SYV_GEOSE
ID SYV_GEOSE Reviewed; 880 AA.
AC P11931;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Valine--tRNA ligase;
DE EC=6.1.1.9;
DE AltName: Full=Valyl-tRNA synthetase;
DE Short=ValRS;
GN Name=valS;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3300774; DOI=10.1021/bi00383a012;
RA Borgford T.J., Brand N.J., Gray T.E., Fersht A.R.;
RT "The valyl-tRNA synthetase from Bacillus stearothermophilus has
RT considerable sequence homology with the isoleucyl-tRNA synthetase from
RT Escherichia coli.";
RL Biochemistry 26:2480-2486(1987).
RN [2]
RP EDITING ACTIVITY.
RX PubMed=182209; DOI=10.1021/bi00660a026;
RA Fersht A.R., Kaethner M.M.;
RT "Enzyme hyperspecificity. Rejection of threonine by the valyl-tRNA
RT synthetase by misacylation and hydrolytic editing.";
RL Biochemistry 15:3342-3346(1976).
RN [3]
RP KINETIC PARAMETERS, AND MUTAGENESIS OF PRO-47; GLY-85 AND ASP-87.
RX PubMed=8611551; DOI=10.1021/bi960011y;
RA Lin L., Schimmel P.;
RT "Mutational analysis suggests the same design for editing activities of two
RT tRNA synthetases.";
RL Biochemistry 35:5596-5601(1996).
CC -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can
CC inadvertently accommodate and process structurally similar amino acids
CC such as threonine, to avoid such errors, it has a 'posttransfer'
CC editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-
CC dependent manner.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=59 uM for valine {ECO:0000269|PubMed:8611551};
CC KM=16 mM for threonine {ECO:0000269|PubMed:8611551};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: ValRS has two distinct active sites: one for aminoacylation and
CC one for editing. The misactivated threonine is translocated from the
CC active site to the editing site.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000305}.
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DR EMBL; M16318; AAA22879.1; -; Genomic_DNA.
DR PIR; A26738; SYBSVS.
DR AlphaFoldDB; P11931; -.
DR SMR; P11931; -.
DR SABIO-RK; P11931; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 1.10.287.380; -; 1.
DR Gene3D; 3.40.50.620; -; 3.
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; IPR019499; Val-tRNA_synth_tRNA-bd.
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 Pfam; PF10458; Val_tRNA-synt_C; 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 Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..880
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106213"
FT COILED 809..880
FT /evidence="ECO:0000255"
FT MOTIF 49..59
FT /note="'HIGH' region"
FT MOTIF 525..529
FT /note="'KMSKS' region"
FT BINDING 528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 47
FT /note="P->A: Has little effect on amino acid activation."
FT /evidence="ECO:0000269|PubMed:8611551"
FT MUTAGEN 47
FT /note="P->G: Strong decrease in amino acid activation."
FT /evidence="ECO:0000269|PubMed:8611551"
FT MUTAGEN 47
FT /note="P->I: Strong decrease in amino acid activation. No
FT effect on posttransfer editing activity."
FT /evidence="ECO:0000269|PubMed:8611551"
FT MUTAGEN 85
FT /note="G->R: Strong decrease in amino acid activation."
FT /evidence="ECO:0000269|PubMed:8611551"
FT MUTAGEN 87
FT /note="D->A: Strong decrease in amino acid activation. No
FT effect on posttransfer editing activity."
FT /evidence="ECO:0000269|PubMed:8611551"
SQ SEQUENCE 880 AA; 102048 MW; 462B0AE4E38B87A2 CRC64;
MAQHEVSMPP KYDHRAVEAG RYEWWLKGKF FEATGDPNKR PFTIVIPPPN VTGKLHLGHA
WDTTLQDIIT RMKRMQGYDV LWLPGMDHAG IATQAKVEEK LRQQGLSRYD LGREKFLEET
WKWKEEYAGH IRSQWAKLGL GLDYTRERFT LDEGLSKAVR EVFVSLYRKG LIYRGEYIIN
WDPVTKTALS DIEVVYKEVK GALYHMRYPL ADGSGFIEVA TTRPETMLGD TAVAVHPDDE
RYKHLIGKMV KLPIVGREIP IIADEYVDME FGSGAVKITP AHDPNDFEIG NRHNLPRILV
MNEDGTMNEN AMQYQGLDRF ECRKQIVRDL QEQGVLFKIE EHVHSVGHSE RSGAVIEPYL
STQWFVKMKP LAEAAIKLQQ TDGKVQFVPE RFEKTYLHWL ENIRHWCISR QLWWGHRIPA
WYHKETGEIY VDHEPPKDIE NWEQDPDVLD TWFSSALWPF STMGWPDTDS PDYKRYYPTD
VLVTGYDIIF FWVSRMIFQG LEFTGKRPFK DVLIHGLVRD AQGRKMSKSL GNGVDPMDVI
DQYGADALRY FLATGSSPGQ DLRFSTEKVE ATWNFANKIW NASRFALMNM GGMTYEELDL
SGEKTVADHW ILTRLNETIE TVTKLAEKYE FGERGRTLYN FIWDDLCDWY IEMAKLPLYG
DDEAAKKTTR SVLAYVLDNT MRLLHPFMPF ITEEIWQNLP HEGESITVAP WPQVRPELSN
EEAAEEMRML VDIIRAVRNV RAEVNTPPSK PIALYIKTKD EHVRAALLKN RAYLERFCNP
SELLIDTNVP APDKAMTAVV TGAELIMPLE GLINIEEEIK RLEKELDKWN KEVERVEKKL
ANEGFLAKAP AHVVEEERRK RQDYIEKREA VKARLAELKR
