ID RNC_ECOLI Reviewed; 226 AA. AC P0A7Y0; P05797; P06141; Q2MAG3; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 27-MAR-2024, entry version 144. DE RecName: Full=Ribonuclease 3; DE EC=3.1.26.3; DE AltName: Full=Ribonuclease III; DE Short=RNase III; GN Name=rnc; OrderedLocusNames=b2567, JW2551; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS AN ENDORIBONUCLEASE, AND RP MUTAGENESIS OF GLY-44. RC STRAIN=K12; RX PubMed=3903434; DOI=10.1007/bf00397981; RA Nashimoto H., Uchida H.; RT "DNA sequencing of the Escherichia coli ribonuclease III gene and its RT mutations."; RL Mol. Gen. Genet. 201:25-29(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12 / CS520; RX PubMed=3895158; DOI=10.1093/nar/13.13.4677; RA March P.E., Ahnn J., Inouye M.; RT "The DNA sequence of the gene (rnc) encoding ribonuclease III of RT Escherichia coli."; RL Nucleic Acids Res. 13:4677-4685(1985). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RA Nashimoto H., Saito N.; RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45, DISRUPTION PHENOTYPE, AND OPERON RP STRUCTURE. RC STRAIN=K12 / W3110; RX PubMed=2540151; DOI=10.1128/jb.171.5.2581-2590.1989; RA Takiff H.E., Chen S.M., Court D.L.; RT "Genetic analysis of the rnc operon of Escherichia coli."; RL J. Bacteriol. 171:2581-2590(1989). RN [7] RP PROTEIN SEQUENCE OF 1-30, MRNA PROCESSING, AND ATP-BINDING. RC STRAIN=K12 / W3110; RX PubMed=2105934; DOI=10.1016/s0021-9258(19)39884-9; RA Chen S.M., Takiff H.E., Barber A.M., Dubois G.C., Bardwell J.C., RA Court D.L.; RT "Expression and characterization of RNase III and Era proteins. Products of RT the rnc operon of Escherichia coli."; RL J. Biol. Chem. 265:2888-2895(1990). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 211-226. RX PubMed=3097637; DOI=10.1073/pnas.83.23.8849; RA Ahnn J., March P.E., Takiff H.E., Inouye M.; RT "A GTP-binding protein of Escherichia coli has homology to yeast RAS RT proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 83:8849-8853(1986). RN [9] RP FUNCTION AS A DS-RNA SPECIFIC ENDORIBONUCLEASE, SUBCELLULAR LOCATION, AND RP ASSOCIATION WITH RIBOSOMES. RC STRAIN=K12 / K38 / S26; RX PubMed=4865702; DOI=10.1016/s0021-9258(18)99327-0; RA Robertson H.D., Webster R.E., Zinder N.D.; RT "Purification and properties of ribonuclease III from Escherichia coli."; RL J. Biol. Chem. 243:82-91(1968). RN [10] RP FUNCTION IN ENTEROBACTERIA PHAGE T7 RNA PROCESSING, FUNCTION IN PROCESSING RP OF RRNA, AND DISRUPTION PHENOTYPE. RC STRAIN=K12 / A19; RX PubMed=4587248; DOI=10.1073/pnas.70.12.3296; RA Dunn J.J., Studier F.W.; RT "T7 early RNAs and Escherichia coli ribosomal RNAs are cut from large RT precursor RNAs in vivo by ribonuclease 3."; RL Proc. Natl. Acad. Sci. U.S.A. 70:3296-3300(1973). RN [11] RP FUNCTION AS A DS-RNA SPECIFIC ENDORIBONUCLEASE, AND CATALYTIC ACTIVITY. RC STRAIN=K12 / D10; RX PubMed=4592261; DOI=10.1016/s0021-9258(19)42977-3; RA Crouch R.J.; RT "Ribonuclease 3 does not degrade deoxyribonucleic acid-ribonucleic acid RT hybrids."; RL J. Biol. Chem. 249:1314-1316(1974). RN [12] RP FUNCTION IN PROCESSING OF RRNA. RX PubMed=4610145; DOI=10.1016/0022-2836(74)90350-7; RA Nikolaev N., Schlessinger D., Wellauer P.K.; RT "30 S pre-ribosomal RNA of Escherichia coli and products of cleavage by RT ribonuclease III: length and molecular weight."; RL J. Mol. Biol. 86:741-747(1974). RN [13] RP FUNCTION IN PROCESSING OF RRNA, COFACTOR, AND SUBUNIT. RX PubMed=932008; DOI=10.1016/s0021-9258(17)33416-6; RA Dunn J.J.; RT "RNase III cleavage of single-stranded RNA. Effect of ionic strength on the RT fideltiy of cleavage."; RL J. Biol. Chem. 251:3807-3814(1976). RN [14] RP ROLE IN PROTEIN SYNTHESIS. RX PubMed=6159890; DOI=10.1016/0006-291x(80)90060-1; RA Gitelman D.R., Apirion D.; RT "The synthesis of some proteins is affected in RNA processing mutants of RT Escherichia coli."; RL Biochem. Biophys. Res. Commun. 96:1063-1070(1980). RN [15] RP DISRUPTION PHENOTYPE. RX PubMed=6364133; DOI=10.1073/pnas.81.1.185; RA King T.C., Sirdeshmukh R., Schlessinger D.; RT "RNase III cleavage is obligate for maturation but not for function of RT Escherichia coli pre-23S rRNA."; RL Proc. Natl. Acad. Sci. U.S.A. 81:185-188(1984). RN [16] RP FUNCTION IN PROCESSING OF TRNA. RX PubMed=2481042; DOI=10.1016/0022-2836(89)90331-8; RA Regnier P., Grunberg-Manago M.; RT "Cleavage by RNase III in the transcripts of the met Y-nus-A-infB operon of RT Escherichia coli releases the tRNA and initiates the decay of the RT downstream mRNA."; RL J. Mol. Biol. 210:293-302(1989). RN [17] RP FUNCTION IN PROCESSING OF MRNA, AND INDUCTION. RX PubMed=2085545; DOI=10.1016/0300-9084(90)90192-j; RA Regnier P., Grunberg-Manago M.; RT "RNase III cleavages in non-coding leaders of Escherichia coli transcripts RT control mRNA stability and genetic expression."; RL Biochimie 72:825-834(1990). RN [18] RP ROLE IN EXCISION OF INTERVENING SEQUENCES. RC STRAIN=N2076; RX PubMed=2406020; DOI=10.1016/0092-8674(90)90592-3; RA Burgin A.B., Parodos K., Lane D.J., Pace N.R.; RT "The excision of intervening sequences from Salmonella 23S ribosomal RNA."; RL Cell 60:405-414(1990). RN [19] RP MUTAGENESIS OF GLY-44 AND GLU-117, AND DISRUPTION PHENOTYPE. RC STRAIN=K12 / W3110; RX PubMed=9632264; DOI=10.1046/j.1365-2958.1998.00828.x; RA Dasgupta S., Fernandez L., Kameyama L., Inada T., Nakamura Y., Pappas A., RA Court D.L.; RT "Genetic uncoupling of the dsRNA-binding and RNA cleavage activities of the RT Escherichia coli endoribonuclease RNase III--the effect of dsRNA binding on RT gene expression."; RL Mol. Microbiol. 28:629-640(1998). RN [20] RP INDUCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=K12 / W3110; RX PubMed=9515700; DOI=10.1046/j.1365-2958.1998.00719.x; RA Britton R.A., Powell B.S., Dasgupta S., Sun Q., Margolin W., Lupski J.R., RA Court D.L.; RT "Cell cycle arrest in Era GTPase mutants: a potential growth rate-regulated RT checkpoint in Escherichia coli."; RL Mol. Microbiol. 