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Database: UniProt
Entry: M0AZ61_9EURY
LinkDB: M0AZ61_9EURY
Original site: M0AZ61_9EURY 
ID   M0AZ61_9EURY            Unreviewed;       226 AA.
AC   M0AZ61;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=DtxR family iron (Metal) dependent repressor {ECO:0000313|EMBL:ELZ03263.1};
GN   ORFNames=C480_16060 {ECO:0000313|EMBL:ELZ03263.1};
OS   Natrialba aegyptia DSM 13077.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrialba.
OX   NCBI_TaxID=1227491 {ECO:0000313|EMBL:ELZ03263.1, ECO:0000313|Proteomes:UP000011591};
RN   [1] {ECO:0000313|EMBL:ELZ03263.1, ECO:0000313|Proteomes:UP000011591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13077 {ECO:0000313|EMBL:ELZ03263.1,
RC   ECO:0000313|Proteomes:UP000011591};
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the DtxR/MntR family.
CC       {ECO:0000256|ARBA:ARBA00007871}.
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:ELZ03263.1}.
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DR   EMBL; AOIP01000033; ELZ03263.1; -; Genomic_DNA.
DR   RefSeq; WP_006666622.1; NZ_AOIP01000033.1.
DR   AlphaFoldDB; M0AZ61; -.
DR   PATRIC; fig|1227491.4.peg.3299; -.
DR   OrthoDB; 24735at2157; -.
DR   Proteomes; UP000011591; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR   Gene3D; 2.30.30.90; -; 1.
DR   Gene3D; 1.10.60.10; Iron dependent repressor, metal binding and dimerisation domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR007167; Fe-transptr_FeoA.
DR   InterPro; IPR001367; Fe_dep_repressor.
DR   InterPro; IPR036421; Fe_dep_repressor_sf.
DR   InterPro; IPR038157; FeoA_core_dom.
DR   InterPro; IPR022687; HTH_DTXR.
DR   InterPro; IPR022689; Iron_dep_repressor.
DR   InterPro; IPR008988; Transcriptional_repressor_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR33238; IRON (METAL) DEPENDENT REPRESSOR, DTXR FAMILY; 1.
DR   PANTHER; PTHR33238:SF7; TRANSCRIPTIONAL REGULATOR MNTR; 1.
DR   Pfam; PF02742; Fe_dep_repr_C; 1.
DR   Pfam; PF01325; Fe_dep_repress; 1.
DR   Pfam; PF04023; FeoA; 1.
DR   SMART; SM00899; FeoA; 1.
DR   SMART; SM00529; HTH_DTXR; 1.
DR   SUPFAM; SSF50037; C-terminal domain of transcriptional repressors; 1.
DR   SUPFAM; SSF47979; Iron-dependent repressor protein, dimerization domain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50944; HTH_DTXR; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          3..65
FT                   /note="HTH dtxR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50944"
FT   REGION          122..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   226 AA;  25024 MW;  E1A3590F1D9ACE4D CRC64;
     MMLSDVMEDY LKAIYQLQGE HEERIKTSAI ADALEVTSPT VTSMLEKLEE RGLVDREKYR
     GVTLTDEGET VALEVVRHHR LLEAYLTEHL DYDWSEVHAE ADRLEHHISE DFEARVADAL
     DEPEVDPHGS PIPSADLEPP DRSAGKSVTE FAEGDVVVVE EVADHDPEVL SYLATHGVEP
     GVELEILEVA PFGMVTARSS ETVDDVSLPE GVAHHVRVTP LPQAES
//
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