Q7W5J6 (RNC_BORPA) 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:	BPP3295

Organism

Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253) [Complete proteome] [HAMAP]

Taxonomic identifier

257311 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	256 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 – 256	256	Ribonuclease 3 HAMAP-Rule MF_00104		PRO_0000228506
Regions
	Domain	6 – 128	123	RNase III
	Domain	155 – 225	71	DRBM
Sites
	Active site	45	1	Potential
	Active site	117	1	By similarity
	Metal binding	41	1	Magnesium By similarity
	Metal binding	114	1	Magnesium By similarity
	Metal binding	117	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7W5J6 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 36B8A148A035A807	FASTA	256	27,829
	10 20 30 40 50 60 MTAMSLATLE TRLDHRFGDK ALLEQALTHR SHGARHNERL EFLGDSVLNF VVAAMLFERY 70 80 90 100 110 120 GKLDEGDLSR LRANLVKQAS LADIAQRLDL SQYLRLGEGE LKSGGFRRPS ILADTVEALF 130 140 150 160 170 180 GAVFLDAGFE AARRVIVRQY QPVMAHVDPK TLGKDAKTLL QEFLQGRKLA LPQYTVVATH 190 200 210 220 230 240 GAAHSQQFEV ECAIPALEIK IVAPGASRRA AEQSAAKVAL EAAQAVLPAA RAARKSGKAR 250 KTAQLSLPVA VAQEVK

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 12822 / ATCC BAA-587 / NCTC 13253.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640433 Genomic DNA. Translation: CAE38580.1.
RefSeq	NP_885462.1. NC_002928.3.
3D structure databases
ProteinModelPortal	Q7W5J6.
ModBase	Search...
Protein-protein interaction databases
STRING	257311.BPP3295.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAE38580; CAE38580; BPP3295.
GeneID	1666150.
KEGG	bpa:BPP3295.
PATRIC	21150570. VBIBorPar43418_3460.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0571.
HOGENOM	HOG000246809.
KO	K03685.
OMA	LTHKSCK.
ProtClustDB	PRK00102.
Enzyme and pathway databases
BioCyc	BPAR257311:BPP3295-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_BORPA

Accession

Primary (citable) accession number: Q7W5J6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	October 1, 2003
Last modified:	May 1, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program