Ribonuclease
Has ribonuclease activity towards yeast tRNA, polyadenine, polycytosine and polyguanine, but lacks ribonuclease activity against polyuracil. Has antiproliferative activity towards L1210 tumor cell line with an IC(50) of 41 uM. Lacks mitogenic activity towards murine splenocytes and does not inhibit HIV-1 reverse transcriptase.
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Ribonuclease 1
Ribonuclease 2
Ribonuclease 2B
Ear5:
Molecular Function: endonuclease activity; ribonuclease activity
Ribonuclease 3
Ribonuclease 3 1
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Ribonuclease 3 2
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism ().
Ribonuclease 4
RNASE4: This RNase has marked specificity towards the 3' side of uridine nucleotides. Belongs to the pancreatic ribonuclease family.
Protein type: EC 3.1.27.-; Ribonuclease; Secreted; Secreted, signal peptide
Cellular Component: extracellular region
Molecular Function: endonuclease activity; ribonuclease activity
Biological Process: cellular response to starvation
Ribonuclease 7
RNASE7: Exhibits a potent RNase activity. Has broad-spectrum antimicrobial activity against many pathogenic microorganisms and remarkably potent activity (lethal dose of 90% < 30 nM) against a vancomycin resistant Enterococcus faecium. Belongs to the pancreatic ribonuclease family.
Protein type: EC 3.1.27.-; RNA-binding; Ribonuclease; Secreted; Secreted, signal peptide
Chromosomal Location of Human Ortholog: 14q11.2
Cellular Component: extracellular region
Molecular Function: endonuclease activity; lipopolysaccharide binding; peptidoglycan binding; ribonuclease activity
Biological Process: antibacterial humoral response; defense response to Gram-negative bacterium; defense response to Gram-positive bacterium; innate immune response; membrane disruption in another organism
Ribonuclease 8
Has a low ribonuclease activity.
Ribonuclease ARB_07070
This purine-specific ribonuclease cleaves 28S RNA in eukaryotic ribosomes, inhibits protein synthesis, and shows antitumor activity.
Ribonuclease BC_0920
Toxic component of a toxin-antitoxin (TA) module. The C-terminus (residues 322-545) has RNase activity which is neutralized by cognate antitoxin BC-0921, but not by antitoxins specific to other toxins with the LXG domain.
Ribonuclease BN
Zinc phosphodiesterase, which has both exoribonuclease and endoribonuclease activities.
Ribonuclease D
Exonuclease involved in the 3' processing of various precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA molecule and releases 5'-mononucleotides.
Ribonuclease DdI
Releases mononucleotides from RNA in the order of 3'-GMP > 3'-UMP > 3'-AMP > 3'-CMP.
Ribonuclease E
Endoribonuclease that plays a central role in RNA processing and decay. Plays a major role in pre-16S rRNA maturation, probably generating the mature 5'-end, and a minor role in pre-5S and pre-23S rRNA maturation.
Ribonuclease G
Involved in the processing of the 5'-end of 16S rRNA. Could be involved in chromosome segregation and cell division. It may be one of the components of the cytoplasmic axial filaments bundles or merely regulate the formation of this structure ().
Ribonuclease H
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Ribonuclease H1
RNASEH1: Endonuclease that specifically degrades the RNA of RNA- DNA hybrids. Belongs to the RNase H family.
Protein type: EC 3.1.26.4; Mitochondrial; RNA-binding; Ribonuclease
Cellular Component: mitochondrion; nucleus
Molecular Function: protein homodimerization activity; ribonuclease H activity
Biological Process: DNA replication, removal of RNA primer; mitochondrial DNA replication
Ribonuclease H2 subunit A
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. Participates in DNA replication ().
Ribonuclease H2 subunit B
RNASEH2B: Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging- strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes. Defects in RNASEH2B are a cause of Aicardi-Goutieres syndrome type 2 (AGS2). A form of Aicardi-Goutieres syndrome, a genetically heterogeneous disease characterized by cerebral atrophy, leukoencephalopathy, intracranial calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, increased CSF alpha-interferon, and negative serologic investigations for common prenatal infection. Clinical features as thrombocytopenia, hepatosplenomegaly and elevated hepatic transaminases along with intermittent fever may erroneously suggest an infective process. Severe neurological dysfunctions manifest in infancy as progressive microcephaly, spasticity, dystonic posturing and profound psychomotor retardation. Death often occurs in early childhood. Belongs to the RNase H2 subunit B family.
