ID RNC_XANCP Reviewed; 226 AA. AC Q8PB52; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 122. 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=XCC1273; OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB OS 528 / LMG 568 / P 25). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=190485; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25; RX PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing host RT specificities."; RL Nature 417:459-463(2002). 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; AE008922; AAM40571.1; -; Genomic_DNA. DR RefSeq; NP_636647.1; NC_003902.1. DR RefSeq; WP_011036467.1; NC_003902.1. DR AlphaFoldDB; Q8PB52; -. DR SMR; Q8PB52; -. DR STRING; 190485.XCC1273; -. DR EnsemblBacteria; AAM40571; AAM40571; XCC1273. DR GeneID; 58014135; -. DR KEGG; xcc:XCC1273; -. DR PATRIC; fig|190485.4.peg.1363; -. DR eggNOG; COG0571; Bacteria. DR HOGENOM; CLU_000907_1_1_6; -. DR OrthoDB; 9805026at2; -. DR Proteomes; UP000001010; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004525; F:ribonuclease III activity; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule. DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central. DR GO; GO:0006396; P:RNA processing; IBA:GO_Central. 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..226 FT /note="Ribonuclease 3" FT /id="PRO_0000180458" 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 226 AA; 24581 MW; F5076DFB7C6B289D CRC64; MSNRTFQRGD PIGHAFADPG LLAQALRHRS AGTPHNERLE FLGDGIVNLL IAEALYQRWP KADEGALTRA RAELVREGAL AVIGRTLNLG ERLTLGPGEL KSGGHRRDSI LADAVEAIVA AIYLDCGFER CRAVVLPWFE PSLAALPVGK AEKDPKTRLQ EWLQARQLPL PQYALISESG DEHAKQFHVA CILEQPAARA EGQGTSRRLA EQQAAATVIA QLDSNT //