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Database: UniProt
Entry: A0A1I3PDW5_9FLAO
LinkDB: A0A1I3PDW5_9FLAO
Original site: A0A1I3PDW5_9FLAO 
ID   A0A1I3PDW5_9FLAO        Unreviewed;       221 AA.
AC   A0A1I3PDW5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Protein SCO1/2 {ECO:0000313|EMBL:SFJ19725.1};
GN   ORFNames=SAMN05443431_10573 {ECO:0000313|EMBL:SFJ19725.1};
OS   Olleya namhaensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1144750 {ECO:0000313|EMBL:SFJ19725.1, ECO:0000313|Proteomes:UP000199559};
RN   [1] {ECO:0000313|Proteomes:UP000199559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28881 {ECO:0000313|Proteomes:UP000199559};
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; FORM01000005; SFJ19725.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3PDW5; -.
DR   STRING; 1144750.SAMN05443431_10573; -.
DR   Proteomes; UP000199559; 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:UP000199559}.
FT   DOMAIN          53..218
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         91
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         95
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         181
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        91..95
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   221 AA;  25162 MW;  4E710DFDEED8DB33 CRC64;
     MKKYNLIIIA LITLIVLSCK EQVEEKSSRV DGLPYYSDAS FTPHWLDSKS EALSTFHKIP
     KFNLTDQDGQ EVTEKTFDNK IYVTDFFFTS CPGICPKMTE NMSVLQDAFK DDAEVLLLSH
     SVTPVKDSVS TLKHYAEGKG VISNKWHLVT GDRKQIYDLG RQAYFVEEDL GGEKTDDDFL
     HTENFVLIDK DKHIRGIYNG LNKTAVQQLI ADIKTLEIED K
//
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