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Database: UniProt
Entry: A0A1M5ELP4_9BACT
LinkDB: A0A1M5ELP4_9BACT
Original site: A0A1M5ELP4_9BACT 
ID   A0A1M5ELP4_9BACT        Unreviewed;       221 AA.
AC   A0A1M5ELP4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Protein SCO1/2 {ECO:0000313|EMBL:SHF80064.1};
GN   ORFNames=SAMN05443144_11396 {ECO:0000313|EMBL:SHF80064.1};
OS   Fodinibius roseus.
OC   Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Fodinibius.
OX   NCBI_TaxID=1194090 {ECO:0000313|EMBL:SHF80064.1, ECO:0000313|Proteomes:UP000184041};
RN   [1] {ECO:0000313|EMBL:SHF80064.1, ECO:0000313|Proteomes:UP000184041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21986 {ECO:0000313|EMBL:SHF80064.1,
RC   ECO:0000313|Proteomes:UP000184041};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQUS01000013; SHF80064.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M5ELP4; -.
DR   STRING; 1194090.SAMN05443144_11396; -.
DR   OrthoDB; 1523860at2; -.
DR   Proteomes; UP000184041; 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   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.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..221
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012070175"
FT   BINDING         97
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         101
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         185
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        97..101
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   221 AA;  24449 MW;  B2FAA9C9FE9CBA5F CRC64;
     MTIYSYQNTV FLFLVTAVFL AGACSSGEKQ QAAQSDGMAM SDDEHAAHAD MQMDAGEPTG
     ESIYNVSSTW QNRRGESVTL NSLGGKVQVV AMVYTHCEHA CPRILADMQR IRDGLPEKAL
     SATNFTIISI DPERDTPGRL TDFARENNLS DDQWTLLNGD EGDILEIAAL LGVKYKRISD
     TDFTHSNMIT VLNKEGEVAY QRRQLTDQQD KIIDVIHDLG S
//
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