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Database: UniProt
Entry: A0A1W1XK23_9NEIS
LinkDB: A0A1W1XK23_9NEIS
Original site: A0A1W1XK23_9NEIS 
ID   A0A1W1XK23_9NEIS        Unreviewed;       191 AA.
AC   A0A1W1XK23;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Protein SCO1/2 {ECO:0000313|EMBL:SMC24333.1};
GN   ORFNames=SAMN02745857_01850 {ECO:0000313|EMBL:SMC24333.1};
OS   Andreprevotia lacus DSM 23236.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chitinibacteraceae; Andreprevotia.
OX   NCBI_TaxID=1121001 {ECO:0000313|EMBL:SMC24333.1, ECO:0000313|Proteomes:UP000192761};
RN   [1] {ECO:0000313|EMBL:SMC24333.1, ECO:0000313|Proteomes:UP000192761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23236 {ECO:0000313|EMBL:SMC24333.1,
RC   ECO:0000313|Proteomes:UP000192761};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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; FWXD01000009; SMC24333.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W1XK23; -.
DR   STRING; 1121001.SAMN02745857_01850; -.
DR   OrthoDB; 9790194at2; -.
DR   Proteomes; UP000192761; 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   PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   PANTHER; PTHR12151:SF27; PUTATIVE-RELATED; 1.
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:UP000192761};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..191
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012686989"
FT   DOMAIN          16..191
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         68
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         72
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         155
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        68..72
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   191 AA;  20595 MW;  0219676578923321 CRC64;
     MKRILCAFSC LLLLGLLLGC SKASFQGTDL TGAAFGGDFQ LTTHTGKQSK LSDYRGKAVA
     LFFGYTNCPD VCPTTMSELK AAMQQLGPKA DQVQVLFVSV DPERDTQNVL SHYVPAFDPR
     FVGLTGTLAQ VEKVAEQYKI IIQKQGSGSS YTVDHSAGTY LLDKEGKLRV LVNYGAGPQI
     LAHDLGVLVN E
//
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