Q2KWY0 (RNC_BORA1) 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:	BAV1131

Organism

Bordetella avium (strain 197N) [Complete proteome] [HAMAP]

Taxonomic identifier

360910 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella › Bordetella avium

Protein attributes

Sequence length	251 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.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
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 – 251	251	Ribonuclease 3 HAMAP-Rule MF_00104		PRO_1000075727
Regions
	Domain	3 – 125	123	RNase III
	Domain	152 – 222	71	DRBM
Sites
	Active site	42	1	Potential
	Active site	114	1	By similarity
	Metal binding	38	1	Magnesium By similarity
	Metal binding	111	1	Magnesium By similarity
	Metal binding	114	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2KWY0 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: 2822E847AD14BFFE	FASTA	251	27,144
	10 20 30 40 50 60 MSLATLETRL GHHFGDQALL EQALTHRSHG ARHNERLEFL GDSVLNFVVA AMLFERYAKL 70 80 90 100 110 120 DEGDLSRVRA NLVKQASLAD IAQRLELSPY LRLGEGEMKS GGFRRPSILA DAVEALFGAV 130 140 150 160 170 180 FLDAGFDAAR KVIEQQYVPV LANVDPETLG KDAKTLLQEF LQGRKLALPL YTVVATHGAA 190 200 210 220 230 240 HSQQFEVECA IPALEIKVTA AGASRRAAEQ SAAKLALEAA LVVSPRATRK GGRARKTAQL 250 SLPVAVAQEV K

References

[1]

"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction." Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M. J. Bacteriol. 188:6002-6015(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 197N.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM167904 Genomic DNA. Translation: CAJ48740.1.
RefSeq	YP_785654.1. NC_010645.1.
3D structure databases
HSSP	HSSP built from PDB template 1O0W based on UniProtKB Q9X0I6.
ProteinModelPortal	Q2KWY0.
ModBase	Search...
Protein-protein interaction databases
STRING	360910.BAV1131.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6267285.
KEGG	bav:BAV1131.
PATRIC	21128470. VBIBorAvi43433_1159.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0571.
HOGENOM	HOG000246809.
KO	K03685.
OMA	LTHKSCK.
ProtClustDB	PRK00102.
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_BORA1

Accession

Primary (citable) accession number: Q2KWY0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	March 7, 2006
Last modified:	May 1, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program