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Database: UniProt
Entry: Q5WVI4
LinkDB: Q5WVI4
Original site: Q5WVI4 
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   26-NOV-2014, 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};
DE            Short=RNase III {ECO:0000255|HAMAP-Rule:MF_00104};
GN   Name=rnc {ECO:0000255|HAMAP-Rule:MF_00104}; 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). Processes some mRNAs, and
CC       tRNAs when they are encoded in the rRNA operon. Processes pre-
CC       crRNA and tracrRNA of type II CRISPR loci if present in the
CC       organism. {ECO:0000255|HAMAP-Rule:MF_00104}.
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC       phosphomonoester. {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: Contains 1 DRBM (double-stranded RNA-binding) domain.
CC       {ECO:0000255|HAMAP-Rule:MF_00104}.
CC   -!- SIMILARITY: Contains 1 RNase III domain. {ECO:0000255|HAMAP-
CC       Rule:MF_00104}.
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DR   EMBL; CR628337; CAH16070.1; -; Genomic_DNA.
DR   RefSeq; WP_011215832.1; NC_006369.1.
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; AQKDPKT; -.
DR   OrthoDB; EOG6T1WVS; -.
DR   BioCyc; LPNE297245:GJD4-1972-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004525; F:ribonuclease III activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016075; P:rRNA catabolic process; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-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; IPR014720; dsRNA-bd_dom.
DR   InterPro; IPR011907; RNase_III.
DR   InterPro; IPR000999; RNase_III_dom.
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   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. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
FT   DOMAIN      154    224       DRBM. {ECO:0000255|HAMAP-Rule:MF_00104}.
FT   ACT_SITE     44     44       {ECO:0000255|HAMAP-Rule:MF_00104}.
FT   ACT_SITE    116    116       {ECO:0000255|HAMAP-Rule:MF_00104}.
FT   METAL        40     40       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
FT   METAL       113    113       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
FT   METAL       116    116       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
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
//
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