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Database: UniProt
Entry: B5XKB7
LinkDB: B5XKB7
Original site: B5XKB7 
ID   RNC_STRPZ               Reviewed;         230 AA.
AC   B5XKB7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-SEP-2014, entry version 42.
DE   RecName: Full=Ribonuclease 3;
DE            EC=3.1.26.3;
DE   AltName: Full=Ribonuclease III;
DE            Short=RNase III;
GN   Name=rnc; OrderedLocusNames=Spy49_0447;
OS   Streptococcus pyogenes serotype M49 (strain NZ131).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=471876;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZ131;
RX   PubMed=18820018; DOI=10.1128/JB.00672-08;
RA   McShan W.M., Ferretti J.J., Karasawa T., Suvorov A.N., Lin S., Qin B.,
RA   Jia H., Kenton S., Najar F., Wu H., Scott J., Roe B.A., Savic D.J.;
RT   "Genome sequence of a nephritogenic and highly transformable M49
RT   strain of Streptococcus pyogenes.";
RL   J. Bacteriol. 190:7773-7785(2008).
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 (By 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; CP000829; ACI60779.1; -; Genomic_DNA.
DR   RefSeq; YP_002285474.1; NC_011375.1.
DR   ProteinModelPortal; B5XKB7; -.
DR   STRING; 471876.Spy49_0447; -.
DR   EnsemblBacteria; ACI60779; ACI60779; Spy49_0447.
DR   GeneID; 6985466; -.
DR   KEGG; soz:Spy49_0447; -.
DR   PATRIC; 19755916; VBIStrPyo129711_0471.
DR   eggNOG; COG0571; -.
DR   HOGENOM; HOG000246808; -.
DR   KO; K03685; -.
DR   OMA; AQKDPKT; -.
DR   OrthoDB; EOG6T1WVS; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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    230       Ribonuclease 3.
FT                                /FTId=PRO_1000094138.
FT   DOMAIN        1    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   230 AA;  25876 MW;  D0107D9055B58273 CRC64;
     MKQLEELLST SFDIQFNDLT LLETAFTHTS YANEHRLLNV SHNERLEFLG DAVLQLIISE
     YLFAKYPKKT EGDMSKLRSM IVREESLAGF SRFCSFDAYI KLGKGEEKSG GRRRDTILGD
     LFEAFLGALL LDKGIDAVRR FLKQVMIPQV EKGNFERVKD YKTCLQEFLQ TKGDVVIDYQ
     VISEKGPAHA KQFEVSIVVN GAVLSKGLGK SKKLAEQDAA KNALAQLSEV
//
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