ID RNC_STRP2 Reviewed; 232 AA.
AC Q04K72;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 01-MAY-2013, entry version 45.
DE RecName: Full=Ribonuclease 3;
DE EC=3.1.26.3;
DE AltName: Full=Ribonuclease III;
DE Short=RNase III;
GN Name=rnc; OrderedLocusNames=SPD_1105;
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466;
RX PubMed=17041037; DOI=10.1128/JB.01148-06;
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M.,
RA Davidsen T.M., Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of
RT Streptococcus pneumoniae and comparison with that of unencapsulated
RT laboratory strain R6.";
RL J. Bacteriol. 189:38-51(2007).
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; CP000410; ABJ55368.1; -; Genomic_DNA.
DR RefSeq; YP_816576.1; NC_008533.1.
DR ProteinModelPortal; Q04K72; -.
DR STRING; 373153.SPD_1105; -.
DR EnsemblBacteria; ABJ55368; ABJ55368; SPD_1105.
DR GeneID; 4441922; -.
DR KEGG; spd:SPD_1105; -.
DR PATRIC; 19683388; VBIStrPne27904_1229.
DR eggNOG; COG0571; -.
DR HOGENOM; HOG000246808; -.
DR KO; K03685; -.
DR OMA; LTHKSCK; -.
DR ProtClustDB; PRK00102; -.
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 1 232 Ribonuclease 3.
FT /FTId=PRO_1000075834.
FT DOMAIN 5 134 RNase III.
FT DOMAIN 160 229 DRBM.
FT ACT_SITE 51 51 Potential.
FT ACT_SITE 123 123 By similarity.
FT METAL 47 47 Magnesium (By similarity).
FT METAL 120 120 Magnesium (By similarity).
FT METAL 123 123 Magnesium (By similarity).
SQ SEQUENCE 232 AA; 26226 MW; E95C0901B81E4C9B CRC64;
MKELQTVLKN HFEIEFADKK LLETAFTHTS YANEHRLLKI SHNERLEFLG DAVLQLLISE
YLYKKYPKKP EGDLSKLRAM IVREESLAGF ARDCQFDQFI KLGKGEEKSG GRNRDTILGD
AFEAFLGALL LDKDVAKVKE FIYQVMIPKV EAGEFEMITD YKTHLQELLQ VNGDVAIRYQ
VISETGPAHD KVFDVEVLVE GKSIGQGQGR SKKLAEQEAA KNAVEKGLDS CI
//
