B1LCY9 (RNC_THESQ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonuclease 3
EC=3.1.26.3

Alternative name(s):
Ribonuclease III
Short name=RNase III

Gene names

Name:	rnc
Ordered Locus Names:	TRQ2_1714

Organism

Thermotoga sp. (strain RQ2) [Complete proteome] [HAMAP]

Taxonomic identifier

126740 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Thermotogae › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	240 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	mRNA processing rRNA processing tRNA processing
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding RNA-binding rRNA-binding
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	mRNA processing Inferred from electronic annotation. Source: HAMAP nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC rRNA catabolic process Inferred from electronic annotation. Source: InterPro rRNA processing Inferred from electronic annotation. Source: HAMAP tRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	double-stranded RNA binding Inferred from electronic annotation. Source: InterPro metal 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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 240	240	Ribonuclease 3 HAMAP-Rule MF_00104		PRO_1000094139
Regions
	Domain	9 – 141	133	RNase III
	Domain	168 – 237	70	DRBM
Sites
	Active site	58	1	Potential
	Active site	130	1	By similarity
	Metal binding	54	1	Magnesium By similarity
	Metal binding	127	1	Magnesium By similarity
	Metal binding	130	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	B1LCY9 [UniParc]. Last modified April 29, 2008. Version 1. Checksum: B111D2B2A7E1C573	FASTA	240	27,509
	10 20 30 40 50 60 MNESERKIVE EFQKKTGINF KNEELLFRAL CHSSYANEQN QAGRKNVESN EKLEFLGDAV 70 80 90 100 110 120 LELFVCEILY KKYPEAEVGD LARVKSAAAS EEVLALVSRK MNLGKFLFLG KGEEKTGGRD 130 140 150 160 170 180 RDSILADAFE ALLAAIYLDQ GYEKIKELFE QEFEFYIEKI MKGEMLFDYK TALQEIVQSE 190 200 210 220 230 240 HKVPPEYVLV RTEKNDGDRI FVVEVRVDGK TIATGRGRTK KEAEKEAARI AYEKLLKERA

References

[1]

"Complete sequence of Thermotoga sp. RQ2." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Bruce D.B., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. , Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P. Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RQ2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000969 Genomic DNA. Translation: ACB10048.1.
RefSeq	YP_001739731.1. NC_010483.1.
3D structure databases
ProteinModelPortal	B1LCY9.
SMR	B1LCY9. Positions 1-237.
ModBase	Search...
Protein-protein interaction databases
STRING	126740.TRQ2_1714.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACB10048; ACB10048; TRQ2_1714.
GeneID	6093165.
KEGG	trq:TRQ2_1714.
PATRIC	23950088. VBITheSp108950_1749.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0571.
HOGENOM	HOG000246808.
KO	K03685.
OMA	LTHKSCK.
ProtClustDB	PRK00102.
Enzyme and pathway databases
BioCyc	TSP126740:GH49-1766-MONOMER.
Family and domain databases
Gene3D	1.10.1520.10. 1 hit. 3.30.160.20. 1 hit.
HAMAP	MF_00104. RNase_III.
InterPro	IPR001159. Ds-RNA-bd. IPR014720. dsRNA-bd-like_dom. IPR011907. RNase_III. IPR000999. RNase_III_dom. [Graphical view]
PANTHER	PTHR11207. PTHR11207. 1 hit.
Pfam	PF00035. dsrm. 1 hit. PF00636. Ribonuclease_3. 1 hit. [Graphical view]
SMART	SM00358. DSRM. 1 hit. SM00535. RIBOc. 1 hit. [Graphical view]
SUPFAM	SSF69065. RNase_III. 1 hit.
TIGRFAMs	TIGR02191. RNaseIII. 1 hit.
PROSITE	PS50137. DS_RBD. 1 hit. PS00517. RNASE_3_1. 1 hit. PS50142. RNASE_3_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RNC_THESQ

Accession

Primary (citable) accession number: B1LCY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	April 29, 2008
Last modified:	May 29, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program