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 13-SEP-2023, entry version 103. 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; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; 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}. 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; 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; 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 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 //