ID   SYVM2_ARATH             Reviewed;         974 AA.
AC   F4KE63;
DT   22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Valine--tRNA ligase, chloroplastic/mitochondrial 2 {ECO:0000305};
DE            EC=6.1.1.9 {ECO:0000305};
DE   AltName: Full=Protein EMBRYO DEFECTIVE 2247 {ECO:0000303|PubMed:16297076};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000305};
DE            Short=ValRS {ECO:0000305};
DE   Flags: Precursor;
GN   Name=EMB2247 {ECO:0000303|PubMed:16297076};
GN   OrderedLocusNames=At5g16715 {ECO:0000312|Araport:AT5G16715};
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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   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   [4]
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC         tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC         COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC         Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:16251277}. Mitochondrion
CC       {ECO:0000269|PubMed:16251277}.
CC   -!- DISRUPTION PHENOTYPE: Embryo defective. Developmental arrest of the
CC       embryo at the globular stage. {ECO:0000305|PubMed:16297076}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC01835.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At5g16710 and At5g16715.; Evidence={ECO:0000305};
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DR   EMBL; AL391147; CAC01835.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED92329.1; -; Genomic_DNA.
DR   RefSeq; NP_568337.4; NM_121677.6.
DR   AlphaFoldDB; F4KE63; -.
DR   SMR; F4KE63; -.
DR   STRING; 3702.AT5G16715.1; -.
DR   iPTMnet; F4KE63; -.
DR   PaxDb; F4KE63; -.
DR   PRIDE; F4KE63; -.
DR   ProteomicsDB; 245291; -.
DR   EnsemblPlants; AT5G16715.1; AT5G16715.1; AT5G16715.
DR   GeneID; 831533; -.
DR   Gramene; AT5G16715.1; AT5G16715.1; AT5G16715.
DR   KEGG; ath:AT5G16715; -.
DR   Araport; AT5G16715; -.
DR   TAIR; locus:505006620; AT5G16715.
DR   eggNOG; KOG0432; Eukaryota.
DR   HOGENOM; CLU_001493_0_2_1; -.
DR   InParanoid; F4KE63; -.
DR   OMA; AMFVTLQ; -.
DR   OrthoDB; 229591at2759; -.
DR   PRO; PR:F4KE63; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; F4KE63; baseline and differential.
DR   Genevisible; F4KE63; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 1.10.287.380; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 2.
DR   HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033705; Anticodon_Ia_Val.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR   InterPro; IPR019499; Val-tRNA_synth_tRNA-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   PANTHER; PTHR11946; PTHR11946; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF10458; Val_tRNA-synt_C; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00422; valS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast; Coiled coil;
KW   Leucine-rich repeat; Ligase; Mitochondrion; Nucleotide-binding; Plastid;
KW   Protein biosynthesis; Reference proteome; Repeat; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast and mitochondrion"
FT                   /evidence="ECO:0000305"
FT   CHAIN           ?..974
FT                   /note="Valine--tRNA ligase, chloroplastic/mitochondrial 2"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000433550"
FT   REPEAT          432..454
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          857..880
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000255"
FT   COILED          489..518
FT                   /evidence="ECO:0000255"
FT   MOTIF           109..119
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000305"
FT   MOTIF           598..602
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000305"
FT   BINDING         601
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   974 AA;  110629 MW;  9D7F7BABF7214A9D CRC64;
     MILKTAFSLP TPTTTLLSPS SPHQLNTLFF TRRRRRLISP SRLNSIFSQR RFSFSAAASG
     NNVFTSPETS KTFDFSSEEK IYKWWESQGY FKPNFDQGGS PFVIPMPPPN VTGSLHMGHA
     MFVTLEDIMV RYNRMNGRPT LWLPGTDHAG IATQLVVEKM LASEGIKRVD LGRDEFTKRV
     WEWKEKYGGT ITNQIKRLGA SCDWSRERFT LDEQLSRAVV EAFVKLHDKG LIYQGSYMVN
     WSPNLQTAVS DLEVEYSEEP GFLYHIKYRV AGSPDFLTIA TTRPETLFGD VALAVHPEDD
     RYSKYVGQTA IVPMTYGRHV PIIADKYVDK DFGTGVLKIS PGHDHNDYLL ARKLGLPILN
     VMNKDATLND VAGLFCGLDR FEVREKLWAD LEEIGLAVKK EPHTLRVPRS QRGGEVIEPL
     VSKQWFVHMD PLAEKALLAV ENKELTIIPE RFEKIYNHWL TNIKDWCISR QLWWGHRIPV
     WYVVGKDCEE DYIVAKSAEE ALEKALEKYG KDVEIYQDPD VLDTWFSSSL WPFSTLGWPD
     VAAKDFNNFY PTNMLETGHD ILFFWVARMV MMGIEFTGTV PFSHVYLHGL IRDSQGRKMS
     KSLGNVIDPL DTIKDFGTDA LRFTIALGTA GQDLNLSTER LTANKAFTNK LWNAGKFVLH
     SLPSLSDTSA WENLLDLKLD KEETLLSLPL PECWAVSKLH ILIDSVTASY EKLFFGDVGR
     ETYDFFWSDF ADWYIEASKS RLYGSGGNSV SLASQAVLLY VFENILKLLH PFMPFVTEDL
     WQALPYRKEA LIVSPWPQNS LPRNVESIKR FENLQALTRA IRNARAEYSV EPVKRISASV
     VGSAEVIEYI SKEKEVLALL SRLDLNNVHF SNAPPGDANL SVHLVASEGL EAYLPLAAMV
     DISSEVQRIS KRLSKMQTEY DALITRLSSP KFVEKAPEEV VRGVKEQVEE LEEKIKLTKA
     RLDFLKSTTS LVSQ