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Database: UniProt
Entry: Q04K72
LinkDB: Q04K72
Original site: Q04K72 
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-OCT-2014, entry version 54.
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};
GN   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). 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: Mg(2+). {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; 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; AQKDPKT; -.
DR   OrthoDB; EOG6T1WVS; -.
DR   BioCyc; SPNE373153:GIX6-1105-MONOMER; -.
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    232       Ribonuclease 3.
FT                                /FTId=PRO_1000075834.
FT   DOMAIN        5    134       RNase III. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
FT   DOMAIN      160    229       DRBM. {ECO:0000255|HAMAP-Rule:MF_00104}.
FT   ACT_SITE     51     51       {ECO:0000255|HAMAP-Rule:MF_00104}.
FT   ACT_SITE    123    123       {ECO:0000255|HAMAP-Rule:MF_00104}.
FT   METAL        47     47       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
FT   METAL       120    120       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
FT   METAL       123    123       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
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
//
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