ID A0A0P1GQ34_9RHOB Unreviewed; 1025 AA.
AC A0A0P1GQ34;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 ECO:0000313|EMBL:CUH76247.1};
GN ORFNames=TRN7648_00853 {ECO:0000313|EMBL:CUH76247.1};
OS Tropicibacter naphthalenivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tropicibacter.
OX NCBI_TaxID=441103 {ECO:0000313|EMBL:CUH76247.1, ECO:0000313|Proteomes:UP000054935};
RN [1] {ECO:0000313|EMBL:CUH76247.1, ECO:0000313|Proteomes:UP000054935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7648 {ECO:0000313|EMBL:CUH76247.1,
RC ECO:0000313|Proteomes:UP000054935};
RG Swine Surveillance;
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}.
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DR EMBL; CYSE01000001; CUH76247.1; -; Genomic_DNA.
DR RefSeq; WP_058246359.1; NZ_FWXX01000001.1.
DR AlphaFoldDB; A0A0P1GQ34; -.
DR STRING; 441103.TRN7648_00853; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000054935; 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 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000054935}.
FT DOMAIN 16..704
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 752..894
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 957..1021
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 672..676
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 675
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 1025 AA; 114019 MW; D9EBA3C0B524DBB3 CRC64;
MPLEKTFNAA EAEPRLMQTW LDAGAFAAGA NKSRDESFTI MLPPPNVTGA LHVGHAFNHT
LMDILTRWHR MRGFDTLWQP GQDHAGIATQ LQVEKKLKAE QGIRRTDLTR ADFLNHVWDW
KTQYGGTIIE QMKRLGDSCD WDRNAFTMSG APGAPEADAD GNFHDAVIKV FVDMYEKGLI
YRGKRLVNWD PHFETAISDL EVENIEVAGH MWHFKYPLAD GVTYEYLEKD EEGNVIFRET
RDYISIATTR PETMLGDGAV AVFTNDERYA PIVGKLCEIP VGPKEHRRLI PIITDEYPDP
NFGSGAVKIT GAHDFNDYQV AKRNDIPMYR LMDTRGAMRA DGLPYAEAAK IAMDVAAGKR
TLSEVEADTI NLVPDHLRGL DRMEAREAVI REITEEGLAV MTEATDPRLG AAAVKSPVEP
SEGGEMRTEE EQLVPLVESK PIMQPFGDRS KVVIEPMLTD QWFVDAEKVV GPALDAVRSG
KIKIMPESGE KTYYHWLENI EPWCISRQLW WGHQIPVWYV PGEEDWYPIC AATEAEAIEA
AKARFVDGTE FRIVEDANEA AAVLAEALKH MDVADEGAIR TFDAPMQLPM FRDPDVLDTW
FSSGLWPIGT LGWPEDTPEM QKYFPTDVLV TGSDILFFWV ARMIMMQLAV VDEIPFHTVY
LHQLVRDEKG KKMSKTTGNV IDPLEIINDY GADALRMNNA AMASIGGVLK MSVDRIAGYR
NFGTKLWNAA RFAEMNDAVG LGGTPAPNAT LNKWIMGETA KVREVVDQAL TDYRFNDAAN
ALYAFVWGKV CDWYVEFSKP LFGSDDAAVA QETRETMSWV IDQCLILLHP IMPFITEELW
GTLGARAKML VHTNWPTYAA ADMVDAEAEA EIDWVIGVIE GVRSARAQMH VPAGLYVPLL
ATQMGAAEQT AWDNNETLIK RLARIESLET VGEFPKGCVV VPVGGATLGM PLADIIDVAE
EKARLEKTLG KLAKELGGLR GRLNNPKFAA SAPAEVVEEA RANLAAREAD EAKIKDALAR
LAEIG
//
