ID A0A0A0M7Q9_9GAMM Unreviewed; 975 AA.
AC A0A0A0M7Q9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=N791_12505 {ECO:0000313|EMBL:KGO98998.1};
OS Lysobacter defluvii IMMIB APB-9 = DSM 18482.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1385515 {ECO:0000313|EMBL:KGO98998.1, ECO:0000313|Proteomes:UP000030003};
RN [1] {ECO:0000313|EMBL:KGO98998.1, ECO:0000313|Proteomes:UP000030003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMMIB APB-9 {ECO:0000313|EMBL:KGO98998.1,
RC ECO:0000313|Proteomes:UP000030003};
RA Wang Q., Wang G.;
RT "Genomic analysis of Lysobacter defluvii.";
RL Submitted (AUG-2013) 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}.
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:KGO98998.1}.
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DR EMBL; AVBH01000036; KGO98998.1; -; Genomic_DNA.
DR RefSeq; WP_027070711.1; NZ_KE384007.1.
DR AlphaFoldDB; A0A0A0M7Q9; -.
DR STRING; 1385515.GCA_000423325_02038; -.
DR eggNOG; COG0525; Bacteria.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000030003; 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}; Reference proteome {ECO:0000313|Proteomes:UP000030003}.
FT DOMAIN 18..624
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 694..849
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 910..974
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT REGION 663..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 908..935
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 44..54
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 547..551
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT COMPBIAS 675..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 550
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 975 AA; 108701 MW; 1D76BEBA87FD0C8D CRC64;
MTDTLPASYD PTQFESRLYE RWEAEGLFKP SGTGTPYSVL LPPPNVTGTL HMGHAFQHTL
QDALVRYHRM RGFDTLWQMG SDHAGIATEM VVSRNLDREG KGETRDSLGR DGFIGKVWEW
KHESGGTIER QMRRMGTSGD WSRSVFTMDP MPAKAVVEAF VRLHEEGLVY RGQRLVNWDP
VLQTAISDLE VANEEEDGHL WSIAYPLADG SGQLVVATTR PETMLGDTAV MVHPDDERYV
HLVGRTVALP LTGREIPIIA DAYVDREFGT GVVKVTPAHD FNDYQVGLRH ALPLLNILTP
TAKVIGGEDA SEGELERANT AGIPQHYRGL DRYEARKAVL ADLEAAGLLV EDKPHKLQVP
RGDRTGQVIE PYLTDQWFVK MDALGARGLE LAESGKVRFV PGNWINTYRH WMENIQDWCI
SRQLWWGHRI PAWYDPAGNI HVGRDEAEVR AKYGLADDVP LRQDEDVLET WFSSALWPFS
TQGWPDEAAM AGLGIDRYLP SSVLVTGFDI IFFWVARMIM MTDHFTGEVP FHDVYVTGLV
RDKDGQKMSK SKGNILDPLD LIDGISLDDL VAKRTTGLMQ PKMAEKIAKA TRREFPDGIP
AFGADALRFT MAALAGHGRD IKFDLGRAEG YKNFCNKLWN ATRFVLMNTE GFSLPAAPSL
LPPAGEGARR ADEGSSQVHQ ATPLPPTPTT DAQRWILSRL EATAAEAARH FADYRFDLLS
QALYEFAWND FCDWFVELAK PALHGDTDTG EGRAAADSTR HTLLYVLERL LALLHPLVPF
VTEELWQQVA PRLGLPAGSI MVQRYPEPGD IQVDDQARAE ADVEWLKAMV SAIRRVRGEL
NVPPSKQVTL LLADASEDDR RRIDRFDASL RFLGKLERID LLASTADAPA AATAVVGELK
LLVPLEGLVD LDAERARLDK ELKKVDAEIA KCKGKLANET FVANAPAAVV EQERKRLVDW
TTQREALASQ RARMG
//
