ID D3SLC5_THEAH Unreviewed; 194 AA.
AC D3SLC5;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Electron transport protein SCO1/SenC {ECO:0000313|EMBL:ADC89555.1};
GN OrderedLocusNames=Thal_0923 {ECO:0000313|EMBL:ADC89555.1};
OS Thermocrinis albus (strain DSM 14484 / JCM 11386 / HI 11/12).
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Thermocrinis.
OX NCBI_TaxID=638303 {ECO:0000313|EMBL:ADC89555.1, ECO:0000313|Proteomes:UP000002043};
RN [1] {ECO:0000313|Proteomes:UP000002043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14484 / JCM 11386 / HI 11/12
RC {ECO:0000313|Proteomes:UP000002043};
RX DOI=10.4056/sigs.761490;
RA Wirth R., Sikorski J., Brambilla E., Misra M., Lapidus A., Copeland A.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Tapia R., Bruce D., Goodwin L., Pitluck S., Pati A., Anderson I.,
RA Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K.,
RA Bilek Y., Hader T., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Tindall B.J., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Thermocrinis albus type strain (HI 11/12T).";
RL Stand. Genomic Sci. 2:194-202(2010).
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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DR EMBL; CP001931; ADC89555.1; -; Genomic_DNA.
DR RefSeq; WP_012991961.1; NC_013894.1.
DR AlphaFoldDB; D3SLC5; -.
DR STRING; 638303.Thal_0923; -.
DR KEGG; tal:Thal_0923; -.
DR eggNOG; COG1999; Bacteria.
DR HOGENOM; CLU_050131_3_2_0; -.
DR OrthoDB; 9811998at2; -.
DR Proteomes; UP000002043; 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; PS51257; PROKAR_LIPOPROTEIN; 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:UP000002043}.
FT DOMAIN 27..193
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 67
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 71
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 157
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 67..71
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 194 AA; 22232 MW; 5307D44F0778BBA8 CRC64;
MRSLLAVWIV LALLVSSCKK EHKFYGYLYD KPAYDFELTS QDGNRVRLSQ FLKDGGVVLL
FFGYTHCPDV CPTALSTMAK VMKNLSEKER EKVKVLFVSV DPERDTPAVL KNYVPFFYPT
FVGLTGTPDE IAKVAKEYNV YYRKVKEETA AGYLVDHTAT IYLITPDMKI KLLYTTNRQD
PQKIAEDIRY LLSS
//
