ID   RNC_ROSHA               Reviewed;         357 AA.
AC   G2SYN4;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Ribonuclease 3;
DE            EC=3.1.26.3;
DE   AltName: Full=Ribonuclease III;
DE            Short=RNase III;
GN   Name=rnc; OrderedLocusNames=RHOM_15125;
OS   Roseburia hominis (strain DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX   NCBI_TaxID=585394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183;
RX   PubMed=26543119; DOI=10.1128/genomea.01286-15;
RA   Travis A.J., Kelly D., Flint H.J., Aminov R.I.;
RT   "Complete genome sequence of the human gut symbiont Roseburia hominis.";
RL   Genome Announc. 3:E0128615-E0128615(2015).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000305}.
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DR   EMBL; CP003040; AEN98131.1; -; Genomic_DNA.
DR   RefSeq; WP_014081094.1; NC_015977.1.
DR   AlphaFoldDB; G2SYN4; -.
DR   SMR; G2SYN4; -.
DR   STRING; 585394.RHOM_15125; -.
DR   GeneID; 77460568; -.
DR   KEGG; rho:RHOM_15125; -.
DR   eggNOG; COG0571; Bacteria.
DR   HOGENOM; CLU_775860_0_0_9; -.
DR   OrthoDB; 9805026at2; -.
DR   Proteomes; UP000008178; 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; cd00048; DSRM_SF; 2.
DR   CDD; cd00593; RIBOc; 1.
DR   Gene3D; 3.30.160.20; -; 2.
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   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; 2.
DR   SMART; SM00535; RIBOc; 1.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR   SUPFAM; SSF69065; RNase III domain-like; 1.
DR   PROSITE; PS50137; DS_RBD; 2.
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; Repeat; RNA-binding;
KW   rRNA processing; rRNA-binding; tRNA processing.
FT   CHAIN           1..357
FT                   /note="Ribonuclease 3"
FT                   /id="PRO_0000416613"
FT   DOMAIN          6..155
FT                   /note="RNase III"
FT   DOMAIN          198..267
FT                   /note="DRBM 1"
FT   DOMAIN          285..355
FT                   /note="DRBM 2"
FT   ACT_SITE        49
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        144
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   357 AA;  41045 MW;  9D9FE4E68BD9B326 CRC64;
     MDEKEIKFIQ DQIGYTFKNQ ELLVQAFTRR SYSMENGGQD NEVLEFIGDK ALDFVVVKQL
     SEEFGHYSKK YQNWEKWGKT EETGTFISDL DEGELTEIKK QLVQKNTLAD AIDNLGIAYY
     LIMGKGDVEK NIQDSLSVKE DLFEAILGAI ALDSNWDIEA LQDSMNVMLN PGELMFDEDV
     NYVAEIQAWS SANSGNIPLH CFYPTSMQGT WYMPRHHMCI YGKAEQDTHF ACEVLIPGID
     YHFVGYGRSK NLARMDASRL AYEYLKDEDM LFSIRDEIDD PNYNDSIGQL EILARRGYFS
     IPQYDFKETH DEDGNPVWNC KCSIKEKDTV TNGRSSSKKD AKKQAAYDML TFVLEEE
//