ID   B5JFT0_9BACT            Unreviewed;       244 AA.
AC   B5JFT0;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=SCO1/SenC superfamily {ECO:0000313|EMBL:EDY84048.1};
GN   ORFNames=VDG1235_3675 {ECO:0000313|EMBL:EDY84048.1};
OS   Verrucomicrobiae bacterium DG1235.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae.
OX   NCBI_TaxID=382464 {ECO:0000313|EMBL:EDY84048.1, ECO:0000313|Proteomes:UP000003839};
RN   [1] {ECO:0000313|EMBL:EDY84048.1, ECO:0000313|Proteomes:UP000003839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG1235 {ECO:0000313|EMBL:EDY84048.1,
RC   ECO:0000313|Proteomes:UP000003839};
RA   Hart M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) 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; DS990592; EDY84048.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5JFT0; -.
DR   STRING; 382464.VDG1235_3675; -.
DR   eggNOG; COG1999; Bacteria.
DR   eggNOG; COG5569; Bacteria.
DR   HOGENOM; CLU_066625_0_0_0; -.
DR   Proteomes; UP000003839; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02968; SCO; 1.
DR   Gene3D; 2.40.50.320; Copper binding periplasmic protein CusF; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR021647; CusF_Ec.
DR   InterPro; IPR042230; CusF_sf.
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; PF11604; CusF_Ec; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003839}.
FT   DOMAIN          83..244
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         121
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         127
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         210
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        121..127
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   244 AA;  27371 MW;  90D46CA968563303 CRC64;
     MTVAHEEIPD FMPPMTMVFR VGPGDVKVIK AGDQIRARMV RDEDGGFRLI KIWKIDDQAA
     MEMRKVNKQL AAKLEELGSG YYVGEGEAFP EFALLDQYGD TITPARYEGK PFMLNFIFTR
     CTDGEMCPLS TSKMASLQKM AAERGLDDLE FISVTLDPKY DTPGVLRTYA DAYGIDGENF
     RFVTGERAAV RQLIKTMALT HIETDDDIIH SLATVLVGRD RKIVMRSVKK AWDPNAFLEA
     AAEL
//