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PredicateValue (sorted: default)
rdfs:label
"2'-Deoxyadenosine 5'-Triphosphate"
rdf:type
ns1:drugs
ns1:description
" 1927-31-7 experimental This compound belongs to the purine 2'-deoxyribonucleoside triphosphates. These are purine nucleotides with triphosphate group linked to the ribose moiety lacking an hydroxyl group at position 2. Purine 2'-deoxyribonucleoside Triphosphates Organic Compounds Organooxygen Compounds Carbohydrates and Carbohydrate Conjugates Glycosyl Compounds Pentoses Organic Pyrophosphates Purines and Purine Derivatives Aminopyrimidines and Derivatives Primary Aromatic Amines Organic Phosphoric Acids N-substituted Imidazoles Organophosphate Esters Oxolanes Tetrahydrofurans Secondary Alcohols Ethers Polyamines organic pyrophosphate pentose monosaccharide purine imidazopyrimidine aminopyrimidine pyrimidine primary aromatic amine n-substituted imidazole monosaccharide organic phosphate phosphoric acid ester azole tetrahydrofuran oxolane imidazole secondary alcohol polyamine ether primary amine organonitrogen compound amine alcohol logP -0.66 ALOGPS logS -2.1 ALOGPS Water Solubility 3.83e+00 g/l ALOGPS logP -5.3 ChemAxon IUPAC Name ({[({[(2S,3R,5R)-5-(6-amino-9H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)phosphonic acid ChemAxon Traditional IUPAC Name ({[(2S,3R,5R)-5-(6-aminopurin-9-yl)-3-hydroxyoxolan-2-yl]methoxy(hydroxy)phosphoryl}oxy(hydroxy)phosphoryl)oxyphosphonic acid ChemAxon Molecular Weight 491.1816 ChemAxon Monoisotopic Weight 491.000830537 ChemAxon SMILES NC1=NC=NC2=C1N=CN2[C@H]1C[C@@H](O)[C@H](CO[P@@](O)(=O)O[P@](O)(=O)OP(O)(O)=O)O1 ChemAxon Molecular Formula C10H16N5O12P3 ChemAxon InChI InChI=1S/C10H16N5O12P3/c11-9-8-10(13-3-12-9)15(4-14-8)7-1-5(16)6(25-7)2-24-29(20,21)27-30(22,23)26-28(17,18)19/h3-7,16H,1-2H2,(H,20,21)(H,22,23)(H2,11,12,13)(H2,17,18,19)/t5-,6+,7-/m1/s1 ChemAxon InChIKey InChIKey=SUYVUBYJARFZHO-DSYKOEDSSA-N ChemAxon Polar Surface Area (PSA) 258.9 ChemAxon Refractivity 94.3 ChemAxon Polarizability 37.5 ChemAxon Rotatable Bond Count 8 ChemAxon H Bond Acceptor Count 13 ChemAxon H Bond Donor Count 6 ChemAxon pKa (strongest acidic) 0.9 ChemAxon pKa (strongest basic) 5.01 ChemAxon Physiological Charge -3 ChemAxon Number of Rings 3 ChemAxon Bioavailability 0 ChemAxon MDDR-Like Rule true ChemAxon ChEBI 16284 PubChem Compound 46936612 PubChem Substance 46507738 KEGG Compound C00131 PDB DTP BE0001811 DNA primase/helicase Enterobacteria phage T7 # 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 DNA primase/helicase Replication, recombination and repair DNA primase synthesizes RNA primers necessary for replication by DNA polymerase. It also functions as an ATP- dependent unwinding protein. Has a 5'->3' helicase activity; 4a also has a DNA primase activity 4 Cytoplasmic None 5.23 62656.0 Enterobacteria phage T7 GenBank Gene Database V01127 GenBank Protein Database 15519 UniProtKB P03692 UniProt Accession PRIM_BPT7 EC 2.7.7.