ID   RNC_THENN               Reviewed;         240 AA.
AC   B9K9K8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=CTN_1465;
OS   Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Thermotoga.
OX   NCBI_TaxID=309803;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E;
RA   Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J.,
RA   Kim J.J., Park K.J., Lee S.Y.;
RT   "The genome sequence of the hyperthermophilic bacterium Thermotoga
RT   neapolitana.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000916; ACM23641.1; -; Genomic_DNA.
DR   RefSeq; WP_015919930.1; NC_011978.1.
DR   AlphaFoldDB; B9K9K8; -.
DR   SMR; B9K9K8; -.
DR   STRING; 309803.CTN_1465; -.
DR   KEGG; tna:CTN_1465; -.
DR   eggNOG; COG0571; Bacteria.
DR   HOGENOM; CLU_000907_1_3_0; -.
DR   Proteomes; UP000000445; 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; cd10845; DSRM_RNAse_III_family; 1.
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; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW   mRNA processing; Nuclease; RNA-binding; rRNA processing; rRNA-binding;
KW   tRNA processing.
FT   CHAIN           1..240
FT                   /note="Ribonuclease 3"
FT                   /id="PRO_1000118940"
FT   DOMAIN          9..141
FT                   /note="RNase III"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   DOMAIN          168..237
FT                   /note="DRBM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   ACT_SITE        58
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   BINDING         54
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   240 AA;  27571 MW;  7FDA7CEF2179D665 CRC64;
     MTESERRTVE ELQKRLGVLF NDEELLFRAL CHSSYANEQK QAGREDVESN EKLEFLGDAV
     LELFVCEILY RKYPEAEVGD LARVKSAVAS EEVLARVSRR LELGKYLFLG KGEEKTGGRE
     RDSILADAFE ALLAALYLDQ GYQKIKDLFE DEFESYIEKI MKGEILFDYK TALQEIVQRE
     HKTPPEYVLV RTEKNGSEKL FVVEVRVNDE TLAVGRGRTK KEAEKDAARK AYEKLVAEKT
//