ID RNC_PELLD Reviewed; 276 AA.
AC Q3B6L3;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, 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=Plut_0128;
OS Pelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM
OS 273)).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=319225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 273;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelodictyon luteolum DSM 273.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000096; ABB23018.1; -; Genomic_DNA.
DR RefSeq; YP_374061.1; NC_007512.1.
DR ProteinModelPortal; Q3B6L3; -.
DR STRING; 319225.Plut_0128; -.
DR EnsemblBacteria; ABB23018; ABB23018; Plut_0128.
DR GeneID; 3744685; -.
DR KEGG; plt:Plut_0128; -.
DR PATRIC; 21377689; VBIChlLut1287_0134.
DR eggNOG; COG0571; -.
DR HOGENOM; HOG000246808; -.
DR KO; K03685; -.
DR OMA; RACELPR; -.
DR ProtClustDB; CLSK2772499; -.
DR BioCyc; PLUT319225:GHDM-180-MONOMER; -.
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 1 276 Ribonuclease 3.
FT /FTId=PRO_0000228562.
FT DOMAIN 30 161 RNase III.
FT DOMAIN 188 257 DRBM.
FT ACT_SITE 78 78 Potential.
FT ACT_SITE 150 150 By similarity.
FT METAL 74 74 Magnesium (By similarity).
FT METAL 147 147 Magnesium (By similarity).
FT METAL 150 150 Magnesium (By similarity).
SQ SEQUENCE 276 AA; 30413 MW; D2CF8A075DA76E73 CRC64;
MEPLWHKLSA LPFFSSRPEK WEGSGAPPSL TAFIRSLFKG KALSLELYAT ALTHRSMVHD
TTAPEITRSN QRLEFLGDSV LGLIISEYLY RRFPEGTEGE LSSYRAKIVN GKSLAGFARN
LDLGIHLIIG ESADQQRIRT STSTLADAFE ALTGAIYLDR GLDAVREFIE EQIIDSPAFE
AMVSTENNHK SRLIEHTQSH QLPPPVYTVL SEEGAEHEKT FTIEVSCNGR RLGRGTALRK
KDAEQLAAEE AMGALERALT GDVAEDTPAP EETGRG
//
