Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB03222"
Predicate | Value (sorted: default) |
---|---|
rdfs:label |
"2'-Deoxyadenosine 5'-Triphosphate"
|
rdf:type | |
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 |
All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines/drugbank_small.nt
The resource does not appear as an object