- >DNA primase/helicase MDNSHDSDSVFLYHIPCDNCGSSDGNSLFSDGHTFCYVCEKWTAGNEDTKERASKRKPSG GKPMTYNVWNFGESNGRYSALTARGISKETCQKAGYWIAKVDGVMYQVADYRDQNGNIVS QKVRDKDKNFKTTGSHKSDALFGKHLWNGGKKIVVTEGEIDMLTVMELQDCKYPVVSLGH GASAAKKTCAANYEYFDQFEQIILMFDMDEAGRKAVEEAAQVLPAGKVRVAVLPCKDANE CHLNGHDREIMEQVWNAGPWIPDGVVSALSLRERIREHLSSEESVGLLFSGCTGINDKTL GARGGEVIMVTSGSGMGKSTFVRQQALQWGTAMGKKVGLAMLEESVEETAEDLIGLHNRV RLRQSDSLKREIIENGKFDQWFDELFGNDTFHLYDSFAEAETDRLLAKLAYMRSGLGCDV IILDHISIVVSASGESDERKMIDNLMTKLKGFAKSTGVVLVVICHLKNPDKGKAHEEGRP VSITDLRGSGALRQLSDTIIALERNQQGDMPNLVLVRILKCRFTGDTGIAGYMEYNKETG WLEPSSYSGEEESHSESTDWSNDTDF >1701 bp ATGGACAATTCGCACGATTCCGATAGTGTATTTCTTTACCACATTCCTTGTGACAACTGT GGGAGTAGTGATGGGAACTCGCTGTTCTCTGACGGACACACGTTCTGCTACGTATGCGAG AAGTGGACTGCTGGTAATGAAGACACTAAAGAGAGGGCTTCAAAACGGAAACCCTCAGGA GGTAAACCAATGACTTACAACGTGTGGAACTTCGGGGAATCCAATGGACGCTACTCCGCG TTAACTGCGAGAGGAATCTCCAAGGAAACCTGTCAGAAGGCTGGCTACTGGATTGCCAAA GTAGACGGTGTGATGTACCAAGTGGCTGACTATCGGGACCAGAACGGCAACATTGTGAGT CAGAAGGTTCGAGATAAAGATAAGAACTTTAAGACCACTGGTAGTCACAAGAGTGACGCT CTGTTCGGGAAGCACTTGTGGAATGGTGGTAAGAAGATTGTCGTTACAGAAGGTGAAATC GACATGCTTACCGTGATGGAACTTCAAGACTGTAAGTATCCTGTAGTGTCGTTGGGTCAC GGTGCCTCTGCCGCTAAGAAGACATGCGCTGCCAACTACGAATACTTTGACCAGTTCGAA CAGATTATCTTAATGTTCGATATGGACGAAGCAGGGCGCAAAGCAGTCGAAGAGGCTGCA CAGGTTCTACCTGCTGGTAAGGTACGAGTGGCAGTTCTTCCGTGTAAGGATGCAAACGAG TGTCACCTAAATGGTCACGACCGTGAAATCATGGAGCAAGTGTGGAATGCTGGTCCTTGG ATTCCTGATGGTGTGGTATCGGCTCTTTCGTTACGTGAACGAATCCGTGAGCACCTATCG TCCGAGGAATCAGTAGGTTTACTTTTCAGTGGCTGCACTGGTATCAACGATAAGACCTTA GGTGCCCGTGGTGGTGAAGTCATTATGGTCACTTCCGGTTCCGGTATGGGTAAGTCAACG TTCGTCCGTCAACAAGCTCTACAATGGGGCACAGCGATGGGCAAGAAGGTAGGCTTAGCG ATGCTTGAGGAGTCCGTTGAGGAGACCGCTGAGGACCTTATAGGTCTACACAACCGTGTC CGACTGAGACAATCCGACTCACTAAAGAGAGAGATTATTGAGAACGGTAAGTTCGACCAA TGGTTCGATGAACTGTTCGGCAACGATACGTTCCATCTATATGACTCATTCGCCGAGGCT GAGACGGATAGACTGCTCGCTAAGCTGGCCTACATGCGCTCAGGCTTGGGCTGTGACGTA ATCATTCTAGACCACATCTCAATCGTCGTATCCGCTTCTGGTGAATCCGATGAGCGTAAG ATGATTGACAACCTGATGACCAAGCTCAAAGGGTTCGCTAAGTCAACTGGGGTGGTGCTG GTCGTAATTTGTCACCTTAAGAACCCAGACAAAGGTAAAGCACATGAGGAAGGTCGCCCC GTTTCTATTACTGACCTACGTGGTTCTGGCGCACTACGCCAACTATCTGATACTATTATT GCCCTTGAGCGTAATCAGCAAGGCGATATGCCTAACCTTGTCCTCGTTCGTATTCTCAAG TGCCGCTTTACTGGTGATACTGGTATCGCTGGCTACATGGAATACAACAAGGAAACCGGA TGGCTTGAACCATCAAGTTACTCAGGGGAAGAAGAGTCACACTCAGAGTCAACAGACTGG TCCAACGACACTGACTTCTGA PF01751 Toprim PF08273 Prim_Zn_Ribbon function catalytic activity function nucleotide binding function nucleotidyltransferase