ID RNC_XYLFT Reviewed; 227 AA. AC Q87C06; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 107. 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=PD_1290; OS Xylella fastidiosa (strain Temecula1 / ATCC 700964). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=183190; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Temecula1 / ATCC 700964; RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003; RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y., RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A., RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S., RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H., RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L., RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L., RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S., RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F., RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G., RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A., RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L., RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.; RT "Comparative analyses of the complete genome sequences of Pierce's disease RT and citrus variegated chlorosis strains of Xylella fastidiosa."; RL J. Bacteriol. 185:1018-1026(2003). 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; AE009442; AAO29139.1; -; Genomic_DNA. DR RefSeq; WP_004088291.1; NC_004556.1. DR AlphaFoldDB; Q87C06; -. DR SMR; Q87C06; -. DR GeneID; 58016822; -. DR KEGG; xft:PD_1290; -. DR HOGENOM; CLU_000907_1_1_6; -. DR Proteomes; UP000002516; 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..227 FT /note="Ribonuclease 3" FT /id="PRO_0000180460" FT DOMAIN 6..128 FT /note="RNase III" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT DOMAIN 155..225 FT /note="DRBM" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT REGION 203..227 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 45 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT ACT_SITE 117 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT BINDING 41 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT BINDING 114 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" FT BINDING 117 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104" SQ SEQUENCE 227 AA; 25243 MW; 044B124299C97CFF CRC64; MISSKASDYQ QRIGYVFTDP SLLLQALRHR SAGTPHNERL EFLGDSVVNL LIAEALFQRW PRADEGALTR ARSELVRETS LASIARTMQL GEQLILGPGE LKSGGHRRDS ILADAVEAVI AAIYLDADLA TCRTVVLPWF ETALTALPVG KPEKDPKTRL QEWLQARQWS LPVYELIFES GDPHTKHFRV SCTLGELKLR TEGEGSSRRL AEQDAASHAI DQLDSNK //