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B2TJ22 (RNC_CLOBB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease 3

EC=3.1.26.3
Alternative name(s):
Ribonuclease III
Short name=RNase III
Gene names
Name:rnc
Ordered Locus Names:CLL_A1240
OrganismClostridium botulinum (strain Eklund 17B / Type B) [Complete proteome] [HAMAP]
Taxonomic identifier508765 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length232 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon By similarity. HAMAP-Rule MF_00104

Catalytic activity

Endonucleolytic cleavage to 5'-phosphomonoester. HAMAP-Rule MF_00104

Cofactor

Mg2+ By similarity. HAMAP-Rule MF_00104

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00104

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00104.

Sequence similarities

Contains 1 DRBM (double-stranded RNA-binding) domain.

Contains 1 RNase III domain.

Ontologies

Keywords
   Biological processmRNA processing
rRNA processing
tRNA processing
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
RNA-binding
rRNA-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processmRNA processing

Inferred from electronic annotation. Source: UniProtKB-HAMAP

rRNA catabolic process

Inferred from electronic annotation. Source: InterPro

rRNA processing

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

rRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

ribonuclease III activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 232232Ribonuclease 3 HAMAP-Rule MF_00104
PRO_1000094102

Regions

Domain6 – 133128RNase III
Domain160 – 22970DRBM

Sites

Active site501 Potential
Active site1221 By similarity
Metal binding461Magnesium By similarity
Metal binding1191Magnesium By similarity
Metal binding1221Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
B2TJ22 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: EEF0636D1717940C

FASTA23226,803
        10         20         30         40         50         60 
MNRYKFNDIE NRLGVYFNNP SLIKTALTHS SFGNQFKDAK YNERLEFLGD SVLQLCITEY 

        70         80         90        100        110        120 
LFNKFKDKSE GELTKIRSLI VCENSLYEIA KKLSLGEYIR MSKGEELTGG RERMSIQADA 

       130        140        150        160        170        180 
VEAVIAAVYL DKGIGFVNDF ILLHFEEMIN KAINNEIVLD FKTKLQELLQ KDGEILIQYE 

       190        200        210        220        230 
LVKYEGPPHR RKFFTNVIIN EKVMGIGEGY SKKEAEQNAA KEALKRLEKN YE 

« Hide

References

[1]"Complete sequence of Clostridium botulinum strain Eklund."
Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Eklund 17B / Type B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001056 Genomic DNA. Translation: ACD22926.1.
RefSeqYP_001885438.1. NC_010674.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING508765.CLL_A1240.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD22926; ACD22926; CLL_A1240.
GeneID6295060.
KEGGcbk:CLL_A1240.
PATRIC19395322. VBICloBot123574_1171.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0571.
HOGENOMHOG000246808.
KOK03685.
OMALTHKSCK.
OrthoDBEOG6T1WVS.
ProtClustDBPRK00102.

Enzyme and pathway databases

BioCycCBOT508765:GJ4H-1234-MONOMER.

Family and domain databases

Gene3D1.10.1520.10. 1 hit.
3.30.160.20. 1 hit.
HAMAPMF_00104. RNase_III.
InterProIPR014720. dsRNA-bd_dom.
IPR011907. RNase_III.
IPR000999. RNase_III_dom.
[Graphical view]
PANTHERPTHR11207. PTHR11207. 1 hit.
PfamPF00035. dsrm. 1 hit.
PF14622. Ribonucleas_3_3. 1 hit.
[Graphical view]
SMARTSM00358. DSRM. 1 hit.
SM00535. RIBOc. 1 hit.
[Graphical view]
SUPFAMSSF69065. SSF69065. 1 hit.
TIGRFAMsTIGR02191. RNaseIII. 1 hit.
PROSITEPS50137. DS_RBD. 1 hit.
PS00517. RNASE_3_1. 1 hit.
PS50142. RNASE_3_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRNC_CLOBB
AccessionPrimary (citable) accession number: B2TJ22
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: April 16, 2014
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families