27:739-750(1998). RN [21] RP SUBSTRATE SPECIFICITY. RX PubMed=9742248; DOI=10.1093/nar/26.19.4446; RA Conrad C., Rauhut R., Klug G.; RT "Different cleavage specificities of RNases III from Rhodobacter capsulatus RT and Escherichia coli."; RL Nucleic Acids Res. 26:4446-4453(1998). RN [22] RP COFACTOR, MUTAGENESIS OF GLU-117, AND CATALYTIC MODEL. RX PubMed=11305928; DOI=10.1021/bi010022d; RA Sun W., Nicholson A.W.; RT "Mechanism of action of Escherichia coli ribonuclease III. Stringent RT chemical requirement for the glutamic acid 117 side chain and Mn2+ rescue RT of the Glu117Asp mutant."; RL Biochemistry 40:5102-5110(2001). RN [23] RP MUTAGENESIS OF LEU-40. RX PubMed=11738048; DOI=10.1016/s0969-2126(01)00685-2; RA Blaszczyk J., Tropea J.E., Bubunenko M., Routzahn K.M., Waugh D.S., RA Court D.L., Ji X.; RT "Crystallographic and modeling studies of RNase III suggest a mechanism for RT double-stranded RNA cleavage."; RL Structure 9:1225-1236(2001). RN [24] RP ASSOCIATION WITH RIBOSOMES. RX PubMed=12814522; DOI=10.1186/1471-2199-4-8; RA Allas U., Liiv A., Remme J.; RT "Functional interaction between RNase III and the Escherichia coli RT ribosome."; RL BMC Mol. Biol. 4:8-8(2003). RN [25] RP MUTAGENESIS OF GLU-38; GLU-41; ASP-45; GLU-65; GLU-100 AND ASP-114. RX PubMed=15476399; DOI=10.1021/bi049258i; RA Sun W., Li G., Nicholson A.W.; RT "Mutational analysis of the nuclease domain of Escherichia coli RT ribonuclease III. Identification of conserved acidic residues that are RT important for catalytic function in vitro."; RL Biochemistry 43:13054-13062(2004). RN [26] RP ACTIVITY REGULATION, COFACTOR, AND CATALYTIC MODEL. RX PubMed=15699182; DOI=10.1093/nar/gki197; RA Sun W., Pertzev A., Nicholson A.W.; RT "Catalytic mechanism of Escherichia coli ribonuclease III: kinetic and RT inhibitor evidence for the involvement of two magnesium ions in RNA RT phosphodiester hydrolysis."; RL Nucleic Acids Res. 33:807-815(2005). RN [27] RP ACTIVITY REGULATION. RX PubMed=19141481; DOI=10.1101/gad.1729508; RA Kim K.S., Manasherob R., Cohen S.N.; RT "YmdB: a stress-responsive ribonuclease-binding regulator of E. coli RNase RT III activity."; RL Genes Dev. 22:3497-3508(2008). RN [28] RP FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=HT115, and TOP10; RX PubMed=23535272; DOI=10.4161/rna.24203; RA Karvelis T., Gasiunas G., Miksys A., Barrangou R., Horvath P., Siksnys V.; RT "crRNA and tracrRNA guide Cas9-mediated DNA interference in Streptococcus RT thermophilus."; RL RNA Biol. 10:841-851(2013). RN [29] RP STRUCTURE BY NMR OF 153-226, AND RNA-BINDING. RX PubMed=7628457; DOI=10.1002/j.1460-2075.1995.tb07363.x; RA Kharrat A., Macias M.J., Gibson T.J., Nilges M., Pastore A.; RT "Structure of the dsRNA binding domain of E. coli RNase III."; RL EMBO J. 14:3572-3584(1995). CC -!- FUNCTION: Digests double-stranded RNA formed within single-strand CC substrates, but not RNA-DNA hybrids. Involved in the processing of rRNA CC precursors, viral transcripts, some mRNAs and at least 1 tRNA (metY, a CC minor form of tRNA-init-Met). Cleaves the 30S primary rRNA transcript CC to yield the immediate precursors to the 16S and 23S rRNAs; cleavage CC can occur in assembled 30S, 50S and even 70S subunits and is influenced CC by the presence of ribosomal proteins. The E.coli enzyme does not CC cleave R.capsulatus rRNA precursor, although R.capsulatus will CC complement an E.coli disruption, showing substrate recognition is CC different. Removes the intervening sequences from Salmonella CC typhimurium rRNA precursor. Complements the pre-crRNA processing defect CC in an rnc deletion in S.pyogenes