ID RNC_STAS1 Reviewed; 244 AA. AC Q49X17; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-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}; OrderedLocusNames=SSP1536; OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM OS 20229 / NCIMB 8711 / NCTC 7292 / S-41). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=342451; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41; RX PubMed=16135568; DOI=10.1073/pnas.0502950102; RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M., RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.; RT "Whole genome sequence of Staphylococcus saprophyticus reveals the RT pathogenesis of uncomplicated urinary tract infection."; RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005). 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; AP008934; BAE18681.1; -; Genomic_DNA. DR RefSeq; WP_011303283.1; NZ_MTGA01000034.1. DR AlphaFoldDB; Q49X17; -. DR SMR; Q49X17; -. DR GeneID; 66867748; -. DR KEGG; ssp:SSP1536; -. DR eggNOG; COG0571; Bacteria. DR HOGENOM; CLU_000907_1_3_9; -. DR OrthoDB; 9805026at2; -. DR Proteomes; UP000006371; 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; Reference proteome; RNA-binding; KW rRNA processing; rRNA-binding; tRNA processing. FT CHAIN 1..244 FT /note="Ribonuclease 3" FT /id="PRO_0000228586" FT DOMAIN 17..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 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 244 AA; 28228 MW; 7842F44C2CAF6465 CRC64; MTNQKKKEMV QTFQNKFEKK MQELNLDFNR VDLYQQAFSH SSFINDFNMN RLDHNERLEF LGDAVLELTV SRYLFDKYPE LPEGNLTKMR ATIVCEPSLV IFANKIQLND LILLGKGEEK TGGRTRPSLV SDAFEAFVGA LYLDQGLEAV WQFSEQIIFP YVEDDELDGV VDFKTQFQEY VHRQNKGDVT YRLINEEGPA HHRLFTSEVI LEEDAVAEGK GKTKKESEQK AAERAYKILK NKNA //