Resource Adenosyl-Ornithine

Predicate	Value (sorted: default)
rdfs:label	"Adenosyl-Ornithine"
rdf:type	ns1:drugs
ns1:description	" experimental This compound belongs to the purine nucleosides and analogues. These are compounds comprising a purine base attached to a sugar. Purine Nucleosides and Analogues Organic Compounds Organooxygen Compounds Carbohydrates and Carbohydrate Conjugates Glycosyl Compounds Glycoamino Acids and Derivatives Pentoses Alpha Amino Acids and Derivatives Purines and Purine Derivatives Amino Fatty Acids Aminopyrimidines and Derivatives Heterocyclic Fatty Acids Sugar Acids and Derivatives Primary Aromatic Amines N-substituted Imidazoles Tetrahydrofurans Oxolanes Secondary Alcohols 1,2-Diols Carboxylic Acids Enolates Polyamines Ethers Monoalkylamines alpha-amino acid or derivative pentose monosaccharide imidazopyrimidine purine sugar acid aminopyrimidine pyrimidine primary aromatic amine monosaccharide n-substituted imidazole oxolane azole tetrahydrofuran imidazole secondary alcohol 1,2-diol polyamine carboxylic acid carboxylic acid derivative ether enolate alcohol organonitrogen compound amine primary amine primary aliphatic amine Antifungal Agents logP -3 ALOGPS logS -1.9 ALOGPS Water Solubility 4.63e+00 g/l ALOGPS logP -5.1 ChemAxon IUPAC Name (2R,5R)-2,5-diamino-6-[(2S,3R,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]hexanoic acid ChemAxon Traditional IUPAC Name adenosyl-ornithine ChemAxon Molecular Weight 381.387 ChemAxon Monoisotopic Weight 381.176066881 ChemAxon SMILES N[C@H](CC[C@@H](N)C(O)=O)C[C@@H]1O[C@H]([C@H](O)[C@H]1O)N1C=NC2=C1N=CN=C2N ChemAxon Molecular Formula C15H23N7O5 ChemAxon InChI InChI=1S/C15H23N7O5/c16-6(1-2-7(17)15(25)26)3-8-10(23)11(24)14(27-8)22-5-21-9-12(18)19-4-20-13(9)22/h4-8,10-11,14,23-24H,1-3,16-17H2,(H,25,26)(H2,18,19,20)/t6-,7-,8+,10+,11-,14-/m1/s1 ChemAxon InChIKey InChIKey=LMXOHSDXUQEUSF-CMDGEXLLSA-N ChemAxon Polar Surface Area (PSA) 208.65 ChemAxon Refractivity 92.68 ChemAxon Polarizability 37.63 ChemAxon Rotatable Bond Count 7 ChemAxon H Bond Acceptor Count 11 ChemAxon H Bond Donor Count 6 ChemAxon pKa (strongest acidic) 1.95 ChemAxon pKa (strongest basic) 10.18 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 0 ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 46936257 PubChem Substance 46508037 ChemSpider 3280577 PDB SFG BE0002526 RdmB Streptomyces purpurascens unknown RdmB Involved in O-methyltransferase activity rdmB None 4.48 39797.0 Streptomyces purpurascens GenBank Gene Database U10405 UniProtKB Q54527 UniProt Accession Q54527_9ACTO >RdmB MSSSSPGEPLEPTDQDLDVLLKNLGNLVTPMALRVAATLRLVDHLLAGADTLAGLADRTD THPQALSRLVRHLTVVGVLEGGEKQGRPLRPTRLGMLLADGHPAQQRAWLDLNGAVSHAD LAFTGLLDVVRTGRPAYAGRYGRPFWEDLSADVALADSFDALMSCDEDLAYEAPADAYDW SAVRHVLDVGGGNGGMLAAIALRAPHLRGTLVELAGPAERARRRFADAGLADRVTVAEGD FFKPLPVTADVVLLSFVLLNWSDEDALTILRGCVRALEPGGRLLVLDRADVEGDGADRFF STLLDLRMLTFMGGRVRTRDEVVDLAGSAGLALASERTSGSTTLPFDFSILEFTAVSEEA