ID A0A0G1ELR7_9BACT Unreviewed; 718 AA.
AC A0A0G1ELR7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=UV91_C0009G0008 {ECO:0000313|EMBL:KKT11001.1};
OS Candidatus Nomurabacteria bacterium GW2011_GWF2_43_24.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1618778 {ECO:0000313|EMBL:KKT11001.1, ECO:0000313|Proteomes:UP000033907};
RN [1] {ECO:0000313|EMBL:KKT11001.1, ECO:0000313|Proteomes:UP000033907}
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:KKT11001.1}.
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DR EMBL; LCGH01000009; KKT11001.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1ELR7; -.
DR PATRIC; fig|1618778.3.peg.560; -.
DR Proteomes; UP000033907; 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 CDD; cd00817; ValRS_core; 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; 2.
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..443
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 453..565
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 620..717
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 718 AA; 83767 MW; AABC1B32571F0D04 CRC64;
MDEKLLKPYD PKNTEERIYK LWEESGFFAP EAHPPWVDNP STNPNFREPF TIVLPPPNAT
GVLHLGHTLE VSMQDTMIRY NRMQGKKTLW LPGTDHAAIA TDSKVTKILE KEGLRKKDIG
REKFLKRVEE FVEESRKIIA SQLRKIGASL DWSREAFTLD DKRNLAVRTA FKQMYDDGLI
YRSHRIVNWD PKGQTVISDD EIVYEERKTK FYTFKYGPFE IGTARPETKF GDKYVVMHPN
DKRYKKWKHG DKMTVEWING LIQATVVKDE MIDMEFGTGV MTITPWHSHE DFVLAEKYKL
EKEQIIDRYG KLLPIAGEFA GMKIADAREK VIEKLKTKGL LVSIDENYVN RIATAERTGG
IIEPQIMLQW FVDVNKKIKS RGDKSLKELM LKPVREGKIK ILPEHFEKVY FNWLENLRDW
CISRQIWYGH RIPVWYLNNE VYCGIDAPKE SGWVQDEDTL DTWFSSGLWT FSTLGWPEKT
EDLKNFHPTS VINPGYEILF FWVARMILMS QYLIGEIPFK TVYLHGILRD AKGQKFSKSL
GNGVDPIEVI ETYGADALRM AMIVGIGPGA DSKFDIQKVK AYGKFSNKIW NATRFVLDNV
QNFDLLSPVV YDEEDKKSDE ELKALIKEIT KEMDEYKFYI VAEKLYHYFW HTFADVIIER
SKKKILENRN ADSAKRLFYT QLTILLTALH PFMPFITEEI WSMLPESKGL LMVKKWPS
//