activity function purine nucleotide binding function DNA-directed RNA polymerase activity function adenyl nucleotide binding function helicase activity function transferase activity function ATP binding function DNA helicase activity function transferase activity, transferring phosphorus-containing groups function DNA primase activity function binding function nucleic acid binding process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process lagging strand elongation process DNA replication process DNA replication, synthesis of RNA primer process metabolism process DNA-dependent DNA replication process cellular metabolism process DNA metabolism process DNA modification process DNA strand elongation process physiological process BE0000113 DNA polymerase beta Human # 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 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown DNA polymerase beta Replication, recombination and repair Repair polymerase. Conducts "gap-filling" DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. Has a 5'-deoxyribose-5- phosphate lyase (dRP lyase) activity POLB 8p11.2 Nucleus None 9.41 38047.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:9174 GenAtlas POLB GeneCards POLB GenBank Gene Database L11607 GenBank Protein Database 292397 UniProtKB P06746 UniProt Accession DPOLB_HUMAN EC 2.7.7.7 EC 4.2.99.- >DNA polymerase beta SKRKAPQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKK LPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIKT LEDLRKNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGSF RRGAESSGDMDVLLTHPSFTSESTKQPKLLHQVVEQLQKVHFITDTLSKGETKFMGVCQL PSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPL GVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE >1008 bp ATGAGCAAACGGAAGGCGCCGCAGGAGACTCTCAACGGGGGAATCACCGACATGCTCACA GAACTCGCAAACTTTGAGAAGAACGTGAGCCAAGCTATCCACAAGTACAATGCTTACAGA AAAGCAGCATCTGTTATAGCAAAATACCCACACAAAATAAAGAGTGGAGCTGAAGCTAAG AAATTGCCTGGAGTAGGAACAAAAATTGCTGAAAAGATTGATGAGTTTTTAGCAACTGGA AAATTACGTAAACTGGAAAAGATTCGGCAGGATGATACGAGTTCATCCATCAATTTCCTG ACTCGAGTTAGTGGCATTGGTCCATCTGCTGCAAGGAAGTTTGTAGATGAAGGAATTAAA ACACTAGAAGATCTCAGAAAAAATGAAGATAAATTGAACCATCATCAGCGAATTGGGCTG AAATATTTTGGGGACTTTGAAAAAAGAATTCCTCGTGAAGAGATGTTACAAATGCAAGAT ATTGTACTAAATGAAGTTAAAAAAGTGGATTCTGAATACATTGCTACAGTCTGTGGCAGT TTCAGAAGAGGTGCAGAGTCCAGTGGTGACATGGATGTTCTCCTGACCCATCCCAGCTTC ACTTCAGAATCAACCAAACAGCCAAAACTGTTACATCAGGTTGTGGAGCAGTTACAAAAG GTTCATTTTATCACAGATACCCTGTCAAAGGGTGAGACAAAGTTCATGGGTGTTTGCCAG CTTCCCAGTAAAAATGATGAAAAAGAATATCCACACAGAAGAATTGATATCAGGTTGATA CCCAAAGATCAGTATTACTGTGGTGTTCTCTATTTCACTGGGAGTGATATTTTCAATAAG AATATGAGGGCTCATGCCCTAGAAAAGGGTTTCACAATCAATGAGTACACCATCCGTCCC TTGGGAGTCACTGGAGTTGCAGGAGAACCCCTGCCAGTGGATAGTGAAAAAGACATCTTT