F4JKB6 (PRRP3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proteinaceous RNase P 3
EC=3.1.26.5

Gene names

Name:	PRORP3
Ordered Locus Names:	At4g21900
ORF Names:	T8O5.110

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	576 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Double mutant prorp2/prorp3 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

Keywords
Biological process	tRNA processing
Cellular component	Nucleus
Domain	Repeat
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA processing Inferred from mutant phenotype Ref.5. Source: UniProtKB snoRNA processing Inferred from mutant phenotype Ref.5. Source: UniProtKB tRNA 5'-leader removal Inferred from direct assay Ref.5. Source: UniProtKB
Cellular_component	nucleus Inferred from direct assay Ref.4. Source: TAIR
Molecular_function	ribonuclease P activity Inferred from direct assay Ref.5. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 576	576	Proteinaceous RNase P 3		PRO_0000420274
Regions
	Repeat	88 – 123	36	PPR 1
	Repeat	129 – 166	38	PPR 2
	Repeat	167 – 201	35	PPR 3
	Repeat	204 – 238	35	PPR 4
	Compositional bias	80 – 83	4	Poly-Lys
Experimental info
	Mutagenesis	480 – 481	2	DD → AA: Loss of activity. Ref.5
	Sequence conflict	185	1	D → G in BAF02238. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	F4JKB6 [UniParc]. Last modified June 28, 2011. Version 1. Checksum: 10A34B9C5F166DAD	FASTA	576	64,396
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
IPI	IPI00543150. IPI00892032.
PIR	T05472.
RefSeq	NP_193921.2. NM_118311.6.
UniGene	At.74070.
3D structure databases
ProteinModelPortal	F4JKB6.
SMR	F4JKB6. Positions 87-573.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT4G21900.1-P.
Proteomic databases
PRIDE	F4JKB6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G21900.1; AT4G21900.1; AT4G21900.
GeneID	828279.
KEGG	ath:AT4G21900.
Organism-specific databases
TAIR	At4g21900.
Phylogenomic databases
eggNOG	NOG68490.
HOGENOM	HOG000006117.
OMA	SCEPMAD.
Family and domain databases
InterPro	IPR021869. RNase_Zc3h12. [Graphical view]
Pfam	PF11977. RNase_Zc3h12a. 1 hit. [Graphical view]
PROSITE	PS51375. PPR. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PRRP3_ARATH

Accession

Primary (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:	May 1, 2013
This is version 17 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program