ID RNC_STAAC Reviewed; 243 AA. AC Q5HGJ9; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 108. 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=SACOL1248; OS Staphylococcus aureus (strain COL). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=93062; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=COL; RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005; RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L., RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., RA Fraser C.M.; RT "Insights on evolution of virulence and resistance from the complete genome RT analysis of an early methicillin-resistant Staphylococcus aureus strain and RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis RT strain."; RL J. Bacteriol. 187:2426-2438(2005). 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). Complements CC pre-crRNA and tracrRNA coprocessing defects in an rnc deletion in CC S.pyogenes strain 370, although this S.aureus strain does not have the CC corresponding CRISPR locus (PubMed:24270795). {ECO:0000250, CC ECO:0000269|PubMed:24270795}. 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; CP000046; AAW38082.1; -; Genomic_DNA. DR RefSeq; WP_000043237.1; NC_002951.2. DR AlphaFoldDB; Q5HGJ9; -. DR SMR; Q5HGJ9; -. DR KEGG; sac:SACOL1248; -. DR HOGENOM; CLU_000907_1_3_9; -. DR Proteomes; UP000000530; 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; 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 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..243 FT /note="Ribonuclease 3" FT /id="PRO_0000180432" FT DOMAIN 10..146 FT /note="RNase III" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT DOMAIN 172..241 FT /note="DRBM" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT REGION 219..243 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 219..233 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 63 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT ACT_SITE 135 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT BINDING 59 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT BINDING 132 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT BINDING 135 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" SQ SEQUENCE 243 AA; 27922 MW; 875034DEBC3455A9 CRC64; MSKQKKSEIV NRFRKRFDTK MTELGFTYQN IDLYQQAFSH SSFINDFNMN RLDHNERLEF LGDAVLELTV SRYLFDKHPN LPEGNLTKMR ATIVCEPSLV IFANKIGLNE MILLGKGEEK TGGRTRPSLI SDAFEAFIGA LYLDQGLDIV WKFAEKVIFP HVEQNELLGV VDFKTQFQEY VHQQNKGDVT YNLIKEEGPA HHRLFTSEVI LQGEAIAEGK GKTKKESEQR AAESAYKQLK QIK //