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O59425

- RNP1_PYRHO

UniProt

O59425 - RNP1_PYRHO

Protein

Ribonuclease P protein component 1

Gene

rnp1

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 88 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Part of ribonuclease P (RNase P), a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Binds RNase P RNA.4 Publications

    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
    2. RNA binding Source: InterPro

    GO - Biological processi

    1. mRNA cleavage Source: InterPro
    2. RNA phosphodiester bond hydrolysis Source: GOC
    3. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    4. rRNA processing Source: InterPro
    5. tRNA 5'-leader removal Source: UniProtKB

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    tRNA processing

    Enzyme and pathway databases

    BioCyciPHOR70601:GJWR-1769-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonuclease P protein component 1UniRule annotation (EC:3.1.26.5UniRule annotation)
    Short name:
    RNase P component 1UniRule annotation
    Alternative name(s):
    Rpp29UniRule annotation
    Gene namesi
    Name:rnp1UniRule annotation
    Ordered Locus Names:PH1771
    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 MRP complex Source: InterPro
    3. ribonuclease P complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1 – 3131Missing: Does not reconstitute RNase P activity, no longer interacts with Rnp4. Add
    BLAST
    Mutagenesisi47 – 471E → A: Fully reconstitutes RNase P activity. 1 Publication
    Mutagenesisi73 – 731E → A: 40% reconstituted RNase P activity. 1 Publication
    Mutagenesisi75 – 751R → A: 40% reconstituted RNase P activity. 1 Publication
    Mutagenesisi90 – 901K → A: 10% reconstituted RNase P activity. 1 Publication
    Mutagenesisi95 – 951F → A: 75% reconstituted RNase P activity. 1 Publication
    Mutagenesisi115 – 1151R → A: 75% reconstituted RNase P activity. 1 Publication
    Mutagenesisi118 – 12710Missing: Does not reconstitute RNase P activity.
    Mutagenesisi121 – 1222KK → AA: 60% reconstituted RNase P activity. 1 Publication
    Mutagenesisi121 – 1211K → A: 90% reconstituted RNase P activity. 1 Publication
    Mutagenesisi122 – 1221K → A: Fully reconstitutes RNase P activity. 1 Publication
    Mutagenesisi124 – 1274Missing: Fully reconstitutes RNase P activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 127127Ribonuclease P protein component 1PRO_0000128437Add
    BLAST

    Interactioni

    Subunit structurei

    Consists of a catalytic RNA component and at least 5 protein subunits. Forms a heterodimeric subcomplex with Rnp4. Reconstituted enzyme missing individual protein subunits is suboptimally active, showing each subunit contributes to optimization of activity.4 Publications

    Protein-protein interaction databases

    IntActiO59425. 1 interaction.
    STRINGi70601.PH1771.

    Structurei

    Secondary structure

    1
    127
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 233
    Helixi27 – 304
    Turni31 – 333
    Helixi42 – 443
    Beta strandi52 – 609
    Helixi61 – 633
    Beta strandi67 – 737
    Beta strandi75 – 9016
    Beta strandi93 – 986
    Beta strandi104 – 1085
    Helixi109 – 1124
    Helixi116 – 1194
    Helixi120 – 1234

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1V76X-ray2.00A/B32-127[»]
    2ZAEX-ray2.21A/C1-127[»]
    ProteinModelPortaliO59425.
    SMRiO59425. Positions 36-127.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO59425.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the eukaryotic/archaeal RNase P protein component 1 family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1588.
    HOGENOMiHOG000231353.
    KOiK03538.
    OMAiISTKGRV.

    Family and domain databases

    Gene3Di2.30.30.210. 1 hit.
    HAMAPiMF_00754. RNase_P_1.
    InterProiIPR002730. RNase_P/MRP_p29.
    IPR023538. RNase_P_comp-1.
    IPR023534. Rof/RNase_P-like.
    [Graphical view]
    PfamiPF01868. UPF0086. 1 hit.
    [Graphical view]
    SMARTiSM00538. POP4. 1 hit.
    [Graphical view]
    SUPFAMiSSF101744. SSF101744. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O59425-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRRNSKERKN RATRRSQGSY QEIIGRTWIF RGAHRGRVTR RNIIWHELIG    50
    LRVRIVGSTH PAFVGIEGYV IDETRNMLVI AGDRIWKVPK DVCIFEFEAD 100
    DGTKIKIPGE RLVGRPEMRL KKRWKKW 127
    Length:127
    Mass (Da):15,054
    Last modified:August 1, 1998 - v1
    Checksum:i840FE2A1234FF0AD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000001 Genomic DNA. Translation: BAA30886.1.
    PIRiG71186.
    RefSeqiNP_143607.1. NC_000961.1.

    Genome annotation databases

    EnsemblBacteriaiBAA30886; BAA30886; BAA30886.
    GeneIDi1442614.
    KEGGipho:PH1771.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000001 Genomic DNA. Translation: BAA30886.1 .
    PIRi G71186.
    RefSeqi NP_143607.1. NC_000961.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1V76 X-ray 2.00 A/B 32-127 [» ]
    2ZAE X-ray 2.21 A/C 1-127 [» ]
    ProteinModelPortali O59425.
    SMRi O59425. Positions 36-127.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O59425. 1 interaction.
    STRINGi 70601.PH1771.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAA30886 ; BAA30886 ; BAA30886 .
    GeneIDi 1442614.
    KEGGi pho:PH1771.

    Phylogenomic databases

    eggNOGi COG1588.
    HOGENOMi HOG000231353.
    KOi K03538.
    OMAi ISTKGRV.

    Enzyme and pathway databases

    BioCyci PHOR70601:GJWR-1769-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei O59425.

    Family and domain databases

    Gene3Di 2.30.30.210. 1 hit.
    HAMAPi MF_00754. RNase_P_1.
    InterProi IPR002730. RNase_P/MRP_p29.
    IPR023538. RNase_P_comp-1.
    IPR023534. Rof/RNase_P-like.
    [Graphical view ]
    Pfami PF01868. UPF0086. 1 hit.
    [Graphical view ]
    SMARTi SM00538. POP4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101744. SSF101744. 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 archaeal ribonuclease P protein Ph1771p from Pyrococcus horikoshii OT3: an archaeal homolog of eukaryotic ribonuclease P protein Rpp29."
      Numata T., Ishimatsu I., Kakuta Y., Tanaka I., Kimura M.
      RNA 10:1423-1432(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 32-127.
      Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
    6. "Structure of an archaeal homolog of the human protein complex Rpp21-Rpp29 that is a key core component for the assembly of active ribonuclease P."
      Honda T., Kakuta Y., Kimura K., Saho J., Kimura M.
      J. Mol. Biol. 384:652-662(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) IN COMPLEX WITH RNP4, FUNCTION, SUBUNIT, MUTAGENESIS OF 1-MET--ARG-31; GLU-47; GLU-73; ARG-75; LYS-90; PHE-95; ARG-115; 118-MET--TRP-127; LYS-121; 121-LYS-LYS-122; LYS-122 AND 124-TRP--TRP-127.

    Entry informationi

    Entry nameiRNP1_PYRHO
    AccessioniPrimary (citable) accession number: O59425
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: August 1, 1998
    Last modified: October 1, 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