ID D2NRV5_ROTMD Unreviewed; 272 AA.
AC D2NRV5;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Transcriptional regulator {ECO:0000313|EMBL:BAI64381.1};
GN OrderedLocusNames=RMDY18_05490 {ECO:0000313|EMBL:BAI64381.1};
OS Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=680646 {ECO:0000313|EMBL:BAI64381.1, ECO:0000313|Proteomes:UP000001883};
RN [1] {ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA Fukushima H.;
RT "Complete genome sequence of Rothia mucilaginosa DJ.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAI64381.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI64381.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Yoshida M., Fujihira T., Baba T., Tsuji N., Hayashi H.,
RA Sugimori C., Yamanaka T., Mashimo C., Nambu T., Kawai H., Fukushima H.;
RT "Isolation and identification of Rothia mucilaginosa from persistent apical
RT periodontitis lesions.";
RL J Osaka Dent Univ 44:93-98(2010).
RN [3] {ECO:0000313|EMBL:BAI64381.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI64381.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Yamanaka T., Mashimo C., Sugimori C., Leung K.-P.,
RA Fukushima H.;
RT "Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical Isolate
RT with Dense Meshwork-Like Structures from a Persistent Apical Periodontitis
RT Lesion.";
RL Sequencing 2010:457236-457236(2010).
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DR EMBL; AP011540; BAI64381.1; -; Genomic_DNA.
DR AlphaFoldDB; D2NRV5; -.
DR STRING; 680646.RMDY18_05490; -.
DR KEGG; rmu:RMDY18_05490; -.
DR eggNOG; COG1737; Bacteria.
DR HOGENOM; CLU_055769_4_3_11; -.
DR Proteomes; UP000001883; Chromosome.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
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:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR CDD; cd05013; SIS_RpiR; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR000281; HTH_RpiR.
DR InterPro; IPR047640; RpiR-like.
DR InterPro; IPR035472; RpiR-like_SIS.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR30514; GLUCOKINASE; 1.
DR PANTHER; PTHR30514:SF19; HTH-TYPE TRANSCRIPTIONAL REGULATOR GLVR; 1.
DR Pfam; PF01418; HTH_6; 1.
DR Pfam; PF01380; SIS; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51071; HTH_RPIR; 1.
DR PROSITE; PS51464; SIS; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001883}.
FT DOMAIN 1..77
FT /note="HTH rpiR-type"
FT /evidence="ECO:0000259|PROSITE:PS51071"
FT DOMAIN 107..250
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT REGION 251..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 272 AA; 31465 MW; 134BE25C5D95E5AF CRC64;
MDLQDVVNAN QHRFSETERE ILAFMLENEE FVAESTINSL AHKTYTSTSS IIRLTKKLNF
SGFAELKYFI KSSLNRSEPF NPRFIESGRE DIQRTYDYLE HMELSGLLKR IHEARTVYCF
GTGYAQRNAV QEFTKSMQVC GKFCQVIPAR NEFESAMNNM TQDDVVIIVS FSGQTENMRE
HIKMLALRRI PMIAVTAIGV NYMSSHAEYS LHYQTTPTQI STQRKPYYSF VALSVLLDYI
VRRYIEHVEN ERRESLQDQV DDALNAGDET DA
//