ID K2C2P7_9BACT Unreviewed; 189 AA.
AC K2C2P7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Electron transport protein SCO1/SenC {ECO:0000313|EMBL:EKD75438.1};
GN ORFNames=ACD_44C00127G0002 {ECO:0000313|EMBL:EKD75438.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD75438.1};
RN [1] {ECO:0000313|EMBL:EKD75438.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKD75438.1}.
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DR EMBL; AMFJ01018310; EKD75438.1; -; Genomic_DNA.
DR AlphaFoldDB; K2C2P7; -.
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}.
FT DOMAIN 26..189
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 152
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 189 AA; 21517 MW; D4171C01261D06AE CRC64;
MKILSFLFSF IFLVPAFAVE DNVVLLSPPK ALPSFELKDV KNEKFDQHQL QAHWSLLFFG
FTRCQVICPN TMTILKNAYE IMEKNKKTIP QIIFISVDSA HDTPQTTDRY AKSFNAHFMG
LAGGEKQIQL LTKSLGVLYM KVKQNEEETI DHSINLFLVN PQGQVAAIFS APYESSMLAR
EIEKIIKTQ
//