ID A0A673YMP9_SALTR Unreviewed; 1010 AA.
AC A0A673YMP9;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
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=vars2 {ECO:0000313|Ensembl:ENSSTUP00000035918.1};
OS Salmo trutta (Brown trout).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000035918.1, ECO:0000313|Proteomes:UP000472277};
RN [1] {ECO:0000313|Ensembl:ENSSTUP00000035918.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSSTUP00000035918.1}
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; A0A673YMP9; -.
DR Ensembl; ENSSTUT00000037546.1; ENSSTUP00000035918.1; ENSSTUG00000014912.1.
DR GeneTree; ENSGT00940000159890; -.
DR Proteomes; UP000472277; Chromosome 34.
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: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:000120; 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 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000472277};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 40..661
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 707..862
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 975..1002
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1010 AA; 114253 MW; CC51054C166EB078 CRC64;
MKWSEKERIA YSVSTPPGEK KDTTVPFPSS YSPEYVETSW YQWWEKEGFF TPEINDRLPH
AVNHSFSMCI PPPNVTGTLH LGHALTVAIE DALVRWRRMQ GYKVLWVPGC DHAGIATQTV
VERRLFRERG KRRQDLSRED FLKEVWTWKK EKGEEIYHQL RELGASLDWS RACFTMDPGF
SSAVTEAFVR LCDSGLIYRS EGLVNWSCAL ESAISDIEVD SMQLSGRTLL PVPGYQNRVE
FGTMVTFSYP IDGQDGEVAV STTRPETMLG DVAIAVHPED PRYQAIHGKQ CRHPFSDRLL
PIITDTVVDM ELGTGAVKVT PAHDHTDFLL SQRHSLPRLT VIGGDGTMTP LCGQWLEGVK
RFDAREQVMD ALTEKMLFRG KRDHAMSLPV CSRSGDVIEP MVKKQWFVRC GEMAQRAIQA
VDEGQLEIIP HFYTKTWSSW LSNISDWCIS RQLWWGHQIP AYRVTLPDST DTQEEVWVWG
RSEEEARERA AGKYGVAADT ITLTQDPDVL DTWFSSGLFP FAMLGWPQQT SDLRQFYPNT
ILETGSDLIF FWVARMVMLG TELTGQLPFK QVLLHSLVRD KHGRKMSKSL GNVIDPLDVI
SGISLERLQE KVKEGNLDPR ESMVAMEAQR KDFPKGIPEC GTDALRFALC SYKAQGEDIS
LSVSQVLSCR HFCNKMWQTV RFTLGVLEDR GAELGTLEQT SPLNSMDQWV CSRLYSTVLQ
CEQGFERYEL HSVTAALHSF WLHSLCDIYL ECIKPVLSQD SGSQREKQVV RAVLYHCVCV
SLALLSPFMP FLTEELWQRL YLLRGEGGGR SVASLCLQPY PQSSQLAHWH FPQEEADFTL
VQEVVRVARS LRAQCGMTKE KPDMWAVCSP SQAQILLHFG PAVRTLGRIT KLHLHCPQGA
GSLSFPSAPP PPKGSAVGVV DHSCQLHLNV QGGVNVSKLS LQLCQRREKL LSKLEQSLSR
TRLPNYLEKV PERVRVETEN KISALEQELR NIEEQLSALQ GPPKHNSGQK
//
