2.7.7.8: polyribonucleotide nucleotidyltransferase
This is an abbreviated version!
For detailed information about polyribonucleotide nucleotidyltransferase, go to the full flat file.
Word Map on EC 2.7.7.8
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2.7.7.8
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rnase
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exoribonuclease
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polya
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ribonuclease
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polymerization
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polyadenylation
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phosphorolysis
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degradosome
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helicase
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exonuclease
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exonucleolytic
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stem-loop
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luteus
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micrococcus
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5'-diphosphate
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rna-binding
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kh
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hfq
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oligoribonucleotides
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rna-degrading
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heteropolymeric
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antibioticus
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dead-box
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lysodeikticus
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primer-independent
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synthesis
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molecular biology
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medicine
- 2.7.7.8
- rnase
- exoribonuclease
- polya
- ribonuclease
- polymerization
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polyadenylation
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phosphorolysis
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degradosome
- helicase
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exonuclease
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exonucleolytic
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stem-loop
- luteus
- micrococcus
- 5'-diphosphate
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rna-binding
- kh
- hfq
- oligoribonucleotides
-
rna-degrading
-
heteropolymeric
- antibioticus
-
dead-box
- lysodeikticus
-
primer-independent
- synthesis
- molecular biology
- medicine
Reaction
Synonyms
AtcpPNPase, AtmtPNPase, chloroplast PNPase, cpPNPase, hPNPase(old-35), hPNPaseold-35, nucleoside diphosphate:polynucleotidyl transferase, nucleotidyltransferase, polyribonucleotide, PNP, PNPase, PNPT1, polynucleotide phosphorylase, polyribonucleotide phosphorylase, RNase PH
ECTree
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Subunits
Subunits on EC 2.7.7.8 - polyribonucleotide nucleotidyltransferase
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dimer
homotrimer
monomer
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domain organization of the enzyme monomer, homology modeling with KH domain and S1 domain, overview
tetramer
trimer
additional information
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alpha3,beta2 or alpha3,betan, x * 86000 + x * 48000, enzyme form B is obtained by keeping the ionic strength at 200 mM during purification on Sephadex G-200, at lower salt concentrations the beta subunit tends to dissociate and the enzyme reverts to the A form
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x * 71000, enzyme form T, enzyme form I shows several bands of different molecular sizes, SDS-PAGE
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the enzyme has a ring-like, trimeric architecture that creates a central channel where phosphorolytic active sites reside. One face of the ring is decorated with RNA-binding K-homology (KH) and S1 domains, domain organization with modular organization of conserved structural domains, overview
trimer
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the enzyme has a ring-like, trimeric architecture that creates a central channel where phosphorolytic active sites reside. One face of the ring is decorated with RNA-binding K-homology (KH) and S1 domains, domain organization with modular organization of conserved structural domains, overview
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trimer
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alpha3, 3 * 84000-95000, enzyme form A, ultrastructural observations
trimer
3 * 80900, about, sequence calculation, the trimeric hPNPase has a hexameric ring-like structure formed by six RNase PH domains, capped with a trimeric KH pore, the enzyme has a conserved GXXG motif in the KH domain, structural model of hPNPase, overview
trimer
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3 * 92000, SDS-PAGE, prior to purification the enzyme exists in oligomeric forms
enzyme domains within residues 158-262 and 473-577 contain interaction sites for RNase E within a betabetaalphabetabetaalpha domain configuration
additional information
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enzyme domains within residues 158-262 and 473-577 contain interaction sites for RNase E within a betabetaalphabetabetaalpha domain configuration
additional information
enzyme interacts with AKT kinase coactivator TCL1. The AKT interaction domain on TCL1 binds either Rnase PH repeat domain on PNPase without influencing its RNA degrading activity
additional information
polyribonucleotide phosphorylase interacts with AKT kinase coactivator TCL1. The AKT interaction domain on TCL1 binds either polyribonucleotide phosphorylase PH repeat domain without influencing its RNA degrading activity, compatible with predicted docking models for a TCL1-PNPase complex
additional information
domain organization of full-length and S1 domain-truncated hPNPase. overview
additional information
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domain organization of full-length and S1 domain-truncated hPNPase. overview
additional information
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two conserved catalytic RNase PH regions, are present at the N-terminus of the enzyme