ID M0F601_9EURY Unreviewed; 239 AA.
AC M0F601;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=C467_12302 {ECO:0000313|EMBL:ELZ54034.1};
OS Halorubrum hochstenium ATCC 700873.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1227481 {ECO:0000313|EMBL:ELZ54034.1, ECO:0000313|Proteomes:UP000011689};
RN [1] {ECO:0000313|EMBL:ELZ54034.1, ECO:0000313|Proteomes:UP000011689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700873 {ECO:0000313|EMBL:ELZ54034.1,
RC ECO:0000313|Proteomes:UP000011689};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ54034.1}.
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DR EMBL; AOJO01000056; ELZ54034.1; -; Genomic_DNA.
DR RefSeq; WP_008585692.1; NZ_AOJO01000056.1.
DR AlphaFoldDB; M0F601; -.
DR STRING; 1227481.C467_12302; -.
DR GeneID; 72714389; -.
DR PATRIC; fig|1227481.4.peg.2430; -.
DR OrthoDB; 27579at2157; -.
DR Proteomes; UP000011689; 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 Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000011689}.
FT DOMAIN 51..234
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 99
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 103
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 198
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 99..103
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 239 AA; 25541 MW; A850491DC0A28C75 CRC64;
MKRRTLLAGV GTAAAGSVAG CTSRLFGDGP DGVALDPQED QIADSEDLAY PAYGQPLPSF
ELPAPLADGA SDGDALAGGT FDSDELDRTA LVTGVFTFCP AECSILLRQW VTVQRRVADA
GLTDDVYFLP ITFDPERDDA AALRDNAESI GADLDAGNWI YLRPETPERA SAVVEDKLGI
GFERTTDSDR LPGYDFTHIV VTTLVNPDGV VERAYRGERL DPDRVAADVE RVVAAFADE
//
