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 10-MAY-2017, entry version 49.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC 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.,
RA Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA 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.,
RA Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RG The Arabidopsis Information Portal (Araport);
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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
RT embryo 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
RT in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16484-16489(2005).
CC -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate
CC + L-valyl-tRNA(Val). {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
CC the embryo at the globular stage. {ECO:0000305|PubMed:16297076}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC family. {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 UniGene; At.31646; -.
DR ProteinModelPortal; F4KE63; -.
DR SMR; F4KE63; -.
DR STRING; 3702.AT5G16715.1; -.
DR iPTMnet; F4KE63; -.
DR PaxDb; F4KE63; -.
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 eggNOG; COG0525; LUCA.
DR InParanoid; F4KE63; -.
DR KO; K01873; -.
DR OMA; WWRELQL; -.
DR OrthoDB; EOG0936013E; -.
DR PRO; PR:F4KE63; -.
DR Proteomes; UP000006548; Chromosome 5.
DR Genevisible; F4KE63; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
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; 1.10.730.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
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; IPR019499; Val-tRNA_synth_tRNA-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
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 Complete proteome; Leucine-rich repeat; Ligase; Mitochondrion;
KW Nucleotide-binding; Plastid; Protein biosynthesis; Reference proteome;
KW Repeat; Transit peptide.
FT TRANSIT 1 ? Chloroplast and mitochondrion.
FT {ECO:0000305}.
FT CHAIN ? 974 Valine--tRNA ligase,
FT chloroplastic/mitochondrial 2.
FT {ECO:0000305}.
FT /FTId=PRO_0000433550.
FT REPEAT 432 454 LRR 1. {ECO:0000255}.
FT REPEAT 857 880 LRR 2. {ECO:0000255}.
FT COILED 489 518 {ECO:0000255}.
FT MOTIF 109 119 "HIGH" region. {ECO:0000305}.
FT MOTIF 598 602 "KMSKS" region. {ECO:0000305}.
FT BINDING 601 601 ATP. {ECO:0000250}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 69 966 ihamap:Val_tRNA_synth_type1 [T]
FT MYHIT 109 120 ipat:AA_TRNA_LIGASE_I [T]
FT MYHIT 80 637 ipfam:tRNA-synt_1 [T]
FT MYHIT 901 965 ipfam:Val_tRNA-synt_C [T]
FT MYHIT 694 835 ipfam:Anticodon_1 [T]
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
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