ID RNC_PASMU Reviewed; 225 AA. AC P57805; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 1. DT 27-MAR-2024, entry version 130. 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}; OrderedLocusNames=PM0061; OS Pasteurella multocida (strain Pm70). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Pasteurella. OX NCBI_TaxID=272843; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pm70; RX PubMed=11248100; DOI=10.1073/pnas.051634598; RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.; RT "Complete genomic sequence of Pasteurella multocida Pm70."; RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001). RN [2] RP FUNCTION. RX PubMed=24270795; DOI=10.1093/nar/gkt1074; RA Fonfara I., Le Rhun A., Chylinski K., Makarova K.S., Lecrivain A.L., RA Bzdrenga J., Koonin E.V., Charpentier E.; RT "Phylogeny of Cas9 determines functional exchangeability of dual-RNA and RT Cas9 among orthologous type II CRISPR-Cas systems."; RL Nucleic Acids Res. 42:2577-2590(2014). 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). Also processes some mRNAs, and tRNAs CC when they are encoded in the rRNA operon (By similarity). CC {ECO:0000250}. CC -!- FUNCTION: CRISPR (clustered regularly interspaced short palindromic CC repeat) is an adaptive immune system that provides protection against CC mobile genetic elements (viruses, transposable elements and conjugative CC plasmids). CRISPR clusters contain spacers, sequences complementary to CC antecedent mobile elements, and target invading nucleic acids. CRISPR CC clusters are transcribed and processed into CRISPR RNA (crRNA). In this CC organism endogenous ribonuclease 3 and Cas9 are required for correct CC coprocessing of pre-crRNA and the trans-encoded small RNA (tracrRNA). CC Cas9, crRNA and tracrRNA are required for cleavage of invading DNA CC (Probable). Complements pre-crRNA and tracrRNA coprocessing defects in CC an rnc deletion in S.pyogenes strain 370 (PubMed:24270795). CC {ECO:0000269|PubMed:24270795, ECO:0000305}. 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; AE004439; AAK02145.1; -; Genomic_DNA. DR RefSeq; WP_010906462.1; NC_002663.1. DR AlphaFoldDB; P57805; -. DR SMR; P57805; -. DR STRING; 272843.PM0061; -. DR EnsemblBacteria; AAK02145; AAK02145; PM0061. DR KEGG; pmu:PM0061; -. DR HOGENOM; CLU_000907_1_1_6; -. DR OrthoDB; 9805026at2; -. DR Proteomes; UP000000809; 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; Reference proteome; RNA-binding; KW rRNA processing; rRNA-binding; tRNA processing. FT CHAIN 1..225 FT /note="Ribonuclease 3" FT /id="PRO_0000180418" FT DOMAIN 5..127 FT /note="RNase III" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT DOMAIN 154..224 FT /note="DRBM" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT ACT_SITE 44 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT ACT_SITE 116 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT BINDING 40 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT BINDING 113 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT BINDING 116 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" SQ SEQUENCE 225 AA; 25461 MW; 202B6ACCA562B31C CRC64; MTQNLERLQR QIGYQFNQPA LLKQALTHRS AAVKHNERLE FLGDAILNFI IAEALYHQFP KCNEGELSRM RATLVREPTL ASLARQFELG DYLSLGPGEL KSGGFRRESI LADCVEAIIG AISLDSDLAT TTKIVQHWYQ AQLKQIQPGD NQKDPKTRLQ EYLQGKRLPL PTYNVVEIKG EAHCQTFTVE CYVKNIDRTF MGSGASRRKA EQAAAEKILQ LLEMK //