SYVM1_ARATH
ID SYVM1_ARATH Reviewed; 1108 AA.
AC P93736; Q6NPT2; Q8W4A8; Q9MA22;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Valine--tRNA ligase, mitochondrial 1 {ECO:0000305};
DE EC=6.1.1.9 {ECO:0000305};
DE AltName: Full=AtSYV1 {ECO:0000303|PubMed:10583378};
DE AltName: Full=Protein TWIN 2 {ECO:0000305};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000305};
DE Short=ValRS {ECO:0000305};
DE Flags: Precursor;
GN Name=TWN2 {ECO:0000303|PubMed:9207094}; OrderedLocusNames=At1g14610;
GN ORFNames=T5E21.11;
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 [GENOMIC DNA / MRNA], AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=9207094; DOI=10.1073/pnas.94.14.7349;
RA Zhang J.Z., Somerville C.R.;
RT "Suspensor-derived polyembryony caused by altered expression of valyl-tRNA
RT synthetase in the twn2 mutant of Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7349-7355(1997).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-1108.
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-1108.
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=10583378; DOI=10.1046/j.1432-1327.1999.00922.x;
RA Souciet G., Menand B., Ovesna J., Cosset A., Dietrich A., Wintz H.;
RT "Characterization of two bifunctional Arabdopsis thaliana genes coding for
RT mitochondrial and cytosolic forms of valyl-tRNA synthetase and threonyl-
RT tRNA synthetase by alternative use of two in-frame AUGs.";
RL Eur. J. Biochem. 266:848-854(1999).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP SER-46.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
CC -!- FUNCTION: Required for embryo development and seed viability.
CC {ECO:0000269|PubMed:9207094}.
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: Mitochondrion {ECO:0000269|PubMed:10583378,
CC ECO:0000305|PubMed:25732537}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:10583378}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB49704.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF63175.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U89986; AAB49704.1; ALT_FRAME; mRNA.
DR EMBL; BT010735; AAR23705.1; -; mRNA.
DR EMBL; AC010657; AAF63175.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29190.1; -; Genomic_DNA.
DR EMBL; AY062693; AAL32771.1; -; mRNA.
DR EMBL; U93308; AAB51589.1; -; Genomic_DNA.
DR PIR; F86280; F86280.
DR RefSeq; NP_172913.1; NM_101328.4.
DR AlphaFoldDB; P93736; -.
DR SMR; P93736; -.
DR BioGRID; 23263; 2.
DR STRING; 3702.AT1G14610.1; -.
DR iPTMnet; P93736; -.
DR MetOSite; P93736; -.
DR PaxDb; P93736; -.
DR PRIDE; P93736; -.
DR ProteomicsDB; 246389; -.
DR EnsemblPlants; AT1G14610.1; AT1G14610.1; AT1G14610.
DR GeneID; 838023; -.
DR Gramene; AT1G14610.1; AT1G14610.1; AT1G14610.
DR KEGG; ath:AT1G14610; -.
DR Araport; AT1G14610; -.
DR TAIR; locus:2204543; AT1G14610.
DR eggNOG; KOG0432; Eukaryota.
DR HOGENOM; CLU_001493_0_1_1; -.
DR InParanoid; P93736; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 229591at2759; -.
DR PhylomeDB; P93736; -.
DR BRENDA; 6.1.1.9; 399.
DR PRO; PR:P93736; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P93736; baseline and differential.
DR Genevisible; P93736; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
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; -; 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
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 PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00422; valS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Cytoplasm;
KW Developmental protein; Ligase; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 47..1108
FT /note="Valine--tRNA ligase, mitochondrial 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000106258"
FT REGION 57..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1032..1064
FT /evidence="ECO:0000255"
FT MOTIF 177..187
FT /note="'HIGH' region"
FT /evidence="ECO:0000305"
FT MOTIF 695..699
FT /note="'KMSKS' region"
FT /evidence="ECO:0000305"
FT COMPBIAS 57..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 698
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 357..361
FT /note="GGLGE -> ELGR (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 716
FT /note="E -> G (in Ref. 1; AAB49704)"
FT /evidence="ECO:0000305"
FT CONFLICT 799
FT /note="D -> S (in Ref. 1; AAB49704)"
FT /evidence="ECO:0000305"
FT CONFLICT 830
FT /note="T -> A (in Ref. 1; AAB49704)"
FT /evidence="ECO:0000305"
FT CONFLICT 1028
FT /note="E -> K (in Ref. 1; AAB49704)"
FT /evidence="ECO:0000305"
FT CONFLICT 1063
FT /note="S -> F (in Ref. 1; AAB49704)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1108 AA; 125926 MW; 590254624020F494 CRC64;
MSLLFLRRAK PLFVSCCSAT HSRSSFLSPT LTNQLVRSFH GSRTMSESEK KILTEEELER
KKKKEEKAKE KELKKQKALE KERLAELKAK QAKDGTNVPK KSAKKSSKRD ASEENPEDFV
DPETPLGERK RLSSQMAKQY SPATVEKSWY AWWEKSDLFK ADAKSSKPPF VIVLPPPNVT
GALHIGHALT SAIEDTIIRW KRMSGYNALW VPGVDHAGIA TQVVVEKKIM RDRGMTRHDV
GREEFVKEVW KWKNQYGGTI LTQLRRLGAS LDWSRECFTM DEQRSKAVTE AFVRLYKEGL
IYRDIRLVNW DCILRTAISD VEVEYIDIKE KTLLKVPGYE KPVEFGLLTS FAYPLEGGLG
EVIVATTRVE TMLGDTAIAI HPDDARYKHL HGKFAVHPFN GRKLPIICDG ILVDPNFGTG
CVKITPAHDP NDCEVGKRHK LEFINIFTDD GKINTNGGSD FAGMPRFAAR EAVVEALQKQ
GLYRGAKNNE MRLGLCSRTN DVIEPMIKPQ WYVNCSMIGK EALDVAITDE NKKLEFVPKQ
YTAEWRRWLE NIRDWCISRQ LWWGHRIPAW YATLEEDQLK EVGAYSDHWV VARTEDDARE
EAAQKFLGKK FELTRDPDVL DTWFSSGLFP LSVLGWPDVT DDFKAFYPTS VLETGHDILF
FWVARMVMMG MKLGGEVPFS KVYFHPMIRD AHGRKMSKSL GNVIDPLEVI NGVTLEGLHK
RLEEGNLDPK EVIVAKEGQV KDFPNGIPEC GTDALRFALV SYTAQSDKIN LDILRVVGYR
QWCNKLWNAV RFAMMKLGDG YTPPQTLSPE TMPFSCQWIL SVLNKAISKT VVSLDAFEFS
DAANTIYAWW QYQFCDVYIE AIKPYFAGDN PTFASERAHA QHALWISLET GLRLLHPFMP
FVTEELWQRL PAPKDTERKA SIMICDYPSA IENWSNEKVE SEMDTVLATV KCMRALRAGL
LEKQKNERLP AFALCENNVT SEIVKSHELE IRTLANLSSL EVVSKGQHAA PPGSSVETVN
ENLKVYLEVD GAINTEAEQE KIRNKIGELQ KQKEKLQKMM SVSTYEEKVP ANIKEDNANK
LAKILQEFDF FEKESARLAA ETSNSGNQ
