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Database: UniProt
Entry: A3CP46
LinkDB: A3CP46
Original site: A3CP46 
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   29-OCT-2014, entry version 57.
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=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). 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; 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; AQKDPKT; -.
DR   OrthoDB; EOG6T1WVS; -.
DR   BioCyc; SSAN388919:GHEN-1529-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
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_1000075840.
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;  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
//
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