RNC_SALTY
ID RNC_SALTY Reviewed; 226 AA.
AC Q56056;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ribonuclease 3;
DE EC=3.1.26.3;
DE AltName: Full=Ribonuclease III;
DE Short=RNase III;
GN Name=rnc; OrderedLocusNames=STM2581;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TSM117;
RX PubMed=9150881; DOI=10.1016/s0300-9084(97)86726-0;
RA Anderson P.E., Matsunaga J., Simons E.L., Simons R.W.;
RT "Structure and regulation of the Salmonella typhimurium rnc-era-recO
RT operon.";
RL Biochimie 78:1025-1034(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=9503611; DOI=10.1111/j.1574-6968.1998.tb12858.x;
RA Mattatall N.R., Sanderson K.E.;
RT "RNase III deficient Salmonella typhimurium LT2 contains intervening
RT sequences (IVSs) in its 23S rRNA.";
RL FEMS Microbiol. Lett. 159:179-185(1998).
CC -!- FUNCTION: Digests double-stranded RNA. Involved in the processing of
CC ribosomal RNA transcript to yield the immediate precursors to the large
CC and small rRNAs (23S and 16S). Removes small helical intervening
CC sequences (IVSs) from all 7 of the 23S rRNA transcripts. Probably also
CC processes some mRNAs, and tRNAs when they are encoded in the rRNA
CC operon. Probably processes pre-crRNA and tracrRNA of type II CRISPR
CC loci if present in the organism.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Accumulation of full-length 23S rRNA as well as
CC larger precursor rRNA transcripts. Strain grows slower than wild-type.
CC {ECO:0000269|PubMed:9503611}.
CC -!- MISCELLANEOUS: This organism contains small helical (90-110 nucleotide)
CC intervening sequences (IVSs) in all 7 23S rRNA genes at either the 550-
CC bp or 1170-bp positions or both, accumulating the 23S rRNA as 2.4, 1.7,
CC 1.6, 0.7, and 0.5 kb pieces.
CC -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000305}.
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DR EMBL; U48415; AAA92440.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21475.1; -; Genomic_DNA.
DR RefSeq; NP_461516.1; NC_003197.2.
DR RefSeq; WP_001068341.1; NC_003197.2.
DR AlphaFoldDB; Q56056; -.
DR SMR; Q56056; -.
DR STRING; 99287.STM2581; -.
DR PaxDb; Q56056; -.
DR EnsemblBacteria; AAL21475; AAL21475; STM2581.
DR GeneID; 1254103; -.
DR GeneID; 66757008; -.
DR KEGG; stm:STM2581; -.
DR PATRIC; fig|99287.12.peg.2722; -.
DR HOGENOM; CLU_000907_1_1_6; -.
DR OMA; LTHKSCK; -.
DR PhylomeDB; Q56056; -.
DR BioCyc; SENT99287:STM2581-MON; -.
DR PHI-base; PHI:3724; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW mRNA processing; Nuclease; Reference proteome; RNA-binding;
KW rRNA processing; rRNA-binding; tRNA processing.
FT CHAIN 1..226
FT /note="Ribonuclease 3"
FT /id="PRO_0000180429"
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:0000250"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
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:0000250"
FT CONFLICT 57..58
FT /note="YH -> S (in Ref. 1; AAA92440)"
FT /evidence="ECO:0000305"
FT CONFLICT 73..74
FT /note="AT -> DP (in Ref. 1; AAA92440)"
FT /evidence="ECO:0000305"
FT CONFLICT 217..220
FT /note="EQAL -> NSV (in Ref. 1; AAA92440)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 226 AA; 25505 MW; 5752C0113C0A055A CRC64;
MNPIVINRLQ RKLGYTFNHQ ELLQQALTHR SASSKHNERL EFLGDSILSF VIANALYHRF
PRVDEGDMSR MRATLVRGNT LAELAREFDL GECLRLGPGE LKSGGFRRES ILADTVEALI
GGVFLDSNIQ TVEQLILNWY KTRLDEISPG DKQKDPKTRL QEYLQGRHLP LPSYLVVQVR
GEAHDQEFTI HCQVSGLSEP VVGTGSSRRK AEQAAAEQAL KKLELE