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F4JKB6 (PRRP3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteinaceous RNase P 3

EC=3.1.26.5
Gene names
Name:PRORP3
Ordered Locus Names:At4g21900
ORF Names:T8O5.110
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length576 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Subcellular location

Nucleus Ref.4.

Disruption phenotype

No visible phenotype; due to the redundancy with PRORP2. Prorp2 and prorp3 double mutant is lethal. Ref.5

Sequence similarities

Belongs to the PPR family. P subfamily.

Contains 4 PPR (pentatricopeptide) repeats.

Biophysicochemical properties

Kinetic parameters:

KM=0.3 µM for tRNA(Gln) precursor Ref.5

Sequence caution

The sequence BAE98777.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAF02238.1 differs from that shown. Reason: Intron retention.

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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 576576Proteinaceous RNase P 3
PRO_0000420274

Regions

Repeat88 – 12336PPR 1
Repeat129 – 16638PPR 2
Repeat167 – 20135PPR 3
Repeat204 – 23835PPR 4
Compositional bias80 – 834Poly-Lys

Experimental info

Mutagenesis480 – 4812DD → AA: Loss of activity. Ref.5
Sequence conflict1851D → G in BAF02238. Ref.3

Sequences

Sequence LengthMass (Da)Tools
F4JKB6 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: 10A34B9C5F166DAD

FASTA57664,396
        10         20         30         40         50         60 
MKLKKPSLPS SLLCAVPPCL SQIRLLIPRR VRVSSSTFAN AKLVTLRNHT VNLHIYYCSM 

        70         80         90        100        110        120 
AGTDNRRSRH DDESPKNPNK KKKGNRNPEK SLLINLHSCS KRKDLSAALA LYDAAITSSD 

       130        140        150        160        170        180 
IRLNQQHFQS LLYLCSAFIS DPSLQTVAID RGFQIFDRMV SSGISPNESS VTAVARLAAA 

       190        200        210        220        230        240 
KGDGDYAFKL VKDLVAVGGV SVPRLRTYAP ALLCFCDTLE AEKGYEVEDH MDASGIVLEE 

       250        260        270        280        290        300 
AEISALLKVS AATGRENKVY RYLQKLRECV GCVSEETSKA IEEWFYGVKA SEVSDNGIGS 

       310        320        330        340        350        360 
DIELLRAAVL KNGGGWHGLG WVGEGKWIVK KGNVSSAGKC LSCDEHLACV DTNEVETEDF 

       370        380        390        400        410        420 
VNSLVTLAME RKAKMNSCEP MADFSEFQEW LEKHGDYEAI LDGANIGLYQ QNFADGGFSL 

       430        440        450        460        470        480 
PQLEAVVKEL YNKSGSKKQP LILLHKKRVN ALLENPNHRN LVEEWINNNV LYATPPGSND 

       490        500        510        520        530        540 
DWYWLYAAAK LKCLLVTNDE MRDHIFELLS NSFFQKWKER HQVRFTFVKG CLKLEMPPPF 

       550        560        570 
SVVIQESEKG SWHVPITSQD KEESLRSWMC ITRQSS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"A single Arabidopsis organellar protein has RNase P activity."
Gobert A., Gutmann B., Taschner A., Goessringer M., Holzmann J., Hartmann R.K., Rossmanith W., Giege P.
Nat. Struct. Mol. Biol. 17:740-744(2010) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT05472.
RefSeqNP_193921.2. NM_118311.6.
UniGeneAt.74070.

3D structure databases

ProteinModelPortalF4JKB6.
SMRF4JKB6. Positions 87-573.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G21900.1-P.

Proteomic databases

PRIDEF4JKB6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G21900.1; AT4G21900.1; AT4G21900.
GeneID828279.
KEGGath:AT4G21900.

Organism-specific databases

TAIRAT4G21900.

Phylogenomic databases

eggNOGNOG68490.
HOGENOMHOG000006117.
KOK18213.
OMASCEPMAD.

Family and domain databases

InterProIPR021869. RNase_Zc3h12.
[Graphical view]
PfamPF11977. RNase_Zc3h12a. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePRRP3_ARATH
AccessionPrimary (citable) accession number: F4JKB6
Secondary accession number(s): O49713, Q0WKW9, Q0WVS1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: June 28, 2011
Last modified: July 9, 2014
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names