ID A0A0G0QCH9_9BACT Unreviewed; 555 AA.
AC A0A0G0QCH9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
DE Flags: Fragment;
GN ORFNames=UT72_C0031G0005 {ECO:0000313|EMBL:KKR37853.1};
OS Candidatus Woesebacteria bacterium GW2011_GWB1_40_101.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618575 {ECO:0000313|EMBL:KKR37853.1, ECO:0000313|Proteomes:UP000034687};
RN [1] {ECO:0000313|EMBL:KKR37853.1, ECO:0000313|Proteomes:UP000034687}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|RuleBase:RU363035}.
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:KKR37853.1}.
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DR EMBL; LBXW01000031; KKR37853.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0QCH9; -.
DR PATRIC; fig|1618575.3.peg.354; -.
DR Proteomes; UP000034687; 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; cd00817; ValRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
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|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035}.
FT DOMAIN 2..511
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT NON_TER 555
FT /evidence="ECO:0000313|EMBL:KKR37853.1"
SQ SEQUENCE 555 AA; 63555 MW; 74915D185EC00A97 CRC64;
MPPPNANNPL HIGHAREVAT QDILIRYHRM KGEPTLWLPG ADHAGIETQY VFEKRLAKEG
KSRFDYDRDT LYKMIWDYVQ KNKSTMENQL RILGASCDWT RNKFTLDPEI LKVVYKTFKN
LYKDGLVYRG ERIVNYCPRC GTAYSQLEVD SLEREDNLYY LDYGRITIAT TRPETIFADV
AVAVNPEDKR YKDLVEKTAR IPIINREIPI IADVLVDKSF GSGALKITPG HDAVDFEIGQ
KHKLPVVSVI DENGKMTNTP EKYTGMKALA AREEVVADLE KAGAIKKIEK IKHVVGVCYR
DKGLIEPTIS KQWFIKIEPL AKTALVAIRN GKVKFTAKKF EKIAKHWLKN LRDWNISRQI
VWGIRIPAFR CEKCLSWTVT DGTRPVECAT CKHTKLTQDT DTFDTWFSSA QWPFATLQTS
KPEDFEYFYP TSVIDPAYDI LPFWVIRMIM LGLYETKNVP FENVLLHGLV RDKYGVKISK
SKGNIIDPIE MVDKYGADAL RTALIWGALV ENDNSLSEEN VKGQRNFANK IWNVARFVLQ
NDILPSTISH QPLAI
//
