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Protein

Ribonuclease H

Gene

rnhA

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Endonucleolytic cleavage to 5'-phosphomonoester.

Cofactori

Mg2+Note: Binds 1 Mg2+ ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi14 – 141Magnesium 1By similarity
Metal bindingi14 – 141Magnesium 2By similarity
Metal bindingi52 – 521Magnesium 1By similarity
Metal bindingi74 – 741Magnesium 1By similarity
Metal bindingi139 – 1391Magnesium 2By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1595-MONOMER.
BRENDAi3.1.26.4. 2305.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease H (EC:3.1.26.4)
Short name:
RNase H
Gene namesi
Name:rnhA
Ordered Locus Names:TTHA1556
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 166166Ribonuclease HPRO_0000195410Add
BLAST

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi300852.TTHA1556.

Structurei

Secondary structure

1
166
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Beta strandi18 – 3114Combined sources
Beta strandi36 – 4611Combined sources
Helixi48 – 6114Combined sources
Beta strandi68 – 736Combined sources
Helixi76 – 838Combined sources
Helixi86 – 927Combined sources
Beta strandi100 – 1023Combined sources
Helixi106 – 11611Combined sources
Beta strandi119 – 1257Combined sources
Helixi128 – 1303Combined sources
Helixi134 – 14613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JL2X-ray1.76A/B/C/D12-137[»]
1RILX-ray2.80A1-166[»]
2RPINMR-A1-127[»]
ProteinModelPortaliP29253.
SMRiP29253. Positions 6-152.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29253.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 147143RNase HAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108UMW. Bacteria.
COG0328. LUCA.
HOGENOMiHOG000040465.
KOiK03469.
OMAiLVTDSQY.
OrthoDBiEOG696BTR.
PhylomeDBiP29253.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
HAMAPiMF_00042. RNase_H.
InterProiIPR022892. RNaseH.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
[Graphical view]
PfamiPF00075. RNase_H. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS50879. RNASE_H. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29253-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPSPRKRVA LFTDGACLGN PGPGGWAALL RFHAHEKLLS GGEACTTNNR
60 70 80 90 100
MELKAAIEGL KALKEPCEVD LYTDSHYLKK AFTEGWLEGW RKRGWRTAEG
110 120 130 140 150
KPVKNRDLWE ALLLAMAPHR VRFHFVKGHT GHPENERVDR EARRQAQSQA
160
KTPCPPRAPT LFHEEA
Length:166
Mass (Da):18,728
Last modified:July 1, 1993 - v2
Checksum:i6B152B4901BD7172
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451C → W in CAA43026 (PubMed:1653414).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60507 Genomic DNA. Translation: CAA43026.1.
AP008226 Genomic DNA. Translation: BAD71379.1.
RefSeqiWP_011228761.1. NC_006461.1.
YP_144822.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71379; BAD71379; BAD71379.
GeneIDi3168213.
KEGGittj:TTHA1556.
PATRICi23958069. VBITheThe93045_1527.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60507 Genomic DNA. Translation: CAA43026.1.
AP008226 Genomic DNA. Translation: BAD71379.1.
RefSeqiWP_011228761.1. NC_006461.1.
YP_144822.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JL2X-ray1.76A/B/C/D12-137[»]
1RILX-ray2.80A1-166[»]
2RPINMR-A1-127[»]
ProteinModelPortaliP29253.
SMRiP29253. Positions 6-152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1556.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71379; BAD71379; BAD71379.
GeneIDi3168213.
KEGGittj:TTHA1556.
PATRICi23958069. VBITheThe93045_1527.

Phylogenomic databases

eggNOGiENOG4108UMW. Bacteria.
COG0328. LUCA.
HOGENOMiHOG000040465.
KOiK03469.
OMAiLVTDSQY.
OrthoDBiEOG696BTR.
PhylomeDBiP29253.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1595-MONOMER.
BRENDAi3.1.26.4. 2305.

Miscellaneous databases

EvolutionaryTraceiP29253.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
HAMAPiMF_00042. RNase_H.
InterProiIPR022892. RNaseH.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
[Graphical view]
PfamiPF00075. RNase_H. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS50879. RNASE_H. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a ribonuclease H (RNase HI) gene from an extreme thermophile Thermus thermophilus HB8: a thermostable RNase H can functionally replace the Escherichia coli enzyme in vivo."
    Itaya M., Kondo K.
    Nucleic Acids Res. 19:4443-4449(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  3. "Expression, purification, and characterization of a recombinant ribonuclease H from Thermus thermophilus HB8."
    Kanaya S., Itaya M.
    J. Biol. Chem. 267:10184-10192(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, SEQUENCE REVISION, CHARACTERIZATION.
  4. "Crystal structure of ribonuclease H from Thermus thermophilus HB8 refined at 2.8-A resolution."
    Ishikawa K., Okumura M., Katayanagi K., Kimura S., Kanaya S., Nakamura H., Morikawa K.
    J. Mol. Biol. 230:529-542(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Entry informationi

Entry nameiRNH_THET8
AccessioniPrimary (citable) accession number: P29253
Secondary accession number(s): Q5SI24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: July 1, 1993
Last modified: July 6, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.