ID A0A1F6XZ77_9BACT Unreviewed; 737 AA.
AC A0A1F6XZ77;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=A3H53_01560 {ECO:0000313|EMBL:OGI99404.1};
OS Candidatus Nomurabacteria bacterium RIFCSPLOWO2_02_FULL_40_10.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801786 {ECO:0000313|EMBL:OGI99404.1, ECO:0000313|Proteomes:UP000176479};
RN [1] {ECO:0000313|EMBL:OGI99404.1, ECO:0000313|Proteomes:UP000176479}
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:OGI99404.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MFVK01000023; OGI99404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6XZ77; -.
DR Proteomes; UP000176479; 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:OGI99404.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 18..591
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 636..735
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 737 AA; 85921 MW; 4F1CAAEE62326D4B CRC64;
MGEKLKKPYN PKETEERIYK LWEDSGFFNP DVCIEKGATR ADAPHFSIVL PPPNVTGNLH
TGHALMLVIQ DIMVRFERMQ GKKTLWLPGT DHAAIATQSK VEKLLEKEGL RKNDLGREEF
LKRVEKFAQE SHDTIVSQCK KMGASLDWSR EAFTLDEKRN LAIKTAFKKM YDDGLIYRGH
RIVNWDPKGQ TVISDDEIVY EERKSKIYTF KYGPFEIYTV RPETKFGDKY VVMHPDDKRY
KKWKHLDKIT VEWINGSIEA TIIKDEMMDM EFGTGVMTIT PSHSHADFLL AEKYKLDKEQ
IIDKFGKLLP VAQEFVGMKI SDAREKIVEK LKAKGLLVSV DENYVNRVAT AERTGGIIEP
QIMLQWFVDV NKKISSRNNK SLKELMLEPV RGKKIKIIPN HFEKVYFNWI ENLRDWCISR
QIWYGHRIPV WYHEPICIPK TGKEKEISKC VEIIVSEKKP VCKYCDAHYT QDEDTLDTWF
SSGLWTFSTL GWPKETKDLK TYHPTSVLET GHDILFFWVA RMILMSQYLL DEVPFENVYL
HGMVRTKDGK KMSKSLGEKA IDPLDIIKKY GNDALRMAMI VGNTPGNDLK LDENDIRGYG
KFANKIWNAA RFVLEQTKDL NLENLPKLDE EDKKSDKELQ KILAEVSKEM EEFKFSIVAE
KLYHYFWHTF ADIIIERSKK KILENKNADS AKVLLFTHLT TLLKALHPFM PFVTEEIWSM
MPEQKNLLMV EKWPSND
//