APAAQASEALPAQE >1125 bp GTGAGCTCTTCCTCACCCGGGGAACCCCTGGAACCGACCGACCAGGACCTCGACGTACTC CTGAAGAACCTCGGCAATCTGGTGACCCCGATGGCCCTGAGGGTCGCCGCGACACTCCGC CTGGTCGATCACCTGCTGGCCGGAGCCGACACCCTCGCCGGCCTCGCCGACCGTACGGAC ACCCATCCCCAGGCGCTCTCCCGCCTGGTCCGGCACCTGACCGTCGTCGGCGTCCTGGAG GGCGGCGAGAAGCAGGGCCGGCCGCTGCGCCCCACCCGGCTCGGGATGCTCCTCGCCGAC GGCCACCCGGCCCAGCAGCGGGCCTGGCTGGACCTGAACGGGGCCGTCTCCCACGCCGAC CTGGCCTTCACCGGGCTCCTCGACGTGGTCCGCACCGGCCGCCCCGCCTACGCCGGGCGG TACGGGCGGCCCTTCTGGGAGGACCTCTCGGCGGACGTGGCGCTGGCCGACTCCTTCGAC GCGCTCATGTCCTGCGACGAGGACCTGGCCTACGAGGCCCCGGCCGACGCGTACGACTGG TCGGCGGTCCGGCACGTCCTCGACGTGGGCGGCGGCAACGGCGGCATGCTCGCGGCGATC GCCCTGCGGGCCCCGCACCTGCGCGGCACCCTGGTCGAACTGGCCGGTCCCGCCGAGCGC GCCCGGCGCAGGTTCGCGGACGCCGGTCTGGCCGACCGGGTCACGGTGGCGGAGGGCGAC TTCTTCAAGCCGCTGCCCGTCACCGCCGACGTCGTCCTGCTGTCGTTCGTCCTGCTCAAC TGGTCCGACGAGGACGCGCTGACGATCCTGCGCGGCTGCGTCAGGGCGCTGGAGCCGGGA GGCAGGCTCCTGGTCCTCGACCGTGCCGATGTCGAGGGGGACGGCGCCGACCGGTTCTTC AGCACGCTGCTCGACCTGCGGATGCTGACGTTCATGGGCGGACGGGTGCGCACCCGGGAC GAGGTCGTGGACCTGGCCGGATCGGCCGGACTCGCCCTGGCCTCGGAGCGCACGAGCGGC TCCACGACCCTCCCGTTCGACTTCTCGATCCTCGAGTTCACGGCCGTCTCCGAGGAAGCG GCCCCGGCCGCCCAGGCCTCCGAAGCCCTCCCAGCACAGGAGTAG PF00891 Methyltransf_2 function catalytic activity function transferase activity function transferase activity, transferring one-carbon groups function methyltransferase activity function O-methyltransferase activity BE0002516 rRNA adenine N-6-methyltransferase Bacillus subtilis unknown rRNA adenine N-6-methyltransferase Involved in rRNA (adenine-N6,N6-)-dimethyltransferase activity This protein produces a dimethylation of the adenine residue at position 2058 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics ermC' None 10.2 28908.0 Bacillus subtilis GenBank Gene Database M13761 UniProtKB P13956 UniProt Accession ERM_BACIU EC 2.1.1.48 Erythromycin resistance protein Macrolide- lincosamide-streptogramin B resistance protein >rRNA adenine N-6-methyltransferase MNEKNIKHSQNFITSKHNIDKIMTNIRLNEHDNIFEIGSGKGHFTLELVQRCNFVTAIEI DHKLCKTTENKLVDHDNFQVLNKDILQFKFPKNQSYKIFGNIPYNISTDIIRKIVFDSIA DEIYLIVEYGFAKRLLNTKRSLALFLMAEVDISILSMVPREYFHPKPKVNSSLIRLNRKK SRISHKDKQKYNYFVMKWVNKEYKKIFTKNQFNNSLKHAGIDDLNNISFEQFLSLFNSYK LFNK >735 bp ATGAACGAGAAAAATATAAAACACAGTCAAAACTTTATTACTTCAAAACATAATATAGAT AAAATAATGACAAATATAAGATTAAATGAACATGATAATATCTTTGAAATCGGCTCAGGA AAAGGGCATTTTACCCTTGAATTAGTACAGAGGTGTAATTTCGTAACTGCCATTGAAATA GACCATAAATTATGCAAAACTACAGAAAATAAACTTGTTGATCACGATAATTTCCAAGTT TTAAACAAGGATATATTGCAGTTTAAATTTCCTAAAAACCAATCCTATAAAATATTTGGT AATATACCTTATAACATAAGTACGGATATAATACGCAAAATTGTTTTTGATAGTATAGCT GATGAGATTTATTTAATCGTGGAATACGGGTTTGCTAAAAGATTATTAAATACAAAACGC TCATTGGCATTATTTTTAATGGCAGAAGTTGATATTTCTATATTAAGTATGGTTCCAAGA GAATATTTTCATCCTAAACCTAAAGTGAATAGCTCACTTATCAGATTAAATAGAAAAAAA TCAAGAATATCACACAAAGATAAACAGAAGTATAATTATTTCGTTATGAAATGGGTTAAC AAAGAATACAAGAAAATATTTACAAAAAATCAATTTAACAATTCCTTAAAACATGCAGGA