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Database: UniProt
Entry: Q8G7H1
LinkDB: Q8G7H1
Original site: Q8G7H1 
ID   RNC_BIFLO               Reviewed;         242 AA.
AC   Q8G7H1;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   03-SEP-2014, entry version 66.
DE   RecName: Full=Ribonuclease 3;
DE            EC=3.1.26.3;
DE   AltName: Full=Ribonuclease III;
DE            Short=RNase III;
GN   Name=rnc; OrderedLocusNames=BL0295;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B.,
RA   Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M.,
RA   Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation
RT   to the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN24135.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; AE014295; AAN24135.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_695499.1; NC_004307.2.
DR   ProteinModelPortal; Q8G7H1; -.
DR   STRING; 206672.BL0295; -.
DR   EnsemblBacteria; AAN24135; AAN24135; BL0295.
DR   GeneID; 1022381; -.
DR   KEGG; blo:BL0295; -.
DR   PATRIC; 21119145; VBIBifLon107831_1032.
DR   eggNOG; COG0571; -.
DR   HOGENOM; HOG000246808; -.
DR   KO; K03685; -.
DR   OMA; FANENGH; -.
DR   OrthoDB; EOG6T1WVS; -.
DR   BioCyc; BLON206672:GI1E-973-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; Reference proteome;
KW   RNA-binding; rRNA processing; rRNA-binding; tRNA processing.
FT   CHAIN         1    242       Ribonuclease 3.
FT                                /FTId=PRO_0000228502.
FT   DOMAIN       12    139       RNase III.
FT   DOMAIN      165    236       DRBM.
FT   ACT_SITE     55     55       Potential.
FT   ACT_SITE    128    128       By similarity.
FT   METAL        51     51       Magnesium (By similarity).
FT   METAL       125    125       Magnesium (By similarity).
FT   METAL       128    128       Magnesium (By similarity).
SQ   SEQUENCE   242 AA;  26080 MW;  AA294ECE97373D1C CRC64;
     MSNETPQQPT PANELLEALG TTLSPDLLVQ ALTHRSFSHE HPGVANYERL EFLGDAVLEL
     VSTETLFTIH PDMTEGQLAK MRAKAVSEDA LSAIAKTKLK VGPYILLGHG EAEQGGAEKN
     SILCDIVESL IGATFLEHGI DEARKVIHRL IDDTLAEVAT EGPALDWKTS LTVKAHGLGK
     EEPVYHMEVS GPEYAQIFTA RVSLGENGDI IGIGKGSSKR KAQLAAAEAG WKSLDSFKTR
     TK
//
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