ID RNC_SHIDS Reviewed; 226 AA.
AC Q32CV4;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 01-MAY-2013, entry version 47.
DE RecName: Full=Ribonuclease 3;
DE EC=3.1.26.3;
DE AltName: Full=Ribonuclease III;
DE Short=RNase III;
GN Name=rnc; OrderedLocusNames=SDY_2808;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA Qiang B., Hou Y., Yu J., Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic
RT agents of bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP000034; ABB62851.1; -; Genomic_DNA.
DR RefSeq; YP_404342.1; NC_007606.1.
DR ProteinModelPortal; Q32CV4; -.
DR SMR; Q32CV4; 5-224.
DR STRING; 300267.SDY_2808; -.
DR PRIDE; Q32CV4; -.
DR EnsemblBacteria; ABB62851; ABB62851; SDY_2808.
DR GeneID; 3795509; -.
DR KEGG; sdy:SDY_2808; -.
DR PATRIC; 18695934; VBIShiDys99784_3383.
DR eggNOG; COG0571; -.
DR HOGENOM; HOG000246809; -.
DR KO; K03685; -.
DR OMA; LTHKSCK; -.
DR ProtClustDB; PRK00102; -.
DR BioCyc; SDYS300267:GJEW-2804-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; Reference proteome;
KW RNA-binding; rRNA processing; rRNA-binding; tRNA processing.
FT CHAIN 1 226 Ribonuclease 3.
FT /FTId=PRO_0000228581.
FT DOMAIN 6 128 RNase III.
FT DOMAIN 155 225 DRBM.
FT ACT_SITE 45 45 Potential.
FT ACT_SITE 117 117 By similarity.
FT METAL 41 41 Magnesium (By similarity).
FT METAL 114 114 Magnesium (By similarity).
FT METAL 117 117 Magnesium (By similarity).
SQ SEQUENCE 226 AA; 25550 MW; D9E2858F2E0AA3A5 CRC64;
MNPIVINRLQ RKLGYTFNHQ ELLQQALTHR SASSKHNERL EFLGDSILSY VIANALYHRF
PRVDEGDMSR MRATLVRGNT LAELAREFEL GECLRLGPGE LKSGGFRRES ILADTVEALI
GGVFLDSDIQ TVEKLILNWY QTRLDEISPG DKQKDPKTRL QEYLQGRHLP LPTYLVVQVR
GEAHDQEFTI HCQVSGLSEP VVGTGSSRRK AEQAAAEQAL KKLELE
//
