RNC_ECOLI
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 03-AUG-2022, entry version 135.
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; Proteobacteria; 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 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; P0A7Y0; -.
DR PRIDE; P0A7Y0; -.
DR EnsemblBacteria; AAC75620; AAC75620; b2567.
DR EnsemblBacteria; BAE76743; BAE76743; BAE76743.
DR GeneID; 67416946; -.
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 PhylomeDB; P0A7Y0; -.
DR BioCyc; EcoCyc:EG10857-MON; -.
DR BioCyc; MetaCyc:EG10857-MON; -.
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:0000287; F:magnesium ion binding; IDA: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; cd00593; RIBOc; 1.
DR Gene3D; 1.10.1520.10; -; 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 PANTHER; PTHR11207; PTHR11207; 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; SSF69065; SSF69065; 1.
DR TIGRFAMs; TIGR02191; RNaseIII; 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 ATP-binding; Cytoplasm; Direct protein sequencing; Endonuclease; Hydrolase;
KW Magnesium; Metal-binding; mRNA processing; Nuclease; Nucleotide-binding;
KW Reference proteome; RNA-binding; rRNA processing; rRNA-binding;
KW 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 mM Mg(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 mM Mg(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 mM Mg(2+). 85-fold reduced affinity for
FT Mg(2+); 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"
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
