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Database: UniProt
Entry: Q3B6L3
LinkDB: Q3B6L3
Original site: Q3B6L3 
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   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=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). 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; CP000096; ABB23018.1; -; Genomic_DNA.
DR   RefSeq; WP_011356894.1; NC_007512.1.
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; YGFQEAR; -.
DR   OrthoDB; EOG6T1WVS; -.
DR   BioCyc; PLUT319225:GHDM-138-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; Reference proteome;
KW   RNA-binding; rRNA processing; rRNA-binding; tRNA processing.
FT   CHAIN         1    276       Ribonuclease 3.
FT                                /FTId=PRO_0000228562.
FT   DOMAIN       30    161       RNase III. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
FT   DOMAIN      188    257       DRBM. {ECO:0000255|HAMAP-Rule:MF_00104}.
FT   ACT_SITE     78     78       {ECO:0000255|HAMAP-Rule:MF_00104}.
FT   ACT_SITE    150    150       {ECO:0000255|HAMAP-Rule:MF_00104}.
FT   METAL        74     74       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
FT   METAL       147    147       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
FT   METAL       150    150       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
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
//
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