ID A0A157SUU0_9BORD Unreviewed; 959 AA.
AC A0A157SUU0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02004};
DE EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02004};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02004};
DE Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02004};
GN Name=valS {ECO:0000256|HAMAP-Rule:MF_02004,
GN ECO:0000313|EMBL:SAI74104.1};
GN ORFNames=SAMEA3906487_04034 {ECO:0000313|EMBL:SAI74104.1};
OS Bordetella trematum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=123899 {ECO:0000313|EMBL:SAI74104.1, ECO:0000313|Proteomes:UP000076825};
RN [1] {ECO:0000313|EMBL:SAI74104.1, ECO:0000313|Proteomes:UP000076825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H044680328 {ECO:0000313|EMBL:SAI74104.1,
RC ECO:0000313|Proteomes:UP000076825};
RG Pathogen Informatics;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00001624, ECO:0000256|HAMAP-
CC Rule:MF_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000256|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:0000256|HAMAP-Rule:MF_02004}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02004}.
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DR EMBL; LT546645; SAI74104.1; -; Genomic_DNA.
DR RefSeq; WP_025512590.1; NZ_UFUJ01000001.1.
DR AlphaFoldDB; A0A157SUU0; -.
DR STRING; 123899.SAMEA3906487_04034; -.
DR GeneID; 56588749; -.
DR KEGG; btrm:SAMEA390648704034; -.
DR PATRIC; fig|123899.6.peg.4030; -.
DR eggNOG; COG0525; Bacteria.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000076825; Chromosome 1.
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 CDD; cd00817; ValRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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 NCBIfam; TIGR00422; valS; 1.
DR PANTHER; PTHR11946:SF93; VALINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 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; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF46589; tRNA-binding arm; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02004};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02004}; Coiled coil {ECO:0000256|HAMAP-Rule:MF_02004};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02004};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02004};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02004};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02004}; Reference proteome {ECO:0000313|Proteomes:UP000076825}.
FT DOMAIN 27..644
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 686..839
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 893..957
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT MOTIF 59..69
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 567..571
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 570
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 959 AA; 107960 MW; 5ACCFF1D8B068E63 CRC64;
MTQAADPKND SPELSKSFEP SDIESRWYDV WNQRGYFQAG RHVETGTEGK PYCIQFPPPN
VTGTLHMGHA FNQTIMDGLI RYRRMSGDDT VFIPGTDHAG IATQIVVERQ LDAQKLSRHD
LGRERFIEKV WSWKEQSGNT ITSQVRRLGA SADWPREYFT MDERMSRGVL ETFVELYRQG
LIYRGKRLVN WDPKLLTAVS DLEVQSEETD GHMWHILYPF VDGPQTITDK DGNTVTLRGL
TIATTRPETM LADGALCVHP EDPRYQHLVG KLVELPLCDR NIPIIADDFV DPEFGTGCVK
ITGAHDFNDY ACAMRHNLPL IVIFTLDAHI NDNGPEQFRG LERYEARKAV VAQLEAEGYL
VKVEPHRMMQ PKGDRTGVVL EPMLTDQWFV AMSKPAPEGT RNPGKSITEV ALQAVADGSI
QFYPENWTTI YNQWLNNIQD WCISRQLWWG HQIPAWYAED GQCFVAHSEQ EALEQARAAG
VQGPLKRDPD VLDTWFSSAL VPFTTLGWPE KTEDLARYLP SSVLVTGFDI IFFWVARMVM
LTMHMTGKIP FKHVYVHGLI LDAEGQKMSK SKGNTLDPVD LIDGIDLEKL VAKRTYGLMN
PKQAGAIEKA TRRQFPDGIP AFGTDALRFT MAAYATLGRN MNFDLKRCEG YRNFCNKLWN
ATRFVLMNTE GHALHGEETG ELSFADRWIV SQLQTLESDI ERGFADYRFD NVANALYRYV
WDEYCDWYVE LAKVQIQTGT PAQQLGTRRT LIRVLEAVLR LAHPIIPFIT EELWQKVSVV
AGKRRADEPG SVSVQPYPRA NPEAVDAQAE AAVAELKAQV EAVRALRGEM NLSPAQRVPL
IAQGDATMLK RNAPYLAALA KLSQVDVADT LPDAGAPVQV VGDARLMLHV EIDVAAECAR
LDKEIARLEG EIAKANGKLS NPSFVERAPA AVVQQEQARV GQFNETLTKV REQRSKLSR
//
