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O59543

- RNP3_PYRHO

UniProt

O59543 - RNP3_PYRHO

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
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    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. protein binding Source: IntAct
    2. 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

    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-SubCell
    2. ribonuclease P complex Source: UniProtKB

    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

    MVGGGGVKFI EMDIRDKEAY ELAKEWFDEV VVSIKFNEEV DKEKLREARK    50
    EYGKVAILLS NPKPSLVRDT VQKFKSYLIY VESNDLRVIR YSIEKGVDAI 100
    ISPWVNRKDP GIDHVLAKLM VKKNVALGFS LRPLLYSNPY ERANLLRFMM 150
    KAWKLVEKYK VRRFLTSSAQ EKWDVRYPRD LISLGVVIGM EIPQAKASIS 200
    MYPEIILKRL KY 212
    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

    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 1, 2014
    This is version 87 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