ID A0A1X4J114_9RHOB Unreviewed; 1044 AA.
AC A0A1X4J114;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, 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=BV911_04395 {ECO:0000313|EMBL:OSP56175.1};
OS Pseudoruegeria sp. SK021.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudoruegeria.
OX NCBI_TaxID=1933035 {ECO:0000313|EMBL:OSP56175.1, ECO:0000313|Proteomes:UP000194129};
RN [1] {ECO:0000313|EMBL:OSP56175.1, ECO:0000313|Proteomes:UP000194129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK021 {ECO:0000313|EMBL:OSP56175.1,
RC ECO:0000313|Proteomes:UP000194129};
RA Pohlner M., Marshall I., Schreiber L., Cypionka H., Engelen B.;
RT "Draft genome sequence of Pseudoruegeria str. SK021, a representative of
RT the marine Rosebacter group, isolated from North Sea sediment.";
RL Submitted (JAN-2017) 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:OSP56175.1}.
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DR EMBL; MTBG01000003; OSP56175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X4J114; -.
DR STRING; 1933035.BV911_04395; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000194129; 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:UP000194129}.
FT DOMAIN 17..505
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 602..723
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 770..916
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 975..1039
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 683..687
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 686
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 1044 AA; 116136 MW; 1A53FC0E27A6C919 CRC64;
MTMDKTFNAA EAEARISKAW EDAHAFAAGA NAKPGAETFS VLIPPPNVTG SLHMGHAFNN
TLQDILVRWH RMRGHDTLWQ PGTDHAGIAT QMVVERELAK SGRRRTDMTR AEFTDLVWQQ
KKQSGGTIIG QLKRLGASCD WDRLAFTMSG APGAPEDEGG NFHDAVIKVF VDMYDKGLIY
RGKRLVNWDP HFQTAISDLE VENIEVDGHM WHFKYPLADG ATYDYVEKDE DGTVTLRETR
DYIAIATTRP ETMLGDGAVA VHPSDARYAP IVGMMCEIPV GPKETRRLIP IITDEYPDQN
FGSGAVKITG AHDFNDYQVA KRGGIPLYRL MDTKGTLRDD GLSYDDSAAR AAQLAAGDTA
SENEVDTINL VPEDLRGLDR FEARKAVIDQ ITAEGLAVMI ANPKYDPDAE EPGPALIPYV
ENKKVMQPFG DRSKVVIEPM LTDQWFVDAE AIVGPAIDAV RSGEIKILPE QQEKVYFNWL
DNIEPWCISR QLWWGHQIPV WYGLDLSDDQ PEDTSGDLDE VDIGHLLIES GIVHRGTRHH
CASAFDGVVD GFHADLASLP VPLNAARIVE VADRAAANHA FAASLAEYAV SQDPTHLIYP
VWRDADVLDT WFSSGLWPIG TLGWPEQTPE LEKYFPTSVL ITGFDIIFFW VARMMMMQYA
VVGQKPFDTI YLHALVRDEK GKKMSKSLGN VLDPLDLIDD YGTDAVRFTL TSMAAMGRDL
RLSKDRIAGY RNFGTKLWNA VRFAEMNGVY QSDKSPTKVR HKSDVTQTAN KWIMGETAKI
REEVDAALAS YRFNDAANGL YAFVWGKVCD WYVEFAKPLF ASGDEAIIAE TRDVMGWTLD
QCMILLHPTM PFITEELWGL TATREKMLVH TDWPTYQALD MVDETADREM NWVISMIEEI
RSVRSQMHVP AGLKLPLLQL DLDAAGQAAF TRSEALILRL ARIESVSTVD TMPKGCATLT
VDGGTFGLPL AGAIDLDEER ARLDKALGKL AKDIGGLKGR LNNPKFIASA PDEIVEENRE
LLSQKQQEEA RIHSALARLA ELAS
//