GATTACATCCAGTGGAAATACCGGGAACCCAAGGACCGGAGCGAATGA component cell component intracellular function catalytic activity function beta DNA polymerase activity function nucleotidyltransferase activity function transferase activity function DNA-directed DNA polymerase activity function transferase activity, transferring phosphorus-containing groups function nucleic acid binding function binding function DNA binding process DNA metabolism process metabolism process cellular metabolism process DNA repair process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process physiological process process DNA replication BE0001782 Ribonucleoside-diphosphate reductase 2 subunit alpha Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) # 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 Ribonucleoside-diphosphate reductase 2 subunit alpha Nucleotide transport and metabolism Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1E contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide nrdE None 7.04 80588.0 Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) GenBank Gene Database X73226 GenBank Protein Database 1050838 UniProtKB Q08698 UniProt Accession RIR3_SALTY EC 1.17.4.1 R1E protein Ribonucleotide reductase 2 >Ribonucleoside-diphosphate reductase 2 alpha subunit MATTTPERVMQETMDYHALNAMLNLYDKAGHIQFDKDQQAIDAFFATHVRPHSVTFASQH ERLGTLVREGYYDDAVLARYDRAFVLRLFEHAHASGFRFQTFLGAWKFYTSYTLKTFDGK RYLEHFEDRVTMVALTLAQGDETLATQLTDEMLSGRFQPATPTFLNCGKQQRGELVSCFL LRIEDNMESIGRAVNSALQLSKRGGGVAFLLSNLREAGAPIKRIENQSSGVIPVMKMLED AFSYANQLGARQGAGAVYLHAHHPDILRFLDTKRENADEKIRIKTLSLGVVIPDITFRLA KENAQMALFSPYDIQRRYGKPFGDIAISERYDELIADPHVRKTYINARDFFQTLAEIQFE SGYPYIMFEDTVNRANPIAGRINMSNLCSEILQVNSASRYDDNLDYTHIGHDISCNLGSL NIAHVMDSPDIGRTVETAIRGLTAVSDMSHIRSVPSIAAGNAASHAIGLGQMNLHGYLAR EGIAYGSPEALDFTNLYFYTITWHAVHTSMRLARERGKTFAGFAQSRYASGDYFTQYLQD DWQPKTAKVRALFARSGITLPTREMWLKLRDDVMRYGIYNQNLQAVPPTGSISYINHATS SIHPIVAKIEIRKEGKTGRVYYPAPFMTNENLDMYQDAYDIGPEKIIDTYAEATRHVDQG LSLTLFFPDTATTRDINKAQIYAWRKGIKSLYYIRLRQLALEGTEIEGCVSCAL >2145 bp TTGGCAACAACTACCCCGGAGCGCGTAATGCAGGAAACCATGGATTACCACGCCCTGAAC GCGATGCTGAATCTTTACGATAAAGCAGGCCATATTCAGTTCGACAAGGACCAGCAGGCG ATCGACGCCTTCTTTGCCACCCACGTCCGCCCGCATTCCGTGACGTTTGCCAGCCAGCAT GAACGTCTGGGGACGCTGGTTCGGGAAGGGTATTACGATGACGCCGTCCTCGCGCGTTAC GACCGCGCCTTCGTCCTTCGCCTGTTCGAGCACGCCCATGCCAGCGGCTTTCGCTTCCAG ACGTTTCTTGGCGCCTGGAAGTTCTATACCAGTTACACGCTGAAAACCTTCGACGGCAAA CGTTATCTGGAACACTTTGAAGATCGGGTGACAATGGTGGCGTTGACGCTGGCGCAGGGT GACGAAACGCTGGCCACCCAACTGACCGATGAAATGCTTTCTGGTCGCTTTCAGCCCGCT ACCCCGACTTTTTTAAATTGCGGCAAACAGCAGCGTGGGGAACTGGTCTCCTGCTTCCTG CTCCGTATCGAAGACAACATGGAGTCGATCGGGCGGGCGGTGAATTCGGCGCTGCAACTC TCCAAACGCGGCGGCGGCGTCGCGTTTTTACTCTCCAATCTGCGCGAGGCGGGCGCGCCG