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Database: UniProt
Entry: A0A0D1XHC9_ANEMI
LinkDB: A0A0D1XHC9_ANEMI
Original site: A0A0D1XHC9_ANEMI 
ID   A0A0D1XHC9_ANEMI        Unreviewed;       202 AA.
AC   A0A0D1XHC9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Protein SCO1/2 {ECO:0000313|EMBL:SDJ12100.1};
GN   ORFNames=AF333_03885 {ECO:0000313|EMBL:KON94754.1}, SAMN04487909_11252
GN   {ECO:0000313|EMBL:SDJ12100.1};
OS   Aneurinibacillus migulanus (Bacillus migulanus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC   Aneurinibacillus group; Aneurinibacillus.
OX   NCBI_TaxID=47500 {ECO:0000313|EMBL:KON94754.1, ECO:0000313|Proteomes:UP000037269};
RN   [1] {ECO:0000313|EMBL:KON94754.1, ECO:0000313|Proteomes:UP000037269}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2895 {ECO:0000313|EMBL:KON94754.1,
RC   ECO:0000313|Proteomes:UP000037269};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-14205 dsm 2895.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SDJ12100.1, ECO:0000313|Proteomes:UP000182836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2895 {ECO:0000313|EMBL:SDJ12100.1,
RC   ECO:0000313|Proteomes:UP000182836};
RA   de Groot N.N.;
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; LGUG01000004; KON94754.1; -; Genomic_DNA.
DR   EMBL; FNED01000012; SDJ12100.1; -; Genomic_DNA.
DR   RefSeq; WP_043068513.1; NZ_LIXL01000166.1.
DR   AlphaFoldDB; A0A0D1XHC9; -.
DR   STRING; 47500.AF333_03885; -.
DR   PATRIC; fig|47500.12.peg.2423; -.
DR   OrthoDB; 9811998at2; -.
DR   Proteomes; UP000037269; Unassembled WGS sequence.
DR   Proteomes; UP000182836; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037269};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          36..201
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         74
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         78
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         164
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        74..78
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   202 AA;  22949 MW;  09A9CA8E67EE404D CRC64;
     MASFMKRYWF IVVAGTLIAA VLLTIVYQLW WGSNKLPTLD RAPSFTMSDM YGKPVSLRDS
     DGKVRLVSFH YTHCPDICQA TNFNLIRVQQ KLKEQGVLGD KALLMTITFD PKRDTEQMLQ
     KYTASQGIKS EGWSFLRGTP EQTEQVLQGF KVLAEDQGNG IFMHSNNLFL VDGSENIRAI
     YKMGSSMDNE QIVKDIHNLL DD
//
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