RNC_RHOCA
ID RNC_RHOCA Reviewed; 228 AA.
AC Q52698;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Ribonuclease 3;
DE EC=3.1.26.3;
DE AltName: Full=Ribonuclease III;
DE Short=RNase III;
GN Name=rnc;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN RRNA PROCESSING, EXPRESSION
RP IN E.COLI, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33303 / B10, and DSM 938 / 37b4;
RX PubMed=8614626; DOI=10.1093/nar/24.7.1246;
RA Rauhut R., Jaeger A., Conrad C., Klug G.;
RT "Identification and analysis of the rnc gene for RNase III in Rhodobacter
RT capsulatus.";
RL Nucleic Acids Res. 24:1246-1251(1996).
RN [2]
RP FUNCTION.
RC STRAIN=DSM 938 / 37b4;
RX PubMed=8106323; DOI=10.1128/jb.176.4.1121-1127.1994;
RA Kordes E., Jock S., Fritsch J., Bosch F., Klug G.;
RT "Cloning of a gene involved in rRNA precursor processing and 23S rRNA
RT cleavage in Rhodobacter capsulatus.";
RL J. Bacteriol. 176:1121-1127(1994).
RN [3]
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, FUNCTION IN RRNA PROCESSING,
RP RRNA-BINDING, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 33303 / B10;
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).
CC -!- FUNCTION: Digests double-stranded RNA. Involved in the processing of
CC ribosomal RNA precursors and of some mRNAs. Complements an E.coli
CC disruption mutant, but the E.coli enzyme does not cleave R.capsulatus
CC rRNA precursor, showing substrate recognition is different. Probably
CC also 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. {ECO:0000269|PubMed:8106323,
CC ECO:0000269|PubMed:8614626, ECO:0000269|PubMed:9742248}.
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;
CC Evidence={ECO:0000269|PubMed:9742248};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5 at 32 degrees Celsius.
CC {ECO:0000269|PubMed:9742248};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Loss of processing of 23S rRNA. Full
CC complementation requires both lep and rnc genes, suggesting they form
CC an operon. {ECO:0000269|PubMed:8614626}.
CC -!- MISCELLANEOUS: The protein in strain DMS 938 / 37b4 has 5 other
CC sequence differences. In Rhodobacter species, 23S rRNA is further
CC processed to 16S and 14S rRNA species in vivo, probably by RNase III.
CC -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000305}.
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DR EMBL; Z68305; CAA92647.1; -; Genomic_DNA.
DR PIR; S66596; S66596.
DR AlphaFoldDB; Q52698; -.
DR SMR; Q52698; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
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 1: Evidence at protein level;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW mRNA processing; Nuclease; RNA-binding; rRNA processing; rRNA-binding;
KW tRNA processing.
FT CHAIN 1..228
FT /note="Ribonuclease 3"
FT /id="PRO_0000180427"
FT DOMAIN 7..132
FT /note="RNase III"
FT DOMAIN 157..226
FT /note="DRBM"
FT ACT_SITE 49
FT /evidence="ECO:0000255"
FT ACT_SITE 121
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VARIANT 62
FT /note="H -> D (in strain: DSM 938)"
SQ SEQUENCE 228 AA; 24663 MW; 8B4AEFF3434E699C CRC64;
MKVAADLSAF MDRLGHRFTT PEHLVRALTH SSLGSATRPD NQRLEFLGDR VLGLSMAEAL
FHADGRASEG QLAPRFNALV RKETCAAVAR DIDLGAVLKL GRSEMMSGGR RKDALLGDAM
EAVIAAVYLD AGFEVARALV LRLWAARIQS VDNDARDPKT ALQEWAQARG LPPPRYETLG
RDGPDHAPQF RIAVVLASGE TEEAQAGSKR NAEQAAAKAL LERLERGA
