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Q9KEI9

- RNH1_BACHD

UniProt

Q9KEI9 - RNH1_BACHD

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Protein

Ribonuclease H

Gene

rnhA

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.1 Publication

Catalytic activityi

Endonucleolytic cleavage to 5'-phosphomonoester.

Cofactori

Mn2+, Mg2+Note: Binds 2 metal ions per subunit. Manganese or magnesium.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi71 – 711Magnesium 11 Publication
Metal bindingi71 – 711Magnesium 21 Publication
Metal bindingi109 – 1091Magnesium 21 Publication
Metal bindingi132 – 1321Magnesium 21 Publication
Metal bindingi192 – 1921Magnesium 11 Publication

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. nucleic acid binding Source: InterPro
  3. RNA-DNA hybrid ribonuclease activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciBHAL272558:GJC5-921-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease H (EC:3.1.26.4)
Short name:
RNase H
Gene namesi
Name:rnhA
Ordered Locus Names:BH0863
OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Taxonomic identifieri272558 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001258: Chromosome

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi109 – 1091E → Q: Loss of activity. 1 Publication
Mutagenesisi132 – 1321D → N: Loss of activity. 1 Publication
Mutagenesisi188 – 1881E → A: Strongly reduces activity. 1 Publication
Mutagenesisi188 – 1881E → Q: No effect. 1 Publication
Mutagenesisi192 – 1921D → N: Strongly reduced activity with manganese. Loss of activity with magnesium. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 196196Ribonuclease HPRO_0000195430Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi272558.BH0863.

Structurei

Secondary structure

1
196
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi65 – 7511Combined sources
Turni76 – 783Combined sources
Beta strandi79 – 879Combined sources
Turni88 – 903Combined sources
Beta strandi93 – 10311Combined sources
Helixi105 – 12218Combined sources
Beta strandi129 – 1324Combined sources
Helixi134 – 1429Combined sources
Turni153 – 1553Combined sources
Helixi156 – 17116Combined sources
Beta strandi178 – 1803Combined sources
Helixi183 – 1864Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ9KEI9.
SMRiQ9KEI9. Positions 61-196.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9KEI9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini88 – 196109RNase HAdd
BLAST

Sequence similaritiesi

Belongs to the RNase H family.Curated
Contains 1 RNase H domain.Curated

Phylogenomic databases

eggNOGiCOG3341.
HOGENOMiHOG000251719.
KOiK03469.
OMAiGPMEYRG.
OrthoDBiEOG6358C1.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
3.40.970.10. 1 hit.
InterProiIPR009027. Ribosomal_L9/RNase_H1_N.
IPR011320. RNase_H1_N.
IPR017290. RNase_H_bac.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
[Graphical view]
PfamiPF01693. Cauli_VI. 1 hit.
PF00075. RNase_H. 1 hit.
[Graphical view]
PIRSFiPIRSF037839. Ribonuclease_H. 1 hit.
SUPFAMiSSF53098. SSF53098. 1 hit.
SSF55658. SSF55658. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9KEI9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKSKYYVVW NGRKPGIYTS WSACEAQVKG YTGAKFKSYP SKEEAEAAFR
60 70 80 90 100
GEEATPKLAK EEIIWESLSV DVGSQGNPGI VEYKGVDTKT GEVLFEREPI
110 120 130 140 150
PIGTNNMGEF LAIVHGLRYL KERNSRKPIY SDSQTAIKWV KDKKAKSTLV
160 170 180 190
RNEETALIWK LVDEAEEWLN THTYETPILK WQTDKWGEIK ADYGRK
Length:196
Mass (Da):22,373
Last modified:October 1, 2000 - v1
Checksum:i4130558FA37D2A86
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB04582.1.
PIRiG83757.
RefSeqiNP_241729.1. NC_002570.2.

Genome annotation databases

EnsemblBacteriaiBAB04582; BAB04582; BAB04582.
GeneIDi893801.
KEGGibha:BH0863.
PATRICi18938738. VBIBacHal18977_0907.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB04582.1 .
PIRi G83757.
RefSeqi NP_241729.1. NC_002570.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZBF X-ray 1.50 A 59-196 [» ]
1ZBI X-ray 1.85 A/B 59-196 [» ]
1ZBL X-ray 2.20 A/B 59-191 [» ]
2G8F X-ray 1.65 A 59-196 [» ]
2G8H X-ray 1.85 A 59-196 [» ]
2G8I X-ray 1.65 A 59-196 [» ]
2G8K X-ray 1.65 A 59-196 [» ]
2G8U X-ray 2.70 A 59-196 [» ]
2G8V X-ray 1.85 A 59-196 [» ]
2G8W X-ray 2.05 A 59-196 [» ]
2R7Y X-ray 1.80 A 62-193 [» ]
3D0P X-ray 1.80 A/C 61-194 [» ]
3EY1 X-ray 1.60 A 59-196 [» ]
3I8D X-ray 1.61 A/C 62-193 [» ]
3TWH X-ray 1.79 A 59-196 [» ]
3ULD X-ray 1.60 A 59-196 [» ]
4HTU X-ray 1.49 A/B 61-194 [» ]
4HUE X-ray 1.56 A/B 61-194 [» ]
4HUF X-ray 1.69 A/B 61-194 [» ]
4HUG X-ray 1.64 A/B 61-194 [» ]
ProteinModelPortali Q9KEI9.
SMRi Q9KEI9. Positions 61-196.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272558.BH0863.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB04582 ; BAB04582 ; BAB04582 .
GeneIDi 893801.
KEGGi bha:BH0863.
PATRICi 18938738. VBIBacHal18977_0907.

Phylogenomic databases

eggNOGi COG3341.
HOGENOMi HOG000251719.
KOi K03469.
OMAi GPMEYRG.
OrthoDBi EOG6358C1.

Enzyme and pathway databases

BioCyci BHAL272558:GJC5-921-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q9KEI9.

Family and domain databases

Gene3Di 3.30.420.10. 1 hit.
3.40.970.10. 1 hit.
InterProi IPR009027. Ribosomal_L9/RNase_H1_N.
IPR011320. RNase_H1_N.
IPR017290. RNase_H_bac.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
[Graphical view ]
Pfami PF01693. Cauli_VI. 1 hit.
PF00075. RNase_H. 1 hit.
[Graphical view ]
PIRSFi PIRSF037839. Ribonuclease_H. 1 hit.
SUPFAMi SSF53098. SSF53098. 1 hit.
SSF55658. SSF55658. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiRNH1_BACHD
AccessioniPrimary (citable) accession number: Q9KEI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3