ID D7L7D0_ARALL Unreviewed; 916 AA.
AC D7L7D0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
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_342735 {ECO:0000313|EMBL:EFH59876.1};
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 -!- 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; GL348715; EFH59876.1; -; Genomic_DNA.
DR RefSeq; XP_002883617.1; XM_002883571.1.
DR AlphaFoldDB; D7L7D0; -.
DR STRING; 81972.D7L7D0; -.
DR EnsemblPlants; fgenesh1_pg.C_scaffold_3002498; fgenesh1_pg.C_scaffold_3002498; fgenesh1_pg.C_scaffold_3002498.
DR Gramene; fgenesh1_pg.C_scaffold_3002498; fgenesh1_pg.C_scaffold_3002498; fgenesh1_pg.C_scaffold_3002498.
DR eggNOG; KOG0432; Eukaryota.
DR HOGENOM; CLU_001493_0_2_1; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
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:0009791; P:post-embryonic development; IEA:UniProt.
DR GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
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; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR PANTHER; PTHR11946:SF113; 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 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 86..477
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 701..849
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 36..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 916 AA; 103116 MW; 9BFCBF2ACAA18DA5 CRC64;
MELEMERRLK KEHNAKVKAL KKQKAIEKAK LGELNAKSKK SAAKKIGKEE ENHADFSDPE
TPIGERKRLS SQMAKHYSPS AVEKSWYEWW ETSEFFKADA TSSKPQFVIV LPPPNVTGAL
HIGHALTCAV QDTLIRWKRM SGFNALWVPG FDHAGIATQV VVEKHLSRET GLTRHDFGRE
EFLNHVWQWT ESKSGTIKSQ LRRMGSSLDW SRECFTMDEH RSKAVTEAFV RLHKEGLIYR
DLRLVHWDCF LSTAISKREV EHIEIKERTP IKVPGYEKPV VFGLITSFAY PLERGGGEVV
VATTRVETML GDTAIAVHPD DARYKHLHGE FAVHPFNGRK LPIICDEILV DPNVGTGCVK
ITPAHDTNDF DVGRRHNLEF INVFTNDGRI NANGGPDFTG MPRFAAREAI VEALRKKGLY
RGEENNKMTI GVCSRSSDVA EPMLKPQWYV SCSLMAKEAL DVAANGKIEF IPKQNEEDAQ
KEAAQKFSGK KLLELSQDPD VLDTWFSSGL FPLSVLGWPD ETEDFKAFYP ASVLETGHDI
LFFWVARMVM LGMKVGGGDV PFRKVFLHPM IRDAHGRKMS KSLGNGIDPL EVINGVTLAG
LHARLEEGNL DPKELVVAKE GQVKDFPNGI PECGADSLRF ALVSYTAQSD KINMDVLRVV
GYRQWCNKLW NAVRFAMMKL GDGYTPPSQA LSPRAMPFSC QWILSVLNTA ISKTVDSLNA
FELSDAANTV YAWWQYQFCD VFIEAVKPYF SAENPGRTHA QDALWVCLET GLRLLHPFMP
FVTEELWQRL PSPQDCERKA SIMICDYPSP EEKWTNEKVE TEMDVVLVTV KTLRALRAAE
SLKRRINERL HAFALCENAL TLGIVQSHEL EIRTLANLSS FEVVLKGEDK AAQSGSAVVE
TVREPQGVSK IGWSFH
//
