PTHC_ARATH
ID PTHC_ARATH Reviewed; 288 AA.
AC Q8GW64; Q9LPQ9;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Peptidyl-tRNA hydrolase, chloroplastic;
DE EC=3.1.1.29;
DE AltName: Full=C-PTH;
DE Flags: Precursor;
GN OrderedLocusNames=At1g18440; ORFNames=F15H18.24;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC which drop off the ribosome during protein synthesis. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-
CC amino acid + H(+); Xref=Rhea:RHEA:54448, Rhea:RHEA-COMP:10123,
CC Rhea:RHEA-COMP:13883, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:59874, ChEBI:CHEBI:78442, ChEBI:CHEBI:138191;
CC EC=3.1.1.29;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PTH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF25998.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At1g18440 and At1g18450.; Evidence={ECO:0000305};
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DR EMBL; AC013354; AAF25998.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29714.1; -; Genomic_DNA.
DR EMBL; AK119054; BAC43630.1; -; mRNA.
DR EMBL; BT005284; AAO63348.1; -; mRNA.
DR PIR; C86318; C86318.
DR RefSeq; NP_173279.2; NM_101701.4.
DR AlphaFoldDB; Q8GW64; -.
DR SMR; Q8GW64; -.
DR BioGRID; 23663; 1.
DR STRING; 3702.AT1G18440.1; -.
DR PaxDb; Q8GW64; -.
DR PRIDE; Q8GW64; -.
DR ProteomicsDB; 248807; -.
DR EnsemblPlants; AT1G18440.1; AT1G18440.1; AT1G18440.
DR GeneID; 838424; -.
DR Gramene; AT1G18440.1; AT1G18440.1; AT1G18440.
DR KEGG; ath:AT1G18440; -.
DR Araport; AT1G18440; -.
DR TAIR; locus:2014134; AT1G18440.
DR eggNOG; KOG2255; Eukaryota.
DR HOGENOM; CLU_062456_5_0_1; -.
DR InParanoid; Q8GW64; -.
DR OMA; FTFQHGI; -.
DR OrthoDB; 1514615at2759; -.
DR PhylomeDB; Q8GW64; -.
DR PRO; PR:Q8GW64; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GW64; baseline and differential.
DR Genevisible; Q8GW64; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IBA:GO_Central.
DR Gene3D; 3.40.50.1470; -; 1.
DR HAMAP; MF_00083; Pept_tRNA_hydro_bact; 1.
DR InterPro; IPR001328; Pept_tRNA_hydro.
DR InterPro; IPR018171; Pept_tRNA_hydro_CS.
DR InterPro; IPR036416; Pept_tRNA_hydro_sf.
DR PANTHER; PTHR17224; PTHR17224; 1.
DR Pfam; PF01195; Pept_tRNA_hydro; 1.
DR SUPFAM; SSF53178; SSF53178; 1.
DR TIGRFAMs; TIGR00447; pth; 1.
DR PROSITE; PS01195; PEPT_TRNA_HYDROL_1; 1.
DR PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Hydrolase; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..288
FT /note="Peptidyl-tRNA hydrolase, chloroplastic"
FT /id="PRO_0000280527"
FT CONFLICT 159
FT /note="N -> D (in Ref. 3; BAC43630 and 4; AAO63348)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 288 AA; 31562 MW; 9CD118CA2915DD0F CRC64;
MKAVAFPAKI ANLSFPSNCC SLFFRSPATF LSPALPCRKL TKGIRGLEGL MSQCLSSSSQ
SLSFSSNSFS SQPESELLQA LPSSKPKSPP LQLPWLIVGL GNPGKKYQGT RHNVGFEMVD
ALADAEGISM NTVNFKALFG KGVIGNIPIM LAKPQTFMNL SGESVGQIVS FYKIPLKQVL
VVYDDLDLPF GKLRLLPKGG HGGHNGMRSI IDRLKGSRDF PRLRIGIGRP PGKMDTANFV
LRQFNRQEQE ELDHTFQTGL EAIRILLLEG FNKSATFVNT RKSMEQLS
