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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//