ID D7KBM5_ARALL Unreviewed; 1108 AA.
AC D7KBM5;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=valine--tRNA ligase {ECO:0000256|ARBA:ARBA00013169};
DE EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
GN ORFNames=ARALYDRAFT_471639 {ECO:0000313|EMBL:EFH69077.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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:0000256|ARBA:ARBA00001624};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR EMBL; GL348713; EFH69077.1; -; Genomic_DNA.
DR RefSeq; XP_002892818.1; XM_002892772.1.
DR AlphaFoldDB; D7KBM5; -.
DR STRING; 81972.D7KBM5; -.
DR EnsemblPlants; fgenesh2_kg.1__1593__AT1G14610.1; fgenesh2_kg.1__1593__AT1G14610.1; fgenesh2_kg.1__1593__AT1G14610.1.
DR GeneID; 9328880; -.
DR Gramene; fgenesh2_kg.1__1593__AT1G14610.1; fgenesh2_kg.1__1593__AT1G14610.1; fgenesh2_kg.1__1593__AT1G14610.1.
DR KEGG; aly:9328880; -.
DR eggNOG; KOG0432; Eukaryota.
DR HOGENOM; CLU_001493_0_1_1; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblPlants.
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; IEA:UniProtKB-EC.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IEA:EnsemblPlants.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR CDD; cd00817; ValRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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 NCBIfam; TIGR00422; valS; 1.
DR PANTHER; PTHR11946:SF109; VALINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT DOMAIN 149..771
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 817..965
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 58..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1032..1059
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 58..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1108 AA; 125853 MW; D65EA1035F7CA293 CRC64;
MSLLFLRRAK PLFVSCSSAS RSQATFLSPT LTNQLLRSFH GSRTMSESEK KILTEEELER
KKKKEEKNKE KELKKQKALE KARLAELKAK QAKDGTNVPK KSAKKSSKRD VSEENPEDFV
DPETPLGERK RLSSQMAKQY SPAAVEKSWY AWWEKSDLFK ADAKSSKKPF VIVLPPPNVT
GALHIGHALT AAIEDTIIRW KRMSGYNALW VPGVDHAGIA TQVVVEKKLM RERGMTRHDV
GREEFVKEVW KWKNQYGGTI LTQLRSLGAS LDWSRECFTM DEQRSKAVTE AFVRLYKEGL
IYRDIRLVNW DCVLRTAISD EEVEYIDIKE RTLLKVPGYE KPVEFGLLTS FAYPLEGGLG
EVVVATTRVE TMLGDTAIAI HPDDARYKHL HGKFAVHPFN GRKLPIICDG ILVDPNFGTG
CVKITPAHDP NDCEVGKRHK LEFINIFTDD GKINTNGGSD FAGMPRFAAR EAVVEALQKQ
GLYRGAKNNE MRLGLCSRTS DVIEPMIKPQ WYVNCSMIGK EALDVAITDE NKKLEFVPKQ
YTAEWRRWLE NIRDWCISRQ LWWGHRIPAW YATLEEDQLK EVGAYSDHWV VARTEDDAQK
EAAQKFAGKK FELTRDPDVL DTWFSAGLFP LSVLGWPDVT EDFKAFYPTS VLETGHDILF
FWVARMVMMG MKLGGEVPFS KVYFHPMIRD AHGRKMSKSL GNVIDPLEVI NGVTLEGLHK
RLEEGNLDPK EVVVAKEGQV KDFPNGIPEC GADALRFALV SYTAQSDKIN LDILRVVGYR
QWCNKLWNAV RFAMMKLGDD YTPPQTLSPE TMPFSCQWIL SVLNKAVSKT VESLDAFEFS
DAATTVYAWW QYQFCDVYIE AIKPYFAGDN PTFASERAHA QHALWISLET GLRLLHPLMP
FVTEELWQRL PSPKDTERKA SIMICDYPSA IENWTNEKVE SEMETILATV KCMRALRAGL
LEKQKNERLP AFALCENNVT AEIVKSHELE IRTLANLSSL EVLLKGEHAA PPGSSVETVN
ENLKVYLKVD GAINTEAEQE KIRNKIGELQ KQKEKLQKMM SVSTYEEKVP ANIKEDNANK
LTKILQEFDF FEKESARLAA ETSNSGNQ
//