Protein type: DNA replication; RNA processing
Chromosomal Location of Human Ortholog: 13q14.3
Biological Process: RNA catabolic process
Disease: Aicardi-goutieres Syndrome 2
Ribonuclease H2 subunit C
RNASEH2C: Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging- strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes. Defects in RNASEH2C are the cause of Aicardi-Goutieres syndrome type 3 (AGS3). A form of Aicardi-Goutieres syndrome, a genetically heterogeneous disease characterized by cerebral atrophy, leukoencephalopathy, intracranial calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, increased CSF alpha-interferon, and negative serologic investigations for common prenatal infection. Clinical features as thrombocytopenia, hepatosplenomegaly and elevated hepatic transaminases along with intermittent fever may erroneously suggest an infective process. Severe neurological dysfunctions manifest in infancy as progressive microcephaly, spasticity, dystonic posturing and profound psychomotor retardation. Death often occurs in early childhood. Belongs to the RNase H2 subunit C family. 2 isoforms of the human protein are produced by alternative splicing.
Protein type: DNA replication
Chromosomal Location of Human Ortholog: 11q13.1
Molecular Function: ribonuclease H activity
Biological Process: RNA catabolic process
Disease: Aicardi-goutieres Syndrome 3
Ribonuclease HI
Nuclease that specifically degrades the RNA of RNA-DNA hybrids; seems to act exonucleolytically on RNA/DNA hybrids. Endonucleolytically removes RNA primers from the Okazaki fragments of lagging strand synthesis on its own. Complements the temperature-sensitive phenotype of an E.coli double rnhA/rnhB (RNase H) disruption mutant.
Ribonuclease HII
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Ribonuclease HII 1
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Ribonuclease HII 2
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Ribonuclease HIII
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Ribonuclease I
One of the few RNases that cleaves the phosphodiester bond between any two nucleotide. Shows a preference for cytidylic or guanylic acid.
Ribonuclease II
Encodes a exoribonuclease involved in rRNA processing in mitochondria and chloroplasts.Loss of function mutations are pale green and require supplementation with sucrose for germination and early development. Plants are pale green due to defects in chloroplast biogenesis.
Ribonuclease J
Ribonuclease J 1
An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay (). Has an overlapping but not completely redundant role with RNase J2 in the decay of mRNA.
Ribonuclease J 2
An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay (). Has an overlapping but not completely redundant role with RNase J1 in the decay of mRNA.
Ribonuclease J1
An RNase that has endonuclease and 5'-3' exonuclease activity, playing a role in both rRNA and mRNA stability and degradation. Endonuclease activity can cleave within 4 nucleotides of the 5'-end of a triphosphorylated RNA. Endonuclease digestion by the RNase J1/J2 complex occurs at a different site and in some cases more efficiently than J1 or J2 alone. The exonuclease activity of the J1/J2 complex is highly processive on substrates longer than 5 nucleotides, on shorter substrates is distributive. Preferentially cleaves ssRNA, possibly in AU-rich regions. The 5'-exonuclease activity acts on 5'-hydroxyl and 5'-monophosphate but not 5'-triphosphate ends; it can digest through stem-loop structures if they are not too stable. Required for maturation of 16S rRNA. Acts preferentially on 16S rRNA precursors after association of the 30S and 50S ribosomal subunits. Plays a role in the secondary pathway of 23S rRNA 5' end maturation. Probably also participates in processing of pre-scRNA (the precursor of the signal recognition particle RNA).
Ribonuclease J2
Endonucleolytically cleaves the 5'-leader sequence of certain mRNAs. Endonuclease digestion by the RNase J1/J2 complex occurs at a different site and in some cases more efficiently than J1 or J2 alone. The exonuclease activity of the J1/J2 complex is highly processive on substrates longer than 5 nucleotides, on shorter substrates is distributive. Plays a role in mRNA maturation and stability. Appears to have a limited effect on 16S rRNA maturation, despite its similarity to RNase J1. This subunit alone has very poor 5'-3' exonuclease activity.
Ribonuclease K3
Pyrimidine specific nuclease with a preference for U.
Ribonuclease K6
May have a role in host defense.
Ribonuclease kappa
RNAse K: Endoribonuclease which preferentially cleaves ApU and ApG phosphodiester bonds. Hydrolyzes UpU bonds at a lower rate. Belongs to the RNase K family.
