SYVC_RAT
ID SYVC_RAT Reviewed; 1264 AA.
AC Q04462; Q6MG65;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Valine--tRNA ligase {ECO:0000305};
DE EC=6.1.1.9 {ECO:0000269|PubMed:8428657};
DE AltName: Full=Valyl-tRNA synthetase;
DE Short=ValRS;
GN Name=Vars1; Synonyms=Vars, 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 498-1091.
RX PubMed=8428657; DOI=10.1016/0378-1119(93)90122-j;
RA Vilalta A., Donovan D., Wood L., Vogeli G., Yang D.C.H.;
RT "Cloning, sequencing and expression of a cDNA encoding mammalian valyl-tRNA
RT synthetase.";
RL Gene 123:181-186(1993).
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:0000269|PubMed:8428657};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10705;
CC Evidence={ECO:0000305|PubMed:8428657};
CC -!- ACTIVITY REGULATION: Can be regulated by protein kinase C-dependent
CC phosphorylation.
CC -!- SUBUNIT: Forms high-molecular-mass aggregates with elongation factor 1.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; BX883045; CAE83981.1; -; Genomic_DNA.
DR EMBL; M98327; AAA42320.1; -; mRNA.
DR PIR; PN0473; PN0473.
DR RefSeq; NP_445744.1; NM_053292.1.
DR RefSeq; XP_006256109.1; XM_006256047.3.
DR AlphaFoldDB; Q04462; -.
DR SMR; Q04462; -.
DR BioGRID; 247092; 3.
DR IntAct; Q04462; 6.
DR MINT; Q04462; -.
DR STRING; 10116.ENSRNOP00000001160; -.
DR iPTMnet; Q04462; -.
DR PhosphoSitePlus; Q04462; -.
DR SwissPalm; Q04462; -.
DR jPOST; Q04462; -.
DR PaxDb; Q04462; -.
DR PRIDE; Q04462; -.
DR Ensembl; ENSRNOT00000001160; ENSRNOP00000001160; ENSRNOG00000000867.
DR GeneID; 25009; -.
DR KEGG; rno:25009; -.
DR UCSC; RGD:3950; rat.
DR CTD; 7407; -.
DR RGD; 3950; Vars.
DR eggNOG; KOG0432; Eukaryota.
DR eggNOG; KOG0867; Eukaryota.
DR GeneTree; ENSGT00940000157775; -.
DR InParanoid; Q04462; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 229591at2759; -.
DR PhylomeDB; Q04462; -.
DR TreeFam; TF300648; -.
DR PRO; PR:Q04462; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000867; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; Q04462; baseline and differential.
DR Genevisible; Q04462; RN.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IDA:RGD.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 1.10.287.380; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 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; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004046; GST_C.
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; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR PANTHER; PTHR11946; PTHR11946; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00422; valS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P26640"
FT CHAIN 2..1264
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106255"
FT DOMAIN 89..219
FT /note="GST C-terminal"
FT REGION 218..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 344..354
FT /note="'HIGH' region"
FT MOTIF 862..866
FT /note="'KMSKS' region"
FT COMPBIAS 233..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 865
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P26640"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26640"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26640"
FT MOD_RES 645
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26640"
FT CONFLICT 498..500
FT /note="RTL -> EFR (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="Y -> C (in Ref. 2; AAA42320)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="I -> V (in Ref. 2; AAA42320)"
FT /evidence="ECO:0000305"
FT CONFLICT 842
FT /note="E -> G (in Ref. 2; AAA42320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1056..1057
FT /note="GL -> AV (in Ref. 2; AAA42320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1089..1091
FT /note="TPY -> RNS (in Ref. 2; AAA42320)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1264 AA; 140368 MW; 11DE06D1D04FAE00 CRC64;
MSILYVSPHP DAFPSLRALI AARYGEAGDG PGWGGPHPRI CLQPPPSSRT PFPPPRLPAL
EQGPGGLWVW GAPAVAQLLW PAGLGGPGGS RAAVLVQQWV SYADTELTPA ACGATLPALG
LRGPGQDPQA ALGALGKALN PLEEWLRLHT YLAGDAPTLA DLAAVTALLL PFRYVLDPSA
RRIWGNVTRW FNTCVRQPEF RAVLGEVVLY SGARSVTQQP GSEITAPQKT AAQLKKEAKK
REKLEKFQQK QKTQQQQPAH GEKKPKPEKK EKRDPGVITY DLPTPPGEKK DVSGTMPDSY
SPQYVEAAWY PWWERQGFFK PEYGRPSVSA PNPRGVFMMC IPPPNVTGSL HLGHALTNAI
QDSLTRWHRM RGETTLWNPG CDHAGIATQV VVEKKLWKER GLNRHQLGRE AFLQEVWKWK
AEKGDRIYHQ LKKLGSSLDW DRACFTMDPK LSATVTEAFV RLHEEGVIYR STRLVNWSCT
LNSAISDIEV DKKELTGRTL LSVPGYKEKV EFGVLVSFAY KVQGSDSDEE VVVATTRIET
MLGDVAVAVH PKDPRYQHLK GKSVVHPFLS RSLPIVFDDF VDMEFGTGAV KITPAHDQND
YEVGQRHRLE AISIMDSKGA LVNVPPPFLG LPRFEARKAV LAALKEQGLF RGIKDNPMVV
PLCNRSKDVV EPLLRPQWYV RCGEMAQAAS AAVTRGDLRI LPEAHQRTWH SWMDNIRDWC
ISRQLWWGHR IPAYFITVHD PAVPPGEDPD GRYWVSGRTE AEAREKAARE FGVSPDKISL
QQDEDVLDTW FSSGLFPFSI FGWPNQSEDL SVFYPGTLLE TGHDILFFWV ARMVMLGLKL
TEKLPFREVY LHAIVRDAHG RKMSKSLGNV IDPLDVIHGV SLQGLHDQLL NSNLDPSEVE
KAKEGQRADF PAGIPECGTD ALRFGLCAYT SQGRDINLDV NRILGYRHFC NKLWNATKFA
LRGLGKGFVP SPTSKPEGHE SLVDRWIRSR LAEAVRLSNE GFQAYDFPAV TTAQYSFWLY
ELCDVYLECL KPVLNGVDQV AADCARQTLY TCLDVGLRLL SPFMPFVTEE LFQRLPRRTP
NAPASLCVTP YPEPSECSWK DPEAEAALEL ALSITRAVRS LRADYNLTRT RPDCFLEVAD
EATGALASAV SAYVQTLASA GVVAVLALGA PAPQGCAVAV ASDRCSIHLQ LQGLVDPARE
LGKLQAKRSE AQRQAQRLQE RRAASGYSAK VPLEVQEADE VKLQQTEAEL RKVDEAIALF
QKML