strain 370, although this E.coli CC strain does not have the corresponding CRISPR locus (strain TOP10) CC (PubMed:23535272). {ECO:0000269|PubMed:2085545, CC ECO:0000269|PubMed:23535272, ECO:0000269|PubMed:2406020, CC ECO:0000269|PubMed:2481042, ECO:0000269|PubMed:3903434, CC ECO:0000269|PubMed:4587248, ECO:0000269|PubMed:4592261, CC ECO:0000269|PubMed:4610145, ECO:0000269|PubMed:4865702, CC ECO:0000269|PubMed:6159890, ECO:0000269|PubMed:932008}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3; CC Evidence={ECO:0000269|PubMed:4592261}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:11305928, ECO:0000269|PubMed:15699182, CC ECO:0000269|PubMed:932008}; CC Note=Divalent metal cations, preferably Mg(2+). While only 1 Mg(2+) is CC detected by crystallography, other evidence indicates there may be more CC than 1 metal necessary for catalysis. Binding of the second metal my be CC promoted by substrate binding. {ECO:0000269|PubMed:11305928, CC ECO:0000269|PubMed:15699182, ECO:0000269|PubMed:932008}; CC -!- ACTIVITY REGULATION: Non-competitively inhibited by 2-hydroxy-4H- CC isoquinoline-1,3-dione. Activity is down-regulated during cold shock by CC direct interaction with YmdB. Also down-regulated during entry into CC stationary phase by an YmdB-independent mechanism. CC {ECO:0000269|PubMed:15699182, ECO:0000269|PubMed:19141481}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:932008}. CC -!- INTERACTION: CC P0A7Y0; P30850: rnb; NbExp=2; IntAct=EBI-557336, EBI-557325; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:4865702}. CC Note=Loosely associated with ribosomes. CC -!- INDUCTION: Expression increases as the growth rate increases. Encoded CC in the rnc-era-recO operon. Processes the 5' end of its own transcript CC leading to mRNA instability. {ECO:0000269|PubMed:2085545, CC ECO:0000269|PubMed:9515700}. CC -!- DISRUPTION PHENOTYPE: Slower than wild-type growth. Transient CC accumulation of the 30S rRNA precursor occurs; 90% of 16S rRNA is CC correctly processed while an extended version of 23S rRNA accumulates CC in the ribosome. Half-life of a number of RNase III processed CC transcripts increases. In the absence of era and rnc there is a defect CC in chromosome partitioning. In strain HT115, loss of immunity against a CC plasmid with homology to CRISPR spacer sequences (PubMed:23535272). CC {ECO:0000269|PubMed:23535272, ECO:0000269|PubMed:2540151, CC ECO:0000269|PubMed:4587248, ECO:0000269|PubMed:6364133, CC ECO:0000269|PubMed:9515700, ECO:0000269|PubMed:9632264}. CC -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000305}. CC -!- CAUTION: The original rnc-105 mutation is described as G44->D but the CC nucleotide sequence given indicates G44->S (PubMed:3903434). A later CC paper calls the same mutation G45->K (PubMed:9632264), which alters the CC residue and mutation. {ECO:0000305|PubMed:3903434, CC ECO:0000305|PubMed:9632264}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X02946; CAA26692.1; -; Genomic_DNA. DR EMBL; X02673; CAA26504.1; -; Genomic_DNA. DR EMBL; D64044; BAA10914.1; -; Genomic_DNA. DR EMBL; U36841; AAA79829.1; -; Genomic_DNA. DR EMBL; U00096; AAC75620.1; -; Genomic_DNA. DR