Protein type: EC 3.1.-.-; Membrane protein, integral; Membrane protein, multi-pass; Ribonuclease
Molecular Function: endoribonuclease activity
Biological Process: rRNA transcription
Ribonuclease kappa-B
Endoribonuclease which preferentially cleaves ApU and ApG phosphodiester bonds.
Ribonuclease M5
Required for correct processing of both the 5' and 3' ends of 5S rRNA precursor. Cleaves both sides of a double-stranded region yielding mature 5S rRNA in one step.
Ribonuclease M5 1
Required for correct processing of both the 5' and 3' ends of 5S rRNA precursor. Cleaves both sides of a double-stranded region yielding mature 5S rRNA in one step.
Ribonuclease M5 2
Required for correct processing of both the 5' and 3' ends of 5S rRNA precursor. Cleaves both sides of a double-stranded region yielding mature 5S rRNA in one step.
Ribonuclease PH
Phosphorolytic exoribonuclease that removes nucleotide residues following the -CCA terminus of tRNA and adds nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates.
Ribonuclease R
3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Ribonuclease R 1
3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Ribonuclease R 2
3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Ribonuclease T
Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis.
Ribonuclease T2
Ribonuclease T2-like
Rnase which modulates cell survival under stress conditions. Released from the vacuole to the cytoplasm during stress to promote tRNA and rRNA cleavage and to activate separately a downstream pathway that promotes cell death. Involved in cell size, vacuolar morphology and growth at high temperatures and high salt concentration ().
Ribonuclease T2-like 1-A
Rnase which modulates cell survival under stress conditions. Released from the vacuole to the cytoplasm during stress to promote tRNA and rRNA cleavage and to activate separately a downstream pathway that promotes cell death. Involved in cell size, vacuolar morphology and growth at high temperatures and high salt concentration ().
Ribonuclease T2-like 1-B
Rnase which modulates cell survival under stress conditions. Released from the vacuole to the cytoplasm during stress to promote tRNA and rRNA cleavage and to activate separately a downstream pathway that promotes cell death. Involved in cell size, vacuolar morphology and growth at high temperatures and high salt concentration ().
Ribonuclease TTHA0252
Ribonuclease TUDOR 1
RNA binding protein with nuclease activity essential for stress response. Involved in mechanisms acting on mRNAs entering the secretory pathway. Functionally redundant with TSN2.
Ribonuclease TUDOR 2
Involved in the regulation of AtGA20ox3 expression, as well as seed germination.
Ribonuclease U2
Ribonuclease UK114
Ribonuclease VapC
Toxic component of a type II toxin-antitoxin (TA) module. A sequence-specific endoribonuclease, cleavage occurs after the first AU in the consensus sequence AUA(U/A); RNA secondary structure is probably important in substrate choice. Cuts in 5' and 3' UTRs. The TA module acts as a post-transcriptional regulator of carbon metabolism; in M.smegmatis 3 TA modules (VapB-VapC, MazE-MazF and Phd-Doc) may be involved in monitoring the nutritional supply and physiological state of the cell, linking catabolic with anabolic reactions. When overexpressed inhibits cell growth, via translation; 10-fold in a wild-type strain, 100-fold in a vapB-vapC disruption mutant (PubMed:19445953). Overexpression of VapC leads to differential expression of 205 genes; many down-regulated genes are predicted to be involved in the transport and catabolism of carbohydrates, while genes involved in phosphate transport and scavenging are up-regulated. VapC is bacteriostatic, not bacteriocidal; cells are ovoid, non-replicating and have decreased transcription, becoming dormant (PubMed:24417293). Digests ssRNA but not tRNA, dsRNA, ssDNA or dsDNA. The VapB-VapC complex binds its own promoter DNA, and VapC alone binds RNA.
Ribonuclease VapC1
Toxic component of a toxin-antitoxin (TA) module. Acts as an RNase, its toxic effect is neutralized by VapB1 antitoxin ().
Ribonuclease VapC10
Toxic component of a type II toxin-antitoxin (TA) module. An RNase. The cognate antitoxin is VapB10 ().
Ribonuclease VapC11
Toxic component of a toxin-antitoxin (TA) module. Acts as an RNase. Its toxic effects on cell growth and colony formation are neutralized by coexpression with cognate antitoxin VapB11 ().
