O59543 (RNP3_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonuclease P protein component 3
Short name=RNase P component 3
EC=3.1.26.5

Gene names

Name:	rnp3
Ordered Locus Names:	PH1877

Organism

Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	212 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends By similarity. HAMAP MF_00756
Catalytic activity	Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. HAMAP MF_00756
Subunit structure	Consists of a catalytic RNA component and at least 4 protein subunits Potential.
Sequence similarities	Belongs to the eukaryotic/archaeal RNase P protein component 3 family.

Ontologies

Keywords
Biological process	tRNA processing
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	tRNA 5'-leader removal Inferred from electronic annotation. Source: InterPro
Molecular function	protein binding Inferred from physical interaction. Source: IntAct ribonuclease P activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
rnp2	O59150	2	EBI-2603192,EBI-2603177

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 212

212

Ribonuclease P protein component 3 HAMAP MF_00756

PRO_0000140046

Experimental info

Mutagenesis

90

1

R → A: Reduced activity.

Mutagenesis

107

1

R → A: Reduced activity.

Mutagenesis

123

1

K → A: Reduced activity.

Mutagenesis

176

1

R → A: Reduced activity.

Mutagenesis

196

1

K → A: Reduced activity.

Secondary structure

1

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212

Helix Strand Turn

Details...

Beta strand

4 – 6

3

Beta strand

10 – 14

5

Helix

17 – 26

10

Beta strand

28 – 38

11

Helix

42 – 52

11

Beta strand

55 – 61

7

Helix

64 – 73

10

Beta strand

75 – 82

8

Helix

86 – 94

9

Beta strand

98 – 101

4

Turn

103 – 106

4

Beta strand

107 – 109

3

Helix

114 – 123

10

Beta strand

126 – 131

6

Helix

132 – 136

5

Helix

139 – 159

21

Beta strand

163 – 166

4

Helix

172 – 174

3

Helix

178 – 187

10

Helix

192 – 197

6

Turn

198 – 200

3

Helix

201 – 207

7

Sequences

	Sequence		Length	Mass (Da)
	O59543 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 321490D4A2859C24	FASTA	212	24,694
	10 20 30 40 50 60 MVGGGGVKFI EMDIRDKEAY ELAKEWFDEV VVSIKFNEEV DKEKLREARK EYGKVAILLS 70 80 90 100 110 120 NPKPSLVRDT VQKFKSYLIY VESNDLRVIR YSIEKGVDAI ISPWVNRKDP GIDHVLAKLM 130 140 150 160 170 180 VKKNVALGFS LRPLLYSNPY ERANLLRFMM KAWKLVEKYK VRRFLTSSAQ EKWDVRYPRD 190 200 210 LISLGVVIGM EIPQAKASIS MYPEIILKRL KY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H. DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
[2]	"Crystal structure of the ribonuclease P protein Ph1877p from hyperthermophilic archaeon Pyrococcus horikoshii OT3." Takagi H., Watanabe M., Kakuta Y., Kamachi R., Numata T., Tanaka I., Kimura M. Biochem. Biophys. Res. Commun. 319:787-794(2004) [PubMed: 15184052] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), MUTAGENESIS. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000001 Genomic DNA. Translation: BAA30999.1.

PIR

H71200.

RefSeq

NP_143706.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1V77	X-ray	1.80	A	1-212	[»]
2CZV	X-ray	2.00	A/B	1-212	[»]

ProteinModelPortal

O59543.

SMR

O59543. Positions 2-209.

ModBase

Search...

Protein-protein interaction databases

IntAct

O59543. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBPYRT00000001980; EBPYRP00000001980; EBPYRG00000001980.

GeneID

1442721.

GenomeReviews

Gene locus PH1877 in contig BA000001_GR.

KEGG

pho:PH1877.

NMPDR

fig|70601.1.peg.1835.

Organism-specific databases

CMR

Search...

Phylogenomic databases

GeneTree

EBGT00050000022696.

HOGENOM

HBG645643.

OMA

WFDEVVF.

ProtClustDB

PRK03892.

Enzyme and pathway databases

BioCyc

PHOR70601:PH1877-MONOMER.

Family and domain databases

HAMAP

MF_00756. RNase_P_3.
[Tree]

InterPro

IPR016195. Pol/histidinol_Pase-like.
IPR023539. RNase_P_comp-3.
IPR002738. RNase_P_p30.
[Graphical view]

KO

K03539.

Pfam

PF01876. RNase_P_p30. 1 hit.
[Graphical view]

SUPFAM

SSF89550. PHP-like. 1 hit.

ProtoNet

Search...

Entry information

Entry name

RNP3_PYRHO

Accession

Primary (citable) accession number: O59543

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	August 1, 1998
Last modified:	November 16, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program