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

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

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 MF_00052_B
Catalytic activity	Endonucleolytic cleavage to 5'-phosphomonoester. HAMAP 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 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)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	RNA binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 238

238

Ribonuclease HII HAMAP 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

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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

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

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: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

+

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	[»]

ProteinModelPortal

Q9X017.

SMR

Q9X017. Positions 1-221.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

898589.

GenomeReviews

Gene locus TM_0915 in contig AE000512_GR.

KEGG

tma:TM0915.

NMPDR

fig|243274.1.peg.907.

PATRIC

23936761. VBITheMar51294_0929.

TIGR

TM_0915.

Phylogenomic databases

HOGENOM

HBG584843.

OMA

RLGPTPI.

PhylomeDB

Q9X017.

ProtClustDB

PRK00015.

Enzyme and pathway databases

BioCyc

TMAR243274:TM_0915-MONOMER.

Family and domain databases

HAMAP

MF_00052_B. RNase_HII_B.
[Tree]

InterPro

IPR022898. RNase_HII.
IPR001352. RNase_HII/HIII.
IPR024567. RNase_HII/HIII_dom.
IPR012337. RNaseH-like_dom.
[Graphical view]

KO

K03470.

PANTHER

PTHR10954. RNase_HII/HIII. 1 hit.

Pfam

PF01351. RNase_HII. 1 hit.
[Graphical view]

SUPFAM

SSF53098. RNaseH_fold. 1 hit.

ProtoNet

Search...

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:	January 25, 2012
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program