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O59543

- RNP3_PYRHO

UniProt

O59543 - RNP3_PYRHO

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Protein

Ribonuclease P protein component 3

Gene

rnp3

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Not absolutely essential for activity in vitro, however it strongly stimulates activity. Binds RNase P RNA.3 PublicationsUniRule annotation

Catalytic activityi

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.UniRule annotation

Temperature dependencei

Optimum temperature is 70 degrees Celsius.2 Publications

GO - Molecular functioni

  1. ribonuclease P activity Source: UniProtKB

GO - Biological processi

  1. RNA phosphodiester bond hydrolysis Source: GOC
  2. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  3. tRNA 5'-leader removal Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

tRNA processing

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1877-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease P protein component 3UniRule annotation (EC:3.1.26.5UniRule annotation)
Short name:
RNase P component 3UniRule annotation
Alternative name(s):
Rpp30UniRule annotation
Gene namesi
Name:rnp3UniRule annotation
Ordered Locus Names:PH1877
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000000752: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
  2. ribonuclease P complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi42 – 421K → A: Fully reconstitutes RNase P activity. 1 Publication
Mutagenesisi68 – 681R → A: 75% reconstituted RNase P activity. 1 Publication
Mutagenesisi87 – 871R → A: Fully reconstitutes RNase P activity. 1 Publication
Mutagenesisi90 – 901R → A: 45% reconstituted RNase P activity. 1 Publication
Mutagenesisi98 – 981D → A: 80% reconstituted RNase P activity. 1 Publication
Mutagenesisi107 – 1071R → A: 45% reconstituted RNase P activity. 1 Publication
Mutagenesisi114 – 1141H → A: 75% reconstituted RNase P activity. 1 Publication
Mutagenesisi123 – 1231K → A: 45% reconstituted RNase P activity. 1 Publication
Mutagenesisi158 – 1581K → A: 75% reconstituted RNase P activity. 1 Publication
Mutagenesisi176 – 1761R → A: 45% reconstituted RNase P activity. 1 Publication
Mutagenesisi180 – 1801D → A: 50% reconstituted RNase P activity. 1 Publication
Mutagenesisi196 – 1961K → A: 45% reconstituted RNase P activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 212212Ribonuclease P protein component 3PRO_0000140046Add
BLAST

Interactioni

Subunit structurei

Consists of a catalytic RNA component and at least 5 protein subunits. Forms a heterotetrameric subcomplex with Rnp2. Reconstituted enzyme missing individual protein subunits is suboptimally active, showing each subunit contributes to optimization of activity.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
rnp2O591502EBI-2603192,EBI-2603177

Protein-protein interaction databases

IntActiO59543. 1 interaction.
STRINGi70601.PH1877.

Structurei

Secondary structure

1
212
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63
Beta strandi10 – 145
Helixi17 – 2610
Beta strandi28 – 3811
Helixi42 – 5211
Beta strandi55 – 617
Helixi64 – 7310
Beta strandi75 – 828
Helixi86 – 949
Beta strandi98 – 1014
Turni103 – 1064
Beta strandi107 – 1093
Helixi114 – 12310
Beta strandi126 – 1316
Helixi132 – 1365
Helixi139 – 15921
Beta strandi163 – 1664
Helixi172 – 1743
Helixi178 – 18710
Helixi192 – 1976
Turni198 – 2003
Helixi201 – 2077

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V77X-ray1.80A1-212[»]
2CZVX-ray2.00A/B1-212[»]
ProteinModelPortaliO59543.
SMRiO59543. Positions 2-209.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO59543.

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic/archaeal RNase P protein component 3 family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1603.
HOGENOMiHOG000073988.
KOiK03539.
OMAiDALISPW.

Family and domain databases

HAMAPiMF_00756. RNase_P_3.
InterProiIPR016195. Pol/histidinol_Pase-like.
IPR023539. RNase_P_comp-3_arc.
IPR002738. RNase_P_p30.
[Graphical view]
PANTHERiPTHR13031. PTHR13031. 1 hit.
PfamiPF01876. RNase_P_p30. 1 hit.
[Graphical view]
SUPFAMiSSF89550. SSF89550. 1 hit.

