ID W0F0E0_9BACT Unreviewed; 208 AA.
AC W0F0E0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Electron transporter {ECO:0000313|EMBL:AHF16520.1};
GN ORFNames=NIASO_17780 {ECO:0000313|EMBL:AHF16520.1};
OS Niabella soli DSM 19437.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niabella.
OX NCBI_TaxID=929713 {ECO:0000313|EMBL:AHF16520.1, ECO:0000313|Proteomes:UP000003586};
RN [1] {ECO:0000313|EMBL:AHF16520.1, ECO:0000313|Proteomes:UP000003586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19437 {ECO:0000313|Proteomes:UP000003586};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) 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; CP007035; AHF16520.1; -; Genomic_DNA.
DR AlphaFoldDB; W0F0E0; -.
DR STRING; 929713.NIASO_17780; -.
DR KEGG; nso:NIASO_17780; -.
DR eggNOG; COG1999; Bacteria.
DR HOGENOM; CLU_050131_2_1_10; -.
DR Proteomes; UP000003586; Chromosome.
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; 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:UP000003586}.
FT DOMAIN 37..203
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 75
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 79
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 166
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 75..79
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 208 AA; 23783 MW; B65A123BCAC52845 CRC64;
MKMSKKAIFY TLFFVALSIA FYAAAVHFIP GFNSRKLEPV SKVGRFSFTD QDGQPFSNKD
VAGKVYVAEY FFTTCPGICP IMNTNMKQVY EKYKGVPGFL ILSHTCDPEK DSAARLKHYA
DSMKVDTRQW VFLTGRKDSL YKMARLSYTI DDPANNLNSD QDDFLHTQFW ALVDRKGNVL
KIYDGLKQKE INQLIADIAN ELKEPDDK
//