EMBL; AP009048; BAE76743.1; -; Genomic_DNA. DR EMBL; M26415; AAA21843.1; -; Genomic_DNA. DR EMBL; M14658; AAA03241.1; -; Unassigned_DNA. DR PIR; F65034; NREC3. DR RefSeq; NP_417062.1; NC_000913.3. DR RefSeq; WP_001068343.1; NZ_STEB01000011.1. DR PDB; 7R97; X-ray; 1.80 A; A/B=1-226. DR PDBsum; 7R97; -. DR AlphaFoldDB; P0A7Y0; -. DR SMR; P0A7Y0; -. DR BioGRID; 4260597; 62. DR BioGRID; 851372; 1. DR DIP; DIP-48223N; -. DR IntAct; P0A7Y0; 6. DR STRING; 511145.b2567; -. DR jPOST; P0A7Y0; -. DR PaxDb; 511145-b2567; -. DR EnsemblBacteria; AAC75620; AAC75620; b2567. DR GeneID; 83579887; -. DR GeneID; 947033; -. DR KEGG; ecj:JW2551; -. DR KEGG; eco:b2567; -. DR PATRIC; fig|1411691.4.peg.4167; -. DR EchoBASE; EB0850; -. DR eggNOG; COG0571; Bacteria. DR HOGENOM; CLU_000907_1_1_6; -. DR InParanoid; P0A7Y0; -. DR OMA; LTHKSCK; -. DR OrthoDB; 9805026at2; -. DR PhylomeDB; P0A7Y0; -. DR BioCyc; EcoCyc:EG10857-MONOMER; -. DR BioCyc; MetaCyc:EG10857-MONOMER; -. DR BRENDA; 3.1.26.3; 2026. DR PRO; PR:P0A7Y0; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central. DR GO; GO:0019899; F:enzyme binding; IPI:EcoCyc. DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc. DR GO; GO:0042803; F:protein homodimerization activity; IPI:EcoCyc. DR GO; GO:0004525; F:ribonuclease III activity; IDA:EcoCyc. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006397; P:mRNA processing; IMP:EcoCyc. DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central. DR GO; GO:0006396; P:RNA processing; IMP:EcoCyc. DR GO; GO:0006364; P:rRNA processing; IMP:EcoCyc. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. DR CDD; cd10845; DSRM_RNAse_III_family; 1. DR CDD; cd00593; RIBOc; 1. DR Gene3D; 3.30.160.20; -; 1. DR Gene3D; 1.10.1520.10; Ribonuclease III domain; 1. DR HAMAP; MF_00104; RNase_III; 1. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR011907; RNase_III. DR InterPro; IPR000999; RNase_III_dom. DR InterPro; IPR036389; RNase_III_sf. DR NCBIfam; TIGR02191; RNaseIII; 1. DR PANTHER; PTHR11207:SF0; RIBONUCLEASE 3; 1. DR PANTHER; PTHR11207; RIBONUCLEASE III; 1. DR Pfam; PF00035; dsrm; 1. DR Pfam; PF14622; Ribonucleas_3_3; 1. DR SMART; SM00358; DSRM; 1. DR SMART; SM00535; RIBOc; 1. DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1. DR SUPFAM; SSF69065; RNase III domain-like; 1. DR PROSITE; PS50137; DS_RBD; 1. DR PROSITE; PS00517; RNASE_3_1; 1. DR PROSITE; PS50142; RNASE_3_2; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; KW Endonuclease; Hydrolase; Magnesium; Metal-binding; mRNA processing; KW Nuclease; Nucleotide-binding; Reference proteome; RNA-binding; KW rRNA processing; rRNA-binding; tRNA processing. FT CHAIN 1..226 FT /note="Ribonuclease 3" FT /id="PRO_0000180395" FT DOMAIN 6..128 FT /note="RNase III" FT DOMAIN 155..225 FT /note="DRBM" FT ACT_SITE 45 FT /evidence="ECO:0000255" FT ACT_SITE 117 FT /evidence="ECO:0000305" FT BINDING 41 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000305" FT BINDING 114 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 117 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000305" FT MUTAGEN 38 FT /note="E->A: Reduced affinity for Mg(2+), no catalytic FT defect at 10 mMMg(2+)." FT /evidence="ECO:0000269|PubMed:15476399" FT