9GAMM            Unreviewed;       210 AA.
AC   W0DYZ2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN   ORFNames=THIAE_01870 {ECO:0000313|EMBL:AHF02184.1};
OS   Thiomicrospira aerophila AL3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Thiomicrospira.
OX   NCBI_TaxID=717772 {ECO:0000313|EMBL:AHF02184.1, ECO:0000313|Proteomes:UP000005380};
RN   [1] {ECO:0000313|EMBL:AHF02184.1, ECO:0000313|Proteomes:UP000005380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AL2 {ECO:0000313|Proteomes:UP000005380};
RG   DOE Joint Genome Institute;
RA   Kappler U., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) 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; CP007030; AHF02184.1; -; Genomic_DNA.
DR   RefSeq; WP_006459796.1; NZ_CP007030.1.
DR   AlphaFoldDB; W0DYZ2; -.
DR   STRING; 717772.THIAE_01870; -.
DR   KEGG; tao:THIAE_01870; -.
DR   eggNOG; COG1999; Bacteria.
DR   HOGENOM; CLU_050131_3_0_6; -.
DR   InParanoid; W0DYZ2; -.
DR   OrthoDB; 5616157at2; -.
DR   Proteomes; UP000005380; Chromosome.
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}.
FT   DOMAIN          41..203
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         79
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         83
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         167
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        79..83
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   210 AA;  23899 MW;  023DC21A2742AD37 CRC64;
     MTKKQWWLSG LFITLTLLLW GVMLILPGTL AKWSDHQAYG LVVDRPAPSW SLIDTTGQPL
     SLDRFAGKYV YFYIGYLNCN GVCQTHLSTL FQLDRNASPD LPFDIIFMTM DPERDTPAVL
     ESRINSLGAR FNGALPHDFA AGQVIARQFN VPFAKQPSRI QPYEIEHAAF MFLIDPNGQW
     VRTYTGRFLN AERMLDELTQ LLQGHYHATS
//
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