ATCAAACGCATTGAGAATCAGTCTTCCGGCGTGATCCCGGTGATGAAAATGCTGGAAGAC GCGTTTTCGTATGCCAACCAACTTGGCGCGCGCCAGGGGGCCGGCGCGGTTTATCTCCAT GCGCACCATCCGGATATTCTGCGTTTTCTGGATACCAAACGAGAAAACGCTGACGAAAAA ATCCGGATCAAAACGCTCTCTCTCGGCGTGGTGATCCCGGATATCACCTTCCGGCTGGCG AAAGAAAACGCGCAAATGGCGCTCTTTTCGCCCTATGACATACAACGACGCTACGGCAAA CCGTTTGGCGATATCGCCATTAGCGAACGGTACGATGAATTAATTGCCGATCCGCACGTG CGCAAAACCTATATTAACGCCCGTGACTTTTTTCAAACACTGGCGGAGATTCAGTTCGAA TCCGGGTATCCCTACATCATGTTTGAAGATACGGTAAACCGCGCGAATCCCATTGCTGGT CGCATTAATATGAGCAACCTGTGCTCAGAAATTTTACAGGTCAATAGCGCTTCCCGTTAC GACGATAACCTTGACTATACCCACATCGGGCATGACATCTCCTGCAATCTCGGCTCGCTG AATATCGCTCACGTCATGGATTCACCGGACATTGGCCGTACCGTAGAAACCGCTATTCGC GGCCTGACGGCGGTGTCGGACATGAGCCATATACGCAGCGTGCCCTCAATAGCCGCCGGT AATGCCGCCTCTCATGCCATCGGTCTGGGCCAGATGAATCTGCATGGCTATCTGGCGAGG GAAGGTATTGCCTACGGTTCGCCGGAGGCGTTGGATTTCACCAATCTCTATTTTTACACC ATTACCTGGCATGCCGTGCATACTTCAATGCGGCTAGCCCGCGAACGCGGCAAAACCTTC GCCGGATTTGCGCAGTCGCGCTATGCCAGCGGCGACTATTTTACGCAGTATTTACAGGAC GACTGGCAACCGAAAACAGCGAAAGTCAGGGCGCTATTTGCCCGCAGCGGCATTACGCTG CCCACACGAGAAATGTGGCTAAAGCTGCGCGACGATGTGATGCGCTATGGCATCTATAAC CAAAATTTGCAGGCGGTGCCGCCGACCGGTTCGATTTCTTACATTAATCATGCGACCTCC AGCATTCATCCGATTGTGGCCAAAATTGAGATTCGCAAAGAGGGCAAAACCGGGCGTGTG TATTACCCCGCGCCGTTTATGACCAATGAAAACCTGGACATGTATCAGGATGCTTACGAT ATCGGTCCGGAAAAAATTATTGATACCTATGCCGAGGCCACGCGCCACGTCGATCAAGGG CTGTCGCTCACCCTGTTTTTCCCCGATACCGCCACGACCCGCGATATCAACAAGGCGCAG ATCTATGCCTGGCGAAAAGGTATTAAGTCCCTGTATTACATCCGGCTTCGCCAGTTGGCG CTGGAAGGTACTGAAATTGAAGGCTGCGTATCCTGCGCGCTATAA PF02867 Ribonuc_red_lgC PF00317 Ribonuc_red_lgN PF08343 RNR_N component ribonucleoside-diphosphate reductase complex component protein complex function oxidoreductase activity, acting on CH2 groups function oxidoreductase activity, acting on CH2 groups, disulfide as acceptor function ribonucleoside-diphosphate reductase activity function catalytic activity function oxidoreductase activity process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process DNA replication process DNA metabolism process physiological process process metabolism process cellular metabolism BE0001442 Anaerobic ribonucleoside-triphosphate reductase Enterobacteria phage T4 # 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 Anaerobic ribonucleoside-triphosphate reductase Nucleotide transport and metabolism 2'-deoxyribonucleoside triphosphate + thioredoxin disulfide + H(2)O = ribonucleoside triphosphate + thioredoxin NRDD None 7.06 67957.0 Enterobacteria phage T4 GenBank Gene Database Y00122 GenBank Protein Database 1177560 UniProtKB P07071 UniProt Accession NRDD_BPT4 EC 1.17.4.2 >Anaerobic ribonucleoside-triphosphate reductase MTIEKEIEGLIHKTNKDLLNENANKDSRVFPTQRDLMAGIVSKHIAKNMVPSFIMKAHES GIIHVHDIDYSPALPFTNCCLVDLKGMLENGFKLGNAQIETPKSIGVATAIMAQITAQVA