MUTAGEN 40 FT /note="L->G,D,R: Loss of activity." FT /evidence="ECO:0000269|PubMed:11738048" FT MUTAGEN 40 FT /note="L->M,W: No effect." FT /evidence="ECO:0000269|PubMed:11738048" FT MUTAGEN 41 FT /note="E->A: Reduced affinity for Mg(2+), catalytic defect. FT 85-fold reduced affinity for Mg(2+); when associated with FT A-114." FT /evidence="ECO:0000269|PubMed:15476399" FT MUTAGEN 44 FT /note="G->S: In rnc-105; slower growth, loss of RNase FT activity." FT /evidence="ECO:0000269|PubMed:3903434, FT ECO:0000269|PubMed:9632264" FT MUTAGEN 45 FT /note="D->A,E,N: 30000-fold reduction in catalytic FT efficiency, binds RNA normally. Partially rescued by FT Mn(2+)." FT /evidence="ECO:0000269|PubMed:15476399" FT MUTAGEN 65 FT /note="E->A: Reduced affinity for Mg(2+), no catalytic FT defect at 10 mMMg(2+)." FT /evidence="ECO:0000269|PubMed:15476399" FT MUTAGEN 100 FT /note="E->A: Reduced affinity for Mg(2+) and RNA." FT /evidence="ECO:0000269|PubMed:15476399" FT MUTAGEN 114 FT /note="D->A: Reduced affinity for Mg(2+), no catalytic FT defect at 10 mMMg(2+). 85-fold reduced affinity for Mg(2+); FT when associated with A-41." FT /evidence="ECO:0000269|PubMed:15476399" FT MUTAGEN 117 FT /note="E->D: Nearly complete loss of RNase activity, still FT binds RNA. Partially rescued by Mn(2+)." FT /evidence="ECO:0000269|PubMed:11305928, FT ECO:0000269|PubMed:9632264" FT MUTAGEN 117 FT /note="E->K: In rnc70; slower growth, loss of RNase FT activity. Dominant over wild-type. Binds ds-RNA." FT /evidence="ECO:0000269|PubMed:11305928, FT ECO:0000269|PubMed:9632264" FT MUTAGEN 117 FT /note="E->Q: Loss of RNase activity, still binds RNA." FT /evidence="ECO:0000269|PubMed:11305928, FT ECO:0000269|PubMed:9632264" FT CONFLICT 168..195 FT /note="HLPLPTYLVVQVRGEAHDQEFTIHCQVS -> PSAAADLSGSPGTWSKRTIR FT NLLSTARSV (in Ref. 2; CAA26504)" FT /evidence="ECO:0000305" FT HELIX 3..13 FT /evidence="ECO:0007829|PDB:7R97" FT HELIX 20..26 FT /evidence="ECO:0007829|PDB:7R97" FT TURN 30..32 FT /evidence="ECO:0007829|PDB:7R97" FT HELIX 38..59 FT /evidence="ECO:0007829|PDB:7R97" FT HELIX 65..76 FT /evidence="ECO:0007829|PDB:7R97" FT HELIX 78..87 FT /evidence="ECO:0007829|PDB:7R97" FT HELIX 90..93 FT /evidence="ECO:0007829|PDB:7R97" FT HELIX 98..101 FT /evidence="ECO:0007829|PDB:7R97" FT TURN 102..104 FT /evidence="ECO:0007829|PDB:7R97" FT HELIX 105..107 FT /evidence="ECO:0007829|PDB:7R97" FT HELIX 109..126 FT /evidence="ECO:0007829|PDB:7R97" FT HELIX 129..139 FT /evidence="ECO:0007829|PDB:7R97" FT HELIX 141..146 FT /evidence="ECO:0007829|PDB:7R97" FT HELIX 151..153 FT /evidence="ECO:0007829|PDB:7R97" FT HELIX 156..166 FT /evidence="ECO:0007829|PDB:7R97" FT STRAND 173..182 FT /evidence="ECO:0007829|PDB:7R97" FT STRAND 185..193 FT /evidence="ECO:0007829|PDB:7R97" FT STRAND 201..207 FT /evidence="ECO:0007829|PDB:7R97" FT HELIX 208..222 FT /evidence="ECO:0007829|PDB:7R97" SQ SEQUENCE 226 AA; 25550 MW; D9E2858F2E0AA3A5 CRC64; MNPIVINRLQ RKLGYTFNHQ ELLQQALTHR SASSKHNERL EFLGDSILSY VIANALYHRF PRVDEGDMSR MRATLVRGNT LAELAREFEL GECLRLGPGE LKSGGFRRES ILADTVEALI GGVFLDSDIQ TVEKLILNWY QTRLDEISPG DKQKDPKTRL QEYLQGRHLP LPTYLVVQVR GEAHDQEFTI HCQVSGLSEP VVGTGSSRRK AEQAAAEQAL KKLELE //