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B2GD42 (RNC_LACF3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 43. 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:LAF_1238
OrganismLactobacillus fermentum (strain NBRC 3956 / LMG 18251) [Complete proteome] [HAMAP]
Taxonomic identifier334390 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

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_1000094117

Regions

Domain6 – 135130RNase III
Domain161 – 23070DRBM

Sites

Active site521 Potential
Active site1241 By similarity
Metal binding481Magnesium By similarity
Metal binding1211Magnesium By similarity
Metal binding1241Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
B2GD42 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: D94449495F16DA5B

FASTA23226,461
        10         20         30         40         50         60 
MITQLQDYLA KTYGIHFNNP ALLAEAFTQA SYVNEHPHEN LKYYERIEFL GDAVLQLFVS 

        70         80         90        100        110        120 
EYIYRRYPEL PQGKLTRLRA AMVCEDSFSK FAKECHFDQY IRLGKGEEMA GARNRASLLC 

       130        140        150        160        170        180 
DIFESFIGAL YLDQGRQAVE QFIQTVIFPK LDLGWFDHAV DAKTSLQEFL QRNGDVAIEY 

       190        200        210        220        230 
DLLSEGGTEN DPVFEVEVTV DGKKVATGQG SSKKHAEMEA AKHALEKLRM DK 

« Hide

References

[1]"Comparative genome analysis of Lactobacillus reuteri and Lactobacillus fermentum reveal a genomic island for reuterin and cobalamin production."
Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T., Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T., Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T., Hattori M.
DNA Res. 15:151-161(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NBRC 3956 / LMG 18251.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008937 Genomic DNA. Translation: BAG27574.1.
RefSeqYP_001844054.1. NC_010610.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING334390.LAF_1238.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG27574; BAG27574; LAF_1238.
GeneID6232106.
KEGGlfe:LAF_1238.
PATRIC22226754. VBILacFer15497_1361.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycLFER334390:GJ2S-1285-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.
PS50142. RNASE_3_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRNC_LACF3
AccessionPrimary (citable) accession number: B2GD42
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: April 16, 2014
This is version 43 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