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LOCUS WP_009931217 334 aa linear BCT 21-JAN-2025 ACCESSION WP_009931217 VERSION WP_009931217.1 KEYWORDS RefSeq. SOURCE Listeria monocytogenes ORGANISM Listeria monocytogenes Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. REFERENCE 1 (residues 1 to 334) AUTHORS Conejo,M.S., Thompson,S.M. and Miller,B.G. TITLE Evolutionary bases of carbohydrate recognition and substrate discrimination in the ROK protein family JOURNAL J Mol Evol 70 (6), 545-556 (2010) PUBMED 20512568 REFERENCE 2 (residues 1 to 334) AUTHORS Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G. TITLE Divergent evolution of function in the ROK sugar kinase superfamily: role of enzyme loops in substrate specificity JOURNAL Biochemistry 46 (47), 13564-13572 (2007) PUBMED 17979299 REFERENCE 3 (residues 1 to 334) AUTHORS Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M. TITLE The many faces of the helix-turn-helix domain: transcription regulation and beyond JOURNAL FEMS Microbiol Rev 29 (2), 231-262 (2005) PUBMED 15808743 REFERENCE 4 (residues 1 to 334) AUTHORS Wintjens,R. and Rooman,M. TITLE Structural classification of HTH DNA-binding domains and protein-DNA interaction modes JOURNAL J Mol Biol 262 (2), 294-313 (1996) PUBMED 8831795 REFERENCE 5 (residues 1 to 334) AUTHORS Hurley,J.H. TITLE The sugar kinase/heat shock protein 70/actin superfamily: implications of conserved structure for mechanism JOURNAL Annu Rev Biophys Biomol Struct 25, 137-162 (1996) PUBMED 8800467 REFERENCE 6 (residues 1 to 334) AUTHORS Kabsch,W. and Holmes,K.C. TITLE The actin fold JOURNAL FASEB J 9 (2), 167-174 (1995) PUBMED 7781919 REFERENCE 7 (residues 1 to 334) AUTHORS Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr. TITLE Evolutionary relationships between sugar kinases and transcriptional repressors in bacteria JOURNAL Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994) PUBMED 7952186 REFERENCE 8 (residues 1 to 334) AUTHORS Brennan,R.G. and Matthews,B.W. TITLE The helix-turn-helix DNA binding motif JOURNAL J Biol Chem 264 (4), 1903-1906 (1989) PUBMED 2644244 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 20283862 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..334 /organism="Listeria monocytogenes" /db_xref="taxon:1639" Protein 1..334 /product="ROK family transcriptional regulator" /GO_function="GO:0003677 - DNA binding [Evidence IEA]" /GO_function="GO:0003700 - DNA-binding transcription factor activity [Evidence IEA]" /GO_function="GO:0005524 - ATP binding [Evidence IEA]" /GO_process="GO:0006355 - regulation of DNA-templated transcription [Evidence IEA]" /calculated_mol_wt=37882 Region <18..75 /region_name="HTH_CRP" /note="helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic regulatory proteins belonging to the catabolite activator protein family; cl46859" /db_xref="CDD:481199" Site order(24,26..28,37) /site_type="other" /note="non-specific DNA interactions [nucleotide binding]" /db_xref="CDD:238044" Site 37..43 /site_type="DNA binding" /note="DNA binding site [nucleotide binding]" /db_xref="CDD:238044" Site order(38..39,43) /site_type="other" /note="sequence specific DNA binding site [nucleotide binding]" /db_xref="CDD:238044" Site 38..39 /site_type="other" /note="putative cAMP binding site [chemical binding]" /db_xref="CDD:238044" Region <134..307 /region_name="ASKHA_ATPase_ROK" /note="ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; cd23763" /db_xref="CDD:466849" ORIGIN 1 maiprdlkel nkkniksilr qqgamtkaei aevtglsvvt vnklirdlve neeileqdns 61 vatggrravs yeinpnfqqv lvislqekwk kitysfsvyn llgepefved msgedldita 121 lkrntkdiic afpkiscvvi gvpgieiggk lramdfplll nvqlretlea evnlpvlvet 181 dtnaailgyk nrpmkeeniv glyyperfpp gagllmngei lkgqnglage ikhmplqvdw 241 dnfdfsvdei kahirkmall tmsfydpeti vlytnfyfgq kdfmeelkee lkqvypyavl 301 peivlsrkft tdyrigllaf gidylennmt dwri