RNC_NEIM8
ID RNC_NEIM8 Reviewed; 239 AA.
AC C9X0M5;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
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};
GN Name=rnc {ECO:0000255|HAMAP-Rule:MF_00104}; OrderedLocusNames=NMV_1713;
OS Neisseria meningitidis serogroup C (strain 8013).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=604162;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8013;
RX PubMed=19818133; DOI=10.1186/gb-2009-10-10-r110;
RA Rusniok C., Vallenet D., Floquet S., Ewles H., Mouze-Soulama C., Brown D.,
RA Lajus A., Buchrieser C., Medigue C., Glaser P., Pelicic V.;
RT "NeMeSys: a biological resource for narrowing the gap between sequence and
RT function in the human pathogen Neisseria meningitidis.";
RL Genome Biol. 10:R110.1-R110.13(2009).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=8013;
RX PubMed=23706818; DOI=10.1016/j.molcel.2013.05.001;
RA Zhang Y., Heidrich N., Ampattu B.J., Gunderson C.W., Seifert H.S.,
RA Schoen C., Vogel J., Sontheimer E.J.;
RT "Processing-independent CRISPR RNAs limit natural transformation in
RT Neisseria meningitidis.";
RL Mol. Cell 50:488-503(2013).
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). Also processes some mRNAs, and tRNAs
CC when they are encoded in the rRNA operon.
CC {ECO:0000269|PubMed:23706818}.
CC -!- FUNCTION: CRISPR (clustered regularly interspaced short palindromic
CC repeat) is an adaptive immune system that provides protection against
CC mobile genetic elements (viruses, transposable elements and conjugative
CC plasmids). CRISPR clusters contain spacers, sequences complementary to
CC antecedent mobile elements, and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA). In this
CC organism endogenous ribonuclease 3 and Cas9 are required for correct
CC coprocessing of pre-crRNA and the trans-encoded small RNA (tracrRNA).
CC Cas9, crRNA and tracRNA are required for cleavage of invading DNA.
CC Involved in 3'-end processing but not 5'-end processing of crRNA and
CC tracrRNA (PubMed:23706818). {ECO:0000269|PubMed:23706818}.
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 -!- DISRUPTION PHENOTYPE: Altered processing of 3' end of CRISPR crRNA and
CC tracrRNA, but no effect on CRISPR interference during plasmid
CC transformation. {ECO:0000269|PubMed:23706818}.
CC -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000255|HAMAP-
CC Rule:MF_00104}.
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DR EMBL; FM999788; CAX50526.1; -; Genomic_DNA.
DR RefSeq; WP_002225498.1; NC_017501.1.
DR AlphaFoldDB; C9X0M5; -.
DR SMR; C9X0M5; -.
DR KEGG; nmt:NMV_1713; -.
DR PATRIC; fig|604162.3.peg.2008; -.
DR HOGENOM; CLU_000907_1_1_4; -.
DR OMA; LTHKSCK; -.
DR Proteomes; UP000002076; 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_0000429990"
FT DOMAIN 11..133
FT /note="RNase III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT DOMAIN 160..230
FT /note="DRBM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT ACT_SITE 50
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
SQ SEQUENCE 239 AA; 26853 MW; 54D0F0473049607C CRC64;
MKDDVLKQQA HAAIQKKLGY AFRDISLLRQ ALTHRSHHAK HNERFEFVGD SILNYTVARM
LFDAFPKLTE GELSRLRASL VNEGVLAEMA AEMNVGDGLY LGAGELKSGG FRRPSILADA
MEAMFAAVSF DADFNTAEKV VRHLFADRVR RADFQNQAKD GKTALQEALQ ARRFALPKYR
IEEQIGYAND SMFVISCDLG ELGFVCRAKG TSRKAAEQEA AKEALKWLEE KLPLKRKKK
