ID RNC_THEMA Reviewed; 240 AA. AC Q9X0I6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 151. DE RecName: Full=Ribonuclease 3; DE EC=3.1.26.3; DE AltName: Full=Ribonuclease III; DE Short=RNase III; GN Name=rnc; OrderedLocusNames=TM_1102; OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 OS / MSB8). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F., RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION AS AN RNASE, FUNCTION AS AN ENDONUCLEASE, BIOPHYSICOCHEMICAL RP PROPERTIES, COFACTOR, AND RRNA-BINDING. RX PubMed=20677811; DOI=10.1021/bi100930u; RA Nathania L., Nicholson A.W.; RT "Thermotoga maritima ribonuclease III. Characterization of thermostable RT biochemical behavior and analysis of conserved base pairs that function as RT reactivity epitopes for the Thermotoga 23S rRNA precursor."; RL Biochemistry 49:7164-7178(2010). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT. RG Joint center for structural genomics (JCSG); RT "Crystal structure of ribonuclease III (TM1102) from Thermotoga maritima at RT 2.0 A resolution."; RL Submitted (FEB-2009) to the PDB data bank. 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. Probably processes pre-crRNA CC and tracrRNA of type II CRISPR loci if present in the organism. CC {ECO:0000269|PubMed:20677811}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:20677811}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 8.0. {ECO:0000269|PubMed:20677811}; CC Temperature dependence: CC Optimum temperature is 40-70 degrees Celsius. CC {ECO:0000269|PubMed:20677811}; CC -!- SUBUNIT: Homodimer. {ECO:0000305|Ref.3}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000305}. 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; AE000512; AAD36178.1; -; Genomic_DNA. DR PIR; H72294; H72294. DR RefSeq; NP_228908.1; NC_000853.1. DR RefSeq; WP_004080335.1; NZ_CP011107.1. DR PDB; 1O0W; X-ray; 2.00 A; A/B=1-240. DR PDBsum; 1O0W; -. DR AlphaFoldDB; Q9X0I6; -. DR SMR; Q9X0I6; -. DR STRING; 243274.TM_1102; -. DR PaxDb; 243274-THEMA_08835; -. DR EnsemblBacteria; AAD36178; AAD36178; TM_1102. DR KEGG; tma:TM1102; -. DR eggNOG; COG0571; Bacteria. DR InParanoid; Q9X0I6; -. DR OrthoDB; 9805026at2; -. DR BRENDA; 3.1.26.3; 6331. DR EvolutionaryTrace; Q9X0I6; -. DR Proteomes; UP000008183; 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; 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 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; KW mRNA processing; Nuclease; Reference proteome; RNA-binding; KW rRNA processing; rRNA-binding; tRNA processing. FT CHAIN 1..240 FT /note="Ribonuclease 3" FT /id="PRO_0000180448" FT DOMAIN 9..141 FT /note="RNase III" FT DOMAIN 168..237 FT /note="DRBM" FT ACT_SITE 58 FT /evidence="ECO:0000255" FT ACT_SITE 130 FT /evidence="ECO:0000250" FT BINDING 54 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 127 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 130 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT HELIX 3..16 FT /evidence="ECO:0007829|PDB:1O0W" FT HELIX 23..30 FT /evidence="ECO:0007829|PDB:1O0W" FT HELIX 33..41 FT /evidence="ECO:0007829|PDB:1O0W" FT HELIX 51..72 FT /evidence="ECO:0007829|PDB:1O0W" FT HELIX 78..88 FT /evidence="ECO:0007829|PDB:1O0W" FT HELIX 91..100 FT /evidence="ECO:0007829|PDB:1O0W" FT HELIX 103..106 FT /evidence="ECO:0007829|PDB:1O0W" FT HELIX 111..115 FT /evidence="ECO:0007829|PDB:1O0W" FT HELIX 118..120 FT /evidence="ECO:0007829|PDB:1O0W" FT HELIX 122..140 FT /evidence="ECO:0007829|PDB:1O0W" FT HELIX 142..161 FT /evidence="ECO:0007829|PDB:1O0W" FT HELIX 169..181 FT /evidence="ECO:0007829|PDB:1O0W" FT STRAND 186..193 FT /evidence="ECO:0007829|PDB:1O0W" FT STRAND 200..207 FT /evidence="ECO:0007829|PDB:1O0W" FT STRAND 210..219 FT /evidence="ECO:0007829|PDB:1O0W" FT HELIX 220..235 FT /evidence="ECO:0007829|PDB:1O0W" SQ SEQUENCE 240 AA; 27530 MW; 94330E8898D48A0D CRC64; MNESERKIVE EFQKETGINF KNEELLFRAL CHSSYANEQN QAGRKDVESN EKLEFLGDAV LELFVCEILY KKYPEAEVGD LARVKSAAAS EEVLAMVSRK MNLGKFLFLG KGEEKTGGRD RDSILADAFE ALLAAIYLDQ GYEKIKELFE QEFEFYIEKI MKGEMLFDYK TALQEIVQSE HKVPPEYILV RTEKNDGDRI FVVEVRVNGK TIATGKGRTK KEAEKEAARI AYEKLLKERS //