SYWM_ARATH
ID SYWM_ARATH Reviewed; 408 AA.
AC Q8RXE9; O82313;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Tryptophan--tRNA ligase, chloroplastic/mitochondrial {ECO:0000305};
DE EC=6.1.1.2 {ECO:0000305};
DE AltName: Full=Protein OVULE ABORTION 4 {ECO:0000303|PubMed:16297076};
DE AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000305};
DE Short=TrpRS {ECO:0000305};
DE Flags: Precursor;
GN Name=OVA4 {ECO:0000303|PubMed:16297076};
GN OrderedLocusNames=At2g25840 {ECO:0000312|Araport:AT2G25840};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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=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).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=16297076; DOI=10.1111/j.1365-313x.2005.02580.x;
RA Berg M., Rogers R., Muralla R., Meinke D.;
RT "Requirement of aminoacyl-tRNA synthetases for gametogenesis and embryo
RT development in Arabidopsis.";
RL Plant J. 44:866-878(2005).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=16251277; DOI=10.1073/pnas.0504682102;
RA Duchene A.-M., Giritch A., Hoffmann B., Cognat V., Lancelin D.,
RA Peeters N.M., Zaepfel M., Marechal-Drouard L., Small I.D.;
RT "Dual targeting is the rule for organellar aminoacyl-tRNA synthetases in
RT Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16484-16489(2005).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-53, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER CYS-52, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-
CC tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671,
CC Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2;
CC Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16251277}. Mitochondrion
CC {ECO:0000269|PubMed:16251277}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q8RXE9-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Lethal. In heterozygous plants, aborted ovules.
CC {ECO:0000269|PubMed:16297076}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC42246.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005395; AAC42246.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07758.1; -; Genomic_DNA.
DR EMBL; AY081299; AAL91188.1; -; mRNA.
DR EMBL; BT001221; AAN65108.1; -; mRNA.
DR PIR; D84653; D84653.
DR RefSeq; NP_850070.1; NM_179739.4. [Q8RXE9-1]
DR AlphaFoldDB; Q8RXE9; -.
DR SMR; Q8RXE9; -.
DR STRING; 3702.AT2G25840.2; -.
DR iPTMnet; Q8RXE9; -.
DR PaxDb; Q8RXE9; -.
DR PRIDE; Q8RXE9; -.
DR ProteomicsDB; 245297; -. [Q8RXE9-1]
DR EnsemblPlants; AT2G25840.1; AT2G25840.1; AT2G25840. [Q8RXE9-1]
DR GeneID; 817126; -.
DR Gramene; AT2G25840.1; AT2G25840.1; AT2G25840. [Q8RXE9-1]
DR KEGG; ath:AT2G25840; -.
DR Araport; AT2G25840; -.
DR eggNOG; KOG2713; Eukaryota.
DR OMA; GWGQFKP; -.
DR PhylomeDB; Q8RXE9; -.
DR PRO; PR:Q8RXE9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8RXE9; baseline and differential.
DR Genevisible; Q8RXE9; AT.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00806; TrpRS_core; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00140_B; Trp_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002306; Trp-tRNA-ligase.
DR InterPro; IPR024109; Trp-tRNA-ligase_bac-type.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR TIGRFAMs; TIGR00233; trpS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding;
KW Chloroplast; Ligase; Mitochondrion; Nucleotide-binding; Plastid;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 53..408
FT /note="Tryptophan--tRNA ligase,
FT chloroplastic/mitochondrial"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433539"
FT MOTIF 73..81
FT /note="'HIGH' region"
FT /evidence="ECO:0000305"
FT MOTIF 269..273
FT /note="'KMSKS' region"
FT /evidence="ECO:0000305"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 78..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 197
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 209..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 269..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 53
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 408 AA; 45300 MW; 48890DE7A3731636 CRC64;
MGHATSLSHF LILSSSRFSR LGSLTRLLSK PTSLSGSFSS ISVTGQGFRC CCSVATDDTS
PSVKKRVVSG VQPTGSVHLG NYLGAIKNWV ALQDTYETLF IIVDHHAITL PYDTRQLGKA
TTDTAALYLA CGIDVSKASV FVQSHVPAHV ELMWLLCSST PIGWLQKMIQ FKEKSRKEGV
ENASVGLFTY PDLMTADILL YQSDFVPVGE DQKQHIELAR EIAQRVNHLY GGKKWKKLGG
RGGSLFKIPE PLIPQAGARV MSLTDGLSKM SKSAPSDQSR INLLDSKDLI VDKIKRCKTD
SFAGLEFDNA ERPECNNLLS IYQIVSGKKK EEVMEECKDM SWGTFKPLLA DALIEHLSPI
QARYQEIIAE PEYLDKILSE GADRAEELGA VTMRNMYQAM GYYQRRRY
