Entry euk:SYVM2_ARATH

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       109    120       ipat:AA_TRNA_LIGASE_I [T]
FT   MYHIT        80    637       ipfam:tRNA-synt_1 [T]
FT   MYHIT       694    835       ipfam:Anticodon_1 [T]
FT   MYHIT       901    965       ipfam:Val_tRNA-synt_C [T]
FT   MYHIT        69    966       ihamap:Val_tRNA_synth_type1 [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
//