ID A0A087DN61_9BIFI Unreviewed; 930 AA.
AC A0A087DN61;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 18-JUN-2025, entry version 56.
DE RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02005};
DE EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02005};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02005};
DE Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02005};
GN Name=valS {ECO:0000256|HAMAP-Rule:MF_02005};
GN ORFNames=BSTEL_1870 {ECO:0000313|EMBL:KFI96961.1};
OS Bifidobacterium stellenboschense.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=762211 {ECO:0000313|EMBL:KFI96961.1, ECO:0000313|Proteomes:UP000029004};
RN [1] {ECO:0000313|EMBL:KFI96961.1, ECO:0000313|Proteomes:UP000029004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23968 {ECO:0000313|EMBL:KFI96961.1,
RC ECO:0000313|Proteomes:UP000029004};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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_02005}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tRNA(Val) + L-valine + ATP = L-valyl-tRNA(Val) + AMP +
CC diphosphate; 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:ARBA00047552, ECO:0000256|HAMAP-
CC Rule:MF_02005};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02005}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02005}.
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_02005}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02005}.
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:KFI96961.1}.
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DR EMBL; JGZP01000014; KFI96961.1; -; Genomic_DNA.
DR RefSeq; WP_034528852.1; NZ_JGZP01000014.1.
DR AlphaFoldDB; A0A087DN61; -.
DR STRING; 762211.BSTEL_1870; -.
DR eggNOG; COG0525; Bacteria.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000029004; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_02005; Val_tRNA_synth_type2; 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR022874; Valine-tRNA_ligase_type_2.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR InterPro; IPR048044; Valyl-tRNA_ligase_actino.
DR NCBIfam; NF000540; alt_ValS; 1.
DR NCBIfam; NF009687; PRK13208.1; 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; 2.
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; 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_02005};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02005};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02005};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02005};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02005};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02005}; Reference proteome {ECO:0000313|Proteomes:UP000029004}.
FT DOMAIN 27..112
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 136..633
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 688..844
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 56..66
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT MOTIF 598..602
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT BINDING 601
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
SQ SEQUENCE 930 AA; 104090 MW; 3F4DADC480AFD406 CRC64;
MTEAKSITAN LTPLPDRVGV DGLEDKWRAV WDEQGTYKFN DTRDRKAVYS IDTPPPTVSG
HLHVGHVFSY THTDVIARFK RMQGFDVFYP MGWDDNGLPT ERRVQNYYGV RVDTSLKYDP
DFKPPFEGTD GKKIDAKDQV PCSRQNFIEL CEKLTAEDEK LFEALWRKLG LSIDWSQTYH
TIGEHPRRVA QKAFLRNLAH GEAYQKDAPG LWDVTFQTAV AQAELESREY PGFYHKIAFR
FEDGTPIYIE TTRPELLAAC GALIAHPDDE RYKQYFGQYV YSPLFKVKVP ILAHPAAEMD
KGAGIAMCCT FGDVTDVQWW RDLNLPTRSI IQRNGRIIMD VPDWIEDEGG KAIFEETEGK
TTFSARKIIV DHLRESGDLD GEPTPTKRMT NFYEKGDKPL EIVTSRQWYL KNGGTDQKLN
AELIERGREL EFHPDFMRVR YENWVHGLNG DWLISRQRFF GVPFPLWYPV KEDGSADYDH
PITPSEDILP IDPTTDVPAG YTEDQRDVPG GFTAEKDIMD TWATSSLTPQ IVTRWEEPGE
ENQALFKATF PMDLRPQGQD IIRTWLFSSV DRAHLENKCL PWKHTTLSGW ILDPDHKKMS
KSKGNVVVPN KPIEQFGADA VRYWAAAARL GLDATYDEGQ MKIGRRLAIK LLNATKFALA
IGREDENHHV SEGAEAVWDP ADVTEPLDRA AMARMALVVR EATAALNNYE HSKALEAIEN
YFWQFCDDYI ELVKNRAYGT ADATGHVPSE AAVKSARTAL GLGLDAFTRL LAPFLPYATE
EVWSWMHAGS GSVHRAAWPT PDVYEAAAFK VAPELLNHAG EALAALRGIK SKAKVSMKTP
ILSVTLGVAD DVRESLAGAL DDIAEAGRVV GKIHFAAAAA AVKAAKETVE AAAAAAKDAA
KEAKAETEAA AEIIVEQSEL GEPPAKKPRK
//