ATTGACGATTTAAACAATATTAGCTTTGAACAATTCTTATCTCTTTTCAATAGCTATAAA TTATTTAATAAGTAA PF00398 RrnaAD function transferase activity, transferring one-carbon groups function methyltransferase activity function RNA methyltransferase activity function rRNA methyltransferase activity function rRNA (adenine) methyltransferase activity function catalytic activity function rRNA (adenine-N6,N6-)-dimethyltransferase activity function transferase activity process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process RNA metabolism process physiological process process metabolism process RNA modification process cellular metabolism process rRNA modification BE0002531 Modification methylase TaqI Thermus aquaticus unknown Modification methylase TaqI Involved in nucleic acid binding This methylase recognizes the double-stranded sequence TCGA, causes specific methylation on A-4 on both strands and protects the DNA from cleavage by the TaqI endonuclease taqIM Cytoplasmic None 9.39 47863.0 Thermus aquaticus GenBank Gene Database M76681 UniProtKB P14385 UniProt Accession MTTA_THEAQ Adenine-specific methyltransferase TaqI EC 2.1.1.72 M.TaqI >Modification methylase TaqI MGLPPLLSLPSNSAPRSLGRVETPPEVVDFMVSLAEAPRGGRVLEPACAHGPFLRAFREA HGTAYRFVGVEIDPKALDLPPWAEGILADFLLWEPGEAFDLILGNPPYGIVGEASKYPIH VFKAVKDLYKKAFSTWKGKYNLYGAFLEKAVRLLKPGGVLVFVVPATWLVLEDFALLREF LAREGKTSVYYLGEVFPQKKVSAVVIRFQKSGKGLSLWDTQESESGFTPILWAEYPHWEG EIIRFETEETRKLEISGMPLGDLFHIRFAARSPEFKKHPAVRKEPGPGLVPVLTGRNLKP GWVDYEKNHSGLWMPKERAKELRDFYATPHLVVAHTKGTRVVAAWDERAYPWREEFHLLP KEGVRLDPSSLVQWLNSEAMQKHVRTLYRDFVPHLTLRMLERLPVRREYGFHTSPESARN F >1266 bp ATGGGCCTGCCACCCCTTCTGTCCTTACCTTCCAACTCCGCCCCCAGGAGCCTGGGCCGG GTGGAGACCCCCCCGGAGGTGGTGGACTTCATGGTCTCCCTGGCCGAGGCGCCCAGGGGG GGAAGGGTGCTGGAGCCCGCCTGCGCCCATGGGCCCTTCCTCCGGGCTTTCCGGGAGGCC CACGGGACGGGCTACCGCTTCGTGGGGGTGGAGATAGACCCAAAAGCCCTGGACCTCCCC CCCTGGGCCGAGGGCATCCTGGCGGACTTCCTCCTCTGGGAGCCGGGGGAGGCCTTTGAC CTGATCCTGGGCAATCCGCCTTACGGCATCGTAGGAGAAGCCAGCAAATACCCCATTCAC GTCTTCAAAGCGGTCAAGGACCTCTACAAGAAGGCCTTTTCCACCTGGAAGGGCAAGTAC AACTTGTACGGGGCCTTTCTTGAAAAGGCCGTTCGCCTTCTTAAGCCTGGTGGGGTCCTC GTCTTTGTAGTCCCGGCCACCTGGCTTGTCCTGGAGGATTTTGCCCTCCTTCGCGAGTTC CTTGCCCGGGAAGGGAAAACATCTGTATACTACCTTGGCGAGGTTTTCCCGCAAAAAAAG GTTAGCGCTGTAGTGATTCGCTTCCAGAAGAGCGGAAAAGGCCTTTCACTTTGGGATACC CAAGAAAGCGAAAGCGGGTTCACGCCCATCCTCTGGGCTGAATATCCACATTGGGAAGGA GAGATTATCCGCTTTGAAACAGAGGAGACGCGGAAGCTGGAAATATCGGGAATGCCACTG GGAGACCTCTTTCATATCCGCTTCGCCGCAAGAAGCCCTGAATTCAAGAAACATCCAGCA GTGAGAAAGGAACCGGGGCCAGGTCTTGTGCCTGTGCTCACAGGAAGAAATTTAAAGCCG GGGTGGGTAGATTACGAGAAAAACCACTCCGGGCTTTGGATGCCCAAGGAAAGGGCCAAG GAGCTCAGGGACTTCTATGCCACGCCCCACCTGGTGGTAGCCCACACCAAGGGGACTAGA GTGGTGGCCGCTTGGGACGAAAGGGCCTACCCCTGGCGGGAGGAGTTCCACCTCCTGCCC AAGGAAGGTGTGAGACTGGACCCCTCGTCCCTGGTGCAGTGGTTAAACTCCGAAGCGATG CAGAAGCACGTCAGGACGCTTTATCGCGACTTCGTGCCCCACCTGACGCTGAGGATGCTA GAAAGGCTTCCTGTAAGGAGGGAATATGGCTTCCACACAAGCCCAGAAAGCGCTCGAAAC TTTTGA function catalytic activity function