P29253 (RNH_THET8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	rnhA
Ordered Locus Names:	TTHA1556

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	166 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. HAMAP MF_00042
Catalytic activity	Endonucleolytic cleavage to 5'-phosphomonoester. HAMAP MF_00042
Cofactor	Binds 1 magnesium ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Subunit structure	Monomer.
Sequence similarities	Belongs to the RNase H family. Contains 1 RNase H domain.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid binding Inferred from electronic annotation. Source: InterPro ribonuclease H activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 166

166

Ribonuclease H HAMAP MF_00042

PRO_0000195410

Regions

Domain

5 – 147

143

RNase H

Sites

Metal binding

14

1

Magnesium 1 By similarity

Metal binding

14

1

Magnesium 2 By similarity

Metal binding

52

1

Magnesium 1 By similarity

Metal binding

74

1

Magnesium 1 By similarity

Metal binding

139

1

Magnesium 2 By similarity

Experimental info

Sequence conflict

45

1

C → W in CAA43026. Ref.1

Secondary structure

1

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166

Helix Strand Turn

Details...

Beta strand

11 – 19

9

Beta strand

22 – 30

9

Beta strand

42 – 46

5

Helix

48 – 61

14

Beta strand

68 – 72

5

Helix

76 – 83

8

Helix

86 – 92

7

Beta strand

100 – 102

3

Helix

106 – 116

11

Beta strand

119 – 122

4

Helix

128 – 130

3

Helix

134 – 146

13

Sequences

	Sequence		Length	Mass (Da)
	P29253 [UniParc]. Last modified July 1, 1993. Version 2. Checksum: 6B152B4901BD7172	FASTA	166	18,728
	10 20 30 40 50 60 MNPSPRKRVA LFTDGACLGN PGPGGWAALL RFHAHEKLLS GGEACTTNNR MELKAAIEGL 70 80 90 100 110 120 KALKEPCEVD LYTDSHYLKK AFTEGWLEGW RKRGWRTAEG KPVKNRDLWE ALLLAMAPHR 130 140 150 160 VRFHFVKGHT GHPENERVDR EARRQAQSQA KTPCPPRAPT LFHEEA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1653414] [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: 1315754] [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: 8385228] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X60507 Genomic DNA. Translation: CAA43026.1.
AP008226 Genomic DNA. Translation: BAD71379.1.

RefSeq

YP_144822.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JL2	X-ray	1.76	A/B/C/D	-	[»]
1RIL	X-ray	2.80	A	1-166	[»]
2RPI	NMR	-	A	1-127	[»]

ProteinModelPortal

P29253.

SMR

P29253. Positions 6-152.

ModBase

Search...

Protein-protein interaction databases

STRING

P29253.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3168213.

GenomeReviews

Gene locus TTHA1556 in contig AP008226_GR.

KEGG

ttj:TTHA1556.

NMPDR

fig|300852.3.peg.1868.

PATRIC

23958069. VBITheThe93045_1527.

Phylogenomic databases

eggNOG

COG0328.

HOGENOM

HBG742437.

OMA

NGWRTAD.

PhylomeDB

P29253.

ProtClustDB

PRK00203.

Enzyme and pathway databases

BioCyc

TTHE300852:TTHA1556-MONOMER.

Family and domain databases

HAMAP

MF_00042. RNase_H.
[Tree]

InterPro

IPR022892. RNaseH.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
[Graphical view]

KO

K03469.

Pfam

PF00075. RNase_H. 1 hit.
[Graphical view]

SUPFAM

SSF53098. RNaseH_fold. 1 hit.

PROSITE

PS50879. RNASE_H. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RNH_THET8

Accession

Primary (citable) accession number: P29253
Secondary accession number(s): Q5SI24

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	July 1, 1993
Last modified:	January 25, 2012
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program