ID RNC_RICCK Reviewed; 227 AA. AC A8EXI3; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 27-MAR-2024, entry version 84. DE RecName: Full=Ribonuclease 3 {ECO:0000255|HAMAP-Rule:MF_00104}; DE EC=3.1.26.3 {ECO:0000255|HAMAP-Rule:MF_00104}; DE AltName: Full=Ribonuclease III {ECO:0000255|HAMAP-Rule:MF_00104}; DE Short=RNase III {ECO:0000255|HAMAP-Rule:MF_00104}; GN Name=rnc {ECO:0000255|HAMAP-Rule:MF_00104}; GN OrderedLocusNames=A1E_00590; OS Rickettsia canadensis (strain McKiel). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group. OX NCBI_TaxID=293613; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=McKiel; RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Dasch G., Eremeeva M.; RT "Complete genome sequence of Rickettsia canadensis."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Digests double-stranded RNA. Involved in the processing of CC primary rRNA transcript to yield the immediate precursors to the large CC and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when CC they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA CC of type II CRISPR loci if present in the organism. {ECO:0000255|HAMAP- CC Rule:MF_00104}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00104}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00104}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00104}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00104}. CC -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000255|HAMAP- CC Rule:MF_00104}. 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; CP000409; ABV73066.1; -; Genomic_DNA. DR RefSeq; WP_012148267.1; NC_009879.1. DR AlphaFoldDB; A8EXI3; -. DR SMR; A8EXI3; -. DR STRING; 293613.A1E_00590; -. DR KEGG; rcm:A1E_00590; -. DR eggNOG; COG0571; Bacteria. DR HOGENOM; CLU_000907_1_1_5; -. DR Proteomes; UP000007056; Chromosome. 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; PTHR14950; DICER-RELATED; 1. DR PANTHER; PTHR14950:SF37; ENDORIBONUCLEASE DICER; 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 3: Inferred from homology; KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; KW mRNA processing; Nuclease; RNA-binding; rRNA processing; rRNA-binding; KW tRNA processing. FT CHAIN 1..227 FT /note="Ribonuclease 3" FT /id="PRO_1000075802" FT DOMAIN 4..133 FT /note="RNase III" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT DOMAIN 158..226 FT /note="DRBM" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT ACT_SITE 50 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT ACT_SITE 122 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT BINDING 46 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT BINDING 119 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT BINDING 122 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" SQ SEQUENCE 227 AA; 25787 MW; 7899F5B658FFF467 CRC64; MSSFNELEKL LGYSFKNKEL LIEALSHPSL RQHHEYKDNK DYERLEFLGD AVLNLVITKI LFSNFASYNE GNLAKIRSYL VCKETICMVG AKLALKDYII MTYGEEVAGG RDNPNNIENA TEALIAAIYL DSNIETTHNI IGQLWAEFIK VQNLTDYDPK TALQEWAQAS DHHLPIYCLI KREGAAHSST FTVLVKVKDY EQIGIGYSIK EAEKNAARSL LHRLKND //