ID W7QXC2_9ALTE Unreviewed; 948 AA.
AC W7QXC2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=DS2_09897 {ECO:0000313|EMBL:EWH09930.1};
OS Catenovulum agarivorans DS-2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Catenovulum.
OX NCBI_TaxID=1328313 {ECO:0000313|EMBL:EWH09930.1, ECO:0000313|Proteomes:UP000019276};
RN [1] {ECO:0000313|EMBL:EWH09930.1, ECO:0000313|Proteomes:UP000019276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-2 {ECO:0000313|EMBL:EWH09930.1,
RC ECO:0000313|Proteomes:UP000019276};
RX PubMed=24604650;
RA Shan D., Li X., Gu Z., Wei G., Gao Z., Shao Z.;
RT "Draft Genome Sequence of the Agar-Degrading Bacterium Catenovulum sp.
RT Strain DS-2, Isolated from Intestines of Haliotis diversicolor.";
RL Genome Announc. 2:e00144-14(2014).
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:EWH09930.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ARZY01000017; EWH09930.1; -; Genomic_DNA.
DR RefSeq; WP_035014596.1; NZ_ARZY01000017.1.
DR AlphaFoldDB; W7QXC2; -.
DR SMR; W7QXC2; -.
DR STRING; 1328313.DS2_09897; -.
DR PATRIC; fig|1328313.3.peg.2026; -.
DR eggNOG; COG0525; Bacteria.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000019276; 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:UP000019276}.
FT DOMAIN 14..628
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 671..822
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 883..944
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 879..948
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 40..50
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 551..555
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 554
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 948 AA; 108095 MW; 812ACDD54ACC09DA CRC64;
METKFNPSNI EKALYQAWEE KGYFKPSGEG QAYSIMIPPP NVTGSLHMGH AFQDTIMDTL
IRYKRMDKFN TLWQVGTDHA GIATQMVVER KLAAEEDKTR HDLGREAFID RIWDWKKESG
GTITQQLRRL GASVDWDRER FTMDDGLSEA VKEVFVRLHK EDLIYRGKRL VNWDPKLHTA
ISDLEVENKD KKGHMWNFRY PLADGVTTKD GKNYIVVATT RPETMLGDTG VAVNPEDERY
QDLIGKEIIL PIVERRIKIV ADEHADMEKG TGCVKITPAH DFNDNEVGKR HQLPMINIFD
KDAAILAQGE SFTFDGKPLE LDAPIPERFH GLDRFAARKA IVAEFEQLGL LDVIEDHSLT
VPYGDRSGVV IEPLLTDQWY VRVAPLAEPA IDAVKNGEIK FVPQQYENMY FSWMNDVQDW
CISRQLWWGH RIPAWYDADG NVYVGRDEAE VRSENNIAAD VALTQDEDVL DTWFSSALWT
FSTLGWPEQT PELKTFHPSE VLVTGFDIIF FWVARMIMMT MHFIKDEDGK AQVPFKTVYV
TGLIRDENGD KMSKSKGNVL DPIDMIDGID LESLVTKRCG NMMQPQLAKK IEKNTRKTFE
NGIEAHGTDA LRFTLAAMAS TGRDINWDMK RLEGYRNFCN KLWNASRYVL MNTEEQDCGS
NGGDIELSLA DKWILGRLQQ TIETSRKYID SYRFDLLAQT LYEFTWNQFC DWYLELTKPV
LTNGTEAQQR GTRKTLIQVL ETLLRLMHPV MPYITEEIWQ KVAPLAGVTG ETIMLQAYPQ
FAADKVDEAA IADVEWLKQF ILGIRNIRGE MNISPNKPLN VLLRNLNTDD QRCLAENQTF
LQSLAKLESI EILAADDKGP ASASAFVGDM QILIPMAGLI DKDAELARLK KAMDKAENEL
GRVQNKLSNE KFVNNAPAHV LDKEKDKLAE FEGALTKLKQ QYDEISAL
//
