ID A0A3F3H3S0_9LACO Unreviewed; 893 AA.
AC A0A3F3H3S0;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 18-JUN-2025, entry version 26.
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=FPFC_040400 {ECO:0000313|EMBL:GAP03048.1};
OS Fructobacillus pseudoficulneus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Fructobacillus.
OX NCBI_TaxID=220714 {ECO:0000313|EMBL:GAP03048.1, ECO:0000313|Proteomes:UP000061227};
RN [1] {ECO:0000313|EMBL:GAP03048.1, ECO:0000313|Proteomes:UP000061227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15468 {ECO:0000313|EMBL:GAP03048.1,
RC ECO:0000313|Proteomes:UP000061227};
RX PubMed=26715526; DOI=10.1186/s12864-015-2339-x;
RA Endo A., Tanizawa Y., Tanaka N., Maeno S., Kumar H., Shiwa Y., Okada S.,
RA Yoshikawa H., Dicks L., Nakagawa J., Arita M.;
RT "Comparative genomics of Fructobacillus spp. and Leuconostoc spp. reveals
RT niche-specific evolution of Fructobacillus spp.";
RL BMC Genomics 16:1117-1117(2015).
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; DF968066; GAP03048.1; -; Genomic_DNA.
DR RefSeq; WP_059378312.1; NZ_DF968066.1.
DR AlphaFoldDB; A0A3F3H3S0; -.
DR STRING; 220714.SAMN05660469_0907; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000061227; 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 CDD; cd00817; ValRS_core; 1.
DR FunFam; 1.10.287.380:FF:000001; Valine--tRNA ligase; 1.
DR FunFam; 1.10.730.10:FF:000014; Valine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000032; Valine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000098; Valine--tRNA ligase; 1.
DR FunFam; 3.90.740.10:FF:000005; Valine--tRNA ligase, mitochondrial; 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; 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; 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; 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};
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:UP000061227}.
FT DOMAIN 19..574
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 618..767
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 825..890
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 823..892
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 52..62
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 535..539
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 538
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 893 AA; 102242 MW; 8D77FE6F5AC24211 CRC64;
MREVEMSTKY DPTAVEAGRY QEWLDNDLFS PEANKAIQGQ EPEPYSVVIP PPNVTGKLHL
GHAWDTTLQD MLIRQKRMQG FDTLWLPGMD HAGIATQAKV EQRLREQGVS RYDLGREKFI
EQVWDWKNEY ASTIKQQWGK MGLALDYSRE RFTLDEGLNQ AVNKVFIDLY NKGLIYRGEY
IINWDPQART ALSDIEVIYQ DDEGAFYHVK YPFTDGTTLN GKDYIEIATT RPETMFGDVA
VAVHPSDERY KDLIGKTVKV PLVNREIPII ADEYVEKDFG TGMVKITPAH DPNDFQVGNR
HDLERINTMT EDAHLNENAG KYVGLDRFEG RKAMVADLQE QGFMLEVEPL VHSVGHSERT
GVQIESRLST QWFVKMEPLA KQILAMQENA DEKVNFVPGR FEDTFTRWME NIRDWVISRQ
LWWGHQIPAW YKNKGTDQEE IYVGTEAPGA DWERDPDVLD TWFSSALWPF STMGWPNDLE
GDFAKYYPTN TLVTGYDIIF FWVARMMFQG KEFTGERPFK NVLIHGLIRD GEGRKMSKSL
GNGVDPMDVI EKYGADALRW FLATGSTPGQ DVRFTYEKMD AAWNFINKIW NVARYVIMNL
DDDTKAEVPA KDQQTLADQW ILDRLNQTVQ EVTENFEKFE FGEAGRDLYN FIWSDLADWY
VEMTKESLNG DGDKTAVQQT LAYVLDQTLR LLQPIMPFVS EAIWQEMPQQ KGKDEHLGIQ
AYPVFRDDLV NQEAATAFKS LQDLIVAVRN IRAEAKAPMS KPINVIIKVT DPALQAIFDD
NADYIDRFVK PESLTIGTEV TVPQLSMSQV ITGAEVYVPL AGLIDIEAEV ARLQGEADKF
QKEVARANGK LSNEKFVNSA PEKVVQAERE KLADWEEKLA STKKRIADLQ TQS
//