N-methyltransferase activity function transferase activity function transferase activity, transferring one-carbon groups function methyltransferase activity function nucleic acid binding function DNA binding function binding process DNA modification process DNA alkylation process metabolism process DNA methylation process cellular metabolism process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process DNA metabolism process physiological process BE0001456 Modification methylase RsrI Rhodobacter sphaeroides # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Modification methylase RsrI Replication, recombination and repair This methylase recognizes the double-stranded sequence GAATTC, causes specific methylation on A-? on both strands, and protects the DNA from cleavage by the RsrI endonuclease rsrIM Cytoplasmic None 7.06 35656.0 Rhodobacter sphaeroides GenBank Gene Database X16456 GenBank Protein Database 46455 UniProtKB P14751 UniProt Accession MTR1_RHOSH Adenine-specific methyltransferase RsrI EC 2.1.1.72 M.RsrI >Modification methylase RsrI MANRSHHNAGHRAMNALRKSGQKHSSESQLGSSEIGTTRHVYDVCDCLDTLAKLPDDSVQ LIICDPPYNIMLADWDDHMDYIGWAKRWLAEAERVLSPTGSIAIFGGLQYQGEAGSGDLI SIISHMRQNSKMLLANLIIWNYPNGMSAQRFFANRHEEIAWFAKTKKYFFDLDAVREPYD EETKAAYMKDKRLNPESVEKGRNPTNVWRMSRLNGNSLERVGHPTQKPAAVIERLVRALS HPGSTVLDFFAGSGVTARVAIQEGRNSICTDAAPVFKEYYQKQLTFLQDDGLIDKARSYE IVEGAANFGAALQRGDVAS >960 bp ATGGCAAACCGATCTCACCACAATGCGGGCCACCGAGCGATGAACGCTCTCCGCAAGTCA GGCCAAAAGCATTCGTCCGAGTCTCAGTTGGGATCTTCGGAGATCGGAACCACACGACAT GTGTATGACGTTTGCGATTGCCTCGACACCTTGGCGAAGCTGCCCGACGACTCCGTCCAG TTGATCATTTGTGATCCTCCATACAACATCATGCTGGCGGACTGGGATGATCACATGGAC TACATCGGCTGGGCGAAGCGATGGCTAGCCGAAGCCGAGCGTGTTCTATCCCCAACGGGC AGCATAGCGATTTTCGGCGGCCTACAATACCAAGGGGAGGCTGGTTCAGGTGATCTGATC TCAATCATTTCGCACATGAGACAAAACAGCAAAATGCTGCTCGCAAACCTTATCATCTGG AACTATCCGAACGGCATGAGTGCGCAGCGCTTCTTTGCAAATAGGCACGAGGAAATCGCG TGGTTCGCCAAGACCAAGAAGTATTTCTTCGATCTTGACGCTGTGCGGGAACCATATGAC GAGGAAACCAAAGCCGCTTACATGAAGGACAAGCGGTTGAACCCTGAGTCGGTTGAAAAG GGACGCAACCCAACAAACGTGTGGCGGATGTCTCGGCTTAACGGCAATTCTCTTGAACGT GTCGGCCACCCCACGCAAAAACCAGCCGCAGTGATTGAGAGACTGGTTCGCGCGTTGTCG CATCCGGGTTCAACGGTCCTCGATTTTTTTGCTGGAAGTGGGGTAACGGCGCGCGTTGCA ATTCAAGAGGGACGGAACAGCATTTGCACTGACGCCGCGCCTGTATTCAAAGAATATTAC CAGAAGCAGCTAACTTTCCTTCAAGATGATGGACTGATCGACAAAGCGCGATCATATGAA ATTGTTGAAGGGGCTGCGAACTTTGGTGCAGCATTGCAGCGGGGAGATGTTGCTTCATAA PF01555 N6_N4_Mtase function catalytic activity function N-methyltransferase activity function transferase activity function transferase activity, transferring one-carbon groups function methyltransferase activity function nucleic acid binding function DNA binding function binding process DNA modification process DNA alkylation process metabolism process DNA methylation process cellular metabolism process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process DNA metabolism process physiological process "
