ID A0A0M4QU43_9PSEU Unreviewed; 238 AA.
AC A0A0M4QU43;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Dihydrofolate reductase {ECO:0000313|EMBL:ALE83206.1};
GN ORFNames=XF36_08580 {ECO:0000313|EMBL:ALE83206.1};
OS Pseudonocardia sp. HH130629-09.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1641402 {ECO:0000313|EMBL:ALE83206.1, ECO:0000313|Proteomes:UP000062082};
RN [1] {ECO:0000313|EMBL:ALE83206.1, ECO:0000313|Proteomes:UP000062082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH130629-09 {ECO:0000313|EMBL:ALE83206.1,
RC ECO:0000313|Proteomes:UP000062082};
RX PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT "Variable genetic architectures produce virtually identical molecules in
RT bacterial symbionts of fungus-growing ants.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
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}.
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DR EMBL; CP011868; ALE83206.1; -; Genomic_DNA.
DR RefSeq; WP_060711576.1; NZ_CP011868.1.
DR AlphaFoldDB; A0A0M4QU43; -.
DR KEGG; pseh:XF36_08580; -.
DR PATRIC; fig|1641402.3.peg.1835; -.
DR OrthoDB; 3208141at2; -.
DR Proteomes; UP000062082; Chromosome.
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; IPR012318; HTH_CRP.
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:SF10; IRON-DEPENDENT REPRESSOR IDER; 1.
DR Pfam; PF02742; Fe_dep_repr_C; 1.
DR Pfam; PF01325; Fe_dep_repress; 1.
DR Pfam; PF04023; FeoA; 1.
DR SMART; SM00419; HTH_CRP; 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 Reference proteome {ECO:0000313|Proteomes:UP000062082};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 4..65
FT /note="HTH dtxR-type"
FT /evidence="ECO:0000259|PROSITE:PS50944"
FT REGION 128..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 238 AA; 26187 MW; EF9C7F7E32093AC1 CRC64;
MNDLIDTTEM YLRTIYELEE EGVVPLRARI AERLGQSGPT VSQTVARMER DGLVVVAGDR
HLELTDEGRG RAVAVMRKHR LAERLLIDVI GLEWELVHAE ACRWEHVMSE DVERKLLHLL
DKPTVSPYGN PIPGLEELER GDDTSAPSSV PPTLEVGLQR LDELARRGGG RVEIRRIAEH
VQLDSDLMGE LKLAGIVPGN AVEVGPISRF GDPVPVSSDD EKSTVAPPVA HAVLVRAI
//
