ID RNC_STRSV Reviewed; 232 AA.
AC A3CP46;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, 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=SSA_1561;
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36;
RX PubMed=17277061; DOI=10.1128/JB.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S.,
RA Manque P., Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y.,
RA Chaplin M.D., Akan D., Paik S., Peterson D.L., Macrina F.L.,
RA Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(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; CP000387; ABN44951.1; -; Genomic_DNA.
DR RefSeq; YP_001035501.1; NC_009009.1.
DR ProteinModelPortal; A3CP46; -.
DR STRING; 388919.SSA_1561; -.
DR EnsemblBacteria; ABN44951; ABN44951; SSA_1561.
DR GeneID; 4805927; -.
DR KEGG; ssa:SSA_1561; -.
DR PATRIC; 19770049; VBIStrSan33173_1481.
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_1000075840.
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; 26166 MW; A2D53F3F7EA943D5 CRC64;
MENLKKALLE QFDLVFSDET LLETAFTHTS YANEHRLLKI SHNERLEFLG DAVLQLIISE
YLYTKYPKRP EGDLSKLRSM IVREESLAGF ARDCQFDQFI KLGRGEEKSG GRNRDTILGD
LFEAFLGALL LDKGVEAVKS FLYQVMIPKV EAGDFERVTD YKTKLQELLQ INGDVEIAYQ
VVSETGPAHA KNFEVAVLIN GRKSGQGQGR SKKLAEQEAA KNAFEKESSS CF
//
