SYV_YEAST
ID SYV_YEAST Reviewed; 1104 AA.
AC P07806; D6VUM6;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Valine--tRNA ligase, mitochondrial;
DE EC=6.1.1.9;
DE AltName: Full=Valyl-tRNA synthetase;
DE Short=ValRS;
DE Flags: Precursor;
GN Name=VAS1; OrderedLocusNames=YGR094W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3294828; DOI=10.1016/s0021-9258(18)48222-1;
RA Jordana X., Chatton B., Paz-Weisshaar M., Buhler J.-M., Cramer F.,
RA Ebel J.-P., Fasiolo F.;
RT "Structure of the yeast valyl-tRNA synthetase gene (VASI) and the homology
RT of its translated amino acid sequence with Escherichia coli isoleucyl-tRNA
RT synthetase.";
RL J. Biol. Chem. 262:7189-7194(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-78.
RX PubMed=3275649; DOI=10.1016/s0021-9258(19)57354-9;
RA Chatton B., Walter P., Ebel J.-P., Lacroute F., Fasiolo F.;
RT "The yeast VAS1 gene encodes both mitochondrial and cytoplasmic valyl-tRNA
RT synthetases.";
RL J. Biol. Chem. 263:52-57(1988).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-294; SER-332; SER-707
RP AND THR-1003, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
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 -!- SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial;
CC IsoId=P07806-1; Sequence=Displayed;
CC Name=Cytoplasmic;
CC IsoId=P07806-2; Sequence=VSP_018910;
CC -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: [Isoform Cytoplasmic]: Produced by alternative
CC initiation at Met-47 of isoform Mitochondrial. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; J02719; AAA35207.1; -; Genomic_DNA.
DR EMBL; Z72879; CAA97097.1; -; Genomic_DNA.
DR EMBL; M18392; AAA35205.1; -; Genomic_DNA.
DR EMBL; M18392; AAA35206.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08187.1; -; Genomic_DNA.
DR PIR; S64389; SYBYVT.
DR RefSeq; NP_011608.1; NM_001181223.1. [P07806-1]
DR AlphaFoldDB; P07806; -.
DR SMR; P07806; -.
DR BioGRID; 33337; 89.
DR DIP; DIP-6328N; -.
DR IntAct; P07806; 18.
DR MINT; P07806; -.
DR STRING; 4932.YGR094W; -.
DR iPTMnet; P07806; -.
DR MaxQB; P07806; -.
DR PaxDb; P07806; -.
DR PRIDE; P07806; -.
DR EnsemblFungi; YGR094W_mRNA; YGR094W; YGR094W. [P07806-1]
DR GeneID; 852986; -.
DR KEGG; sce:YGR094W; -.
DR SGD; S000003326; VAS1.
DR VEuPathDB; FungiDB:YGR094W; -.
DR eggNOG; KOG0432; Eukaryota.
DR GeneTree; ENSGT00940000167981; -.
DR HOGENOM; CLU_001493_0_1_1; -.
DR InParanoid; P07806; -.
DR OMA; FATKLWN; -.
DR BioCyc; YEAST:G3O-30804-MON; -.
DR PRO; PR:P07806; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P07806; protein.
DR GO; GO:0005737; C:cytoplasm; IMP:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IMP:SGD.
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:SGD.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IDA:SGD.
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; 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 PANTHER; PTHR11946; PTHR11946; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF46589; SSF46589; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00422; valS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Ligase; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..47
FT /note="Mitochondrion"
FT CHAIN 48..1104
FT /note="Valine--tRNA ligase, mitochondrial"
FT /id="PRO_0000035839"
FT REGION 99..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 190..200
FT /note="'HIGH' region"
FT MOTIF 703..707
FT /note="'KMSKS' region"
FT BINDING 706
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 707
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1003
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT VAR_SEQ 1..46
FT /note="Missing (in isoform Cytoplasmic)"
FT /evidence="ECO:0000305"
FT /id="VSP_018910"
FT CONFLICT 147
FT /note="A -> G (in Ref. 1; AAA35207)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="R -> K (in Ref. 1; AAA35207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1104 AA; 125770 MW; 6493AEF37ECD4A7C CRC64;
MNKWLNTLSK TFTFRLLNCH YRRSLPLCQN FSLKKSLTHN QVRFFKMSDL DNLPPVDPKT
GEVIINPLKE DGSPKTPKEI EKEKKKAEKL LKFAAKQAKK NAAATTGASQ KKPKKKKEVE
PIPEFIDKTV PGEKKILVSL DDPALKAYNP ANVESSWYDW WIKTGVFEPE FTADGKVKPE
GVFCIPAPPP NVTGALHIGH ALTIAIQDSL IRYNRMKGKT VLFLPGFDHA GIATQSVVEK
QIWAKDRKTR HDYGREAFVG KVWEWKEEYH SRIKNQIQKL GASYDWSREA FTLSPELTKS
VEEAFVRLHD EGVIYRASRL VNWSVKLNTA ISNLEVENKD VKSRTLLSVP GYDEKVEFGV
LTSFAYPVIG SDEKLIIATT RPETIFGDTA VAVHPDDDRY KHLHGKFIQH PFLPRKIPII
TDKEAVDMEF GTGAVKITPA HDQNDYNTGK RHNLEFINIL TDDGLLNEEC GPEWQGMKRF
DARKKVIEQL KEKNLYVGQE DNEMTIPTCS RSGDIIEPLL KPQWWVSQSE MAKDAIKVVR
DGQITITPKS SEAEYFHWLG NIQDWCISRQ LWWGHRCPVY FINIEGEEHD RIDGDYWVAG
RSMEEAEKKA AAKYPNSKFT LEQDEDVLDT WFSSGLWPFS TLGWPEKTKD METFYPFSML
ETGWDILFFW VTRMILLGLK LTGSVPFKEV FCHSLVRDAQ GRKMSKSLGN VIDPLDVITG
IKLDDLHAKL LQGNLDPREV EKAKIGQKES YPNGIPQCGT DAMRFALCAY TTGGRDINLD
ILRVEGYRKF CNKIYQATKF ALMRLGDDYQ PPATEGLSGN ESLVEKWILH KLTETSKIVN
EALDKRDFLT STSSIYEFWY LICDVYIENS KYLIQEGSAI EKKSAKDTLY ILLDNALKLI
HPFMPFISEE MWQRLPKRST EKAASIVKAS YPVYVSEYDD VKSANAYDLV LNITKEARSL
LSEYNILKNG KVFVESNHEE YFKTAEDQKD SIVSLIKAID EVTVVRDASE IPEGCVLQSV
NPEVNVHLLV KGHVDIDAEI AKVQKKLEKA KKSKNGIEQT INSKDYETKA NTQAKEANKS
KLDNTVAEIE GLEATIENLK RLKL
