ID A0A238JQL6_9RHOB Unreviewed; 1052 AA.
AC A0A238JQL6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 18-JUN-2025, entry version 30.
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:SMX32978.1};
GN ORFNames=COL8621_00931 {ECO:0000313|EMBL:SMX32978.1};
OS Actibacterium lipolyticum.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Roseobacteraceae; Actibacterium.
OX NCBI_TaxID=1524263 {ECO:0000313|EMBL:SMX32978.1, ECO:0000313|Proteomes:UP000202922};
RN [1] {ECO:0000313|Proteomes:UP000202922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8621 {ECO:0000313|Proteomes:UP000202922};
RA Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL Submitted (MAY-2017) 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=tRNA(Val) + L-valine + ATP = L-valyl-tRNA(Val) + AMP +
CC diphosphate; 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:ARBA00047552, ECO:0000256|HAMAP-
CC Rule:MF_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC 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|ARBA:ARBA00060830,
CC ECO:0000256|HAMAP-Rule:MF_02004}.
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DR EMBL; FXYE01000001; SMX32978.1; -; Genomic_DNA.
DR RefSeq; WP_093966113.1; NZ_FXYE01000001.1.
DR AlphaFoldDB; A0A238JQL6; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000202922; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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 FunFam; 1.10.287.380:FF:000001; Valine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000032; Valine--tRNA ligase; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
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; NF004349; PRK05729.1; 1.
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; 2.
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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW 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:UP000202922}.
FT DOMAIN 16..515
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 614..736
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 780..924
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 984..1049
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 982..1009
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 696..700
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 699
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 1052 AA; 117683 MW; 041A2418D705F94B CRC64;
MPMEKNFDAT AAEARLYAAW EESGCFKAGA NAKPGAETFC IMIPPPNVTG SLHMGHAFNN
TLQDILVRWH RMRGFDTLWQ PGQDHAGIAT QMVVERELAK DKSNATRAEM GRDAFLEKVW
EWKQHSGGTI INQLKRLGAS CDWSRNAFTM SGAPGAPEGE EGNFHDAVIK VFVEMYNKGL
IYRGKRLVNW DPHFETAISD LEVENIEVAG HMWHFKYKLA GGETYEYVEK DEDGNVTLRE
TRDYISIATT RPETMLGDGA VAVHPSDERY APIVGKMVHL PLCDRLIPIV SDEYPDKDFG
SGAVKITGAH DFNDYQVAKR GGLPMYRLMD TKGAMRADGA PYDDAVARAR EIADGATADG
AEIDTLNLVP EKYRGMDRFD ARKAVIEDIS AAGLAVMVEE TTTDKETGEE TTSLVPYVEN
KPVMQPFGDR SKVVIEPMLT DQWYVDTPQI VDPALDAVRK GMAAHEAGEF DENAGYTRIL
PERDAKTYYH WLENIEPWCI SRQLWWGHQI PVWYGLDLSA PDFRDDEGDG ALDEVDLGRL
LLDGMVHAGD VHHCAADFHS VEEAFRDEIA DTPTPLNHAR IIEVADRQEA LEQLAASLAE
YNIGQDPTKL VYPVWRDPDV LDTWFSSGLW PIGTLGWPED TEELKKYFPS DVLITGFDII
FFWVARMMMM QLAVVDHVPF HTVYVHALVR DEKGKKMSKS TGNVLDPLEL IDDYGTDAVR
FTLTAMAAMG RDLKLSTQRI AGYRNFGTKL WNAARFAEMN EVFEGYAPDG TIPQPTKTVN
KWIIGETAKI REATDEALSN YRFNDAANGL YAFVWGKVCD WYVEFSKPLL LDGDDATKAE
TRATMAWVLD QCMILLHPIM PYVTEELWGT LGERQKMLVH ADWPTYGTDL VDQAADREMN
WAIGLIEEIR SVRSQMHVPV GLKLPMLQLE LDKAGQAAWE RNATLIQRLA RIESLTIVDA
LPKGCVTIAV EGGTFALPLA DVIDVAEEKA RLEKTLQKLA KELGGLQGRL KNPKFVASAP
PEVVEETKEL VGVKVEETER LNAALKRLAE LG
//
