ID SYVM_RAT Reviewed; 1065 AA.
AC Q6MG21;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 121.
DE RecName: Full=Valine--tRNA ligase, mitochondrial;
DE EC=6.1.1.9 {ECO:0000250|UniProtKB:Q5ST30};
DE AltName: Full=Valyl-tRNA synthetase;
DE Short=ValRS;
DE Flags: Precursor;
GN Name=Vars2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
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:0000250|UniProtKB:Q5ST30}.
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:0000250|UniProtKB:Q5ST30};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; BX883047; CAE84026.1; -; Genomic_DNA.
DR RefSeq; NP_998728.1; NM_213563.1.
DR AlphaFoldDB; Q6MG21; -.
DR SMR; Q6MG21; -.
DR STRING; 10116.ENSRNOP00000046565; -.
DR CarbonylDB; Q6MG21; -.
DR PhosphoSitePlus; Q6MG21; -.
DR PaxDb; 10116-ENSRNOP00000046565; -.
DR GeneID; 309596; -.
DR KEGG; rno:309596; -.
DR UCSC; RGD:1303122; rat.
DR AGR; RGD:1303122; -.
DR CTD; 57176; -.
DR RGD; 1303122; Vars2.
DR eggNOG; KOG0432; Eukaryota.
DR HOGENOM; CLU_001493_0_1_1; -.
DR InParanoid; Q6MG21; -.
DR OrthoDB; 5473263at2759; -.
DR PhylomeDB; Q6MG21; -.
DR TreeFam; TF354250; -.
DR PRO; PR:Q6MG21; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
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; 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; 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; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..15
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 16..1065
FT /note="Valine--tRNA ligase, mitochondrial"
FT /id="PRO_0000338004"
FT REGION 27..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 146..156
FT /note="'HIGH' region"
FT MOTIF 659..663
FT /note="'KMSKS' region"
FT COMPBIAS 38..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 662
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1065 AA; 118894 MW; 4BF57C6962DA50CC CRC64;
MPHLPLASFR PPLWGLRPSW GLARPRALCT QPEPHGSPVS RRNREAKQKR LREKQAALEA
GLAEKSKTPA VPTKAWSHKE VVLYEIPTRP GEKKDVSGPL PPAYSPQYVE AAWYQWWVRE
GFFKPEYQAR LPQATGETFS MCIPPPNVTG SLHIGHALTV AIQDAFVRWH RMRGDRVLWI
PGSDHAGIAT QAVVEKQLWR ERRVRRHELS REDFLRAVWQ WKQEKGGEIY EQLCALGASL
DWDRECFTMD AGSSAAVTEA FVRLYDLGLL YRNRQLVNWS CTLRSAISDI EVESRPLPGR
TVLRLPGCPI PVSFGLLVSI AFPVDGDPGT EIVVGTTRPE TLPGDVAVAV HPDDPRYTHL
HGRQLRHPLT GQHLPLITDT TVQPHVGTGA VKVTPAHSPA DAEMGTRHGL TPLSVIAEDG
TMTSLCGDWL QGLHRFVARE KIMCTLRERG LFRGLQEHPM VLPICSRSGD VVEYLLKSQW
FVRCQEMGDR AAKAVESGAL ELWPSFHQKS WQHWFAHIGD WCVSRQLWWG HQIPAYRVGG
EKAEDDREEC WVVGRSEAEA RAAAAKQTGR PEAELTLERD PDVLDTWFSS ALFPFSALGW
PQETPDLARF YPLTLLETGS DLLTFWVGRM VMLGTQLTGQ LPFSKVLLHS MVRDRQGRKM
SKSLGNVLDP RDIISGQELQ VLQAKLRDGN LDQGELAVAA AAQKKDFPYG IPECGTDALR
FALCSHGILG GDLHLSVSEV LNYRHFCNKL WNALRFILRA LGDDFVPQPA EKVTPSSPMD
AWILSRLAFA ANECERGFLS RELSLVTHTL YHFWLHNLCD VYLEAVKPVL SSAPCPPGPP
QVLFSCADVG LRLLAPLMPF LAEELWQRLP PRQGGSMAPS ICVAPYPSGH SLVSRGQESW
RQPELEHCFS RVQEIVQALR ALRATYQLTR ARPHVLLQSS DPGEQGLVQP FLEPLGVLSH
CGAVGFLPPG AAAPSGWALA PLGDTIKIYM ELQGLVDPQS QLPRLAARRQ KLQKQLDDLL
NRTVSDGPAE RQQRISSLQL ELSKLDQAAS HLQQLMEEAP DAREL
//
