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Database: UniProt
Entry: A8ZZ11_DESOH
LinkDB: A8ZZ11_DESOH
Original site: A8ZZ11_DESOH 
ID   A8ZZ11_DESOH            Unreviewed;       387 AA.
AC   A8ZZ11;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Helix-turn-helix domain protein {ECO:0000313|EMBL:ABW68784.1};
GN   OrderedLocusNames=Dole_2981 {ECO:0000313|EMBL:ABW68784.1};
OS   Desulfosudis oleivorans (strain DSM 6200 / JCM 39069 / Hxd3) (Desulfococcus
OS   oleovorans).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfosudaceae; Desulfosudis.
OX   NCBI_TaxID=96561 {ECO:0000313|EMBL:ABW68784.1, ECO:0000313|Proteomes:UP000008561};
RN   [1] {ECO:0000313|EMBL:ABW68784.1, ECO:0000313|Proteomes:UP000008561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6200 / JCM 39069 / Hxd3
RC   {ECO:0000313|Proteomes:UP000008561};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA   Richardson P.;
RT   "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the short-chain fatty acyl-CoA assimilation
CC       regulator (ScfR) family. {ECO:0000256|ARBA:ARBA00007227}.
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DR   EMBL; CP000859; ABW68784.1; -; Genomic_DNA.
DR   RefSeq; WP_012176395.1; NC_009943.1.
DR   AlphaFoldDB; A8ZZ11; -.
DR   STRING; 96561.Dole_2981; -.
DR   KEGG; dol:Dole_2981; -.
DR   eggNOG; COG1813; Bacteria.
DR   eggNOG; COG2856; Bacteria.
DR   HOGENOM; CLU_713157_0_0_7; -.
DR   OrthoDB; 9794834at2; -.
DR   Proteomes; UP000008561; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   CDD; cd00093; HTH_XRE; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR010359; IrrE_HExxH.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   PANTHER; PTHR43236; ANTITOXIN HIGA1; 1.
DR   PANTHER; PTHR43236:SF1; BLL7220 PROTEIN; 1.
DR   Pfam; PF01381; HTH_3; 1.
DR   Pfam; PF06114; Peptidase_M78; 1.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR   PROSITE; PS50943; HTH_CROC1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008561}.
FT   DOMAIN          15..69
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50943"
FT   REGION          231..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..253
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   387 AA;  44154 MW;  99866E5826E7A31F CRC64;
     MIQKTTDLTF IGRNIRKLRR QRGWTISRLA GEIGMAEIPL GRIERGGNAP SAAVIFQLSR
     ALGVSVDTLF AEDESDLLAE RVKTPGTGFV PARSVEHLPP SILTPIYEVI DAICSLEDIC
     RAHKRAKIPL NISFETNQRG LQDLSEAARN HMGIGRGVVF DYIELFEAMG FRVIFLPLPK
     ETPSMTFYDM ENSNAFFFIR HKQNPERQIF HLAYGLGRIF FLRQARHTGA NPFPSDDDAR
     TEEMPPAEKE GKKTLTMHRA GRKFAAFFLM PEQAIRATVN QLGIQNKQWS WELLLRIKHR
     FGVSAQAFLF RLKELDLITG KLHDRFSKQI EDHYKKTGYA EPDSSRRILT PNGRVWDLVL
     TARQHAEAKA EVARIEETLN QWKVVKV
//
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