Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.26.3 - ribonuclease III and Organism(s) Thermotoga maritima and UniProt Accession Q9X0I6

for references in articles please use BRENDA:EC3.1.26.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.26 Endoribonucleases producing 5'-phosphomonoesters
                3.1.26.3 ribonuclease III
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Thermotoga maritima
UNIPROT: Q9X0I6 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Thermotoga maritima
The enzyme appears in selected viruses and cellular organisms
Synonyms
dicer, dicer1, drosha, dicer-2, rnt1p, ribonuclease iii, dicer-1, rnase d, dcr-1, rnase3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ribonuclease III
-
HCS protein
-
-
-
-
nuclease, ribo-, D
-
-
-
-
p241
-
-
-
-
ribonuclease D
-
-
-
-
ribonuclease III
-
-
RNase D
-
-
-
-
RNase III
-
-
RNase O
-
-
-
-
Tm-RNase III
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Endonucleolytic cleavage to a 5'-phosphomonoester
show the reaction diagram
catalytic mechanism, overview. The enzyme activates water as a nucleophile to hydrolyze target site phosphodiesters, creating 3'-hydroxyl, 5'-phosphomonoester product termini
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
78413-14-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
double-stranded RNA + H2O
5'-phosphooligonucleotides
show the reaction diagram
-
-
-
?
double-stranded RNA + H2O
5'-phosphooligonucleotides
show the reaction diagram
-
responsible for processing of dsRNA
small duplex products of 10-18 base pairs
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
double-stranded RNA + H2O
5'-phosphooligonucleotides
show the reaction diagram
-
responsible for processing of dsRNA
small duplex products of 10-18 base pairs
-
?
additional information
?
-
processing of dsRNA
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
less effective than Mg2+
Mg2+
-
activates optimally at 1 mM
Mn2+
-
less effective than Mg2+
Ni2+
-
less effective than Mg2+
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 70
-
RNase III catalytic activity exhibits a broad optimal temperature range
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 95
-
activity range
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the ribonuclease III (RNase III) family of divalent-metal-ion-dependent phosphodiesterases. RNase III family members share a unique fold (RNase III domain) that can dimerize to form a structure that binds dsRNA and cleaves phosphodiesters on each strand, providing the characteristic 2 nt, 3'-overhang product ends. Domain structures of ribonuclease III family polypeptides, overview
physiological function
processing of dsRNA by the enzyme is an essential step in the maturation and decay of coding and noncoding RNAs, including miRNAs and siRNAs
evolution
-
Tm-RNase III cleaves an Ec-RNase III substrate with identical specificity and is inhibited by antideterminant bp that also inhibit Ec-RNase III, indicating the conservation, across a broad phylogenetic distance, of positive and negative determinants of reactivity of bacterial RNase III substrates
physiological function
-
cleavage of double-stranded RNA by ribonuclease III is a conserved early step in bacterial rRNA maturation, mechanism of dsRNA cleavage by RNase III, overview
additional information
structure analysis and comparison to other enzyme family members, overview
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis, PDB ID 1O0W
RNA-free structure of full length RNase III, comparison with crystal structures of Aquifex aeolicus RNase-dsRNA complex indicates dramatic conformational changes upon dsRNA binding
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+ affinity column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21(DE3)rnc105,recA
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ji, X.
Structural basis for non-catalytic and catalytic activities of ribonuclease III
Acta Crystallogr. Sect. D
62
933-940
2006
Thermotoga maritima, Aquifex aeolicus (O67082), Escherichia coli (P0A7Y0), Saccharomyces cerevisiae (Q02555), Homo sapiens (Q9NRR4), Homo sapiens (Q9UPY3)
Manually annotated by BRENDA team
Meng, W.; Nicholson, R.H.; Nathania, L.; Pertzev, A.V.; Nicholson, A.W.
New approaches to understanding double-stranded RNA processing by ribonuclease III purification and assays of homodimeric and heterodimeric forms of RNase III from bacterial extremophiles and mesophiles
Methods Enzymol.
447
119-129
2008
Escherichia coli, Aquifex aeolicus (O67082), Aquifex aeolicus, Thermotoga maritima (Q9X0I6), Thermotoga maritima
Manually annotated by BRENDA team
Nathania, L.; Nicholson, A.W.
Thermotoga maritima ribonuclease III. Characterization of thermostable biochemical behavior and analysis of conserved base pairs that function as reactivity epitopes for the Thermotoga 23S rRNA precursor
Biochemistry
49
7164-7178
2010
Thermotoga maritima
Manually annotated by BRENDA team
Nicholson, A.W.
Ribonuclease III mechanisms of double-stranded RNA cleavage
Wiley Interdiscip. Rev. RNA
5
31-48
2013
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Schizosaccharomyces pombe, Giardia intestinalis (A8BQJ3), Aquifex aeolicus (O67082), Mycobacterium tuberculosis (P9WH03), Thermotoga maritima (Q9X0I6), Mycobacterium tuberculosis H37Rv (P9WH03)
Manually annotated by BRENDA team