RNC_FRATN
ID RNC_FRATN Reviewed; 230 AA.
AC A0Q7W6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=FTN_1463;
OS Francisella tularensis subsp. novicida (strain U112).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=401614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U112;
RX PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102;
RA Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M.,
RA Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C.,
RA Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J.,
RA Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A.,
RA Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V.,
RA Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.;
RT "Comparison of Francisella tularensis genomes reveals evolutionary events
RT associated with the emergence of human pathogenic strains.";
RL Genome Biol. 8:R102.1-R102.16(2007).
RN [2]
RP FUNCTION.
RC STRAIN=U112;
RX PubMed=24270795; DOI=10.1093/nar/gkt1074;
RA Fonfara I., Le Rhun A., Chylinski K., Makarova K.S., Lecrivain A.L.,
RA Bzdrenga J., Koonin E.V., Charpentier E.;
RT "Phylogeny of Cas9 determines functional exchangeability of dual-RNA and
RT Cas9 among orthologous type II CRISPR-Cas systems.";
RL Nucleic Acids Res. 42:2577-2590(2014).
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 (By similarity).
CC {ECO:0000250}.
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 tracrRNA are required for cleavage of invading DNA
CC (Probable). Complements pre-crRNA and tracrRNA coprocessing defects in
CC an rnc deletion in S.pyogenes strain 370 (PubMed:24270795).
CC {ECO:0000269|PubMed:24270795, ECO:0000305}.
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; CP000439; ABK90331.1; -; Genomic_DNA.
DR RefSeq; WP_003034807.1; NZ_CP009633.1.
DR AlphaFoldDB; A0Q7W6; -.
DR SMR; A0Q7W6; -.
DR EnsemblBacteria; ABK90331; ABK90331; FTN_1463.
DR GeneID; 60806660; -.
DR KEGG; ftn:FTN_1463; -.
DR OMA; LTHKSCK; -.
DR OrthoDB; 1890943at2; -.
DR BioCyc; FTUL401614:G1G75-1511-MON; -.
DR Proteomes; UP000000762; 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 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..230
FT /note="Ribonuclease 3"
FT /id="PRO_1000075757"
FT DOMAIN 5..125
FT /note="RNase III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT DOMAIN 153..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 114
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 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
SQ SEQUENCE 230 AA; 26229 MW; FC742D0460DF4859 CRC64;
MVPEYSRFYN ILGYNFKDYT LLIRALTHRS KTKKNYERLE FLGDSVLSFV IAEVLYKQFT
DLAEGKLSQL RSKLVKGTTL AQLASSLKMD EYIILGASEQ GGHKREKILE DVFEAVIGAI
YLDSDFATVK KVILKWYQPI ISSINLDTIK VKDSKSKLQE ILLQNALSLP EYSIETIDGK
DHEQQFTVVA MSKDLNLRVK AQGTSRKKAE QKAAEKMIEM LSQQGLHEKK