Sequencei

Sequence statusi: Complete.

O59543-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVGGGGVKFI EMDIRDKEAY ELAKEWFDEV VVSIKFNEEV DKEKLREARK
60 70 80 90 100
EYGKVAILLS NPKPSLVRDT VQKFKSYLIY VESNDLRVIR YSIEKGVDAI
110 120 130 140 150
ISPWVNRKDP GIDHVLAKLM VKKNVALGFS LRPLLYSNPY ERANLLRFMM
160 170 180 190 200
KAWKLVEKYK VRRFLTSSAQ EKWDVRYPRD LISLGVVIGM EIPQAKASIS
210
MYPEIILKRL KY
Length:212
Mass (Da):24,694
Last modified:August 1, 1998 - v1
Checksum:i321490D4A2859C24
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000001 Genomic DNA. Translation: BAA30999.1.
PIRiH71200.
RefSeqiNP_143706.1. NC_000961.1.
WP_010885939.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA30999; BAA30999; BAA30999.
GeneIDi1442721.
KEGGipho:PH1877.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000001 Genomic DNA. Translation: BAA30999.1 .
PIRi H71200.
RefSeqi NP_143706.1. NC_000961.1.
WP_010885939.1. NC_000961.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1V77 X-ray 1.80 A 1-212 [» ]
2CZV X-ray 2.00 A/B 1-212 [» ]
ProteinModelPortali O59543.
SMRi O59543. Positions 2-209.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O59543. 1 interaction.
STRINGi 70601.PH1877.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAA30999 ; BAA30999 ; BAA30999 .
GeneIDi 1442721.
KEGGi pho:PH1877.

Phylogenomic databases

eggNOGi COG1603.
HOGENOMi HOG000073988.
KOi K03539.
OMAi DALISPW.

Enzyme and pathway databases

BioCyci PHOR70601:GJWR-1877-MONOMER.

Miscellaneous databases

EvolutionaryTracei O59543.

Family and domain databases

HAMAPi MF_00756. RNase_P_3.
InterProi IPR016195. Pol/histidinol_Pase-like.
IPR023539. RNase_P_comp-3_arc.
IPR002738. RNase_P_p30.
[Graphical view ]
PANTHERi PTHR13031. PTHR13031. 1 hit.
Pfami PF01876. RNase_P_p30. 1 hit.
[Graphical view ]
SUPFAMi SSF89550. SSF89550. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  2. "Reconstitution of archaeal ribonuclease P from RNA and four protein components."
    Kouzuma Y., Mizoguchi M., Takagi H., Fukuhara H., Tsukamoto M., Numata T., Kimura M.
    Biochem. Biophys. Res. Commun. 306:666-673(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, RNA-BINDING.
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  3. "A fifth protein subunit Ph1496p elevates the optimum temperature for the ribonuclease P activity from Pyrococcus horikoshii OT3."
    Fukuhara H., Kifusa M., Watanabe M., Terada A., Honda T., Numata T., Kakuta Y., Kimura M.
    Biochem. Biophys. Res. Commun. 343:956-964(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  4. "Characterization of the archaeal ribonuclease P proteins from Pyrococcus horikoshii OT3."
    Terada A., Honda T., Fukuhara H., Hada K., Kimura M.
    J. Biochem. 140:293-298(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  5. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), MUTAGENESIS OF LYS-42; ARG-68; ARG-87; ARG-90; ASP-98; ARG-107; HIS-114; LYS-123; LYS-158; ARG-176; ASP-180 AND LYS-196.
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  6. "Crystal structure of protein Ph1481p in complex with protein Ph1877p of archaeal RNase P from Pyrococcus horikoshii OT3: implication of dimer formation of the holoenzyme."
    Kawano S., Nakashima T., Kakuta Y., Tanaka I., Kimura M.
    J. Mol. Biol. 357:583-591(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH RNP2, SUBUNIT.
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Entry informationi

Entry nameiRNP3_PYRHO
AccessioniPrimary (citable) accession number: O59543
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: August 1, 1998
Last modified: October 29, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3