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Q9KEI9 (RNH1_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 H

Short name=RNase H
EC=3.1.26.4
Gene names
Name:rnhA
Ordered Locus Names:BH0863
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. Ref.2

Catalytic activity

Endonucleolytic cleavage to 5'-phosphomonoester.

Cofactor

Binds 2 metal ions per subunit. Manganese or magnesium.

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the RNase H family.

Contains 1 RNase H domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA-DNA hybrid ribonuclease activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 196196Ribonuclease H
PRO_0000195430

Regions

Domain88 – 196109RNase H

Sites

Metal binding711Magnesium 1
Metal binding711Magnesium 2
Metal binding1091Magnesium 2
Metal binding1321Magnesium 2
Metal binding1921Magnesium 1

Experimental info

Mutagenesis1091E → Q: Loss of activity. Ref.2
Mutagenesis1321D → N: Loss of activity. Ref.2
Mutagenesis1881E → A: Strongly reduces activity. Ref.2
Mutagenesis1881E → Q: No effect. Ref.2
Mutagenesis1921D → N: Strongly reduced activity with manganese. Loss of activity with magnesium. Ref.2

Secondary structure

..................... 196
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9KEI9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 4130558FA37D2A86

FASTA19622,373
        10         20         30         40         50         60 
MAKSKYYVVW NGRKPGIYTS WSACEAQVKG YTGAKFKSYP SKEEAEAAFR GEEATPKLAK 

        70         80         90        100        110        120 
EEIIWESLSV DVGSQGNPGI VEYKGVDTKT GEVLFEREPI PIGTNNMGEF LAIVHGLRYL 

       130        140        150        160        170        180 
KERNSRKPIY SDSQTAIKWV KDKKAKSTLV RNEETALIWK LVDEAEEWLN THTYETPILK 

       190 
WQTDKWGEIK ADYGRK 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
[2]"Crystal structures of RNase H bound to an RNA/DNA hybrid: substrate specificity and metal-dependent catalysis."
Nowotny M., Gaidamakov S.A., Crouch R.J., Yang W.
Cell 121:1005-1016(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 59-196 OF MUTANT ASN-132 IN COMPLEX WITH MAGNESIUM AND SUBSTRATE, FUNCTION, MUTAGENESIS OF GLU-109; ASP-132; GLU-188 AND ASP-192.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB04582.1.
PIRG83757.
RefSeqNP_241729.1. NC_002570.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZBFX-ray1.50A59-196[»]
1ZBIX-ray1.85A/B59-196[»]
1ZBLX-ray2.20A/B59-191[»]
2G8FX-ray1.65A59-196[»]
2G8HX-ray1.85A59-196[»]
2G8IX-ray1.65A59-196[»]
2G8KX-ray1.65A59-196[»]
2G8UX-ray2.70A59-196[»]
2G8VX-ray1.85A59-196[»]
2G8WX-ray2.05A59-196[»]
2R7YX-ray1.80A62-193[»]
3D0PX-ray1.80A/C61-194[»]
3EY1X-ray1.60A59-196[»]
3I8DX-ray1.61A/C62-193[»]
3TWHX-ray1.79A59-196[»]
3ULDX-ray1.60A59-196[»]
4HTUX-ray1.49A/B61-194[»]
4HUEX-ray1.56A/B61-194[»]
4HUFX-ray1.69A/B61-194[»]
4HUGX-ray1.64A/B61-194[»]
ProteinModelPortalQ9KEI9.
SMRQ9KEI9. Positions 61-196.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272558.BH0863.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB04582; BAB04582; BAB04582.
GeneID893801.
KEGGbha:BH0863.
PATRIC18938738. VBIBacHal18977_0907.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3341.
HOGENOMHOG000251719.
KOK03469.
OMAGPMEYRG.
OrthoDBEOG6358C1.

Enzyme and pathway databases

BioCycBHAL272558:GJC5-921-MONOMER.

Family and domain databases

Gene3D3.30.420.10. 1 hit.
3.40.970.10. 1 hit.
InterProIPR009027. Ribosomal_L9/RNase_H1_N.
IPR017290. RNase_H1_bac.
IPR011320. RNase_H1_N.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
[Graphical view]
PfamPF01693. Cauli_VI. 1 hit.
PF00075. RNase_H. 1 hit.
[Graphical view]
PIRSFPIRSF037839. Ribonuclease_H. 1 hit.
SUPFAMSSF53098. SSF53098. 1 hit.
SSF55658. SSF55658. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9KEI9.

Entry information

Entry nameRNH1_BACHD
AccessionPrimary (citable) accession number: Q9KEI9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 85 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references