ID E4SKB4_LACAR Unreviewed; 228 AA. AC E4SKB4; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAR-2024, entry version 73. 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:ADQ59387.1}; GN OrderedLocusNames=LA2_07330 {ECO:0000313|EMBL:ADQ59387.1}; OS Lactobacillus amylovorus (strain GRL 1112). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=695560 {ECO:0000313|EMBL:ADQ59387.1, ECO:0000313|Proteomes:UP000007033}; RN [1] {ECO:0000313|EMBL:ADQ59387.1, ECO:0000313|Proteomes:UP000007033} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GRL 1112 {ECO:0000313|EMBL:ADQ59387.1, RC ECO:0000313|Proteomes:UP000007033}; RX PubMed=21131492; DOI=10.1128/JB.01365-10; RA Kant R., Paulin L., Alatalo E., de Vos W.M., Palva A.; RT "Genome sequence of Lactobacillus amylovorus GRL1112."; RL J. Bacteriol. 193:789-790(2011). 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; Evidence={ECO:0000256|HAMAP- CC 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 --------------------------------------------------------------------------- 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; CP002338; ADQ59387.1; -; Genomic_DNA. DR RefSeq; WP_013438175.1; NC_014724.1. DR AlphaFoldDB; E4SKB4; -. DR KEGG; lam:LA2_07330; -. DR PATRIC; fig|695560.3.peg.1445; -. DR HOGENOM; CLU_000907_1_3_9; -. DR Proteomes; UP000007033; 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; 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}; KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP- KW Rule:MF_00104}; rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00104}; KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP- KW Rule:MF_00104}. FT DOMAIN 7..136 FT /note="RNase III" FT /evidence="ECO:0000259|PROSITE:PS50142" FT DOMAIN 162..228 FT /note="DRBM" FT /evidence="ECO:0000259|PROSITE:PS50137" FT REGION 204..228 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 53 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104" FT ACT_SITE 125 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104" FT BINDING 49 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104" FT BINDING 122 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104" FT BINDING 125 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104" SQ SEQUENCE 228 AA; 26091 MW; B0FC04BB6088C991 CRC64; MVSTKFLKKL KDEYNVKFNN EKLLEEAFTH SSYSNEHPDA GIRDYEKLEF LGDAVLELAV SNYLYRHYPK LNEGELTRLR SNIVRTEGFS EFAIECGFQK EIHLGNGEEK AGARNRKTLL EDVFEAFNGA LYLDQGMPAV EHFLHLTVYP LIDKGEFDDS RDYKTDLQEL LQQNGPVNIE YSVISESQLP SHFEVELKIN DEAKTRGEGH NKKAAEQQAA KAALKELE //