SYV_THIDA
ID SYV_THIDA Reviewed; 912 AA.
AC Q3SL86;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=Tbd_0577;
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259;
RX PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ96530.1; -; Genomic_DNA.
DR RefSeq; WP_011311089.1; NC_007404.1.
DR AlphaFoldDB; Q3SL86; -.
DR SMR; Q3SL86; -.
DR STRING; 292415.Tbd_0577; -.
DR EnsemblBacteria; AAZ96530; AAZ96530; Tbd_0577.
DR KEGG; tbd:Tbd_0577; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_4; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000008291; 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; Reference proteome.
FT CHAIN 1..912
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224590"
FT COILED 847..911
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 44..54
FT /note="'HIGH' region"
FT MOTIF 523..527
FT /note="'KMSKS' region"
FT BINDING 526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 912 AA; 103003 MW; 0020868211E09154 CRC64;
MELAKSFEPA EIEKRWYARW ESAGYFKARD KPDAPAYCIM LPPPNVTGTL HMGHAFQHTL
MDALTRYHRM SGDNTLWQPG TDHAGIATQI VVERQLDAQN ISRHDLGREK FLEKVWEWKA
HSGSTITRQM RRLGTSPDWS RERFTMDAGL SKAVTEVFVR LYREGLIYRG KRLVNWDPVL
GTAVSDLEVV STEEDGFIWE INYPLEDGSG HLTVATTRPE TLLGDTAVAV HPEDERYAHL
IGKHVRLPIA ERSIPVIADE YVDREFGTGV VKITPAHDFN DWQVGQRHKL MAISVLTLDA
KMNELCPTEY QGLDRYDARQ TLLDALQAKG LLVSAKPHKL MIPRGDRTHA VLEPMLTDQW
FMSMEGLAKQ GLAAVDSGEL KFVPENWTTT YRQWLENIQD WCVSRQLWWG HRIPAWYDAD
GEFYVAHTEE EARKQAGGRE LTQDNDVLDT WFSSALWPFS TLGWPEQTPE LERYLPTSVL
VTGFDIIFFW VARMVMMSKH LTGKVPFREV YVTGLVRDSE GQKMSKSKGN VLDPIDLIDG
IAVGDLVAKR TQGLMNPKQA ASIEKRTRKE FPDGIAAYGT DALRFTFASL ATHGRDIKFD
LQRAEGYRNF CNKLWNATRF ALMNLEGHDC GQEADQPMDF SDADRWIAAR LQQAIGDVHE
AFAAYRFDQA ARAVYEFVWD EYCDWYLELA KVQLNHGTPE QQRATRRTLA TVLETTLRLA
HPIIPFITEE LWQKVAPLAG VHGDSIMLSA YPQVDEAQRH PGSVARMQLL KELVNACRTL
RGEMNLSPAQ RVPLVIEGDA AVINTLAPYM VALGKLGEVS AVTALPEADA PVALVGDMRM
MLVVEIDKDA ERARLAKEIA RIQGEIRKAE TKLANPSFVD KAPAAVVQQE QARLADFAAM
LQKLEAQHAR LG