ns1:drugCategory	?:Antifungal Agents
owl:sameAs	?:EXPT02890

"Adenosyl-Ornithine"

" experimental This compound belongs to the purine nucleosides and analogues. These are compounds comprising a purine base attached to a sugar. Purine Nucleosides and Analogues Organic Compounds Organooxygen Compounds Carbohydrates and Carbohydrate Conjugates Glycosyl Compounds Glycoamino Acids and Derivatives Pentoses Alpha Amino Acids and Derivatives Purines and Purine Derivatives Amino Fatty Acids Aminopyrimidines and Derivatives Heterocyclic Fatty Acids Sugar Acids and Derivatives Primary Aromatic Amines N-substituted Imidazoles Tetrahydrofurans Oxolanes Secondary Alcohols 1,2-Diols Carboxylic Acids Enolates Polyamines Ethers Monoalkylamines alpha-amino acid or derivative pentose monosaccharide imidazopyrimidine purine sugar acid aminopyrimidine pyrimidine primary aromatic amine monosaccharide n-substituted imidazole oxolane azole tetrahydrofuran imidazole secondary alcohol 1,2-diol polyamine carboxylic acid carboxylic acid derivative ether enolate alcohol organonitrogen compound amine primary amine primary aliphatic amine Antifungal Agents logP -3 ALOGPS logS -1.9 ALOGPS Water Solubility 4.63e+00 g/l ALOGPS logP -5.1 ChemAxon IUPAC Name (2R,5R)-2,5-diamino-6-[(2S,3R,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]hexanoic acid ChemAxon Traditional IUPAC Name adenosyl-ornithine ChemAxon Molecular Weight 381.387 ChemAxon Monoisotopic Weight 381.176066881 ChemAxon SMILES N[C@H](CC[C@@H](N)C(O)=O)C[C@@H]1O[C@H]([C@H](O)[C@H]1O)N1C=NC2=C1N=CN=C2N ChemAxon Molecular Formula C15H23N7O5 ChemAxon InChI InChI=1S/C15H23N7O5/c16-6(1-2-7(17)15(25)26)3-8-10(23)11(24)14(27-8)22-5-21-9-12(18)19-4-20-13(9)22/h4-8,10-11,14,23-24H,1-3,16-17H2,(H,25,26)(H2,18,19,20)/t6-,7-,8+,10+,11-,14-/m1/s1 ChemAxon InChIKey InChIKey=LMXOHSDXUQEUSF-CMDGEXLLSA-N ChemAxon Polar Surface Area (PSA) 208.65 ChemAxon Refractivity 92.68 ChemAxon Polarizability 37.63 ChemAxon Rotatable Bond Count 7 ChemAxon H Bond Acceptor Count 11 ChemAxon H Bond Donor Count 6 ChemAxon pKa (strongest acidic) 1.95 ChemAxon pKa (strongest basic) 10.18 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 0 ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 46936257 PubChem Substance 46508037 ChemSpider 3280577 PDB SFG BE0002526 RdmB Streptomyces purpurascens unknown RdmB Involved in O-methyltransferase activity rdmB None 4.48 39797.0 Streptomyces purpurascens GenBank Gene Database U10405 UniProtKB Q54527 UniProt Accession Q54527_9ACTO >RdmB MSSSSPGEPLEPTDQDLDVLLKNLGNLVTPMALRVAATLRLVDHLLAGADTLAGLADRTD THPQALSRLVRHLTVVGVLEGGEKQGRPLRPTRLGMLLADGHPAQQRAWLDLNGAVSHAD LAFTGLLDVVRTGRPAYAGRYGRPFWEDLSADVALADSFDALMSCDEDLAYEAPADAYDW SAVRHVLDVGGGNGGMLAAIALRAPHLRGTLVELAGPAERARRRFADAGLADRVTVAEGD FFKPLPVTADVVLLSFVLLNWSDEDALTILRGCVRALEPGGRLLVLDRADVEGDGADRFF STLLDLRMLTFMGGRVRTRDEVVDLAGSAGLALASERTSGSTTLPFDFSILEFTAVSEEA APAAQASEALPAQE >1125 bp