ID A0A8D2J7J6_VARKO Unreviewed; 980 AA.
AC A0A8D2J7J6;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-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};
OS Varanus komodoensis (Komodo dragon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Anguimorpha; Paleoanguimorpha; Varanoidea; Varanidae; Varanus.
OX NCBI_TaxID=61221 {ECO:0000313|Ensembl:ENSVKKP00000005537.1, ECO:0000313|Proteomes:UP000694545};
RN [1] {ECO:0000313|Ensembl:ENSVKKP00000005537.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSVKKP00000005537.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val) in a two-step
CC reaction: valine is first activated by ATP to form Val-AMP and then
CC transferred to the acceptor end of tRNA(Val).
CC {ECO:0000256|ARBA:ARBA00043854}.
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: 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 AlphaFoldDB; A0A8D2J7J6; -.
DR Ensembl; ENSVKKT00000005692.1; ENSVKKP00000005537.1; ENSVKKG00000001562.1.
DR Proteomes; UP000694545; Unplaced.
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: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:000019; 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:000120; 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; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 2.
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 NCBIfam; NF004349; PRK05729.1; 1.
DR NCBIfam; TIGR00422; valS; 1.
DR PANTHER; PTHR11946:SF71; VALINE--TRNA LIGASE, MITOCHONDRIAL; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
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:UP000694545};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 81..700
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 745..894
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 980 AA; 110445 MW; 5F2BB47DFE05ACBC CRC64;
MGKINSLPLP DPHLSSKSRK RSSHQAPHFV PISEACAQPP LKKVPRPLQR KLQLQPCMAA
GHDTSRPLPT SYSPRYVEAA WYTWWMKEGF FKPEYQHQVP HWKPETFSLS IPPPNVTGSL
HLGHALTVAI EDALVRWKRM QGYKVLWVPG SDHAGIATQA VVERKIWKER GVLRQQLSRE
EFLQEVWTWK EEKGNEIFQQ LKVMGASLDW DRVCFTMDSG FSQAVTEAFV QLYEQGMIYR
DRRLVNWSCA LQSAISDIEV ENKHLKGRTE LSVPGVQGKV PFGVLVTFAY KVEGEEGVEL
PVATTRPETM LGDVAVAVHP EDPRYTHLHG KRLRHPFTGR LLPVITDPLV EQEMGTGAVK
VTPAHNYLDH EMACGHGLPC VSVIAEDGTM TSECGEWLQG LNRFLAREKV LAALKEKGLY
RGAREHPLVL PLCSRSGDVI EILLKSQWFL RCEEMAHKAL EAVESGCLKF TPRFQEKKWR
TWLLNIKDWC ISRQLWWGHQ IPAYRVSYGH ATEELWVVGR TEAEAQKKAV SMLGKSEEDL
ELVRDADVLD TWFSSGLFPF AALGWPHQTG DLQQFYPNSL LETGSDLLFF WVARMVMLGK
QLTGKLPFSQ VMLHSMVCDA HGRKMSKSLG NVIDPLDVVR GAPLQVLQEN LQKSNLDPRE
VAIAMEGQRR NFPQGIPECG ADALRFALCS YCAQGDSINL DVAAVENANR FCNKVWNALK
FTLAALGDGF APLDPEEVFP SSPMEKWILS HLYHTAEVCA QKFEEYELHS AASSVHLFWL
HNFCDVYLES VKPILRSGDP ARLLSTRHTL HSCVDLALRL LSPFMPFLSE ELWQRLPKIS
SQAPPSICVA RCPNTEHLAH WCHPEEEANF LLVQEVIRAV RALRATYQLT KARPAVYLVC
PEAAPLGVYE KYREPLQTLS LAGSLRFLPD SEAVQPPESC ITARTKYHTT VCVDLQVRAE
SGISGIKTGA WGKSGKMVTK
//
