GenomeNet

Database: UniProt
Entry: A0A1I5V569_9BACI
LinkDB: A0A1I5V569_9BACI
Original site: A0A1I5V569_9BACI 
ID   A0A1I5V569_9BACI        Unreviewed;       196 AA.
AC   A0A1I5V569;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Protein SCO1/2 {ECO:0000313|EMBL:SFQ02591.1};
GN   ORFNames=SAMN05421670_0672 {ECO:0000313|EMBL:SFQ02591.1};
OS   Psychrobacillus psychrotolerans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX   NCBI_TaxID=126156 {ECO:0000313|EMBL:SFQ02591.1, ECO:0000313|Proteomes:UP000198734};
RN   [1] {ECO:0000313|Proteomes:UP000198734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11706 {ECO:0000313|Proteomes:UP000198734};
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}.
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; FOXU01000001; SFQ02591.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5V569; -.
DR   STRING; 126156.SAMN05421670_0672; -.
DR   OrthoDB; 9811998at2; -.
DR   Proteomes; UP000198734; 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:SF25; SCO1 PROTEIN HOMOLOG; 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:UP000198734};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..196
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011653548"
FT   DOMAIN          26..193
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         64
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         68
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         156
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        64..68
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   196 AA;  22026 MW;  CC973945310B2238 CRC64;
     MKKLFILLCI SAIVLVGCGS SGNFEAQTNW EVSEFDYDNQ RGETVSLEDL KGTVWLSTFI
     FTDCETVCPP MTYNMSDIQA MLSEKGIEDY KIVAFSVDPE VDTPEKLQEY IANYDVIDES
     KWELLTGYTQ EHISGFAADS FKTLVRDDPN TNQVIHGTSF YLVDQNGIVV KNYSGNTDVP
     KEEIVIDVET LIEDGK
//
DBGET integrated database retrieval system