Ribonuclease VapC12
Toxic component of a type II toxin-antitoxin (TA) module. An RNase. The cognate antitoxin is VapB12 ().
Ribonuclease VapC13
Toxic component of a type II toxin-antitoxin (TA) module. An RNase. The cognate antitoxin is VapB13 ().
Ribonuclease VapC14
Toxic component of a type II toxin-antitoxin (TA) module. An RNase. The cognate antitoxin is VapB14 ().
Ribonuclease VapC15
Toxic component of a toxin-antitoxin (TA) module. An RNase. Its toxic effect is neutralized by cognate antitoxin VapB15 ().
Ribonuclease VapC16
Toxic component of a type II toxin-antitoxin (TA) module. An RNase. The cognate antitoxin is VapB16 ().
Ribonuclease VapC17
Toxic component of a toxin-antitoxin (TA) module. An RNase. The cognate antitoxin is VapB17 ().
Ribonuclease VapC18
Toxic component of a type II toxin-antitoxin (TA) module. An RNase. The cognate antitoxin is VapB18 ().
Ribonuclease VapC19
Toxic component of a type II toxin-antitoxin (TA) module. An RNase (). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB19.
Ribonuclease VapC2
Toxic component of a toxin-antitoxin (TA) module. An RNase. Its cognate antitoxin is VapB2 ().
Ribonuclease VapC21
Toxic component of a toxin-antitoxin (TA) module. An RNase. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB21 ().
Ribonuclease VapC22
Toxic component of a type II toxin-antitoxin (TA) module. An RNase (). Upon expression in M.smegmatis inhibits translation and colony formation. Its toxic effect on colony formation is neutralized by coexpression with cognate antitoxin VapB22; the effect on translation has not been tested but is probably neutralized also.
Ribonuclease VapC23
Toxic component of a toxin-antitoxin (TA) module. An RNase. The cognate antitoxin is VapB23 ().
Ribonuclease VapC24
Toxic component of a type II toxin-antitoxin (TA) module. An RNase. Its cognate antitoxin is VapB24 ().
Ribonuclease VapC25
Toxic component of a type II toxin-antitoxin (TA) module. An RNase (). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB25.
Ribonuclease VapC26
Toxic component of a type II toxin-antitoxin (TA) module. An RNase (). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB26.
Ribonuclease VapC27
Probably the toxic component of a type II toxin-antitoxin (TA) module. An RNase (). Its cognate antitoxin is VapB27.
Ribonuclease VapC28
Toxic component of a toxin-antitoxin (TA) module. An RNase. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB28 ().
Ribonuclease VapC29
Toxic component of a type II toxin-antitoxin (TA) module. Its cognate antitoxin is VapB29 (). Has ribonuclease activity.
Ribonuclease VapC3
Toxic component of a toxin-antitoxin (TA) module. An RNase. Its cognate antitoxin is VapB3 ().
Ribonuclease VapC30
Toxic component of a type II toxin-antitoxin (TA) module. An RNase (). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB30.
Ribonuclease VapC31
Toxic component of a type II toxin-antitoxin (TA) module. An RNase (). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB31 ().
Ribonuclease VapC32
Toxic component of a type II toxin-antitoxin (TA) module. An RNase (). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB32.
Ribonuclease VapC33
Toxic component of a type II toxin-antitoxin (TA) module. An RNase (). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB33.
Ribonuclease VapC35
Toxic component of a type II toxin-antitoxin (TA) module. An RNase (). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB35.
Ribonuclease VapC36
Toxic component of a type II toxin-antitoxin (TA) module. An RNase. Its cognate antitoxin is VapB36 ().
Ribonuclease VapC37
Probable toxic component of a type II toxin-antitoxin (TA) module. An RNase. Upon expression in M.smegmatis inhibits colony formation. The putative cognate antitoxin is VapB37.
Ribonuclease VapC38
Toxic component of a type II toxin-antitoxin (TA) module. An RNase. Its cognate antitoxin is VapB38 ().
Ribonuclease VapC39
Toxic component of a toxin-antitoxin (TA) module. An RNase. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB39 ().
Ribonuclease VapC4
Toxic component of a toxin-antitoxin (TA) module. An RNase. Its cognate antitoxin is VapB4 ().
Ribonuclease VapC40
Toxic component of a type II toxin-antitoxin (TA) module. An RNase (). Its cognate antitoxin is VapB40.
