ID A0A0G0TS86_9BACT Unreviewed; 753 AA.
AC A0A0G0TS86;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=UU25_C0007G0022 {ECO:0000313|EMBL:KKR79818.1};
OS Microgenomates group bacterium GW2011_GWB1_40_9.
OC Bacteria.
OX NCBI_TaxID=1618504 {ECO:0000313|EMBL:KKR79818.1, ECO:0000313|Proteomes:UP000034379};
RN [1] {ECO:0000313|EMBL:KKR79818.1, ECO:0000313|Proteomes:UP000034379}
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:KKR79818.1}.
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DR EMBL; LBZX01000007; KKR79818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0TS86; -.
DR PATRIC; fig|1618504.3.peg.178; -.
DR Proteomes; UP000034379; 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 32..607
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 646..748
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 753 AA; 86585 MW; 8F7F975AE47AFF2F CRC64;
MDKAYIPKTV EQDVYLLWEK GSPSLGYGGA SGYFTPTINL KKRPFSILLP LPNANDPMHM
GHAMFIVQDI LIRYHRMKGD PTLWLPGGDH AGIETQFVFE KKLAREGKSR FDYDRDTLYK
MIAEFVDANK NINRDQMKRL GFSLDWTRYH YSLEPKIIEQ VLKTFVKLHE DKLLYRAEKL
VNYCTKCGTS FSDLEVKHVE QIDKLYYMKY GPFILATTRP ETKFGDTAVA VHPKDKRYQE
WIGKEIEFEG LNGKVKLTVV ADDVVDPAFG TGVVKVTPAH DMTDYEIGIR HKLPMKQVIG
LDGKLTSLAG PYAGLRVKAA REKVVADLTA RGMIDHIDEV YVHSVGTCYK CGTILEPLPL
PQWFVKTKPL AEKAITVVKE GKTKIVPLKR FEKLYFDWLT TIHDWNISRQ IVWGPRIPVW
YCVDCNKNIK LAFIDAKGKK NIGTYEELKP TYSFDEIVQG LQSVIAPIVA TYELQHDVCG
KCHGKNLIQE TDTFDTWFLS GQWPLTTLGY PEGQDFKYFY PTSVLDTMWD ILFFWVARMM
MFGLYLTGKP PFEIIHLHSR VVDSKGQKMS KSKGNVVNPI ELVDTYGADA LRMALTFGAA
PGSDISLSED KVRGMRNFAN KLWNIARLFL MNMEGMTKEL PEQSKDTEIM KKLHTVVVDV
TKYIEKYRFS DAAQTIYEFT WHTVADSYLE ENKELFKQKN LQALADYQYI LIHILKLLHP
FMPFVTESIW GQISRKHDQP LIISSWPLLN RSE
//
