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Protein

Proteinaceous RNase P 3

Gene

PRORP3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

    • ribonuclease P activity Source: UniProtKB

    GO - Biological processi

    • mRNA processing Source: UniProtKB
    • RNA phosphodiester bond hydrolysis Source: GOC
    • RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    • snoRNA processing Source: UniProtKB
    • tRNA 5'-leader removal Source: UniProtKB
    Complete GO annotation...

    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 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G21900.

    Subcellular locationi

    GO - Cellular componenti

    • nucleus Source: TAIR
    Complete GO annotation...

    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.

    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.
    InParanoidiF4JKB6.
    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

            10         20         30         40         50
    MKLKKPSLPS SLLCAVPPCL SQIRLLIPRR VRVSSSTFAN AKLVTLRNHT
    60 70 80 90 100
    VNLHIYYCSM AGTDNRRSRH DDESPKNPNK KKKGNRNPEK SLLINLHSCS
    110 120 130 140 150
    KRKDLSAALA LYDAAITSSD IRLNQQHFQS LLYLCSAFIS DPSLQTVAID
    160 170 180 190 200
    RGFQIFDRMV SSGISPNESS VTAVARLAAA KGDGDYAFKL VKDLVAVGGV
    210 220 230 240 250
    SVPRLRTYAP ALLCFCDTLE AEKGYEVEDH MDASGIVLEE AEISALLKVS
    260 270 280 290 300
    AATGRENKVY RYLQKLRECV GCVSEETSKA IEEWFYGVKA SEVSDNGIGS
    310 320 330 340 350
    DIELLRAAVL KNGGGWHGLG WVGEGKWIVK KGNVSSAGKC LSCDEHLACV
    360 370 380 390 400
    DTNEVETEDF VNSLVTLAME RKAKMNSCEP MADFSEFQEW LEKHGDYEAI
    410 420 430 440 450
    LDGANIGLYQ QNFADGGFSL PQLEAVVKEL YNKSGSKKQP LILLHKKRVN
    460 470 480 490 500
    ALLENPNHRN LVEEWINNNV LYATPPGSND DWYWLYAAAK LKCLLVTNDE
    510 520 530 540 550
    MRDHIFELLS NSFFQKWKER HQVRFTFVKG CLKLEMPPPF SVVIQESEKG
    560 570
    SWHVPITSQD KEESLRSWMC ITRQSS
    Length:576
    Mass (Da):64,396
    Last modified:June 28, 2011 - v1
    Checksum:i10A34B9C5F166DAD
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti185 – 1851D → G in BAF02238 (Ref. 3) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

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

    Protein-protein interaction databases

    STRINGi3702.AT4G21900.1.

    Proteomic databases

    PRIDEiF4JKB6.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    TAIRiAT4G21900.

    Phylogenomic databases

    eggNOGiNOG68490.
    HOGENOMiHOG000006117.
    InParanoidiF4JKB6.
    KOiK18213.
    OMAiSCEPMAD.

    Miscellaneous databases

    PROiF4JKB6.

    Family and domain databases

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

    Publicationsi

    « Hide 'large scale' publications
    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: June 24, 2015
    This is version 28 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.