SYV_BLOFL
ID SYV_BLOFL Reviewed; 966 AA.
AC Q7VQT2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=Bfl033;
OS Blochmannia floridanus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX NCBI_TaxID=203907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA van Ham R.C.H.J., Gross R., Moya A.;
RT "The genome sequence of Blochmannia floridanus: comparative analysis of
RT reduced genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
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; BX248583; CAD83561.1; -; Genomic_DNA.
DR RefSeq; WP_011126331.1; NC_005061.1.
DR AlphaFoldDB; Q7VQT2; -.
DR SMR; Q7VQT2; -.
DR STRING; 203907.Bfl033; -.
DR EnsemblBacteria; CAD83561; CAD83561; Bfl033.
DR KEGG; bfl:Bfl033; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; RQWYIRN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002192; 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; 3.40.50.620; -; 2.
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; IPR009080; tRNAsynth_Ia_anticodon-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 PRINTS; PR00986; TRNASYNTHVAL.
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..966
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224443"
FT COILED 348..368
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT COILED 939..960
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT MOTIF 566..570
FT /note="'KMSKS' region"
FT BINDING 569
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 966 AA; 114272 MW; 649F3DABD2516445 CRC64;
MIINTIDKIY NPKNIEESIY NFWEKSNYFE PDIINNYKKN YCIMMPPPNI TGGLHLGHAF
QQTIMDILVR YQRMNGKNVL WASGLDHAGI ATQILIEKNF YNKKNSIKDN HDPHSLIKEV
WLWKEKSEKF INYQIKRLGH SVSWKNKHFT MDPEISLAVK EAFIQLYTNN LIYKGKQLVN
WDSKLQTAIS DLEVSHKQKS DFIWYIQYQL EYNTSHINNQ KKNADYLTIA TTRPETILGD
VAIAVNPEDP RYSHLIGKYV FTPITNRRIP IISDKFVNIN KGTGCVKITP AHDFNDYIIG
KKYKLPMINI FSTYKTILTI PEISNNQGQP YIQSNDQYHI PKMFHNLDYK DARKKIIEEC
KRLKILEDIK THQLTVPINN RTGTIIEPML TDQWFIKTKF LAKQAINAVT NEKIKFIPKN
YTNIYLQWMN EIQDWCISRQ IWWGHRIPVW YDNNNTIYVG HCEKDIRIKN QLNKDIQLSQ
DNNVLDTWFS SSLWTFSSLG WPKNNTLLKM FHPTNIIISG FDIIFFWIAR MIMMTMYLVK
DQNNNAQIPF KKIYITGLMR DKFGQKMSKS KGNGIDPIDI IDGISKKKLL KKQLKENSQS
KSISSIIKYI NTQFPNGIKP YGADTLRLTL TALASSGQDI HWDMHKLESY HNFCNKLWNV
SKFVITHTDN YHYDIDTKNK KIFSLSDRWI TSKLHQTIQK FSQALNDYRF DHTVNILYEF
IWHQFCDWYI EFTKPILYHS TNTLQLISTR YTLITSLESI LRLSHPIIPF ITEKIWQKIH
SIVTTNNKHT IMLQSFPKYD SNYIDLESIS DIEWIQNLIA EIRMIRTYTG ISYKIPLDIG
FYNTSNHIKE CISENYHILT KILQLQTINF LEKNDISNNR YFKIPIKESE LIIFIPNIFD
KKTAIHKFNK EIKLINYKIH LLEQKMNNTN YSLNLQHSFK KSQEKLNHYN KTKNKLLNQY
FIVKNL