Ribonuclease VapC41
Toxic component of a type II toxin-antitoxin (TA) module. An RNase (). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB41.
Ribonuclease VapC42
Toxic component of a toxin-antitoxin (TA) module. An RNase. Its cognate antitoxin is VapB42 ().
Ribonuclease VapC43
Toxic component of a toxin-antitoxin (TA) module. An RNase. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB43 ().
Ribonuclease VapC44
Toxic component of a toxin-antitoxin (TA) module. An RNase. Its cognate antitoxin is VapB44 ().
Ribonuclease VapC45
Toxic component of a toxin-antitoxin (TA) module. An RNase. Its cognate antitoxin is VapB45 ().
Ribonuclease VapC46
Toxic component of a type II toxin-antitoxin (TA) module. An RNase (). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB46.
Ribonuclease VapC47
Toxic component of a toxin-antitoxin (TA) module. An RNase. Its toxic effect on colony formation is neutralized by coexpression with cognate antitoxin VapB47 ().
Ribonuclease VapC48
Toxic component of a type II toxin-antitoxin (TA) module. An RNase. Its cognate antitoxin is VapB48.
Ribonuclease VapC49
Toxic component of a type II toxin-antitoxin (TA) module. An RNase. Its cognate antitoxin is VapB49 ().
Ribonuclease VapC5
Probable toxic component of a type II toxin-antitoxin (TA) module. The cognate antitoxin is VapB5. Has limited RNase activity on substrates; activity is seen with a VapC5-VapB5 complex.
Ribonuclease VapC51
Toxic component of a type II toxin-antitoxin (TA) module. An RNase. Its cognate antitoxin is VapB51.
Ribonuclease VapC6
Toxic component of a toxin-antitoxin (TA) module. An RNase.
Ribonuclease VapC7
Toxic component of a type II toxin-antitoxin (TA) module. An RNase. The cognate antitoxin is VapB7 ().
Ribonuclease VapC8
Toxic component of a toxin-antitoxin (TA) module. An RNase. The cognate antitoxin is VapB8 ().
Ribonuclease VapC9
Toxic component of a toxin-antitoxin (TA) module. An RNase.
Ribonuclease Y
Endoribonuclease that initiates mRNA decay.
Ribonuclease Y 1
Endoribonuclease that initiates mRNA decay.
Ribonuclease Y 2
Endoribonuclease that initiates mRNA decay.
Ribonuclease YobL
Toxic component of a toxin-antitoxin (TA) module. The C-terminus (residues 449-600) has RNase activity, and inhibits growth upon expression in E.coli. In vitro RNase activity and in vivo growth inhibition are neutralized by cognate antitoxin YobK, but not by antitoxins specific to other toxins with the LXG domain.
Ribonuclease YqcG
Toxic component of a toxin-antitoxin (TA) module. The C-terminus (residues 379-531) has RNase activity, and inhibits growth upon expression in E.coli. In vitro RNase activity and in vivo growth inhibition are neutralized by cognate antitoxin YqcF, but not by antitoxins specific to other toxins with the LXG domain.
Ribonuclease YxiD
Toxic component of a toxin-antitoxin (TA) module. The C-terminus (residues 409-569) has RNase activity, and inhibits growth upon expression in E.coli. In vitro RNase activity and in vivo growth inhibition are neutralized by cognate antitoxin YxxD, but not by antitoxins specific to other toxins with the LXG domain.
Ribonuclease Z
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA (). Involved in germline proliferation. May be required for both mitosis and meiosis in germ cells.
Ribonuclease Z 1
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. May be involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Ribonuclease Z 2
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. May be involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Ribonuclease ZC3H12A
Has RNase activity and selectively degrades specific target mRNA species. Modulates the immune response and inflammation by regulating the decay of specific mRNA molecules. Recognizes the 3'-untranslated region (UTR) of the mRNA for IL6, CALCR and IL12B. Required for normal decay of IL6 mRNA. Triggers apoptosis and promotes angiogenesis in response to the binding of CCL2 to CCR2. Regulates expression of CDH12 and CHD19 ().
Ribonuclease-like 3
Ribonuclease. Angiogenic. Plays a role in host defense. Exhibits strong antibacterial activity against Gram-negative bacteria but mild antibacterial activity against Gram-positive bacteria. The RNase activity is not required for the bactericidal activity.
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