SYV_BUCAP
ID SYV_BUCAP Reviewed; 960 AA.
AC Q8K9I1;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=BUsg_354;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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; AE013218; AAM67907.1; -; Genomic_DNA.
DR RefSeq; WP_011053874.1; NC_004061.1.
DR AlphaFoldDB; Q8K9I1; -.
DR SMR; Q8K9I1; -.
DR STRING; 198804.BUsg_354; -.
DR EnsemblBacteria; AAM67907; AAM67907; BUsg_354.
DR KEGG; bas:BUsg_354; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000416; 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..960
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106217"
FT COILED 879..950
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 553..557
FT /note="'KMSKS' region"
FT BINDING 556
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 960 AA; 113269 MW; 8D0CB9C4D5B8B8DF CRC64;
MKKNYNPKDI EEHLYNFWEK NGFFKPNNNL NKPAFCIMMP PPNITGNLHM GHAFQQTIMD
ILIRYNRMQG KNTLWQVGTD HAGIATQILI ERQIFSEERK TKKDYSRNDF IKKIWKWKKK
SNFSVKKQMK RLGNSVDWDR EKFTLDPDIS NSVKEAFIIL YKNNLIYQKK RLVHWDSKLE
TVISDLEVEH RLIKSKKWFI RYPIIKNIKN INIEYLLVAT TRPETLLGDT ALAINPKDDK
YNHLIGQSVI CPIVNRIIPI IADHYADMNK DTGCVKITPG HDFNDYEVGQ RHKLPMINIF
TFNGKIKSNF SIYDYQGSKS NFYDSSIPTE FQNLDILSAR KKIIYEIEKL GLLEKIEECN
FFTPYSERSG VIIQPMLTNQ WYLKTSHLSQ SAIDVVREKK IKFIPNQYKS MYLSWMNNIE
DWCISRQLWW GHQIPVWYDD KKNIYVGHSE KKIREEYNIS DDMILNQDND VLDTWFSSGL
WTFSTLGWPE KTEFLKIFHS TDVLVSGFDI IFFWIARMIM LTMYLVKDSY GNPQIPFKDV
YITGLIRDEE GKKMSKSKGN VIDPIDMIDG ISLNELIEKR TSNLLQPHLS QKIRYHTIKQ
FPNGISATGT DALRFTFSAL ASNTRDIQWD MNRLKGYRNF CNKLWNASRF VLKNTKDHDY
FNFSVNDNML LINKWILIKF NNTVKSYRNS LDSYRFDIAA NILYDFIWNV FCDWYLEFVK
SVIKSGSYQD IYFTKNVLIH VLELLLRLSH PIMPFITEAI WQRVKIIKHI KDRTIMLQSF
PEYNDQLFDK STLSNINWIK KIIIFIRNTR SKMNISSTKL LSLFLKNINS EKKKVIQENK
FILKNIASLE KISILSKQDD EPCLSLKEII DGVDILVPVL KAIDKEIELK RLNKEIEKIK
SKMLISEKKM SNQDFLSYAP KNIIDKEIKK LKSLNEIYLT LSQQLESLHD AFCKKNKIFN
