ID A0A0R3D043_9BRAD Unreviewed; 958 AA.
AC A0A0R3D043;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=AOQ71_30790 {ECO:0000313|EMBL:KRQ03143.1};
OS Bradyrhizobium manausense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=989370 {ECO:0000313|EMBL:KRQ03143.1, ECO:0000313|Proteomes:UP000051936};
RN [1] {ECO:0000313|EMBL:KRQ03143.1, ECO:0000313|Proteomes:UP000051936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR3351 {ECO:0000313|EMBL:KRQ03143.1,
RC ECO:0000313|Proteomes:UP000051936};
RA De Araujo J.L., Zilli J.E.;
RT "Draft Genome Sequence of Bradyrhizobium manausense Strain BR 3351T, a
RT Novel Symbiotic Nitrogen-Fixing Alphaproteobacterium Isolated from
RT Brazilian Amazon Rain Forest.";
RL Submitted (SEP-2015) 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:KRQ03143.1}.
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DR EMBL; LJYG01000108; KRQ03143.1; -; Genomic_DNA.
DR RefSeq; WP_057754941.1; NZ_LJYG01000108.1.
DR AlphaFoldDB; A0A0R3D043; -.
DR STRING; 989370.AOQ71_30790; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000051936; 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 18..610
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 653..828
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 890..955
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 895..957
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 571..575
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 958 AA; 108771 MW; 3A8A084DD9DE2E2D CRC64;
MIEKNYQPAD IEARMSVVWE DSLAFKAGRP DRRDAVPFTI VIPPPNVTGS LHMGHALNNT
LQDILCRFER MRGRDVLWQP GTDHAGIATQ MVVERQLMER QQPGRREMGR EKFLERVWQW
KAESGDTIIN QLKRLGASCD WSRERFTMDE GLSKAVIKVF VELHREGLIY KDKRLVNWDT
KLLTAISDLE VQQTEVKGHL WYLRYPIEGK TFDPEDRSTF IVVATTRPET MLGDTGVAVH
PEDERYQKLI GRNVVLPLVG RKIKIVADEY SDPEKGSGAV KVTPAHDFND FEVGNRHGLR
RISVLDKEGC LDLVDNEDYL KGLPEGATQF AEEFNKVDRF VARKRIVERL ESFGFVERIE
PHTHMVPHGD RSGSVIEPYL TDQWYVDAKT LAKPAIAAVR SGETTFVPKN WEKTYYEWME
NIQPWCISRQ LWWGHQIPAW YGPDGKVFVA ETEEEAVSHA LGYYVEQEVI TAEQGREMAL
DRNKREGFIT RDEDVLDTWF SSALWPFSTL GWPEDAPEVQ RYYPTNALVT GFDIIFFWVA
RMMMMGLHFM KEIPFSTIYI HALVRDEKGA KMSKSKGNVI DPLNLIDEYG ADALRFTLAA
MAAQGRDIKL ATSRVEGYRN FATKLWNASR FAEMNHCAVP EGFEPAKAKE TLNRWIAHET
AHTTREVTEA IEAYRFNDAA GSIYRFVWNV YCDWYVELAK PVLLGPDSPA KNETRAMVAW
ARDEILKLLH PFMPFITEEL WEVTAKRDGL LALAEWPLKP AAPSPEQLAI LAAAAGPTDP
LVSPAFVMPI FDHADFTDPK AEAEIGWVID LITQIRSVRA EMNIAPATLT ALVLAGASAE
TRERAPRWTD VIKRMARLSD ISFADRAPDG AVQLLVRGEV AALPLKGVVD FAAERTRLDK
EIGKADADIK RAESKLANEK FVANAAEEVV EEEREKREAA LARKAKLLEA LERLKQAS
//
