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Database: UniProt
Entry: M0LQV4_9EURY
LinkDB: M0LQV4_9EURY
Original site: M0LQV4_9EURY 
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
//
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