GTGAGCTCTTCCTCACCCGGGGAACCCCTGGAACCGACCGACCAGGACCTCGACGTACTC CTGAAGAACCTCGGCAATCTGGTGACCCCGATGGCCCTGAGGGTCGCCGCGACACTCCGC CTGGTCGATCACCTGCTGGCCGGAGCCGACACCCTCGCCGGCCTCGCCGACCGTACGGAC ACCCATCCCCAGGCGCTCTCCCGCCTGGTCCGGCACCTGACCGTCGTCGGCGTCCTGGAG GGCGGCGAGAAGCAGGGCCGGCCGCTGCGCCCCACCCGGCTCGGGATGCTCCTCGCCGAC GGCCACCCGGCCCAGCAGCGGGCCTGGCTGGACCTGAACGGGGCCGTCTCCCACGCCGAC CTGGCCTTCACCGGGCTCCTCGACGTGGTCCGCACCGGCCGCCCCGCCTACGCCGGGCGG TACGGGCGGCCCTTCTGGGAGGACCTCTCGGCGGACGTGGCGCTGGCCGACTCCTTCGAC GCGCTCATGTCCTGCGACGAGGACCTGGCCTACGAGGCCCCGGCCGACGCGTACGACTGG TCGGCGGTCCGGCACGTCCTCGACGTGGGCGGCGGCAACGGCGGCATGCTCGCGGCGATC GCCCTGCGGGCCCCGCACCTGCGCGGCACCCTGGTCGAACTGGCCGGTCCCGCCGAGCGC GCCCGGCGCAGGTTCGCGGACGCCGGTCTGGCCGACCGGGTCACGGTGGCGGAGGGCGAC TTCTTCAAGCCGCTGCCCGTCACCGCCGACGTCGTCCTGCTGTCGTTCGTCCTGCTCAAC TGGTCCGACGAGGACGCGCTGACGATCCTGCGCGGCTGCGTCAGGGCGCTGGAGCCGGGA GGCAGGCTCCTGGTCCTCGACCGTGCCGATGTCGAGGGGGACGGCGCCGACCGGTTCTTC AGCACGCTGCTCGACCTGCGGATGCTGACGTTCATGGGCGGACGGGTGCGCACCCGGGAC GAGGTCGTGGACCTGGCCGGATCGGCCGGACTCGCCCTGGCCTCGGAGCGCACGAGCGGC TCCACGACCCTCCCGTTCGACTTCTCGATCCTCGAGTTCACGGCCGTCTCCGAGGAAGCG GCCCCGGCCGCCCAGGCCTCCGAAGCCCTCCCAGCACAGGAGTAG PF00891 Methyltransf_2 function catalytic activity function transferase activity function transferase activity, transferring one-carbon groups function methyltransferase activity function O-methyltransferase activity BE0002516 rRNA adenine N-6-methyltransferase Bacillus subtilis unknown rRNA adenine N-6-methyltransferase Involved in rRNA (adenine-N6,N6-)-dimethyltransferase activity This protein produces a dimethylation of the adenine residue at position 2058 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics ermC' None 10.2 28908.0 Bacillus subtilis GenBank Gene Database M13761 UniProtKB P13956 UniProt Accession ERM_BACIU EC 2.1.1.48 Erythromycin resistance protein Macrolide- lincosamide-streptogramin B resistance protein >rRNA adenine N-6-methyltransferase MNEKNIKHSQNFITSKHNIDKIMTNIRLNEHDNIFEIGSGKGHFTLELVQRCNFVTAIEI DHKLCKTTENKLVDHDNFQVLNKDILQFKFPKNQSYKIFGNIPYNISTDIIRKIVFDSIA DEIYLIVEYGFAKRLLNTKRSLALFLMAEVDISILSMVPREYFHPKPKVNSSLIRLNRKK SRISHKDKQKYNYFVMKWVNKEYKKIFTKNQFNNSLKHAGIDDLNNISFEQFLSLFNSYK LFNK >735 bp ATGAACGAGAAAAATATAAAACACAGTCAAAACTTTATTACTTCAAAACATAATATAGAT AAAATAATGACAAATATAAGATTAAATGAACATGATAATATCTTTGAAATCGGCTCAGGA AAAGGGCATTTTACCCTTGAATTAGTACAGAGGTGTAATTTCGTAACTGCCATTGAAATA GACCATAAATTATGCAAAACTACAGAAAATAAACTTGTTGATCACGATAATTTCCAAGTT TTAAACAAGGATATATTGCAGTTTAAATTTCCTAAAAACCAATCCTATAAAATATTTGGT AATATACCTTATAACATAAGTACGGATATAATACGCAAAATTGTTTTTGATAGTATAGCT GATGAGATTTATTTAATCGTGGAATACGGGTTTGCTAAAAGATTATTAAATACAAAACGC TCATTGGCATTATTTTTAATGGCAGAAGTTGATATTTCTATATTAAGTATGGTTCCAAGA GAATATTTTCATCCTAAACCTAAAGTGAATAGCTCACTTATCAGATTAAATAGAAAAAAA TCAAGAATATCACACAAAGATAAACAGAAGTATAATTATTTCGTTATGAAATGGGTTAAC AAAGAATACAAGAAAATATTTACAAAAAATCAATTTAACAATTCCTTAAAACATGCAGGA ATTGACGATTTAAACAATATTAGCTTTGAACAATTCTTATCTCTTTTCAATAGCTATAAA TTATTTAATAAGTAA