Q9X1H4 (RNPA_THEMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonuclease P protein component
Short name=RNase P protein
Short name=RNaseP protein
EC=3.1.26.5

Alternative name(s):
Protein C5

Gene names

Name:	rnpA
Ordered Locus Names:	TM_1463

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

General annotation (Comments)

Function	RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme By similarity. HAMAP-Rule MF_00227
Catalytic activity	Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. HAMAP-Rule MF_00227
Subunit structure	Consists of a catalytic RNA component (M1 or RnpB) and a protein subunit By similarity.
Sequence similarities	Belongs to the RnpA family.

Ontologies

Keywords
Biological process	tRNA processing
Ligand	RNA-binding
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC tRNA 5'-leader removal Inferred from electronic annotation. Source: HAMAP
Molecular_function	ribonuclease P activity Inferred from electronic annotation. Source: HAMAP tRNA binding 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 – 117

117

Ribonuclease P protein component HAMAP-Rule MF_00227

PRO_0000198555

Secondary structure

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117

Helix Strand Turn

Details...

Helix

13 – 23

11

Beta strand

24 – 28

5

Beta strand

30 – 38

9

Beta strand

40 – 43

4

Beta strand

45 – 48

4

Helix

52 – 54

3

Helix

57 – 74

18

Turn

75 – 77

3

Beta strand

80 – 88

9

Helix

90 – 95

6

Helix

96 – 98

3

Helix

101 – 112

12

Sequences

	Sequence		Length	Mass (Da)
	Q9X1H4 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 0E68A9B25D023C64	FASTA	117	14,317
	10 20 30 40 50 60 MTESFTRRER LRLRRDFLLI FKEGKSLQNE YFVVLFRKNG LDYSRLGIVV KRKFGKATRR 70 80 90 100 110 NKLKRWVREI FRRNKGVIPK GFDIVVIPRK KLSEEFERVD FWTVREKLLN LLKRIEG

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]	"High-resolution structure of RNase P protein from Thermotoga maritima." Kazantsev A.V., Krivenko A.A., Harrington D.J., Carter R.J., Holbrook S.R., Adams P.D., Pace N.R. Proc. Natl. Acad. Sci. U.S.A. 100:7497-7502(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000512 Genomic DNA. Translation: AAD36531.1.

PIR

H72251.

RefSeq

NP_229262.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NZ0	X-ray	1.20	A/B/C/D	2-117	[»]
3Q1Q	X-ray	3.80	A	3-117	[»]
3Q1R	X-ray	4.21	A	3-117	[»]

ProteinModelPortal

Q9X1H4.

SMR

Q9X1H4. Positions 11-117.

ModBase

Search...

Protein-protein interaction databases

STRING

243274.TM1463.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAD36531; AAD36531; TM_1463.

GeneID

898016.

KEGG

tma:TM1463.

PATRIC

23937878. VBITheMar51294_1477.

Phylogenomic databases

eggNOG

COG0594.

KO

K03536.

OMA

ESFTRRE.

ProtClustDB

CLSK875778.

Family and domain databases

Gene3D

3.30.230.10. 1 hit.

HAMAP

MF_00227. RNase_P.

InterPro

IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000100. RNase_P.
IPR020539. RNase_P_CS.
[Graphical view]

Pfam

PF00825. Ribonuclease_P. 1 hit.
[Graphical view]

ProDom

PD003629. Ribonuclease_P. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.

TIGRFAMs

TIGR00188. rnpA. 1 hit.

PROSITE

PS00648. RIBONUCLEASE_P. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9X1H4.

Entry information

Entry name

RNPA_THEMA

Accession

Primary (citable) accession number: Q9X1H4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program