ID   NODD1_RHITR             Reviewed;         308 AA.
AC   Q02876;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Nodulation protein D 1;
GN   Name=nodD1;
OS   Rhizobium tropici.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8419293; DOI=10.1128/jb.175.2.438-447.1993;
RA   van Rhijn P.J., Feys B., Vanderleyden J.;
RT   "Multiple copies of nodD in Rhizobium tropici CIAT899 and BR816.";
RL   J. Bacteriol. 175:438-447(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7934929; DOI=10.1111/j.1365-2958.1993.tb01245.x;
RA   Sousa C., Folch J.L., Boloix P., Megias M., Nava N., Quinto C.;
RT   "A Rhizobium tropici DNA region carrying the amino-terminal half of a nodD
RT   gene and a nod-box-like sequence confers host-range extension.";
RL   Mol. Microbiol. 9:1157-1168(1993).
CC   -!- FUNCTION: NodD regulates the expression of the nodABCFE genes which
CC       encode other nodulation proteins. NodD is also a negative regulator of
CC       its own expression. Binds flavonoids as inducers.
CC   -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC       {ECO:0000305}.
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DR   EMBL; L01273; AAA26335.1; -; Genomic_DNA.
DR   EMBL; L04660; AAA65533.1; -; Genomic_DNA.
DR   PIR; A40642; A40642.
DR   AlphaFoldDB; Q02876; -.
DR   SMR; Q02876; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   CDD; cd08462; PBP2_NodD; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR005119; LysR_subst-bd.
DR   InterPro; IPR037416; NodD_PBP2.
DR   InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00126; HTH_1; 1.
DR   Pfam; PF03466; LysR_substrate; 1.
DR   PRINTS; PR00039; HTHLYSR.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50931; HTH_LYSR; 1.
PE   3: Inferred from homology;
KW   Activator; DNA-binding; Nodulation; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..308
FT                   /note="Nodulation protein D 1"
FT                   /id="PRO_0000105723"
FT   DOMAIN          6..63
FT                   /note="HTH lysR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT   DNA_BIND        23..42
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
SQ   SEQUENCE   308 AA;  35080 MW;  993227A837403C8B CRC64;
     MRFKGLDLNL LVALDALMTE RNLTAAARSI NLSQPAMSAA VGRLRVYFED ELFTMNGREL
     VLTPRAKGLV SAVREALLHI QLSIISWEPF DPFQSDRRFR IILSDFLTLV FMEKVVKRRA
     REAPGVSFEF LPLADDYDEL LRRGEVDFII LPDVFMPTGH PRAKLFEERL VCVGCGRNQE
     LSQPLTFDRY MSMGHVAAKF GNSRRPSIEE WYLLEHGFKR RIEVVVQGFS MILPVLSNTN
     RIATVPLRLA QHFAEVLPLR IMDLPLPLPP FTEAVQWPAL QNSDPASLWM RGILLQEASR
     LALPSAEH