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F4JKB6

- PRRP3_ARATH

UniProt

F4JKB6 - PRRP3_ARATH

Protein

Proteinaceous RNase P 3

Gene

PRORP3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 24 (01 Oct 2014)
      Sequence version 1 (28 Jun 2011)
      Previous versions | rss
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    Functioni

    Endonuclease RNase P responsible for the 5' maturation of tRNA precursors. Also involved in the maturation of mRNA and small nucleolar RNA (snoRNA).1 Publication

    Catalytic activityi

    Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.1 Publication

    Kineticsi

    1. KM=0.3 µM for tRNA(Gln) precursor1 Publication

    GO - Molecular functioni

    1. ribonuclease P activity Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    tRNA processing

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteinaceous RNase P 3 (EC:3.1.26.5)
    Gene namesi
    Name:PRORP3
    Ordered Locus Names:At4g21900
    ORF Names:T8O5.110
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G21900.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: TAIR

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype; due to the redundancy with PRORP2. Prorp2 and prorp3 double mutant is lethal.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi480 – 4812DD → AA: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 576576Proteinaceous RNase P 3PRO_0000420274Add
    BLAST

    Proteomic databases

    PRIDEiF4JKB6.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT4G21900.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliF4JKB6.
    SMRiF4JKB6. Positions 87-573.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati88 – 12336PPR 1Add
    BLAST
    Repeati129 – 16638PPR 2Add
    BLAST
    Repeati167 – 20135PPR 3Add
    BLAST
    Repeati204 – 23835PPR 4Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi80 – 834Poly-Lys

    Sequence similaritiesi

    Belongs to the PPR family. P subfamily.Curated
    Contains 4 PPR (pentatricopeptide) repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG68490.
    HOGENOMiHOG000006117.
    KOiK18213.
    OMAiSCEPMAD.

    Family and domain databases

    InterProiIPR021869. RNase_Zc3h12.
    [Graphical view]
    PfamiPF11977. RNase_Zc3h12a. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    F4JKB6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLKKPSLPS SLLCAVPPCL SQIRLLIPRR VRVSSSTFAN AKLVTLRNHT    50
    VNLHIYYCSM AGTDNRRSRH DDESPKNPNK KKKGNRNPEK SLLINLHSCS 100
    KRKDLSAALA LYDAAITSSD IRLNQQHFQS LLYLCSAFIS DPSLQTVAID 150
    RGFQIFDRMV SSGISPNESS VTAVARLAAA KGDGDYAFKL VKDLVAVGGV 200
    SVPRLRTYAP ALLCFCDTLE AEKGYEVEDH MDASGIVLEE AEISALLKVS 250
    AATGRENKVY RYLQKLRECV GCVSEETSKA IEEWFYGVKA SEVSDNGIGS 300
    DIELLRAAVL KNGGGWHGLG WVGEGKWIVK KGNVSSAGKC LSCDEHLACV 350
    DTNEVETEDF VNSLVTLAME RKAKMNSCEP MADFSEFQEW LEKHGDYEAI 400
    LDGANIGLYQ QNFADGGFSL PQLEAVVKEL YNKSGSKKQP LILLHKKRVN 450
    ALLENPNHRN LVEEWINNNV LYATPPGSND DWYWLYAAAK LKCLLVTNDE 500
    MRDHIFELLS NSFFQKWKER HQVRFTFVKG CLKLEMPPPF SVVIQESEKG 550
    SWHVPITSQD KEESLRSWMC ITRQSS 576
    Length:576
    Mass (Da):64,396
    Last modified:June 28, 2011 - v1
    Checksum:i10A34B9C5F166DAD
    GO

    Sequence cautioni

    The sequence BAF02238.1 differs from that shown. Reason: Intron retention.
    The sequence BAE98777.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAA17157.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAB79145.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti185 – 1851D → G in BAF02238. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL021890 Genomic DNA. Translation: CAA17157.1. Sequence problems.
    AL161556 Genomic DNA. Translation: CAB79145.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE84521.1.
    AK226669 mRNA. Translation: BAE98777.1. Different initiation.
    AK230440 mRNA. Translation: BAF02238.1. Sequence problems.
    PIRiT05472.
    RefSeqiNP_193921.2. NM_118311.6.
    UniGeneiAt.74070.

    Genome annotation databases

    EnsemblPlantsiAT4G21900.1; AT4G21900.1; AT4G21900.
    GeneIDi828279.
    KEGGiath:AT4G21900.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL021890 Genomic DNA. Translation: CAA17157.1 . Sequence problems.
    AL161556 Genomic DNA. Translation: CAB79145.1 . Sequence problems.
    CP002687 Genomic DNA. Translation: AEE84521.1 .
    AK226669 mRNA. Translation: BAE98777.1 . Different initiation.
    AK230440 mRNA. Translation: BAF02238.1 . Sequence problems.
    PIRi T05472.
    RefSeqi NP_193921.2. NM_118311.6.
    UniGenei At.74070.

    3D structure databases

    ProteinModelPortali F4JKB6.
    SMRi F4JKB6. Positions 87-573.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT4G21900.1-P.

    Proteomic databases

    PRIDEi F4JKB6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G21900.1 ; AT4G21900.1 ; AT4G21900 .
    GeneIDi 828279.
    KEGGi ath:AT4G21900.

    Organism-specific databases

    TAIRi AT4G21900.

    Phylogenomic databases

    eggNOGi NOG68490.
    HOGENOMi HOG000006117.
    KOi K18213.
    OMAi SCEPMAD.

    Family and domain databases

    InterProi IPR021869. RNase_Zc3h12.
    [Graphical view ]
    Pfami PF11977. RNase_Zc3h12a. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Morosawa T., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K.
      , Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. Cited for: IDENTIFICATION, SUBCELLULAR LOCATION.
    5. "PRORP proteins support RNase P activity in both organelles and the nucleus in Arabidopsis."
      Gutmann B., Gobert A., Giege P.
      Genes Dev. 26:1022-1027(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF 480-ASP-ASP-481, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiPRRP3_ARATH
    AccessioniPrimary (citable) accession number: F4JKB6
    Secondary accession number(s): O49713, Q0WKW9, Q0WVS1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2012
    Last sequence update: June 28, 2011
    Last modified: October 1, 2014
    This is version 24 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3