ID   RNC_RICBR               Reviewed;         227 AA.
AC   Q1RHA2;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=RBE_1181;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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;
CC         Evidence={ECO:0000255|HAMAP-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; CP000087; ABE05262.1; -; Genomic_DNA.
DR   RefSeq; WP_011477840.1; NC_007940.1.
DR   AlphaFoldDB; Q1RHA2; -.
DR   SMR; Q1RHA2; -.
DR   STRING; 336407.RBE_1181; -.
DR   EnsemblBacteria; ABE05262; ABE05262; RBE_1181.
DR   KEGG; rbe:RBE_1181; -.
DR   eggNOG; COG0571; Bacteria.
DR   HOGENOM; CLU_000907_1_1_5; -.
DR   OMA; LTHKSCK; -.
DR   OrthoDB; 1890943at2; -.
DR   Proteomes; UP000001951; 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; 1.10.1520.10; -; 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   Pfam; PF00035; dsrm; 1.
DR   Pfam; PF14622; Ribonucleas_3_3; 1.
DR   SMART; SM00358; DSRM; 1.
DR   SMART; SM00535; RIBOc; 1.
DR   SUPFAM; SSF69065; SSF69065; 1.
DR   TIGRFAMs; TIGR02191; RNaseIII; 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; RNA-binding; rRNA processing; rRNA-binding;
KW   tRNA processing.
FT   CHAIN           1..227
FT                   /note="Ribonuclease 3"
FT                   /id="PRO_0000277903"
FT   DOMAIN          4..133
FT                   /note="RNase III"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   DOMAIN          158..226
FT                   /note="DRBM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   ACT_SITE        50
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   ACT_SITE        122
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   BINDING         46
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   BINDING         119
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   BINDING         122
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
SQ   SEQUENCE   227 AA;  25953 MW;  BF2AFCF03189A761 CRC64;
     MESFEELEKL LDYSFKNKAL LTEALSHPSL RQHHEYKANK DYERLEFLGD AVLNLIITEI
     LFNNFKEYNE GNLAKIRSYL VCKETICVVG AKLGLKNYII MTHGEEIAGG RDNPNNIENV
     TEALIAAIYL DSDITTIHNI IGKLWAEFIK VKDLTDYDPK TALQEWAQSK DHHIPIYRLI
     KREGVAHLST FTVSVKINGY EQTGKGHSIK EAEKNAAREL LHKLKLL