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RNC_HELPJ
ID   RNC_HELPJ               Reviewed;         239 AA.
AC   Q9ZLH2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 123.
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=jhp_0607;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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; AE001439; AAD06188.1; -; Genomic_DNA.
DR   PIR; E71911; E71911.
DR   RefSeq; WP_001889758.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZLH2; -.
DR   SMR; Q9ZLH2; -.
DR   STRING; 85963.jhp_0607; -.
DR   EnsemblBacteria; AAD06188; AAD06188; jhp_0607.
DR   KEGG; hpj:jhp_0607; -.
DR   PATRIC; fig|85963.30.peg.378; -.
DR   eggNOG; COG0571; Bacteria.
DR   OMA; LTHKSCK; -.
DR   Proteomes; UP000000804; 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; RNA-binding; rRNA processing; rRNA-binding;
KW   tRNA processing.
FT   CHAIN           1..239
FT                   /note="Ribonuclease 3"
FT                   /id="PRO_0000180402"
FT   DOMAIN          18..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   239 AA;  27276 MW;  197DF81F5BE701D5 CRC64;
     MKNKRSQNSP YVTPDNPYLT LEKALGYSFK DKRLLEQALT HKSCKLALNN ERLEFLGDAV
     LGLVIGELLY HKFYQYDEGK LSKLRASIVS AHGFTKLAKA IALQDYLRVS SSEEISKGRE
     KPSILSSAFE ALMAGVYLEA GLAKVRKIIQ NLLNRAYKRL DLEHLFMDYK TALQELTQAQ
     FCVIPTYQLL QEKGPDHHKE FEMALYIQDK MYATAKGKSK KEAEQQCAYQ ALQKLKEAK
 
 
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