Q2YMC3 (RNH2_BRUA2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonuclease HII
Short name=RNase HII
EC=3.1.26.4

Gene names

Name:	rnhB
Ordered Locus Names:	BAB1_0415

Organism

Brucella abortus (strain 2308) [Complete proteome] [HAMAP]

Taxonomic identifier

359391 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella abortus

Protein attributes

Sequence length	220 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Endonuclease that specifically degrades the RNA of RNA-DNA hybrids By similarity. HAMAP-Rule MF_00052
Catalytic activity	Endonucleolytic cleavage to 5'-phosphomonoester. HAMAP-Rule MF_00052
Cofactor	Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding By similarity.
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_00052.
Sequence similarities	Belongs to the RNase HII family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Manganese Metal-binding
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	RNA catabolic process Inferred from electronic annotation. Source: HAMAP nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA binding Inferred from electronic annotation. Source: InterPro manganese ion binding Inferred from electronic annotation. Source: HAMAP ribonuclease H 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 – 220	220	Ribonuclease HII HAMAP-Rule MF_00052		PRO_0000235704
Sites
	Metal binding	38	1	Divalent metal cation By similarity
	Metal binding	39	1	Divalent metal cation By similarity
	Metal binding	130	1	Divalent metal cation By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2YMC3 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: 87E3AB1CD4844E8E	FASTA	220	23,332
	10 20 30 40 50 60 MKRSASDSPL LFDLPLAPDF SQEQQLMKRG LKHIAGIDEA GRGPLAGPVV AAAVVLDQND 70 80 90 100 110 120 LPEGLDDSKR LTAARREALY EIILTKAITV SVASLSARSI DASDIRKAAL EAMRRAVIGL 130 140 150 160 170 180 TLKPCHALVD GRDVPPGLPC PGSALVKGDQ RSVSIAAASI VAKVTRDRMM IRAGAAHPPY 190 200 210 220 GLEIHAGYAT QKHRAAIESE GPVPGLHRYT FAPIKGCFDC

References

[1]

"Whole-genome analyses of speciation events in pathogenic Brucellae." Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E. Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 2308.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM040264 Genomic DNA. Translation: CAJ10371.1.
RefSeq	YP_413875.1. NC_007618.1.
3D structure databases
ProteinModelPortal	Q2YMC3.
ModBase	Search...
Protein-protein interaction databases
STRING	359391.BAB1_0415.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAJ10371; CAJ10371; BAB1_0415.
GeneID	3788907.
KEGG	bmf:BAB1_0415.
PATRIC	17843702. VBIBruMel86222_0436.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0164.
HOGENOM	HOG000100288.
KO	K03470.
OMA	NRCPKLA.
ProtClustDB	PRK00015.
Enzyme and pathway databases
BioCyc	BMEL359391:GJOQ-422-MONOMER.
Family and domain databases
HAMAP	MF_00052_B. RNase_HII_B.
InterPro	IPR022898. RNase_HII. IPR001352. RNase_HII/HIII. IPR024567. RNase_HII/HIII_dom. IPR012337. RNaseH-like_dom. [Graphical view]
PANTHER	PTHR10954. PTHR10954. 1 hit.
Pfam	PF01351. RNase_HII. 1 hit. [Graphical view]
SUPFAM	SSF53098. RNaseH_fold. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RNH2_BRUA2

Accession

Primary (citable) accession number: Q2YMC3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	December 20, 2005
Last modified:	May 1, 2013
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program