3.1.26.4: ribonuclease H
This is an abbreviated version!
For detailed information about ribonuclease H, go to the full flat file.
Word Map on EC 3.1.26.4
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3.1.26.4
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antiretroviral
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nucleoside
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viruses
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nnrti
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virological
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hiv-infected
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nonnucleoside
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leukemia
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subtype
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integrase
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lymphocyte
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strand
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cd4
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efavirenz
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retroviral
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zidovudine
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drug-resistant
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infectious
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nevirapine
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retroviruses
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telomerase
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nucleic
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tenofovir
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lamivudine
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anti-hiv
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first-line
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virion
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t-cells
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surveillance
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retrotransposons
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haart
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polymerases
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proviral
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swab
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covid-19
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coronavirus
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ritonavir
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sars-cov-2
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outbreak
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telomeric
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nucleocapsid
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rna-dependent
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resistance-associated
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dntp
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treatment-naive
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hiv-positive
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moloney
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viremia
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cross-resistance
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pharmacology
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drug development
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analysis
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once-daily
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molecular biology
- 3.1.26.4
-
antiretroviral
- nucleoside
- viruses
-
nnrti
-
virological
-
hiv-infected
-
nonnucleoside
- leukemia
- subtype
-
integrase
- lymphocyte
- strand
- cd4
- efavirenz
-
retroviral
- zidovudine
-
drug-resistant
- infectious
- nevirapine
- retroviruses
- telomerase
- nucleic
- tenofovir
- lamivudine
-
anti-hiv
-
first-line
- virion
- t-cells
-
surveillance
-
retrotransposons
-
haart
- polymerases
-
proviral
-
swab
- covid-19
- coronavirus
- ritonavir
- sars-cov-2
-
outbreak
-
telomeric
-
nucleocapsid
-
rna-dependent
-
resistance-associated
- dntp
-
treatment-naive
-
hiv-positive
-
moloney
- viremia
-
cross-resistance
- pharmacology
- drug development
- analysis
-
once-daily
- molecular biology
Reaction
Endonucleolytic cleavage to a 5'-phosphomonoester =
Synonyms
Ape-RNase HII, aRNase HII, Bh ribonuclease H, BhRNase H, CtepRNH, EcRNH, endoribonuclease H, endoribonuclease H (calf thymus), ERNH, huRNaseH1, hybrid nuclease, hybrid ribonuclease, hybridase, hybridase (ribonuclease H), KOD1, LC9-RNase H1, lmo1273, LRNase HII, More, nuclease, hybrid ribo-, nuclease, ribo-, H, P32, protein ST0753, reverse transcriptase, ribonuclease H, ribonuclease H I, ribonuclease H(42), ribonuclease H(70), ribonuclease H1, ribonuclease H2, ribonuclease H3, ribonuclease HI, ribonuclease HII, ribonuclease HIII, ribonulease H1, RNA*DNA hybrid ribonucleotidohydrolase, RNA*DNA hybrid ribonucleotiohydrolase, RNase H, RNase H type 2, RNase H(35), RNase H1, RNase H2, RNase H3, RNase HI, RNase HII, RNase HIII, RNaseH, Rnaseh1, RNASEH2A, RNH, RNH1, RNH2, rnhA, RnhB, rnhC, rnhD, Rv2228c, ST0519, STK_07530, Sto-RNase HI, T4 RNase H, Tk-RNase HII, Tk-Tk-RNase HII, TK0805, TRNH, TthRNH, Ty1 reverse transcriptase/RNase H, type 1 ribonuclease H, type 1 RNase H, type 2 ribonuclease H, type 2 RNase H, type II ribonuclease H
ECTree
3.1.26.4 ribonuclease HAdvanced search results
results (
results (Subunits
Subunits on EC 3.1.26.4 - ribonuclease H
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
heterotrimer
arrangement of subunits to form an enzymatically active complex, structure of the heterotrimeric RNase H2 complex, overview
monomer
trimer
additional information
?
