ID A0A6A0B9Y3_9LACT Unreviewed; 888 AA.
AC A0A6A0B9Y3;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 08-OCT-2025, entry version 21.
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:GFH40627.1};
GN ORFNames=Hs20B_10250 {ECO:0000313|EMBL:GFH40627.1};
OS Pseudolactococcus insecticola.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Pseudolactococcus.
OX NCBI_TaxID=2709158 {ECO:0000313|EMBL:GFH40627.1, ECO:0000313|Proteomes:UP000475928};
RN [1] {ECO:0000313|EMBL:GFH40627.1, ECO:0000313|Proteomes:UP000475928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hs20B0-1 {ECO:0000313|EMBL:GFH40627.1,
RC ECO:0000313|Proteomes:UP000475928};
RA Noda S., Yuki M., Ohkuma M.;
RT "Draft genome sequence of Lactococcus sp. Hs20B0-1.";
RL Submitted (FEB-2020) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GFH40627.1}.
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DR EMBL; BLLH01000004; GFH40627.1; -; Genomic_DNA.
DR RefSeq; WP_172356314.1; NZ_BLLH01000004.1.
DR AlphaFoldDB; A0A6A0B9Y3; -.
DR Proteomes; UP000475928; 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 Gene3D; 3.40.50.620; HUPs; 3.
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:UP000475928}.
FT DOMAIN 18..432
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 440..565
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 615..761
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 822..885
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 819..888
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 525..529
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 888 AA; 100772 MW; 3A3356DDB142F036 CRC64;
MTKELSTKFN PTEVEAGRYE KWLAAGVFTP SANPDAAPYS IVIPPPNVTG KLHLGHAWDT
TLQDIIIRAK RMQGYDTLWL PGMDHAGIAT QAKVEARLAE SGISRYDLGR EKFLDKAWEW
KDEYAATIKT QWGKMGLSLD YSRERFTLDE GLNQAVRTVF VKLYEKGWIY RGEKLINWDP
KAMTALSDIE VIHKEIDGAF YHMTYKLADG SGEVEIATTR PETLLGDVAV IVNENDDRYK
NIVGKTVIVP FVNREIPVLT DDHADMEKGT GVVKITPAHD PNDFDVVERL NSKGANLPMI
NMMNNDGTIN EVGGEFNGLD RFEARKQIVA GLKNLGQLIK VEPIRHEVGH SERTGVVVEP
RLSTQWFVKM EDLAKAAIDN QKTDNKVEFF PPRFNDTFTQ WMENVHDWVI SRQLWWGHQI
PAWYNESGEM YVGMTAPEGD GWTQDPDVLD TWFSSALWPF STMGWPDEEA ADFKRYFPTS
TLVTGYDIIF FWVSRMIFQS LEFTGERPFE NVLIHGLIRD EEGRKMSKSL GNGIDPMDVI
EKYGADALRW FLSNGSAPGQ DVRFSYEKMD AAWNFINKIW NISRYIIMNK ESLTPSETLA
NIDKVAGKTA GNVTDRWILT KLNETVENVT KNFDKFEFGE AGRSLYNFIW EDFANWYVEL
TKEVLYGEDA AEKDVTRSVL VYVLDQILRL LHPIMPFVTE EISENLGLIE GSIVVASYPE
VREAFTDEAA VRGVEVLKDI IKSVRNIRAE VNTAPSKAVP ILIKTENAEI EAFLKENTNY
LTRFTNPETL EISANISAPA QAMTAILSNV ELYLPLAGLI NISDEVARLT KELAKWQKEL
DMVSRKLSNE KFVANAKAEV VEKEKAKQAD YQAKYDTTQA RIKELESL
//
