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Database: UniProt
Entry: A0A1H9EM16_9EURY
LinkDB: A0A1H9EM16_9EURY
Original site: A0A1H9EM16_9EURY 
ID   A0A1H9EM16_9EURY        Unreviewed;       249 AA.
AC   A0A1H9EM16;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Protein SCO1/2 {ECO:0000313|EMBL:SEQ26744.1};
GN   ORFNames=SAMN04489841_1331 {ECO:0000313|EMBL:SEQ26744.1};
OS   Natrinema salaciae.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrinema.
OX   NCBI_TaxID=1186196 {ECO:0000313|EMBL:SEQ26744.1, ECO:0000313|Proteomes:UP000199114};
RN   [1] {ECO:0000313|Proteomes:UP000199114}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25055 {ECO:0000313|Proteomes:UP000199114};
RA   Varghese N., Submissions S.;
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; FOFD01000002; SEQ26744.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9EM16; -.
DR   STRING; 1186196.SAMN04489841_1331; -.
DR   OrthoDB; 27579at2157; -.
DR   Proteomes; UP000199114; 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; IPR006311; TAT_signal.
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; PS51318; TAT; 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          61..247
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
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         211
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   249 AA;  27323 MW;  B7901E448A1501A3 CRC64;
     MTPTDVPLDR RTFLRVAGAT TVAASLAGCS QLNRTDDSDD GLVLSPPENH DRIENADLPH
     PIYGESIPEV TVPAPLHDRA VTTTEFAGER HSMLTFIYTS CTTVCPGLTA ALRRVQADAT
     ERGYEDEVAF LPFTFDPEYD TAEVLESYGE TLGVDFDPGN WYFLRPETPD DARTIVEDTY
     GVAFEQGNES DDGRMGDDHD EDGDHARHFV HTSLILLVNK DGRVERAYTG GSPGGNEIVE
     DARAVVEGW
//
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