x * 53000, about, enzyme precursor, sequence calculation, x * 49000, processed enzyme, SDS-PAGE
?
x * 53000, about, enzyme precursor, sequence calculation, x * 49000, processed enzyme, SDS-PAGE
?
x * 18000, recombinant His10-tagged enzyme, SDS-PAGE
dimer
RNases H act as dimers, with two Mg2+ or other divalent cations being essential for correct protein structure, stability and enzyme activity
dimer
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RNases H act as dimers, with two Mg2+ or other divalent cations being essential for correct protein structure, stability and enzyme activity
dimer
-
RNases H act as dimers, with two Mg2+ or other divalent cations being essential for correct protein structure, stability and enzyme activity
dimer
-
RNases H act as dimers, with two Mg2+ or other divalent cations being essential for correct protein structure, stability and enzyme activity
monomer
1 * 33734, amino acid sequence calculation, 1 * 36000, recombinant enzyme, SDS-PAGE
monomer
enzyme is composed of five alpha-helices (A to E) and five beta-strands (I to V). The intermediate mimic is a monomer
trimer
heterotrimer of subunits H2A, H2B, H2C, SDS-PAGE and gel filtration
trimer
heterotrimeric complex of the RNase H2A, RNase H2B, and RNase H2C proteins, crystallization data
additional information
-
polypeptides B and D found in the most purified fractions are shown to be generated during the early steps of the purification, are shown to be generated during the early steps of the purification procedure, suggesting specific protein nicking which does not affect the native molecular weight of the enzyme
additional information
-
identification and analysis of folding core and flexible regions, which are evolutionary conserved important for catalysis, conserved quantitative stability/flexibility relationships, QSFR, overview
additional information
-
the enzyme shows a mixed beta-sheet with asymmetric alpha helices, and contains the C-helix, or basic loop, structure comparisons, overview
additional information
the enzyme contains a TBP-like substrate-binding domain at the N terminus
additional information
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the enzyme contains a TBP-like substrate-binding domain at the N terminus
additional information
RNase HIII consists of the N-terminal domain and C-terminal RNase H domain, the enzyme contains a TBP-like substrate-binding domain at the N terminus
additional information
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RNase HIII consists of the N-terminal domain and C-terminal RNase H domain, the enzyme contains a TBP-like substrate-binding domain at the N terminus
additional information
Halalkalibacterium halodurans
modeling and analysis of mutant enzymes structures with bound DNA/RNA hybrid substrates, overview
additional information
Halalkalibacterium halodurans
secondary enzyme structure analysis, overview. Structures and dynamics of apo state of the RNase H enzyme and DNA-RNA hybrid
additional information
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RNase H1 contains an N-terminal domain known as dsRHbd for binding both dsRNA and RNA/DNA hybrid
additional information
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the enzyme shows a mixed beta-sheet with asymmetric alpha helices, and contains the C-helix, or basic loop, structure comparisons, overview
additional information
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the RNase HII contains a regulatory C-terminal tail. The C-terminus might form a short alpha-helix in which two residues, I195 and L196, are essential for the cleavage activity. The C-terminal alpha-helix is likely involved in the Mn2+-dependent substrate cleavage activity through stabilization of a flexible loop structure
additional information
Tma-RNase HI contains a hybrid binding domain at the N-terminal region. Analysis for interaction between the C-terminal and the hybrid binding domains, overview
additional information
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determination of the stability of residues in different secondary structures, alpha-helices and beta-strands, of the enzyme, comparison of experimental and computational data, correlation of stability in alpha-helices and beta-strands
additional information
-
three-dimensional structure of wild-type enzyme
additional information
-
identification and analysis of folding core and flexible regions, which are evolutionary conserved important for catalysis, conserved quantitative stability/flexibility relationships, QSFR, overview
additional information
-
domain organization, the nuclear targeting, which also binds RNA, and the catalytic domains are localized distinctly to the N-terminal and C-terminal parts bound by a spacer domain