SHQYGGTTFANVDKVLSPYVKRTYAKHIEDAEKWQIADALNYAQSKTEKDVYDAFQAYEY EVNTLFSSNGQTPFVTITFGTGTDWTERMIQKAILKNRIKGLGRDGITPIFPKLVMFVEE GVNLYKDDPNYDIKQLALECASKRMYPDIISAKNNKAITGSSVPVSPMGCRSFLSVWKDS TGNEILDGRNNLGVVTLNLPRIALDSYIGTQFNEQKFVELFNERMDLCFEALMCRISSLK GVKATVAPILYQEGAFGVRLKPDDDIIELFKNGRSSVSLGYIGIHELNILVGRDIGREIL TKMNAHLKQWTERTGFAFSLYSTPAENLCYRFCKLDTEKYGSVKDVTDKGWYTNSFHVSV EENITPFEKISREAPYHFIATGGHISYVELPDMKNNLKGLEAVWDYAAQHLDYFGVNMPV DKCFTCGSTHEMTPTENGFVCSICGETDPKKMNTIRRTCGYLGNPNERGFNLGKNKEIMH RVKHQ >1818 bp ATGACAATTGAAAAAGAAATTGAAGGATTAATTCATAAAACTAATAAAGACCTTTTAAAC GAGAATGCTAATAAAGATTCTCGTGTTTTTCCAACTCAACGGGACCTTATGGCTGGTATT GTGTCTAAACACATTGCCAAAAATATGGTCCCGTCTTTTATTATGAAAGCGCATGAAAGC GGAATTATTCACGTGCATGATATTGATTATTCCCCTGCTCTTCCATTTACTAATTGCTGT TTAGTAGATTTAAAAGGAATGCTTGAAAACGGATTTAAGCTTGGTAATGCGCAGATTGAA ACTCCTAAATCAATTGGAGTTGCTACTGCAATTATGGCACAAATTACTGCGCAAGTTGCT TCTCACCAATACGGCGGAACGACTTTTGCGAATGTAGATAAAGTACTTTCTCCTTATGTT AAACGCACCTATGCAAAACATATTGAGGATGCAGAAAAATGGCAAATCGCTGATGCGTTG AATTATGCTCAATCTAAAACAGAAAAAGACGTATACGATGCATTCCAAGCTTATGAGTAT GAAGTGAACACGTTATTCAGTTCAAACGGACAGACTCCTTTTGTAACAATTACATTTGGT ACGGGAACTGACTGGACTGAACGAATGATTCAGAAAGCAATTCTGAAAAATCGTATTAAA GGTCTTGGTCGTGATGGGATAACTCCTATTTTCCCTAAGCTTGTTATGTTCGTTGAAGAA GGTGTTAATCTTTATAAAGACGATCCGAACTATGATATTAAACAGCTTGCTCTAGAGTGC GCAAGCAAAAGGATGTATCCTGATATTATTTCAGCTAAGAACAATAAAGCTATCACTGGT TCATCTGTTCCTGTTTCTCCGATGGGTTGCCGTAGTTTCTTGAGCGTATGGAAAGATTCG ACTGGCAATGAAATTCTTGATGGACGCAATAATCTTGGTGTTGTAACACTGAATCTTCCT CGCATCGCGTTAGATTCTTATATTGGAACACAGTTCAATGAACAGAAATTTGTTGAGCTA TTTAATGAACGAATGGATTTATGTTTTGAAGCTTTGATGTGTAGAATTAGTTCCTTAAAA GGAGTTAAAGCTACTGTTGCTCCTATTCTTTACCAAGAAGGTGCATTCGGGGTTCGTCTT AAACCTGATGACGACATAATTGAGTTATTTAAAAACGGTAGAAGTTCAGTGTCTTTAGGA TACATTGGTATTCACGAATTGAATATTCTTGTCGGTCGTGATATTGGACGAGAAATTTTA ACTAAAATGAATGCTCATCTTAAACAGTGGACTGAAAGAACCGGATTTGCTTTTAGTTTA TATTCGACTCCTGCTGAAAACCTGTGTTATCGCTTCTGTAAACTCGATACAGAAAAATAT GGAAGCGTAAAAGATGTTACCGATAAAGGCTGGTACACTAACAGTTTCCATGTTTCAGTA GAAGAAAATATTACTCCGTTTGAAAAGATTTCTCGTGAAGCGCCATATCATTTCATTGCG ACAGGTGGTCACATTTCTTATGTTGAACTTCCTGATATGAAAAATAACTTAAAAGGTCTT GAGGCCGTGTGGGATTATGCTGCACAGCATTTAGATTATTTTGGTGTTAATATGCCAGTA GATAAATGTTTTACATGTGGAAGTACCCATGAAATGACTCCTACTGAAAACGGATTTGTT TGTTCTATTTGTGGAGAAACTGATCCTAAAAAGATGAATACCATAAGAAGAACATGTGGT TATTTGGGAAATCCGAACGAACGCGGATTTAATCTCGGTAAAAATAAAGAAATCATGCAT AGGGTTAAGCACCAATGA PF01228 Gly_radical function catalytic activity process metabolism process physiological process BE0001235 Protein RecA Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) # 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 Protein RecA Replication, recombination and repair Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with lexA