ID A0A2V2LFX6_9RHOB Unreviewed; 1068 AA.
AC A0A2V2LFX6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, 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 ORFNames=DKT77_04045 {ECO:0000313|EMBL:PWR03892.1};
OS Meridianimarinicoccus roseus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Meridianimarinicoccus.
OX NCBI_TaxID=2072018 {ECO:0000313|EMBL:PWR03892.1, ECO:0000313|Proteomes:UP000245680};
RN [1] {ECO:0000313|EMBL:PWR03892.1, ECO:0000313|Proteomes:UP000245680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TG-679 {ECO:0000313|EMBL:PWR03892.1,
RC ECO:0000313|Proteomes:UP000245680};
RA Ren Y.;
RT "Rhodobacteraceae gen. nov., sp. nov. isolated from sea water.";
RL Submitted (MAY-2018) 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:PWR03892.1}.
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DR EMBL; QGKU01000015; PWR03892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V2LFX6; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000245680; 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 Gene3D; 3.40.50.620; HUPs; 3.
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 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}; 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:UP000245680}.
FT DOMAIN 16..522
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 623..744
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 795..941
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 1000..1064
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT REGION 408..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1040..1067
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 50..60
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 704..708
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 707
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 1068 AA; 118695 MW; 8ABE9B86954A27EB CRC64;
MAMDKTFNAA EAEARLYAAW EDAGCFKAGA NAKPGPDGKT EAFSIVIPPP NVTGSLHMGH
AFNNTLQDIL VRWHRMRGHD TLWQPGTDHA GIATQMVTER DMAAKGEPTR REMGREAFLD
RVWQQKQNSR GTIIGQLKRL GASCDWSREA FTMGGAPGDP EPGSGPNFHD AVIRVFVDMY
EKGLIYRGKR LVNWDPHFET AISDLEVENV EMPGHMWHFK YPLAGGETYE YVEKDEDGTI
TLRETRDYIS IATTRPETML GDGAVAVHPS DERYAPIVGK MCEIPVGPKE HRRLIPIITD
EYPDPAFGSG AVKITGAHDF NDYAVAKRGG IPMYRLMDTK GRMRDDGAPY ADCAAIAQRL
AAGETATETE VDAINLVPDH LRGLDRFEAR EKVVAEITAE GLAVMVPPTD PRLGKAATKA
PAAPEEGGEE QDNTLVPLVE SKPIMQPFGD RSKVVIEPML TDQWFVDAEK VVGPAIDAVR
DGDVEILPER DARVYFHWLE NIEPWCISRQ LWWGHQIPVW YGLDIWPTGF RDDEGDNALD
EVEIFRLLGD GAFNHAEPTH HCAFDLDRVG EKFRKDLAAL PAPLHAARIV EVADKHAAIE
ALAAAMADYN ISQDPTHLVY PVWRDPDVLD TWFSSGLWPI GTLGWPDETP ELQRYFPTSV
LVTGFDIIFF WVARMMMMQY AVVGQKPFST VYVHALVRDE KGKKMSKSLG NVLDPLDLID
EYGCDAVRFT LSSMAAMGRD LKLSKDRIAG YRNFGTKLWN AVRFAEMNGV FDGDVESYGS
HMRVICDSDT TQTANRWIIG ETARARAEID TALAAFRFND ASAVLYSHVW GKVCDWYVEF
AKPLFASEDA AIVEETRRTM AWVLDQCLIL AHPFMPFITE ELWGLTAKRD KMLVHGDWPT
YQAADMADEK ADAEMGWVIG LIEDIRSLRA QMHVPAGAKL PLLQLGLDAA GQAAWDRNVT
LIQRLARIES VSKVSELPKG AVTIPVEGGT FALPLADVID VAEEQARLEK TLGKLAKDMG
GLRGRLNNPK FVASAPDDVI EETRDLLAQK EDEDAKLRAA LERLAALA
//
