ID A0A2U2RLI1_9MICO Unreviewed; 885 AA.
AC A0A2U2RLI1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 18-JUN-2025, entry version 32.
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 ECO:0000313|EMBL:PWH06691.1};
GN ORFNames=DEO23_07115 {ECO:0000313|EMBL:PWH06691.1};
OS Brachybacterium endophyticum.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC Dermabacteraceae; Brachybacterium.
OX NCBI_TaxID=2182385 {ECO:0000313|EMBL:PWH06691.1, ECO:0000313|Proteomes:UP000245590};
RN [1] {ECO:0000313|EMBL:PWH06691.1, ECO:0000313|Proteomes:UP000245590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1HQ-2 {ECO:0000313|EMBL:PWH06691.1,
RC ECO:0000313|Proteomes:UP000245590};
RA Tuo L.;
RT "Brachybacterium sp. M1HQ-2T, whole genome shotgun sequence.";
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_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:PWH06691.1}.
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DR EMBL; QFKX01000002; PWH06691.1; -; Genomic_DNA.
DR RefSeq; WP_109275286.1; NZ_QFKX01000002.1.
DR AlphaFoldDB; A0A2U2RLI1; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000245590; 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 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:UP000245590}.
FT DOMAIN 28..109
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 138..635
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 684..831
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 115..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 885 AA; 97730 MW; 1F77CECD066AB062 CRC64;
MTDTAPRPNA ASALPDKPTL EGLEDKWDRV WDEAQVYAFD ADTTRDQVFS VDTPPPTASG
SLHIGHVFGY SQADMIVRYQ RMRGKNVFYP LGWDDNGLPT ERRVQNYFGV RCDPSLPYEE
DFTPPQEGGD NKSSKAANQT PISRRNFIEL CEKLTKVDEA SFEEVFRTLG LSVDWNHSYQ
TIDARSRATS QRAFLENLEK GQAYQSEAPT MWDVTYRTAV AQAEQEDRER DGAYHRIGFA
KTDGSGEKVF IETTRPELLP ACVALVAHPD DERYQDLFGT TVTSPLFGVE VPVMAHPLAQ
ADKGAGIAMI CTFGDANDVT WWRELELPTR SVIGRDGRFL PEAPWITSAE GQERYAELAG
LTVFSAQKRV VEMVTESGDL VGEPKKITHP VKFYENGDKA LEYVTSRQWY LTNGGRDSSE
GGLRDALIAR GAEITWHPAY MESRYRNWVE GLVGDWLVSR QRFYGVPIPV WYALDAAGEV
DYDTVLTPEV ERLPIDPTTD VPAGYEEAQR EQPGGFTADP DILDTWATSS LTPQLAGGWD
ADPELFAKVY PMDLRPQGHD IIRTWLFSTI VRSHLQQDSL PWTNTSINGW ILDPDRKKMS
KSKGNVVTPI GLLHSHGSDG VRYWAGRARQ GVDTAFDEGQ MKIGRRLAIK ILNASKFALG
FGEAPADPSG RLAADPAAVT ASLDRAMLAS LAGVVDTATA AFEEMDYARA LEVVEPFFWT
FCDDYIELIK DRAHGSAGEQ GVASARAALA IALEVLLRLF APVVVFATEE VWSWWREGSV
HTQAWPESAP LREAAAGRDA ALLTTVEQAA IVLRRIKSDA KVSQKTPILQ VTVSAPAQAV
EHLEAARGDL TALGRIESLT ITGGGEEIDT ADVELGEPPV KKPRG
//
