ID A0A8N4EVL3_ELAGV Unreviewed; 1144 AA.
AC A0A8N4EVL3;
DT 03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Valine--tRNA ligase, mitochondrial {ECO:0000256|ARBA:ARBA00040837};
DE EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
GN Name=LOC105037449 {ECO:0000313|RefSeq:XP_029118284.1};
OS Elaeis guineensis var. tenera (Oil palm).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Arecaceae; Arecoideae; Cocoseae;
OC Elaeidinae; Elaeis.
OX NCBI_TaxID=51953 {ECO:0000313|Proteomes:UP000504607, ECO:0000313|RefSeq:XP_029118284.1};
RN [1] {ECO:0000313|RefSeq:XP_029118284.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tRNA(Val) + L-valine + ATP = L-valyl-tRNA(Val) + AMP +
CC diphosphate; 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:ARBA00047552};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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 RefSeq; XP_029118284.1; XM_029262451.1.
DR RefSeq; XP_073100982.1; XM_073244881.1.
DR AlphaFoldDB; A0A8N4EVL3; -.
DR GeneID; 105037449; -.
DR OrthoDB; 629407at2759; -.
DR Proteomes; UP000504607; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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:UniProtKB-ARBA.
DR GO; GO:0048608; P:reproductive structure development; IEA:UniProtKB-ARBA.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR CDD; cd00817; ValRS_core; 1.
DR FunFam; 1.10.730.10:FF:000009; Valine--tRNA ligase, mitochondrial; 1.
DR FunFam; 3.40.50.620:FF:000020; Valine--tRNA ligase, mitochondrial; 1.
DR FunFam; 3.40.50.620:FF:000078; Valine--tRNA ligase, mitochondrial; 1.
DR FunFam; 3.90.740.10:FF:000005; Valine--tRNA ligase, mitochondrial; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
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; IPR010978; tRNA-bd_arm.
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; NF004349; PRK05729.1; 1.
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; SSF46589; tRNA-binding arm; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000504607}.
FT DOMAIN 194..816
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 862..1000
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 107..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1144 AA; 129718 MW; 1EF17231D63E31AA CRC64;
MITAFRIRIR IRVRRCKSCP NPKPSSLQIP KPFSPPFLYF CPYFRRLLSF TPPQSPQLLG
AAPPEGVCSG SEFKKPFAAA NPSMSPIGED GLEKTAMEQK LEEENLEKKL KKEKKAKEKE
EKKLKAAQKA ETAKLWAQKA SDGHKKTERK NRKKDAEEEN PEDFVDPVTP PGEKKQLSRQ
MAKQYSPSAV EKSWYAWWEA SGFFVADASS SKPSFVIVLP PPNVTGALHI GHGLTAAIQD
TIIRWCRMSG YNTLWVPGMD HAGIATQVVV EKKLMRERKL TRHDIGRESF VSEVWKWKNE
YGGTILNQER RLGASLDWSR ECFTMDDRRS KAVTEAFVRL YREGLIYRDH RLVNWDCTLR
TAISDIEVDY KEIKAETLLA VPGYESPVQF GVLTSFAYPL EGGLGEIVVA TTRIETMLGD
TAVAIHSKDE RYTHLHGKYA IHPFNGRKLP IICDDILVDP KFGTGAVKIT PAHDPNDFEV
GKRHNLDFVN IFTDDGKVNS NGGAEFEGMP RFKARVAVIE ALQAKGLYRG AQKNEMNLGL
CSRTNDVVEP MVKPQWFVSC NSMAKLALDA VLSEDNKKIE IIPPQYEQDW KRWLENIRDW
CISRQLWWGH RIPAWYVTLD DDQLKDMGSY NDHWVVGRND EEALQEAKQK FPGKTFQIAQ
DPDVLDTWFS SGLFPLSVLG WPDATVDFKA FYPTSLLETG HDILFFWVAR MVMLGMKLGG
DVPFRKVYLH PMIRDARGRK MSKSLGNVID PLEVINGISL EGLHKRLEEG NLDPKELKIA
KEGQVKDFPN GIAECGADAL RFALISYTAQ SDKINLDVLR VVGYRQWCNK LWNAIRFAMS
KLGDNYAPPT ILGVDSFPSI CKWILSVLNK AVAKTVSSFE SYRFSDAATA VYSWWQFQLC
DVFIEAIKPY FFNDSKEFEL ARAASRDTLW VCLDTGLRLL HPFMPFVTEE LWQRLPQAEG
TCRKESIMIS EYPSVVEAWT NDEIEIDMDI IIGAVRKLRA LRPPSDKNER RTAFALCQGD
DVAEMIKGYE FEIVTLASIS SLKVLSENDA SPVGCAIDIV NENLSVYLQL QGTLNAEAER
EKLGKKKQEI EKLHAALAQI MSSSGYKDKA PQSVQEDDIR KLNAYLEELK IINEAERDLD
QIIN
//
