3.1.13.1: exoribonuclease II
This is an abbreviated version!
For detailed information about exoribonuclease II, go to the full flat file.
Word Map on EC 3.1.13.1
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3.1.13.1
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dnase
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nucleic
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pancreatic
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strand
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single-stranded
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endoribonuclease
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viruses
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polynucleotide
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endonuclease
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polyadenylation
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duplex
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polya
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ribonucleoproteins
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transcriptase
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rna-binding
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circrnas
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exosome
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phosphorylase
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chemokine
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dsrnas
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tata
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virion
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rpa
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nucleases
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stem-loops
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actinomycin
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helicase
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endonucleolytic
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dicer
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phosphodiester
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rna-dependent
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pronase
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intermedius
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oligoadenylate
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riboprobes
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rna-protein
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nucleolar
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ribozyme
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3'-terminal
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angiogenin
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argonaute
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encapsidation
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rna-induced
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pre-rrnas
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rna-dna
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antitoxin
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mip-1alpha
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snrnp
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medicine
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drosha
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degradation
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analysis
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norovirus
- 3.1.13.1
- dnase
- nucleic
- pancreatic
- strand
-
single-stranded
-
endoribonuclease
- viruses
- polynucleotide
- endonuclease
-
polyadenylation
- duplex
- polya
- ribonucleoproteins
- transcriptase
-
rna-binding
-
circrnas
-
exosome
- phosphorylase
- chemokine
- dsrnas
- tata
- virion
- rpa
- nucleases
-
stem-loops
- actinomycin
- helicase
-
endonucleolytic
- dicer
-
phosphodiester
-
rna-dependent
- pronase
- intermedius
- oligoadenylate
-
riboprobes
-
rna-protein
-
nucleolar
-
ribozyme
-
3'-terminal
-
angiogenin
-
argonaute
-
encapsidation
-
rna-induced
- pre-rrnas
- rna-dna
- antitoxin
-
mip-1alpha
-
snrnp
- medicine
- drosha
- degradation
- analysis
- norovirus
Reaction
Exonucleolytic cleavage in the 3'- to 5'- direction to yield nucleoside 5'-phosphates =
Synonyms
3'-5'exoribonuclease, 3’-5’exoribonuclease, 5'->3' exoribonuclease 2, AB205_0003320, Dis, Dis3, EC 3.1.4.20, exonuclease ISG20, More, PfRNase II, RC-RNase 2, ribonuclease 2, ribonuclease II, ribonuclease Q, Ribonuclease R, RNase, RNase 2, RNase A, RNase II, RNase R, RNase-2, RNaseR, Rnb, RNR, RNR1, Rrp44, XRN2
ECTree
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Crystallization
Crystallization on EC 3.1.13.1 - exoribonuclease II
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three RNA-binding domains come together to form a clamp-like assembly, which can only accommodate single stranded RNA. This leads into a narrow, basic channel that ends at the putative catalytic center that is completely enclosed within the body of the protein. The putative path for RNA agrees well with biochemical data indicating that a 3' single strand overhang of 7-10 nt is necessary for binding and hydrolysis by RNase II. The presence of the clamp and the narrow channel provides an explanation for the processivity of RNase II and for why its action is limited to single stranded RNA
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Rrp44 in complex with single-stranded RNA, to 2.3 A resolution. Structure of Rrp44 displays CSD1, CSD2, RNB, and S1 domains. The two N-terminal cold shock domains (CSD1, residues 271-399; CSD2, residues 400-475) and the C-terminal S1 domain (residues 911-998) display characteristic OB folds, with five antiparallel beta strands organized in a beta barrel structure. CSD1 is fused to an N-terminal alpha helix (residues 261-268) and the S1 domain has an insertion of three beta strands (between beta3 and beta4) as compared to a standard OB fold. The RNB domain is centered around a core and is surrounded by several alpha helices