causing its activation and leading to its autocatalytic cleavage recA Cytoplasm None 5.05 37301.0 Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) GenBank Gene Database X99208 GenBank Protein Database 1430892 UniProtKB Q59560 UniProt Accession RECA_MYCS2 Recombinase A >Protein recA MAQQAPDREKALELAMAQIDKNFGKGSVMRLGEEVRQPISVIPTGSISLDVALGIGGLPR GRVIEIYGPESSGKTTVALHAVANAQAAGGIAAFIDAEHALDPEYAKKLGVDTDSLLVSQ PDTGEQALEIADMLVRSGALDIIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKM TGALNNSGTTAIFINQLREKIGVMFGSPETTTGGKALKFYASVRLDVRRIETLKDGTDAV GNRTRVKVVKNKVSPPFKQAEFDILYGQGISREGSLIDMGVEHGFIRKSGSWFTYEGEQL GQGKENARKFLLENTDVANEIEKKIKEKLGIGAVVTAEADDVLPAPVDF >1050 bp ATGGCGCAGCAGGCCCCAGATCGCGAAAAGGCCCTCGAACTGGCGATGGCCCAGATCGAC AAGAATTTCGGCAAAGGCTCGGTGATGCGCCTCGGCGAAGAGGTGCGCCAGCCGATCTCG GTGATCCCCACCGGCTCCATCTCGCTGGATGTGGCGCTCGGCATCGGCGGCCTGCCGCGG GGCCGCGTCATCGAGATCTACGGCCCGGAGTCCTCGGGTAAGACCACCGTGGCCCTGCAT GCCGTCGCCAACGCGCAGGCCGCGGGCGGTATCGCGGCGTTCATCGACGCCGAGCACGCG CTGGATCCCGAGTACGCCAAGAAGCTGGGTGTGGACACCGACTCGCTGCTGGTGTCGCAG CCCGACACCGGTGAGCAGGCGCTGGAGATCGCCGACATGCTGGTGCGGTCCGGCGCGCTG GACATCATCGTCATCGACTCGGTCGCCGCCCTGGTGCCGCGCGCCGAGATCGAGGGCGAG ATGGGTGACAGCCACGTCGGCCTGCAGGCCCGCCTGATGAGCCAGGCGCTGCGCAAGATG ACCGGCGCGTTGAACAACTCGGGCACCACCGCGATCTTCATCAACCAGCTCCGCGAGAAG ATCGGTGTGATGTTCGGCTCGCCCGAGACCACCACGGGCGGTAAGGCACTGAAGTTCTAC GCCTCGGTCCGCCTCGACGTGCGCCGTATCGAGACGCTCAAGGACGGCACCGACGCGGTC GGTAACCGCACCCGCGTCAAGGTCGTCAAGAACAAGGTCTCCCCGCCGTTCAAGCAGGCC GAGTTCGACATCCTCTACGGCCAGGGCATCAGCCGCGAGGGTTCGCTCATCGACATGGGC GTCGAGCACGGCTTCATCCGCAAGTCCGGGTCCTGGTTCACCTACGAGGGTGAGCAGCTG GGCCAGGGCAAGGAGAACGCCCGCAAGTTCCTGCTGGAGAACACCGACGTCGCCAACGAG ATCGAGAAGAAGATCAAAGAGAAGCTCGGTATCGGCGCCGTCGTGACCGCTGAAGCCGAT GACGTCCTCCCGGCCCCGGTTGACTTCTGA PF00154 RecA function hydrolase activity function DNA binding function nucleotide binding function purine nucleotide binding function ATPase activity function adenyl nucleotide binding function ATPase activity, coupled function ATP binding function DNA-dependent ATPase activity function nucleic acid binding function binding function hydrolase activity, acting on acid anhydrides function catalytic activity function hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides function pyrophosphatase activity function nucleoside-triphosphatase activity process DNA metabolism process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process physiological process process metabolism process cellular metabolism BE0001269 Protein RecA Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10) # 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 Protein RecA Replication, recombination and repair Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with lexA causing its activation