Q9X017 (RNH2_THEMA) 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:	TM_0915

Organism

Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]

Taxonomic identifier

243274 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Thermotogae › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga › Thermotoga maritima

Protein attributes

Sequence length	238 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Endonuclease that specifically degrades the RNA of RNA-DNA hybrids By similarity. HAMAP-Rule MF_00052_B
Catalytic activity	Endonucleolytic cleavage to 5'-phosphomonoester. HAMAP-Rule MF_00052_B
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_B.
Sequence similarities	Belongs to the RNase HII family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Manganese Metal-binding
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	3D-structure Complete proteome Reference 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 – 238

238

Ribonuclease HII HAMAP-Rule MF_00052_B

PRO_0000111643

Sites

Metal binding

18

1

Divalent metal cation By similarity

Metal binding

19

1

Divalent metal cation By similarity

Metal binding

107

1

Divalent metal cation By similarity

Secondary structure

1

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238

Helix Strand Turn

Details...

Helix

3 – 7

5

Turn

8 – 10

3

Beta strand

11 – 20

10

Beta strand

25 – 27

3

Beta strand

29 – 36

8

Turn

41 – 44

4

Helix

46 – 48

3

Helix

53 – 64

12

Beta strand

65 – 72

8

Helix

74 – 80

7

Helix

82 – 96

15

Beta strand

97 – 99

3

Beta strand

102 – 110

9

Beta strand

117 – 120

4

Helix

123 – 126

4

Helix

128 – 151

24

Helix

157 – 160

4

Helix

166 – 175

10

Helix

186 – 189

4

Helix

194 – 202

9

Helix

208 – 219

12

Turn

220 – 222

3

Sequences

	Sequence		Length	Mass (Da)
	Q9X017 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 2A0C0156954AE923	FASTA	238	26,630
	10 20 30 40 50 60 MGIDELYKKE FGIVAGVDEA GRGCLAGPVV AAAVVLEKEI EGINDSKQLS PAKRERLLDE 70 80 90 100 110 120 IMEKAAVGIG IASPEEIDLY NIFNATKLAM NRALENLSVK PSFVLVDGKG IELSVPGTCL 130 140 150 160 170 180 VKGDQKSKLI GAASIVAKVF RDRLMSEFHR MYPQFSFHKH KGYATKEHLN EIRKNGVLPI 190 200 210 220 230 HRLSFEPVLE LLTDDLLREF FEKGLISENR FERILNLLGA RKSVVFRKER TNHNLPLF

References

[1]

"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

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Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000512 Genomic DNA. Translation: AAD35996.1.

PIR

B72320.

RefSeq

NP_228723.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ETJ	X-ray	1.74	A	1-238	[»]
3O3F	X-ray	2.00	A	2-223	[»]
3O3G	X-ray	2.10	A	2-223	[»]
3O3H	X-ray	2.80	A	2-223	[»]
4HHT	X-ray	3.10	A	2-238	[»]

ProteinModelPortal

Q9X017.

SMR

Q9X017. Positions 1-221.

ModBase

Search...

Protein-protein interaction databases

STRING

243274.TM0915.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAD35996; AAD35996; TM_0915.

GeneID

898589.

KEGG

tma:TM0915.

PATRIC

23936761. VBITheMar51294_0929.

Phylogenomic databases

eggNOG

COG0164.

KO

K03470.

OMA

NRCPKLA.

ProtClustDB

PRK00015.

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...

Other

EvolutionaryTrace

Q9X017.

Entry information

Entry name

RNH2_THEMA

Accession

Primary (citable) accession number: Q9X017

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program