ID D0IDR0_9VIBR Unreviewed; 953 AA.
AC D0IDR0;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
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 ORFNames=VOA_003346 {ECO:0000313|EMBL:EEZ00897.1};
OS Vibrio sp. RC586.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=675815 {ECO:0000313|EMBL:EEZ00897.1, ECO:0000313|Proteomes:UP000006226};
RN [1] {ECO:0000313|EMBL:EEZ00897.1, ECO:0000313|Proteomes:UP000006226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RC586 {ECO:0000313|EMBL:EEZ00897.1,
RC ECO:0000313|Proteomes:UP000006226};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Chertkov O., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C.,
RA Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A.,
RA Bartels D., Vonstein V.;
RL Submitted (NOV-2009) 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; ADBD01000005; EEZ00897.1; -; Genomic_DNA.
DR RefSeq; WP_000416443.1; NZ_ADBD01000005.1.
DR AlphaFoldDB; D0IDR0; -.
DR GeneID; 58290658; -.
DR eggNOG; COG0525; Bacteria.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000006226; Unassembled WGS sequence.
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}.
FT DOMAIN 14..631
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 675..827
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 888..947
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 884..946
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 554..558
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 557
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 953 AA; 108160 MW; 3AFF7ABD4F827D1D CRC64;
MEKTYNPTSI EQDLYKTWEE QGYFKPHGDT SKDAYSIMIP PPNVTGSLHM GHAFQDTIMD
TLIRCQRMKG KNTLWQVGTD HAGIATQMVV ERKIAAEEGK TKHDYGRDAF IDKIWEWKAE
SGGTITKQLR RLGASVDWDR ERFTMDDGFY KAVQEVFVRL YKDDLIYRGK RLVNWDPKLH
TAISDLEVEN KETKGHMWHF RYPLADGVKT ADGKDYIVVA TTRPETMLGD TGVAVNPEDP
RYKDLIGKEI ILPIVGRRIP IVGDEHADME KGTGCVKITP AHDFNDYEVG KRHNLPMINI
LTFDANIRDA AEVFNSNGEA SNAYGTEIPA KYQGMERFAA RKAIVAEFEE LGLLQEIKDH
DLTVPYGDRG GVVIEPMLTD QWYVRAGILA KPAVEAVENG DIQFVPKQYE NMYFSWMRDI
QDWCISRQLW WGHRIPAWYD EQGNVFVGRN EEEVRAENNI AADVALRQDD DVLDTWFSSA
LWTFGTLGWP EKTPELKVFH PTDVLVTGFD IIFFWVARMI MMTMHFCKDE DGKAQVPFKT
VYVTGLIRDE NGDKMSKSKG NVLDPIDMID GIDLESLVAK RTGNMMQPQL AAKIEKNTRK
TFENGIEAYG TDSLRFTLAA MASTGRDINW DMKRLEGYRN FCNKLWNASR YVLMNTEEQD
CGFAAGAELE YSLADKWIES QFELAAKEFN GHIDNFRLDM AANTLYEFIW NQFCDWYLEL
TKPVLWKGTE AQQRATRRTL ITVLEKTLRL AHPVIPYITE TIWQSVKPLV DGVEGDTIML
QALPQYDAAN FNQEALDDIE WVKAFITSIR NLRAEYDINP GKPLEVMLKA ANEQDAARIE
ANKQVLVSLA KLESIRVLAD GEATPACATA LVGKSELMIP MAGLIDKDAE LDRLAKEIAK
TQGEIARIEG KLGNEGFVAK APEAVITKER EKLAGYQEAL VKLEQQKATI AAL
//
