ID S3V082_9LEPT Unreviewed; 201 AA.
AC S3V082;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=SCO1/SenC {ECO:0000313|EMBL:EPG76061.1};
GN ORFNames=LEP1GSC058_0811 {ECO:0000313|EMBL:EPG76061.1};
OS Leptospira fainei serovar Hurstbridge str. BUT 6.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193011 {ECO:0000313|EMBL:EPG76061.1, ECO:0000313|Proteomes:UP000014540};
RN [1] {ECO:0000313|EMBL:EPG76061.1, ECO:0000313|Proteomes:UP000014540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BUT 6 {ECO:0000313|EMBL:EPG76061.1,
RC ECO:0000313|Proteomes:UP000014540};
RA Harkins D.M., Durkin A.S., Selengut J.D., Sanka R., DePew J., Purushe J.,
RA Ahmed A., van der Linden H., Goris M.G.A., Hartskeerl R.A., Vinetz J.M.,
RA Sutton G.G., Nelson W.C., Fouts D.E.;
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:EPG76061.1}.
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DR EMBL; AKWZ02000002; EPG76061.1; -; Genomic_DNA.
DR RefSeq; WP_016548169.1; NZ_AKWZ02000002.1.
DR AlphaFoldDB; S3V082; -.
DR STRING; 1193011.LEP1GSC058_0811; -.
DR OrthoDB; 9811998at2; -.
DR Proteomes; UP000014540; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR603782-1}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..199
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 73
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 77
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 164
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 73..77
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 201 AA; 21886 MW; 8A8C028F97D85F4A CRC64;
MNLKKIIIGF IVLFTGVMVG LAPRFFKRKP AFASDSPIAE WKTISLKNTE GKETVLSGLK
GDIFVVYFGF SHCPDMCPLA IEEIGAALKG LRGFSDRVTP VFISVDPERD SPEILKKYVS
TFPGNSLVAL TGSKKDIDSL QSGFGVVSRK VILPSKAEGY GVDHTLLIYL IDKNGNILAA
FPTGTNPEDL TKAITVWMDK V
//
