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Database: UniProt
Entry: A0A1Q5KR19_9ACTN
LinkDB: A0A1Q5KR19_9ACTN
Original site: A0A1Q5KR19_9ACTN 
ID   A0A1Q5KR19_9ACTN        Unreviewed;       230 AA.
AC   A0A1Q5KR19;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Dihydrofolate reductase {ECO:0000313|EMBL:OKJ83985.1};
GN   ORFNames=AMK31_17845 {ECO:0000313|EMBL:OKJ83985.1};
OS   Streptomyces sp. TSRI0107.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703942 {ECO:0000313|EMBL:OKJ83985.1, ECO:0000313|Proteomes:UP000185813};
RN   [1] {ECO:0000313|EMBL:OKJ83985.1, ECO:0000313|Proteomes:UP000185813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSRI0107 {ECO:0000313|EMBL:OKJ83985.1,
RC   ECO:0000313|Proteomes:UP000185813};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKJ83985.1}.
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DR   EMBL; LIVZ01000006; OKJ83985.1; -; Genomic_DNA.
DR   RefSeq; WP_073941568.1; NZ_LIVZ01000006.1.
DR   AlphaFoldDB; A0A1Q5KR19; -.
DR   STRING; 1703942.AMK31_17845; -.
DR   OrthoDB; 3208141at2; -.
DR   Proteomes; UP000185813; 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: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; 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   Reference proteome {ECO:0000313|Proteomes:UP000185813};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          1..65
FT                   /note="HTH dtxR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50944"
SQ   SEQUENCE   230 AA;  25231 MW;  78FD27155349908B CRC64;
     MSGLIDTTEM YLRTILELEE EGVVPMRARI AERLDQSGPT VSQTVARMER DGLVSVASDR
     HLELTDEGRR LATRVMRKHR LAECLLVDVI GLEWEQVHAE ACRWEHVMSE AVERRVLELL
     RHPTESPYGN PIPGLEELGE KDGADPFLDE GMVSLAELDP GLEGKTVVVR RIGEPIQTDA
     QLMYTLRRAG VQPGSVVSVT ESAGGVLVGS GGEAAELEAD VASHVFVAKR
//
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