ID   RNC_MYCPB               Reviewed;         282 AA.
AC   E1QCT1;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 51.
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=MPNE_0641;
OS   Mycoplasma pneumoniae (strain ATCC 15531 / DSM 23978 / CIP 103766 / NBRC
OS   14401 / NCTC 10119 / FH) (Mycoplasmoides pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=722438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15531 / DSM 23978 / CIP 103766 / NBRC 14401 / NCTC 10119 / FH;
RX   PubMed=20543037; DOI=10.1128/aem.00024-10;
RA   Krishnakumar R., Assad-Garcia N., Benders G.A., Phan Q., Montague M.G.,
RA   Glass J.I.;
RT   "Targeted chromosomal knockouts in Mycoplasma pneumoniae.";
RL   Appl. Environ. Microbiol. 76:5297-5299(2010).
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}.
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; CP002077; ADK87079.1; -; Genomic_DNA.
DR   RefSeq; WP_010874902.1; NZ_CP010546.1.
DR   AlphaFoldDB; E1QCT1; -.
DR   SMR; E1QCT1; -.
DR   STRING; 722438.MPNE_0641; -.
DR   PaxDb; E1QCT1; -.
DR   EnsemblBacteria; ADK87079; ADK87079; MPNE_0641.
DR   GeneID; 66608773; -.
DR   KEGG; mpj:MPNE_0641; -.
DR   PATRIC; fig|722438.3.peg.619; -.
DR   eggNOG; COG0571; Bacteria.
DR   HOGENOM; CLU_1026084_0_0_14; -.
DR   OMA; NRIGMEL; -.
DR   Proteomes; UP000007756; 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: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   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; IPR011907; RNase_III.
DR   InterPro; IPR000999; RNase_III_dom.
DR   InterPro; IPR036389; RNase_III_sf.
DR   Pfam; PF14622; Ribonucleas_3_3; 1.
DR   SMART; SM00535; RIBOc; 1.
DR   SUPFAM; SSF69065; SSF69065; 1.
DR   TIGRFAMs; TIGR02191; RNaseIII; 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; rRNA processing; tRNA processing.
FT   CHAIN           1..282
FT                   /note="Ribonuclease 3"
FT                   /id="PRO_0000416609"
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