ID RNC_LEGPL Reviewed; 224 AA.
AC Q5WVI4;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 01-MAY-2013, entry version 53.
DE RecName: Full=Ribonuclease 3;
DE EC=3.1.26.3;
DE AltName: Full=Ribonuclease III;
DE Short=RNase III;
GN Name=rnc; OrderedLocusNames=lpl1831;
OS Legionella pneumophila (strain Lens).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=297245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lens;
RX PubMed=15467720; DOI=10.1038/ng1447;
RA Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F.,
RA Etienne J., Glaser P., Buchrieser C.;
RT "Evidence in the Legionella pneumophila genome for exploitation of
RT host cell functions and high genome plasticity.";
RL Nat. Genet. 36:1165-1173(2004).
CC -!- FUNCTION: Digests double-stranded RNA. Involved in the processing
CC of primary rRNA transcript to yield the immediate precursors to
CC the large and small rRNAs (23S and 16S). Also processes some
CC mRNAs, and tRNAs when they are encoded in the rRNA operon (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC phosphomonoester.
CC -!- COFACTOR: Mg(2+) (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Contains 1 DRBM (double-stranded RNA-binding) domain.
CC -!- SIMILARITY: Contains 1 RNase III domain.
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DR EMBL; CR628337; CAH16070.1; -; Genomic_DNA.
DR RefSeq; YP_127169.1; NC_006369.1.
DR ProteinModelPortal; Q5WVI4; -.
DR STRING; 297245.lpl1831; -.
DR EnsemblBacteria; CAH16070; CAH16070; lpl1831.
DR GeneID; 3114511; -.
DR KEGG; lpf:lpl1831; -.
DR PATRIC; 22317393; VBILegPne33733_2017.
DR LegioList; lpl1831; -.
DR eggNOG; COG0571; -.
DR HOGENOM; HOG000246809; -.
DR KO; K03685; -.
DR OMA; LTHKSCK; -.
DR ProtClustDB; PRK00102; -.
DR BioCyc; LPNE297245:GJD4-1972-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:HAMAP.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:HAMAP.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0016075; P:rRNA catabolic process; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:HAMAP.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1520.10; -; 1.
DR Gene3D; 3.30.160.20; -; 1.
DR HAMAP; MF_00104; RNase_III; 1; -.
DR InterPro; IPR001159; Ds-RNA-bd.
DR InterPro; IPR014720; dsRNA-bd-like_dom.
DR InterPro; IPR011907; RNase_III.
DR InterPro; IPR000999; RNase_III_dom.
DR PANTHER; PTHR11207; PTHR11207; 1.
DR Pfam; PF00035; dsrm; 1.
DR Pfam; PF00636; Ribonuclease_3; 1.
DR SMART; SM00358; DSRM; 1.
DR SMART; SM00535; RIBOc; 1.
DR SUPFAM; SSF69065; RNase_III; 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 Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Magnesium;
KW Metal-binding; mRNA processing; Nuclease; RNA-binding;
KW rRNA processing; rRNA-binding; tRNA processing.
FT CHAIN 1 224 Ribonuclease 3.
FT /FTId=PRO_0000228542.
FT DOMAIN 5 127 RNase III.
FT DOMAIN 154 224 DRBM.
FT ACT_SITE 44 44 Potential.
FT ACT_SITE 116 116 By similarity.
FT METAL 40 40 Magnesium (By similarity).
FT METAL 113 113 Magnesium (By similarity).
FT METAL 116 116 Magnesium (By similarity).
SQ SEQUENCE 224 AA; 25140 MW; FB570670F91BA392 CRC64;
MKINLERLCR RLNYHFNNMA YLKQALTHCS AGSDNYERFE FLGDSILSFV IANELFNRFP
LHSEGQLSRL RSFLVKGEML AEIAREIGLG DYLFLGQGEL RSGGFRRTSI LADALEAILA
AIYLDGGMTA AKQIILMLYS SRLDDPDLNH CLKDAKTQLQ EFLQASKFAL PEYVLTKVEG
DEHAQIFHVT CTIEGVSQVA YGTGPNRRKA EQLAAKAMLE QLQG
//
