Q66GI4 (PRRP1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proteinaceous RNase P 1, chloroplastic/mitochondrial
EC=3.1.26.5

Alternative name(s):
Pentatricopeptide repeat-containing protein At2g32230

Gene names

Name:	PRORP1
Ordered Locus Names:	At2g32230
ORF Names:	F22D22.2

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	572 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Endonuclease RNase P responsible for the 5' maturation of tRNA precursors. Preferentially cleaves at the unusual cleavage site, but also able to cleave at the classical cleavage site. Also involved in the maturation of mRNAs in mitochondria. Ref.6 Ref.7 Ref.8
Catalytic activity	Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. Ref.6 Ref.8
Subcellular location	Mitochondrion. Plastid › chloroplast Ref.6.
Disruption phenotype	Embryo lethality when homozygous. Ref.6
Sequence similarities	Belongs to the PPR family. P subfamily. Contains 4 PPR (pentatricopeptide) repeats.
Sequence caution	The sequence AAD15382.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Chloroplast Mitochondrion Plastid
Domain	Repeat Transit peptide
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	tRNA processing Inferred from direct assay Ref.6. Source: TAIR
Cellular_component	chloroplast Inferred from direct assay Ref.6. Source: TAIR mitochondrion Inferred from direct assay Ref.6. Source: TAIR
Molecular_function	ribonuclease P activity Inferred from direct assay Ref.6. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 48

48

Chloroplast and mitochondrion Potential

Chain

49 – 572

524

Proteinaceous RNase P 1, chloroplastic/mitochondrial

PRO_0000356038

Regions

Repeat

96 – 130

35

PPR 1

Repeat

136 – 174

39

PPR 2

Repeat

175 – 209

35

PPR 3

Repeat

210 – 244

35

PPR 4

Compositional bias

316 – 319

4

Poly-Gly

Experimental info

Mutagenesis

474 – 475

2

DD → AA: Loss of activity. Ref.6

Sequence conflict

250

1

A → V in AAM13880. Ref.3

Secondary structure

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572

Helix Strand Turn

Details...

Helix

96 – 106

11

Turn

107 – 109

3

Helix

113 – 126

14

Helix

132 – 142

11

Beta strand

149 – 152

4

Helix

155 – 169

15

Helix

176 – 189

14

Helix

192 – 204

13

Helix

211 – 223

13

Helix

227 – 239

13

Helix

246 – 258

13

Helix

262 – 275

14

Beta strand

277 – 279

3

Helix

281 – 292

12

Helix

294 – 297

4

Helix

306 – 316

11

Beta strand

331 – 336

6

Beta strand

342 – 344

3

Turn

345 – 347

3

Helix

358 – 375

18

Helix

378 – 389

12

Beta strand

395 – 399

5

Helix

400 – 405

6

Helix

413 – 426

14

Beta strand

434 – 438

5

Helix

439 – 442

4

Helix

445 – 447

3

Helix

450 – 461

12

Beta strand

465 – 468

4

Helix

474 – 485

12

Beta strand

488 – 490

3

Helix

498 – 503

6

Turn

504 – 506

3

Helix

507 – 515

9

Beta strand

516 – 522

7

Turn

523 – 525

3

Beta strand

526 – 530

5

Beta strand

547 – 551

5

Turn

556 – 558

3

Beta strand

563 – 568

6

Sequences

	Sequence		Length	Mass (Da)
	Q66GI4 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 80857002D71F42FA	FASTA	572	64,877
	10 20 30 40 50 60 MLRLTCFTPS FSRACCPLFA MMLKVPSVHL HHPRFSPFRF YHTSLLVKGT RDRRLILVER 70 80 90 100 110 120 SRHLCTLPLA AAKQSAASPS ENLSRKAKKK AIQQSPEALL KQKLDMCSKK GDVLEALRLY 130 140 150 160 170 180 DEARRNGVQL SQYHYNVLLY VCSLAEAATE SSPNPGLSRG FDIFKQMIVD KVVPNEATFT 190 200 210 220 230 240 NGARLAVAKD DPEMAFDMVK QMKAFGIQPR LRSYGPALFG FCRKGDADKA YEVDAHMVES 250 260 270 280 290 300 EVVPEEPELA ALLKVSMDTK NADKVYKTLQ RLRDLVRQVS KSTFDMIEEW FKSEVATKTG 310 320 330 340 350 360 VKKWDVKKIR DAVVSGGGGW HGQGWLGTGK WNVKRTEMDE NGVCKCCKEK LVCIDINPVE 370 380 390 400 410 420 TETFAASLTR LACEREVKAN FNQFQEWLER HGPFDAVIDG ANMGLVNQRS FSFFQLNNTV 430 440 450 460 470 480 QRCQQISPSK RLPLVILHKS RVNGGPATYP KNRALLEKWK NAGALYATPP GSNDDWYWLY 490 500 510 520 530 540 AAVSCKCLLV TNDEMRDHLF QLLGNSFFPR WKEKHQVRIS VTREDGLKLN MPPPYSIVIQ 550 560 570 ESEDGTWHVP MSVEDDLQTS RQWLCAKRSK TP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(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]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Arabidopsis ORF clones." Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R. Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Genome-wide analysis of Arabidopsis pentatricopeptide repeat proteins reveals their essential role in organelle biogenesis." Lurin C., Andres C., Aubourg S., Bellaoui M., Bitton F., Bruyere C., Caboche M., Debast C., Gualberto J., Hoffmann B., Lecharny A., Le Ret M., Martin-Magniette M.-L., Mireau H., Peeters N., Renou J.-P., Szurek B., Taconnat L., Small I. Plant Cell 16:2089-2103(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY.
[6]	"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: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF 474-ASP-ASP-475.
[7]	"Plant mitochondria use two pathways for the biogenesis of tRNAHis." Placido A., Sieber F., Gobert A., Gallerani R., Giege P., Marechal-Drouard L. Nucleic Acids Res. 38:7711-7717(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"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.
+	Additional computationally mapped references.

Web resources

Arabidopsis PPR Protein Database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AC006223 Genomic DNA. Translation: AAD15382.1. Sequence problems.
CP002685 Genomic DNA. Translation: AEC08652.1.
AY091059 mRNA. Translation: AAM13880.1.
BT015418 mRNA. Translation: AAU05541.1.

IPI

IPI00540508.

PIR

E84730.

RefSeq

NP_850186.1. NM_179855.2.

UniGene

At.38106.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4G23	X-ray	1.98	A	77-572	[»]
4G24	X-ray	1.95	A	77-572	[»]
4G25	X-ray	2.00	A	77-572	[»]
4G26	X-ray	1.75	A	77-572	[»]

ProteinModelPortal

Q66GI4.

SMR

Q66GI4. Positions 95-570.

ModBase

Search...

Proteomic databases

PaxDb

Q66GI4.

PRIDE

Q66GI4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT2G32230.1; AT2G32230.1; AT2G32230.

GeneID

817782.

KEGG

ath:AT2G32230.

Organism-specific databases

GeneFarm

4941. 436.

TAIR

At2g32230.

Phylogenomic databases

eggNOG

NOG68490.

HOGENOM

HOG000006117.

InParanoid

Q66GI4.

OMA

KLDMCSK.

PhylomeDB

Q66GI4.

ProtClustDB

CLSN2679969.

Gene expression databases

Genevestigator

Q66GI4.

Family and domain databases

InterPro

IPR002885. Pentatricopeptide_repeat.
[Graphical view]

Pfam

PF01535. PPR. 1 hit.
PF13812. PPR_3. 1 hit.
[Graphical view]

PROSITE

PS51375. PPR. 3 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PRRP1_ARATH

Accession

Primary (citable) accession number: Q66GI4
Secondary accession number(s): Q8RWW5, Q9SKX7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program