Q9X0I6 (RNC_THEMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonuclease 3
EC=3.1.26.3

Alternative name(s):
Ribonuclease III
Short name=RNase III

Gene names

Name:	rnc
Ordered Locus Names:	TM_1102

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	240 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Ref.2
Catalytic activity	Endonucleolytic cleavage to 5'-phosphomonoester. HAMAP-Rule MF_00104
Cofactor	Magnesium. Ref.2
Subunit structure	Homodimer Probable. Ref.3
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Contains 1 DRBM (double-stranded RNA-binding) domain. Contains 1 RNase III domain.
Biophysicochemical properties	pH dependence: Optimum pH is 8.0. Ref.2 Temperature dependence: Optimum temperature is 40-70 degrees Celsius.

Ontologies

Keywords
Biological process	mRNA processing rRNA processing tRNA processing
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding RNA-binding rRNA-binding
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA processing Inferred from electronic annotation. Source: HAMAP nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC rRNA catabolic process Inferred from electronic annotation. Source: InterPro rRNA processing Inferred from electronic annotation. Source: HAMAP tRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	double-stranded RNA binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW rRNA binding Inferred from electronic annotation. Source: UniProtKB-KW ribonuclease III 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 – 240

240

Ribonuclease 3 HAMAP-Rule MF_00104

PRO_0000180448

Regions

Domain

9 – 141

133

RNase III

Domain

168 – 237

70

DRBM

Sites

Active site

58

1

Potential

Active site

130

1

By similarity

Metal binding

54

1

Magnesium By similarity

Metal binding

127

1

Magnesium By similarity

Metal binding

130

1

Magnesium By similarity

Secondary structure

1

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240

Helix Strand Turn

Details...

Helix

3 – 16

14

Helix

23 – 30

8

Helix

33 – 41

9

Helix

51 – 72

22

Helix

78 – 88

11

Helix

91 – 100

10

Helix

103 – 106

4

Helix

111 – 115

5

Helix

118 – 120

3

Helix

122 – 140

19

Helix

142 – 161

20

Helix

169 – 181

13

Beta strand

186 – 193

8

Beta strand

200 – 207

8

Beta strand

210 – 219

10

Helix

220 – 235

16

Sequences

	Sequence		Length	Mass (Da)
	Q9X0I6 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 94330E8898D48A0D	FASTA	240	27,530
	10 20 30 40 50 60 MNESERKIVE EFQKETGINF KNEELLFRAL CHSSYANEQN QAGRKDVESN EKLEFLGDAV 70 80 90 100 110 120 LELFVCEILY KKYPEAEVGD LARVKSAAAS EEVLAMVSRK MNLGKFLFLG KGEEKTGGRD 130 140 150 160 170 180 RDSILADAFE ALLAAIYLDQ GYEKIKELFE QEFEFYIEKI MKGEMLFDYK TALQEIVQSE 190 200 210 220 230 240 HKVPPEYILV RTEKNDGDRI FVVEVRVNGK TIATGKGRTK KEAEKEAARI AYEKLLKERS

References

	« Hide 'large scale' referencesShow 'large scale' 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.
[2]	"Thermotoga maritima ribonuclease III. Characterization of thermostable biochemical behavior and analysis of conserved base pairs that function as reactivity epitopes for the Thermotoga 23S rRNA precursor." Nathania L., Nicholson A.W. Biochemistry 49:7164-7178(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS AN RNASE, FUNCTION AS AN ENDONUCLEASE, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, RRNA-BINDING.
[3]	"Crystal structure of ribonuclease III (TM1102) from Thermotoga maritima at 2.0 A resolution." Joint center for structural genomics (JCSG) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000512 Genomic DNA. Translation: AAD36178.1.

PIR

H72294.

RefSeq

NP_228908.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1O0W	X-ray	2.00	A/B	1-240	[»]

ProteinModelPortal

Q9X0I6.

SMR

Q9X0I6. Positions 1-237.

ModBase

Search...

Protein-protein interaction databases

STRING

243274.TM1102.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAD36178; AAD36178; TM_1102.

GeneID

898663.

KEGG

tma:TM1102.

PATRIC

23937137. VBITheMar51294_1117.

Phylogenomic databases

eggNOG

COG0571.

KO

K03685.

OMA

LTHKSCK.

ProtClustDB

PRK00102.

Family and domain databases

Gene3D

1.10.1520.10. 1 hit.
3.30.160.20. 1 hit.

HAMAP

MF_00104. RNase_III.

InterPro

IPR001159. Ds-RNA-bd.
IPR014720. dsRNA-bd-like_dom.
IPR011907. RNase_III.
IPR000999. RNase_III_dom.
[Graphical view]

PANTHER

PTHR11207. PTHR11207. 1 hit.

Pfam

PF00035. dsrm. 1 hit.
PF00636. Ribonuclease_3. 1 hit.
[Graphical view]

SMART

SM00358. DSRM. 1 hit.
SM00535. RIBOc. 1 hit.
[Graphical view]

SUPFAM

SSF69065. RNase_III. 1 hit.

TIGRFAMs

TIGR02191. RNaseIII. 1 hit.

PROSITE

PS50137. DS_RBD. 1 hit.
PS00517. RNASE_3_1. 1 hit.
PS50142. RNASE_3_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9X0I6.

Entry information

Entry name

RNC_THEMA

Accession

Primary (citable) accession number: Q9X0I6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program