ID   RNC_MYCPN               Reviewed;         282 AA.
AC   P75233;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   04-NOV-2026, entry version 124.
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=MPN_545;
GN   ORFNames=MP297;
OS   Mycoplasmoides pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
OS   (Mycoplasma pneumoniae).
OC   Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129 / Subtype 1;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB95945.1; -; Genomic_DNA.
DR   PIR; S73623; S73623.
DR   RefSeq; WP_010874902.1; NC_000912.1.
DR   AlphaFoldDB; P75233; -.
DR   SMR; P75233; -.
DR   STRING; 272634.MPN_545; -.
DR   PaxDb; 272634-MPN_545; -.
DR   EnsemblBacteria; AAB95945; AAB95945; MPN_545.
DR   GeneID; 66608773; -.
DR   KEGG; mpn:MPN_545; -.
DR   PATRIC; fig|272634.6.peg.607; -.
DR   HOGENOM; CLU_1026084_0_0_14; -.
DR   OMA; DIFPNNW; -.
DR   OrthoDB; 9805026at2; -.
DR   BioCyc; MPNE272634:G1GJ3-898-MONOMER; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004525; F:ribonuclease III activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   CDD; cd00593; RIBOc; 1.
DR   Gene3D; 1.10.1520.10; Ribonuclease III domain; 1.
DR   HAMAP; MF_00104; RNase_III; 1.
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; PF14622; Ribonucleas_3_3; 1.
DR   SMART; SM00535; RIBOc; 1.
DR   SUPFAM; SSF69065; RNase III domain-like; 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; Reference proteome; rRNA processing;
KW   tRNA processing.
FT   CHAIN           1..282
FT                   /note="Ribonuclease 3"
FT                   /id="PRO_0000180411"
FT   DOMAIN          18..141
FT                   /note="RNase III"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   ACT_SITE        63
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   BINDING         59
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   BINDING         127
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   BINDING         130
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
SQ   SEQUENCE   282 AA;  32653 MW;  47C2BC66F7450D8C CRC64;
     MKNKKDKTQK PKVIDEKFVA FFKSLNIEPQ NWQFYEDAFV HSSYVNENED ARASYDRLEF
     LGDALIDFIV AKKLFELYPN YNEGMLTRTK IEIVKGENLN RIGKELNFGN FIKLGKGMPY
     TETLFGDVLE ALVAAIYEDL GIEKANQFVE EHIFKKTYSE ILKYNFFSLF QEQKLPEPRV
     RVSLTSNNLV LSIIELNGDI IWSQAVPNSK HYDDKSVLEH NAMSAFTQFL KSGKGINFFS
     DIKNKLDSQK PMRALTVRPK KINWKARKPK LKALKNKVKA DS
//