ID A0A1S8CT99_9GAMM Unreviewed; 986 AA.
AC A0A1S8CT99;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=BKE30_09370 {ECO:0000313|EMBL:ONG39549.1};
OS Alkanindiges hydrocarboniclasticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Alkanindiges.
OX NCBI_TaxID=1907941 {ECO:0000313|EMBL:ONG39549.1, ECO:0000313|Proteomes:UP000192132};
RN [1] {ECO:0000313|EMBL:ONG39549.1, ECO:0000313|Proteomes:UP000192132}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1 {ECO:0000313|EMBL:ONG39549.1,
RC ECO:0000313|Proteomes:UP000192132};
RA Subhash Y., Lee S.;
RT "Draft Genome sequence of Alkanindiges sp. strain H1.";
RL Submitted (OCT-2016) 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:ONG39549.1}.
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DR EMBL; MLCN01000023; ONG39549.1; -; Genomic_DNA.
DR RefSeq; WP_076878340.1; NZ_MLCN01000023.1.
DR AlphaFoldDB; A0A1S8CT99; -.
DR STRING; 1907941.BKE30_09370; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000192132; 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}.
FT DOMAIN 39..659
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 702..855
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 921..983
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 924..986
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 65..75
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 582..586
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 585
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 986 AA; 111600 MW; EF8DF4E4DD638281 CRC64;
MTTTVDNSAA DNSAATGNQT ESQQNISTTY DPAAIEAHWY EVWEKQGYFK PQGGAKPFTI
MIPPPNVTGS LHMGHGFNNA IMDAMIRYHR MLGDNTLWQP GTDHAGIATQ MVVERQLAAQ
NISRHDLGRE DFIKKVWEWK EKSGGTITQQ IRRLGSSVDW SRERFTMDEG LSNAVKEVFV
RLHEEGLIYR GKRLVNWDPK LHTALSDLEV ENNEEQGSLW HFKYFFENDS TATSNGDNYL
VVATTRPETL LGDTAVAVHP EDERYKHLIG QNIRLPITGR LVPIVGDDYV EKDFGTGCVK
ITPAHDFNDY ELGKRHNLPL INIFNKNAEI QAEFEWIEKA GQPITQTLAA PSEYAGVERF
AARKKLVAQA ESEGWLEKIE LYTLKAPRGD RSGVIVEPLL TDQWYVKIAP LAEPAIEAVK
NGDIKFVPEQ YSNMYMAWMN NIQDWCISRQ LWWGHRIPAW YAQDGSVYVG RSEDEVRQKY
NLGSDISLNQ DEDVLDTWFS SALWTFSTLD WTGDAAKDAE NYFLKTFHST DVLVTGFDII
FFWVARMIMM TLHFVKDENG KPQVPFKTVY VHGLVRDGEG QKMSKSKGNV LDPLDLVDGI
DLETLIAKRT TGLMNPKDAA KIEKATRKEF PDGINAYGTD ALRFTFCALA NTGRDIKFDL
KRVEGYRNFC NKIWNATRFV LMNVEGKTVG QAPRTDLWEL PEQWIVSRLQ KAEAAVHKAF
ADYRLDMVAQ TMYDFVWNEY CDWYVELTKP VLNSDEVSEE RKAEVRRVLL ATLESSLRLL
HPLMPFLTEE IWQTVAPMIG KKAVDHDDAT IMLAPFPQAE QAKINEQAEA DMTWLQGLIG
AVRNIRGEMG LGNARLLPIL LKNVSDKERE QLGRIEPLFK ALSKVESIEF LSNDQEPPLS
SSSVVGQVSI FVPMKGLIDP QAEIGRLTKK IEKLQKQFDV LNGKLSNQGF LAKAPAHVVD
AEKVVLADLA DQLQKLNAQK EQLAAL
//
