ID A0A519M5A6_9BACT Unreviewed; 199 AA. AC A0A519M5A6; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 02-OCT-2024, entry version 18. DE RecName: Full=Ribonuclease 3 {ECO:0000256|HAMAP-Rule:MF_00104}; DE EC=3.1.26.3 {ECO:0000256|HAMAP-Rule:MF_00104}; DE AltName: Full=Ribonuclease III {ECO:0000256|HAMAP-Rule:MF_00104}; DE Short=RNase III {ECO:0000256|HAMAP-Rule:MF_00104}; GN Name=rnc {ECO:0000256|HAMAP-Rule:MF_00104, GN ECO:0000313|EMBL:RZJ56747.1}; GN ORFNames=EOO55_04665 {ECO:0000313|EMBL:RZJ56747.1}; OS Hymenobacter sp. OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae; OC Hymenobacter. OX NCBI_TaxID=1898978 {ECO:0000313|EMBL:RZJ56747.1, ECO:0000313|Proteomes:UP000319287}; RN [1] {ECO:0000313|EMBL:RZJ56747.1, ECO:0000313|Proteomes:UP000319287} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PMG_005 {ECO:0000313|EMBL:RZJ56747.1}; RX PubMed=30498029; DOI=.1073/pnas.1812668115; RA Crombie A.T., Larke-Mejia N.L., Emery H., Dawson R., Pratscher J., RA Murphy G.P., McGenity T.J., Murrell J.C.; RT "Poplar phyllosphere harbors disparate isoprene-degrading bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 115:13081-13086(2018). 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:0000256|HAMAP- CC Rule:MF_00104}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3; CC Evidence={ECO:0000256|ARBA:ARBA00000109, ECO:0000256|HAMAP- CC Rule:MF_00104}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00104}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00104}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00104}. CC -!- SIMILARITY: Belongs to the ribonuclease III family. CC {ECO:0000256|ARBA:ARBA00010183}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RZJ56747.1}. 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; SEBX01000183; RZJ56747.1; -; Genomic_DNA. DR AlphaFoldDB; A0A519M5A6; -. DR Proteomes; UP000319287; Unassembled WGS sequence. 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; 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 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00104}; KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP- KW Rule:MF_00104}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00104}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00104}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00104}; KW mRNA processing {ECO:0000256|ARBA:ARBA00022664, ECO:0000256|HAMAP- KW Rule:MF_00104}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00104}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_00104}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_00104}; KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00104}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00104}. FT DOMAIN 8..103 FT /note="RNase III" FT /evidence="ECO:0000259|PROSITE:PS50142" FT DOMAIN 131..199 FT /note="DRBM" FT /evidence="ECO:0000259|PROSITE:PS50137" FT ACT_SITE 22 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104" FT ACT_SITE 92 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104" FT BINDING 18 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104" FT BINDING 89 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104" FT BINDING 92 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104" SQ SEQUENCE 199 AA; 21839 MW; 7D81A78ABDE9D454 CRC64; MVRAEPGAGR HQSNERLEFL GDAVLGTVVA EYLFRKFPYE QEGFLTETRS RIVNRESLNA IALKLGLDRL VQLDAAQTRV ARSRSVNGNA LEALVGAVYL DLGYKAARKF VLKGLIKPFV DVNTLTTTTS NYKSKLIEWA QRNGKAVRYD ISGEPRPGGV MEFTATVILN EEVIATGMGL NKKQAEQLAA ERALVALGV //