ID M0LQV4_9EURY Unreviewed; 222 AA.
AC M0LQV4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Electron transporter SCO1/SenC {ECO:0000313|EMBL:EMA35468.1};
GN ORFNames=C446_12272 {ECO:0000313|EMBL:EMA35468.1};
OS Halobiforma nitratireducens JCM 10879.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halobiforma.
OX NCBI_TaxID=1227454 {ECO:0000313|EMBL:EMA35468.1, ECO:0000313|Proteomes:UP000011607};
RN [1] {ECO:0000313|EMBL:EMA35468.1, ECO:0000313|Proteomes:UP000011607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10879 {ECO:0000313|EMBL:EMA35468.1,
RC ECO:0000313|Proteomes:UP000011607};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:EMA35468.1}.
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DR EMBL; AOMA01000122; EMA35468.1; -; Genomic_DNA.
DR RefSeq; WP_006673363.1; NZ_AOMA01000122.1.
DR AlphaFoldDB; M0LQV4; -.
DR STRING; 1227454.C446_12272; -.
DR PATRIC; fig|1227454.3.peg.2506; -.
DR eggNOG; arCOG00313; Archaea.
DR OrthoDB; 27579at2157; -.
DR Proteomes; UP000011607; Unassembled WGS sequence.
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 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:UP000011607}.
FT DOMAIN 49..222
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 87
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 91
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 183
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 87..91
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 222 AA; 24166 MW; 8D7BC74D6EAF711F CRC64;
MHRRHALTLG ATAGLTTVAG CLTGMLDDSA DNAVLEPPEA GVPSGVSYPT YGDPFPTFEL
EDPLAETTVD VDALEDALVA TAFFASCPAE CIPLMDSIAQ VQRNAGERGL ADGTRFLAVT
FDPERDTADA LRDHADMLDI DYEADNWHYL RPDGPEAATA VVDDELGVPF EREELGDDYE
FIHIAVTFLV NPDGYVERAY RGEDPDSNRI TDDLERLLDG LE
//