ID A0A1G2VVZ4_9BACT Unreviewed; 781 AA.
AC A0A1G2VVZ4;
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=A2542_03740 {ECO:0000313|EMBL:OHB25761.1};
OS Parcubacteria group bacterium RIFOXYD2_FULL_52_8.
OC Bacteria.
OX NCBI_TaxID=1817746 {ECO:0000313|EMBL:OHB25761.1, ECO:0000313|Proteomes:UP000177816};
RN [1] {ECO:0000313|EMBL:OHB25761.1, ECO:0000313|Proteomes:UP000177816}
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:OHB25761.1}.
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DR EMBL; MHXK01000006; OHB25761.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2VVZ4; -.
DR Proteomes; UP000177816; 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 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:OHB25761.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 12..565
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 607..750
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 781 AA; 90216 MW; 1056B23A5C67D972 CRC64;
MEYNLKEIEE RWRAWWEKEK IYAFTFDPSK PVYSVDTPPP YVSADHLHAG HIMSYAQAEF
IVRYKRMRGF NVYYPMGFDD NGLPTERFVE KKYNVDKSKI TRSEFIKLCL KETELGAQTY
RDLWNALGIS VDWSKTYSTI SPLATKVSQW SLIDLYKKGV LYRAESPILW CTFCRTALAQ
ADIEDRERIG KMNHIVFKGP NQEKLIIATT RPELLPACVG LYVHPDDARY KNIIGKEATV
PLFKHNVPIK TSTKVDPAFG TGLMMVCTWG DQEDVEKWRE DKLETRVLFT EDGKLSDLGA
QFAELSITDA RTKIIEALQE SGELEKQEDL EQTVKVHERC EVPTEFILSK QWFIKIADQK
ETWLEYGKKL KWYPADREQD YIRWVESLKW DWCVSRQRYY GVPLPIWYCT GCDEPIFASE
KDLPVNPPED AAPIDICPKC GSKEIIAEKD VMDTWATSSC TPFMIRDLVD DPQARAKLFP
TTLRPNAFEI IRTWDFYSVV KSHYHFGHIP FEDVMISGHG LDAEGKKFAK RLGNYIPSNE
LVEKYHADPI RYWATGAMLG QNLRFSLQEI EKGKKTVIKL SNVAKFLQIH LEDFDGTQAI
PKLEHADAWI IQETNSALKK ATEAFEQYAY AKSRDAIDEL FWSKFTDYYL EFVKYRLNGA
EAESKQAACH TLRTVFLAIL KMYAPVLPFI TEEVYSQLFA TQEGSKSIHL SAWPEQIEIT
YSLDVSDFNN AIEAVNEIRK HKSNQGLPLG TILESYQLKT KVDIGKYGDF IRGAIRVKLL
Q
//