and leading to its autocatalytic cleavage recA Cytoplasm None 4.87 37465.0 Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10) GenBank Gene Database AE016958 GenBank Protein Database 41397305 UniProtKB P62219 UniProt Accession RECA_MYCPA Recombinase A >Protein recA MTQAPDREKALELAMAQIEKSYGKGSVMRLGDEMRQPISVIPTGSIALDVALGIGGLPRG RVVEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHALDPEYAKKLGVDTDSLLVSQP DTGEQALEIADMLIRSGALDILVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMT GALNNSGTTAIFINQLREKIGVMFGSPETTTGGKALKFYASVRMDVRRIETLKDGTNAVG NRTRVKIVKNKVSPPFKQAEFDILYGRGISREGSLIDMGVDQGFIRKSGSWFTYEGEQLG QGKENARTFLMENDEVANEIEKKIKEKLGIGAVVTDDLSDDGVLPAPVDF >1230 bp TCAGAAGTCGACGGGGGCGGGCAGGACGCCGTCATCGGACAAGTCATCGGTCACGACCGC GCCAATGCCGAGCTTTTCCTTGATCTTCTTCTCGATCTCGTTGGCGACCTCGTCGTTCTC CATCAAGAAGGTGCGGGCGTTCTCCTTGCCCTGGCCGAGCTGCTCGCCCTCATAGGTGAA CCAGGAACCGGACTTGCGGATGAAGCCCTGATCCACACCCATGTCGATCAGCGAGCCCTC CCGGCTGATCCCGCGGCCGTAGAGGATGTCGAACTCGGCCTGCTTGAACGGCGGCGACAC CTTGTTCTTGACGATCTTGACCCGGGTGCGGTTGCCGACCGCGTTGGTGCCGTCCTTGAG CGTCTCGATCCGGCGCACGTCCATGCGCACCGAGGCGTAGAACTTCAACGCCTTGCCACC CGTCGTGGTCTCCGGGCTGCCGAACATCACCCCGATCTTCTCCCGCAGCTGGTTGATGAA GATCGCGGTGGTGCCCGAATTGTTCAGCGCGCCAGTCATTTTCCGCAGCGCCTGGCTCAT CAGCCGGGCCTGCAGCCCGACGTGGCTGTCCCCCATCTCGCCCTCCAGCTCGGCGCGCGG CACCAGCGCGGCCACCGAGTCGATGACCAGGATGTCCAGCGCGCCGGAGCGGATCAGCAT GTCGGCGATCTCGAGCGCCTGCTCCCCCGTGTCCGGCTGGCTGACCAGCAGCGAATCGGT GTCCACGCCGAGCTTCTTGGCGTACTCGGGGTCCAGCGCGTGCTCGGCGTCGATGAACGC CGCGACACCGCCGGCGGCCTGGGCGTTGGCCACCGCGTGCAGGGCGACGGTGGTCTTACC CGAGGATTCCGGGCCGTAGATCTCCACGACCCGGCCGCGGGGCAGGCCGCCGATGCCCAG GGCGACGTCCAGGGCGATGGATCCGGTCGGGATGACCGAGATCGGTTGACGCATCTCGTC GCCGAGACGCATCACCGAGCCTTTCCCGTAGCTCTTTTCGATCTGGGCCATCGCCAGTTC GAGAGCCTTCTCGCGGTCGGGGGCTTGCGTCATGGTGCCTCTCCTATAGTCGGTGTGTCT TCTGACCGGTATCGGTCGGTTGGCGGTGACACTAGAGAAGGCCACCGACAAGTTGACGCT GCGAACGTCCCCCACAGTAGCCGAACAGGTGTTCGATTCAAGTTCGACACGCCGCGGGCG TCGCAGCAGCCGCGAAAGGCCGGCCGACAT PF00154 RecA function nucleotide binding function purine nucleotide binding function ATPase activity function adenyl nucleotide binding function ATPase activity, coupled function ATP binding function DNA-dependent ATPase activity function nucleic acid binding function binding function hydrolase activity, acting on acid anhydrides function catalytic activity function hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides function pyrophosphatase activity function nucleoside-triphosphatase activity function hydrolase activity function DNA binding process DNA metabolism process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process physiological process process metabolism process cellular metabolism "
owl:sameAs
?:EXPT01288

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