Reviewed, UniProtKB/Swiss-Prot Q8GW64 (PTHC_ARATH)

Names and origin

Protein names

Recommended name:
    Peptidyl-tRNA hydrolase, chloroplastic
    EC=3.1.1.29
Alternative name(s):
    C-PTH

Gene names

Ordered Locus Names:	At1g18440
ORF Names:	F15H18.24

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	288 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 By similarity.
Catalytic activity	N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA.
Subunit structure	Monomer By similarity.
Subcellular location	Plastid › chloroplast stroma By similarity.
Sequence similarities	Belongs to the PTH family.
Sequence caution	The sequence AAF25998.1 differs from that shown. Reason: Erroneous gene model prediction. The predicted gene has been split into 2 genes: At1g18440 and At1g18450.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	translation Inferred from electronic annotation. Source: InterPro
Cellular component	chloroplast stroma Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aminoacyl-tRNA hydrolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 55	55	Chloroplast Potential
	Chain	56 – 288	233	Peptidyl-tRNA hydrolase, chloroplastic		PRO_0000280527
Regions
	Compositional bias	52 – 88	37	Ser-rich
Experimental info
	Sequence conflict	159	1	N → D in BAC43630. Ref.2
	Sequence conflict	159	1	N → D in AAO63348. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q8GW64-1 [UniParc]. Last modified March 20, 2007. Version 2. Checksum: 9CD118CA2915DD0F	FASTA	288	31,562
	10 20 30 40 50 60 MKAVAFPAKI ANLSFPSNCC SLFFRSPATF LSPALPCRKL TKGIRGLEGL MSQCLSSSSQ 70 80 90 100 110 120 SLSFSSNSFS SQPESELLQA LPSSKPKSPP LQLPWLIVGL GNPGKKYQGT RHNVGFEMVD 130 140 150 160 170 180 ALADAEGISM NTVNFKALFG KGVIGNIPIM LAKPQTFMNL SGESVGQIVS FYKIPLKQVL 190 200 210 220 230 240 VVYDDLDLPF GKLRLLPKGG HGGHNGMRSI IDRLKGSRDF PRLRIGIGRP PGKMDTANFV 250 260 270 280 LRQFNRQEQE ELDHTFQTGL EAIRILLLEG FNKSATFVNT RKSMEQLS

References

[1]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed: 11910074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC013354 Genomic DNA. Translation: AAF25998.1. Sequence problems. AK119054 mRNA. Translation: BAC43630.1. BT005284 mRNA. Translation: AAO63348.1.
IPI	IPI00539130.
PIR	C86318.
RefSeq	NP_173279.2.
UniGene	At.22357
3D structure databases
HSSP	HSSP built from PDB template 2PTH based on UniProtKB P23932.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8GW64.
Proteomic databases
PRIDE	Q8GW64.
Genome annotation databases
GeneID	838424.
GenomeReviews	Gene locus AT1G18440 in contig CT485782_GR.
KEGG	ath:AT1G18440.
NMPDR	fig|3702.1.peg.2177.
Organism-specific databases
TAIR	At1g18440.
Phylogenomic databases
OMA	GRPPGKM.
Enzyme and pathway databases
BRENDA	3.1.1.29. 302.
Gene expression databases
Genevestigator	Q8GW64.
Family and domain databases
InterPro	IPR001328. Pept_tRNA_hydro. IPR018171. Pept_tRNA_hydro_CS. [Graphical view]
Gene3D	G3DSA:3.40.50.1470. Pept_tRNA_hydro. 1 hit.
PANTHER	PTHR17224. Pept_tRNA_hydro. 1 hit.
Pfam	PF01195. Pept_tRNA_hydro. 1 hit. [Graphical view]
ProDom	PD005324. PeptRNAhydrolase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00447. pth. 1 hit.
PROSITE	PS01195. PEPT_TRNA_HYDROL_1. 1 hit. PS01196. PEPT_TRNA_HYDROL_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PTHC_ARATH

Accession

Primary (citable) accession number: Q8GW64
Secondary accession number(s): Q9LPQ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	March 20, 2007
Last modified:	November 3, 2009
This is version 48 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)