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Q6NLS8 (PTHM_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptidyl-tRNA hydrolase, mitochondrial
EC=3.1.1.29
Alternative name(s):
M-PTH
Mitochondrial CRS2-like protein
Mitochondrial RNA splicing factor
Gene names
Ordered Locus Names:At5g19830
ORF Names:T29J13.250
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length219 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. May also be required for the splicing of group IIB introns in mitochondrions By similarity.

Catalytic activity

N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA.

Subcellular location

Mitochondrion Potential.

Sequence similarities

Belongs to the PTH family.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionHydrolase
Ribonucleoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

ribonucleoprotein complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionaminoacyl-tRNA hydrolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1010Mitochondrion Potential
Chain11 – 219209Peptidyl-tRNA hydrolase, mitochondrial
PRO_0000280528

Sequences

Sequence LengthMass (Da)Tools
Q6NLS8 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: FA5AADA976824ABF

FASTA21924,599
        10         20         30         40         50         60 
MLSRLSRRCY CTSSVHRPWL FLGLGNPGDK YKGTRHNIGF EMIDVFAESV GIQMNLVNFK 

        70         80         90        100        110        120 
AIMGQGFVAD LPVILAKPQT YMNLSGESSG PLAAYYKLPL NRVLVVHDDM QLPCGVLRLQ 

       130        140        150        160        170        180 
EKGGHGCHNG LKSVMNHFRG NREFARLRIG IGKPPGQMDP KAFLLQKFSM PARERMDKAL 

       190        200        210 
AEGVDALKLV LAKDFGESWR LFNVEQKYKH LKQHTILSA

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed: 11130714] [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]"Arabidopsis ORF clones."
Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., 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. expand/collapse author list , 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].
Strain: cv. Columbia.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF296838 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92753.1.
BT011605 mRNA. Translation: AAS47611.1.
BT012252 mRNA. Translation: AAS76739.1.
AK227887 mRNA. Translation: BAE99859.1.
IPIIPI00521866.
RefSeqNP_197484.4. NM_121988.5.
UniGeneAt.31249.

3D structure databases

HSSPHSSP built from PDB template 2PTH based on UniProtKB P0A7D1.
ProteinModelPortalQ6NLS8.
SMRQ6NLS8. Positions 17-211.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6NLS8.

Proteomic databases

PRIDEQ6NLS8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G19830.1; AT5G19830.1; AT5G19830.
GeneID832103.
GenomeReviewsGene locus AT5G19830 in contig BA000015_GR.
KEGGath:AT5G19830.
NMPDRfig|3702.1.peg.24184.

Organism-specific databases

TAIRAt5g19830.

Phylogenomic databases

eggNOGKOG2255.
GeneTreeEPGT00050000018764.
HOGENOMHBG610927.
InParanoidQ6NLS8.
OMAKYKGTRH.
PhylomeDBQ6NLS8.
ProtClustDBCLSN2681642.

Gene expression databases

GenevestigatorQ6NLS8.

Family and domain databases

InterProIPR001328. Pept_tRNA_hydro.
IPR018171. Pept_tRNA_hydro_CS.
[Graphical view]
Gene3DG3DSA:3.40.50.1470. Pept_tRNA_hydro. 1 hit.
PANTHERPTHR17224. Pept_tRNA_hydro. 1 hit.
PfamPF01195. Pept_tRNA_hydro. 1 hit.
[Graphical view]
SUPFAMSSF53178. Pept_tRNA_hydro. 1 hit.
TIGRFAMsTIGR00447. Pth. 1 hit.
PROSITEPS01195. PEPT_TRNA_HYDROL_1. 1 hit.
PS01196. PEPT_TRNA_HYDROL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTHM_ARATH
AccessionPrimary (citable) accession number: Q6NLS8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 5, 2004
Last modified: October 19, 2011
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents