ID A0A1F8EE82_9BACT Unreviewed; 720 AA.
AC A0A1F8EE82;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=valine--tRNA ligase {ECO:0000256|ARBA:ARBA00013169};
DE EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
GN ORFNames=A2649_03280 {ECO:0000313|EMBL:OGM98285.1};
OS Candidatus Yanofskybacteria bacterium RIFCSPHIGHO2_01_FULL_41_26.
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1802661 {ECO:0000313|EMBL:OGM98285.1, ECO:0000313|Proteomes:UP000176893};
RN [1] {ECO:0000313|EMBL:OGM98285.1, ECO:0000313|Proteomes:UP000176893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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};
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:OGM98285.1}.
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DR EMBL; MGJB01000017; OGM98285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8EE82; -.
DR STRING; 1802661.A2649_03280; -.
DR Proteomes; UP000176893; Unassembled WGS sequence.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR CDD; cd00817; ValRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; 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 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.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OGM98285.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 17..555
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 605..719
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 720 AA; 83087 MW; E530FD4F5FBF38F5 CRC64;
MSIELLKTYN PKEVEDKIYK LWKESGFFNP DNLPKRHQNP FTIIMPPTNA NGSLHAGHGL
VMTIEDIMIR YKRMRGYKTL WLPGLDHAGF ETQVVYEKQL EKEGRSRFQM DPKELYKEIL
DFTLNNKKNI KGQIPKIGSS CDWSREKFTL DGDIVKTVYK IFEKMAKDGL VYRGKKVINW
CPKHQTSLSD LETADTEQVD NFYYLQYGPF VIATARPETK FGDKYVVMHP NDERYKKYKN
GQKIKLEWIN GPITATIIKD EAIDMTFGTG VMTITPWHDS TDFEIAERHN LEKEQIIDFR
GKLLPIAGEF VGISIKEARP LIIEKLKSKG LLVKIDENYK HVVKKCYKCE SIIEPQIKDQ
WFIKMKPLAE PAIKTIEDGD IEYIPEHYKK ISLHWLKNII DWNVSRQIVW GIPIPAKICI
KCDEGIVDID NKISVCPKCG GDVRQETDTF DTWFSSGQWP FASLGFPDSK DYKEFFPTDV
METAGEIIFF WVARMIMFSL YVTGKIPFKT VYLHGLVLDA KGQKMSKSKG NVINPLDLTE
KYGTDAFRIG LVVGNTPGTS LALAEDKIKG YKHFGNKLWN IARFVLMSLP DDMSTVLKSP
LTPEDQKLID ELNVSMKEIT DDMDQYRFYL AAEKIYHYTW HAFADKIIEE SKAKLASEDE
KIRTSAQRML IEILTTCLKT LHPFMPFITE EIYSKLPLHP PPPERADGGK KLLMIEDWPV
//