ID   RNC_LACLM               Reviewed;         231 AA.
AC   A2RLZ8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   02-SEP-2026, entry version 101.
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};
GN   OrderedLocusNames=llmg_1753;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
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}.
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DR   EMBL; AM406671; CAL98325.1; -; Genomic_DNA.
DR   RefSeq; WP_011835540.1; NC_009004.1.
DR   AlphaFoldDB; A2RLZ8; -.
DR   SMR; A2RLZ8; -.
DR   STRING; 416870.llmg_1753; -.
DR   PaxDb; 416870-llmg_1753; -.
DR   KEGG; llm:llmg_1753; -.
DR   eggNOG; COG0571; Bacteria.
DR   HOGENOM; CLU_000907_1_3_9; -.
DR   OrthoDB; 9805026at2; -.
DR   PhylomeDB; A2RLZ8; -.
DR   Proteomes; UP000000364; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:TreeGrafter.
DR   GO; GO:0042802; F:identical protein binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0004525; F:ribonuclease III activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:TreeGrafter.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   CDD; cd10845; DSRM_RNAse_III_family; 1.
DR   CDD; cd00593; RIBOc; 1.
DR   FunFam; 1.10.1520.10:FF:000001; Ribonuclease 3; 1.
DR   FunFam; 3.30.160.20:FF:000003; Ribonuclease 3; 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; 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..231
FT                   /note="Ribonuclease 3"
FT                   /id="PRO_1000075768"
FT   DOMAIN          5..134
FT                   /note="RNase III"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   DOMAIN          160..229
FT                   /note="DRBM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   ACT_SITE        51
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   ACT_SITE        123
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   BINDING         120
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   BINDING         123
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
SQ   SEQUENCE   231 AA;  26185 MW;  90652AC75814CE33 CRC64;
     MLKLQKKLKN DYGLVFNDEY LLKTAFTHSS FTNEERLPKI ANNERLEFLG DVALSLVISD
     YLYRTYPEKL EGELSKMRSS IVRTESLANF SRSCGFGEFL RLGHGEEKMG GRDRETTLEN
     LFEAFLGALF IDQGMDEVRK FIQHVVIPHV KNDDYVKVID YKTELQEVLQ IGGETTISYK
     ILKEEGPAHD RSFVAAVFNN GKELGRGLGK SKKVAEQKAA ENAIKGQNHV S
//