ID A0A1Q8E3U4_9GAMM Unreviewed; 985 AA.
AC A0A1Q8E3U4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=BTV99_00245 {ECO:0000313|EMBL:OLF41692.1};
OS Psychrobacter sp. Rd 27.2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1926479 {ECO:0000313|EMBL:OLF41692.1, ECO:0000313|Proteomes:UP000186500};
RN [1] {ECO:0000313|EMBL:OLF41692.1, ECO:0000313|Proteomes:UP000186500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rd 27.2 {ECO:0000313|EMBL:OLF41692.1,
RC ECO:0000313|Proteomes:UP000186500};
RA Romalde J.L., Lasa A.;
RT "Genome sequence of three Psychrobacter strains.";
RL Submitted (DEC-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:OLF41692.1}.
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DR EMBL; MRYB01000001; OLF41692.1; -; Genomic_DNA.
DR RefSeq; WP_075100359.1; NZ_MRYB01000001.1.
DR AlphaFoldDB; A0A1Q8E3U4; -.
DR STRING; 1926479.BTV99_00245; -.
DR Proteomes; UP000186500; 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; 2.
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 38..657
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 705..858
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 COILED 923..985
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 580..584
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 583
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 985 AA; 112086 MW; 28B5BDB40276CF68 CRC64;
MSNPENHTNS TTNLTESIQA ALSQLENAYN PKDVEAGMYQ GWEESGYFAP TFDKDESFSI
ALPPPNVTGS LHMGHGFNNA IMDALTRYHR MDGDNTLWQP GTDHAGIATQ MVVERRLEAQ
GIRRRDMTRE DFIDKVWEWK EESGGNITRQ IRRLGSSVDW SRERFTMDDG LSNAVKEVFV
RLFDDGLIYR GKRLVNWDPK FQTALSDLEV ENVDEKGSLW HFRYYFTDTD ITTQDGKNYL
VVATTRPETL LGDTAVAVNP SDERYAHLIG KTITLPITGR VVPIVADDYV ESDFGTGCVK
ITPAHDFNDY ELGRRHSLPL INILDERANI LPEMEVYADL QTREPSLETT PSEYAGLERF
AARKQLVEQA SSEGWLEDIE DYALKAPRAE RGGTIVEPWL TDQWYVAVNK LAGPAIDAVE
DGRIEFVPAQ YKNMYMAWMT DLQDWCISRQ LWWGHRIPAW YDDAAGEVYV ARSEAEVRTK
YNLSDDVKLR QDDDVLDTWF SSGLWTFSTL DWADPKADPR VMQTFHPTSV LVTGFDIIFF
WVARMIMMTM HFVKNEDGTP QVPFKTVYVH GLVRDGNGQK MSKSKGNVLD PIDLIDGIDL
EALVEKRTSN MMNPKDAAKI EKQTRKEFPE GIPAYGTDAL RFTFTSLAST GRDINFDLKR
VEGYRNFCNK IWNASRFVLM NCIDNDGNAK PIDQAANVDV WELPEKWIMS RLNSTISNIH
QHFAQYRLDM VSHDIYEFIW NEYCDWYVEL AKASLNDDSV TDERKAQIRY VLLHVLETAL
RFSHPIMPYL TEEIWQTVAP LLNRKDTDSI VIAAYPQADN AQISEQVEAD MAWLQELIAS
IRNIRGEMKL GNAVRLPVLL QNISDEEEAR LSRIKNQFKA LAKVESLEIV KEGDEVPLSS
SSMVGQLRVL VPMKGLIDPT AELARLDKAH EKLQKQADGI ARKLSNEGFV SKAPAQVVEN
EKAKLAELEG QLKTMTAQMA QLKAL
//
