ID   RNC_SULNB               Reviewed;         223 AA.
AC   A6QCJ0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=SUN_2259;
OS   Sulfurovum sp. (strain NBC37-1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurovaceae; Sulfurovum; unclassified Sulfurovum.
OX   NCBI_TaxID=387093;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBC37-1;
RX   PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA   Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA   Horikoshi K.;
RT   "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT   emergence of pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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; AP009179; BAF73199.1; -; Genomic_DNA.
DR   RefSeq; WP_012084037.1; NC_009663.1.
DR   AlphaFoldDB; A6QCJ0; -.
DR   SMR; A6QCJ0; -.
DR   STRING; 387093.SUN_2259; -.
DR   EnsemblBacteria; BAF73199; BAF73199; SUN_2259.
DR   KEGG; sun:SUN_2259; -.
DR   eggNOG; COG0571; Bacteria.
DR   HOGENOM; CLU_000907_1_3_7; -.
DR   OMA; LTHKSCK; -.
DR   OrthoDB; 1890943at2; -.
DR   Proteomes; UP000006378; 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   PANTHER; PTHR11207; PTHR11207; 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; 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; Reference proteome; RNA-binding;
KW   rRNA processing; rRNA-binding; tRNA processing.
FT   CHAIN           1..223
FT                   /note="Ribonuclease 3"
FT                   /id="PRO_1000075842"
FT   DOMAIN          4..127
FT                   /note="RNase III"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   DOMAIN          154..223
FT                   /note="DRBM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   ACT_SITE        116
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   BINDING         40
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   BINDING         113
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
SQ   SEQUENCE   223 AA;  24904 MW;  A6351D94BA59F2C1 CRC64;
     MNDYSQLEKR LNYTFKDKQL IIEALTHKSY KKPYNNERLE FLGDAVLDLI VGEYLFKKFP
     KSDEGILSKI RASLVNESGF TLLARKIDLG SYIYLSLAEE NNNGRDKPSL LSNAFEAIIG
     AVYLEAGLDT AKEISIKLLE ECHPKIDLQS LSKDYKTALQ ELTQATHAVT PGYEMLGSSG
     PDHKKEFEIA VTLDNKTIAT AKGKSKKDAQ QKAAKIALEA LKK