SYV_PSEU2
ID SYV_PSEU2 Reviewed; 948 AA.
AC Q4ZXI0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02004}; OrderedLocusNames=Psyr_1086;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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. {ECO:0000255|HAMAP-Rule:MF_02004}.
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:0000255|HAMAP-Rule:MF_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}.
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. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
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DR EMBL; CP000075; AAY36142.1; -; Genomic_DNA.
DR RefSeq; WP_011266818.1; NC_007005.1.
DR RefSeq; YP_234180.1; NC_007005.1.
DR AlphaFoldDB; Q4ZXI0; -.
DR SMR; Q4ZXI0; -.
DR STRING; 205918.Psyr_1086; -.
DR EnsemblBacteria; AAY36142; AAY36142; Psyr_1086.
DR KEGG; psb:Psyr_1086; -.
DR PATRIC; fig|205918.7.peg.1118; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000000426; Chromosome.
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; -; 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; 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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..948
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224539"
FT COILED 879..945
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 40..50
FT /note="'HIGH' region"
FT MOTIF 551..555
FT /note="'KMSKS' region"
FT BINDING 554
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 948 AA; 107039 MW; 9BDBEA6F74D0DC0D CRC64;
MDKTYQPHAI ETSWYQTWES ENYFAPQGVG DSYTIMIPPP NVTGSLHMGH GFNNAIMDAL
IRFRRMQGRN TLWQPGTDHA GIATQMLVER RLEAQGVSRH ELGREKFLDK IWEWKAESGG
NISRQIRRLG SSVDWSRERF TMDDGLSEAV KEAFVRLHED GLIYRGKRLV NWDTKLHTAI
SDLEVENHDE KGHLWNLRYP LADGAKTAEG LDYLIVATTR PETMLGDAAV AVNPEDERYK
ALIGKFVELP LVGRRIPIIA DDYCDPEFGT GCVKITPAHD FNDYEVGKRH NLPLLNIFDK
NANVLPAAQV FNLDGTLNES VDGSLPAAYA GLDRFEARKQ IVAAFDAAGL LVSVDDHALK
VPKGDRSGTI IEPWLTDQWY VSTKPLAEPA IAAVEDGRIA FVPKQYENMY FSWMRDIQDW
CISRQLWWGH RIPAWYDESG KVYVGRDEAE VRAKNNLGPE VALQQDNDVL DTWFSSGLWT
FSTLGWPEKT KALKTFHSTD VLVTGFDIIF FWVARMIMLT MHLVKNEDGT PQVPFKTVYV
HGLVRDGQGQ KMSKSKGNVL DPLDIVDGID LETLVEKRTS GLMQPQLAKK IEKQTRQEFA
DGIASYGTDA LRFTFCSLAS TGRDIKFDMG RVEGYRNFCN KIWNAARYVL DKGEDCGQNG
EAVELSLADR WIISQLQRTE AEVTRQLDQF RFDLAAQALY EFIWNQYCDW YLELSKPVLW
DETAPVERQR GTRRTLVRVL EVALRLAHPF MPFITEEIWQ RLAPLAGAQG KTIMLQPWPV
ANEARIDQAA EDDIEWLKGL MLAVRNIRGE MNIGPGKPLQ LFLKNVSAED QRRLSENDYL
LKKLAKLESM TVLTEGAEAP LSATALVGDM EVLVPMAGLI DKGAELARLD KEIQRLQGEV
QRVGGKLSNA AFVDKAPPEV IAKERAKLTE AEQALGKLAE QHARIASL