PF00398 RrnaAD function transferase activity, transferring one-carbon groups function methyltransferase activity function RNA methyltransferase activity function rRNA methyltransferase activity function rRNA (adenine) methyltransferase activity function catalytic activity function rRNA (adenine-N6,N6-)-dimethyltransferase activity function transferase activity process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process RNA metabolism process physiological process process metabolism process RNA modification process cellular metabolism process rRNA modification BE0002531 Modification methylase TaqI Thermus aquaticus unknown Modification methylase TaqI Involved in nucleic acid binding This methylase recognizes the double-stranded sequence TCGA, causes specific methylation on A-4 on both strands and protects the DNA from cleavage by the TaqI endonuclease taqIM Cytoplasmic None 9.39 47863.0 Thermus aquaticus GenBank Gene Database M76681 UniProtKB P14385 UniProt Accession MTTA_THEAQ Adenine-specific methyltransferase TaqI EC 2.1.1.72 M.TaqI >Modification methylase TaqI MGLPPLLSLPSNSAPRSLGRVETPPEVVDFMVSLAEAPRGGRVLEPACAHGPFLRAFREA HGTAYRFVGVEIDPKALDLPPWAEGILADFLLWEPGEAFDLILGNPPYGIVGEASKYPIH VFKAVKDLYKKAFSTWKGKYNLYGAFLEKAVRLLKPGGVLVFVVPATWLVLEDFALLREF LAREGKTSVYYLGEVFPQKKVSAVVIRFQKSGKGLSLWDTQESESGFTPILWAEYPHWEG EIIRFETEETRKLEISGMPLGDLFHIRFAARSPEFKKHPAVRKEPGPGLVPVLTGRNLKP GWVDYEKNHSGLWMPKERAKELRDFYATPHLVVAHTKGTRVVAAWDERAYPWREEFHLLP KEGVRLDPSSLVQWLNSEAMQKHVRTLYRDFVPHLTLRMLERLPVRREYGFHTSPESARN F >1266 bp ATGGGCCTGCCACCCCTTCTGTCCTTACCTTCCAACTCCGCCCCCAGGAGCCTGGGCCGG GTGGAGACCCCCCCGGAGGTGGTGGACTTCATGGTCTCCCTGGCCGAGGCGCCCAGGGGG GGAAGGGTGCTGGAGCCCGCCTGCGCCCATGGGCCCTTCCTCCGGGCTTTCCGGGAGGCC CACGGGACGGGCTACCGCTTCGTGGGGGTGGAGATAGACCCAAAAGCCCTGGACCTCCCC CCCTGGGCCGAGGGCATCCTGGCGGACTTCCTCCTCTGGGAGCCGGGGGAGGCCTTTGAC CTGATCCTGGGCAATCCGCCTTACGGCATCGTAGGAGAAGCCAGCAAATACCCCATTCAC GTCTTCAAAGCGGTCAAGGACCTCTACAAGAAGGCCTTTTCCACCTGGAAGGGCAAGTAC AACTTGTACGGGGCCTTTCTTGAAAAGGCCGTTCGCCTTCTTAAGCCTGGTGGGGTCCTC GTCTTTGTAGTCCCGGCCACCTGGCTTGTCCTGGAGGATTTTGCCCTCCTTCGCGAGTTC CTTGCCCGGGAAGGGAAAACATCTGTATACTACCTTGGCGAGGTTTTCCCGCAAAAAAAG GTTAGCGCTGTAGTGATTCGCTTCCAGAAGAGCGGAAAAGGCCTTTCACTTTGGGATACC CAAGAAAGCGAAAGCGGGTTCACGCCCATCCTCTGGGCTGAATATCCACATTGGGAAGGA GAGATTATCCGCTTTGAAACAGAGGAGACGCGGAAGCTGGAAATATCGGGAATGCCACTG GGAGACCTCTTTCATATCCGCTTCGCCGCAAGAAGCCCTGAATTCAAGAAACATCCAGCA GTGAGAAAGGAACCGGGGCCAGGTCTTGTGCCTGTGCTCACAGGAAGAAATTTAAAGCCG GGGTGGGTAGATTACGAGAAAAACCACTCCGGGCTTTGGATGCCCAAGGAAAGGGCCAAG GAGCTCAGGGACTTCTATGCCACGCCCCACCTGGTGGTAGCCCACACCAAGGGGACTAGA GTGGTGGCCGCTTGGGACGAAAGGGCCTACCCCTGGCGGGAGGAGTTCCACCTCCTGCCC AAGGAAGGTGTGAGACTGGACCCCTCGTCCCTGGTGCAGTGGTTAAACTCCGAAGCGATG CAGAAGCACGTCAGGACGCTTTATCGCGACTTCGTGCCCCACCTGACGCTGAGGATGCTA GAAAGGCTTCCTGTAAGGAGGGAATATGGCTTCCACACAAGCCCAGAAAGCGCTCGAAAC TTTTGA function catalytic activity function N-methyltransferase activity function transferase activity