ID A0A0G0NJS6_9BACT Unreviewed; 718 AA.
AC A0A0G0NJS6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=UT41_C0001G0625 {ECO:0000313|EMBL:KKR13081.1};
OS Candidatus Wolfebacteria bacterium GW2011_GWC2_39_22.
OC Bacteria; Candidatus Wolfebacteria.
OX NCBI_TaxID=1619013 {ECO:0000313|EMBL:KKR13081.1, ECO:0000313|Proteomes:UP000034665};
RN [1] {ECO:0000313|EMBL:KKR13081.1, ECO:0000313|Proteomes:UP000034665}
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 -!- 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 -!- 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:KKR13081.1}.
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DR EMBL; LBWR01000001; KKR13081.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0NJS6; -.
DR STRING; 1619013.UT41_C0001G0625; -.
DR PATRIC; fig|1619013.3.peg.648; -.
DR Proteomes; UP000034665; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.620; HUPs; 2.
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; 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.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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 18..572
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 614..718
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 718 AA; 82228 MW; 1E69EB3D5A5B6812 CRC64;
MNELFNKPYE AKEFEEAIYK QWEESGYFNP DNLPERKDDK GPFTIIMPPP NANGHLHAGH
ALFITLEDII TRYKRMRGYK ALWIPGADHA GFETQVVYEK KLEKEGRSRF KMDPQELFDE
IMAFTLENKQ YMEQEVKRMG ASCDWSRERF TLDADIMKKV QGTFAKMYED GLVYRGLRTV
NWCTKHQTSL SDVETESVEK MDKLYYIKYG PFVVATVRPE TIFGDVAVAV NPNDDRYKQY
IGSVIEVENP NGKLILKVIG DDSVDIEFGT GALKVTPAHD NNDFALAQKH GLEHIITIDQ
FGKLNEKAGK YAGMKIAEAR EKVVADLEVM GLIEKIEDYK HQVPTCYKCS TTIEPRLLPQ
WFVKMSSQGG SASGGQSLAE MAAKAVDDGR IEFIPDNYRK IFLYWMNNTI DWNISRQIVW
GIPIPAKLCN ECDFAAPDLE DEISACPKCG GEVRKDADTF DTWFSSGQWP LLTLDFPDGK
DFKTYYPTDV METGHDLIFK WIPRMVIFGL YLANEVPFKT VYMHGLVNDA KGKKMSKSKG
NVINPIDLID KFGTDALRMG LIIGNTPGND TALDENKIKG YRNFANKIWQ ATRFVLMNSE
GVDFTKTPTL TDRDKEVLEE LRVVKEQTTK ELDNFLIHLA AENLYHYFWH TFADKIIEEN
KGRLKGEDEV DKYAAQYVLN EILRTSIKML HPLMPFITEE IYGNLPGNDG KILMVEEW
//