function transferase activity, transferring one-carbon groups function methyltransferase activity function nucleic acid binding function DNA binding function binding process DNA modification process DNA alkylation process metabolism process DNA methylation process cellular metabolism process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process DNA metabolism process physiological process BE0001456 Modification methylase RsrI Rhodobacter sphaeroides # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Modification methylase RsrI Replication, recombination and repair This methylase recognizes the double-stranded sequence GAATTC, causes specific methylation on A-? on both strands, and protects the DNA from cleavage by the RsrI endonuclease rsrIM Cytoplasmic None 7.06 35656.0 Rhodobacter sphaeroides GenBank Gene Database X16456 GenBank Protein Database 46455 UniProtKB P14751 UniProt Accession MTR1_RHOSH Adenine-specific methyltransferase RsrI EC 2.1.1.72 M.RsrI >Modification methylase RsrI MANRSHHNAGHRAMNALRKSGQKHSSESQLGSSEIGTTRHVYDVCDCLDTLAKLPDDSVQ LIICDPPYNIMLADWDDHMDYIGWAKRWLAEAERVLSPTGSIAIFGGLQYQGEAGSGDLI SIISHMRQNSKMLLANLIIWNYPNGMSAQRFFANRHEEIAWFAKTKKYFFDLDAVREPYD EETKAAYMKDKRLNPESVEKGRNPTNVWRMSRLNGNSLERVGHPTQKPAAVIERLVRALS HPGSTVLDFFAGSGVTARVAIQEGRNSICTDAAPVFKEYYQKQLTFLQDDGLIDKARSYE IVEGAANFGAALQRGDVAS >960 bp ATGGCAAACCGATCTCACCACAATGCGGGCCACCGAGCGATGAACGCTCTCCGCAAGTCA GGCCAAAAGCATTCGTCCGAGTCTCAGTTGGGATCTTCGGAGATCGGAACCACACGACAT GTGTATGACGTTTGCGATTGCCTCGACACCTTGGCGAAGCTGCCCGACGACTCCGTCCAG TTGATCATTTGTGATCCTCCATACAACATCATGCTGGCGGACTGGGATGATCACATGGAC TACATCGGCTGGGCGAAGCGATGGCTAGCCGAAGCCGAGCGTGTTCTATCCCCAACGGGC AGCATAGCGATTTTCGGCGGCCTACAATACCAAGGGGAGGCTGGTTCAGGTGATCTGATC TCAATCATTTCGCACATGAGACAAAACAGCAAAATGCTGCTCGCAAACCTTATCATCTGG AACTATCCGAACGGCATGAGTGCGCAGCGCTTCTTTGCAAATAGGCACGAGGAAATCGCG TGGTTCGCCAAGACCAAGAAGTATTTCTTCGATCTTGACGCTGTGCGGGAACCATATGAC GAGGAAACCAAAGCCGCTTACATGAAGGACAAGCGGTTGAACCCTGAGTCGGTTGAAAAG GGACGCAACCCAACAAACGTGTGGCGGATGTCTCGGCTTAACGGCAATTCTCTTGAACGT GTCGGCCACCCCACGCAAAAACCAGCCGCAGTGATTGAGAGACTGGTTCGCGCGTTGTCG CATCCGGGTTCAACGGTCCTCGATTTTTTTGCTGGAAGTGGGGTAACGGCGCGCGTTGCA ATTCAAGAGGGACGGAACAGCATTTGCACTGACGCCGCGCCTGTATTCAAAGAATATTAC CAGAAGCAGCTAACTTTCCTTCAAGATGATGGACTGATCGACAAAGCGCGATCATATGAA ATTGTTGAAGGGGCTGCGAACTTTGGTGCAGCATTGCAGCGGGGAGATGTTGCTTCATAA PF01555 N6_N4_Mtase function catalytic activity function N-methyltransferase activity function transferase activity function transferase activity, transferring one-carbon groups function methyltransferase activity function nucleic acid binding function DNA binding function binding process DNA modification process DNA alkylation process metabolism process DNA methylation process cellular metabolism process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process DNA metabolism process physiological process "

owl:sameAs

?:EXPT02890

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