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Database: UniProt
Entry: A0A0G1N4S3_9BACT
LinkDB: A0A0G1N4S3_9BACT
Original site: A0A0G1N4S3_9BACT 
ID   A0A0G1N4S3_9BACT        Unreviewed;       744 AA.
AC   A0A0G1N4S3;
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=UW89_C0012G0012 {ECO:0000313|EMBL:KKT88072.1};
OS   Parcubacteria group bacterium GW2011_GWB1_45_10.
OC   Bacteria.
OX   NCBI_TaxID=1618877 {ECO:0000313|EMBL:KKT88072.1, ECO:0000313|Proteomes:UP000033817};
RN   [1] {ECO:0000313|EMBL:KKT88072.1, ECO:0000313|Proteomes:UP000033817}
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   -!- 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:KKT88072.1}.
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DR   EMBL; LCKC01000012; KKT88072.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1N4S3; -.
DR   STRING; 1618877.UW89_C0012G0012; -.
DR   PATRIC; fig|1618877.3.peg.386; -.
DR   Proteomes; UP000033817; 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:KKT88072.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          17..592
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          642..743
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   744 AA;  85687 MW;  812295CF70906271 CRC64;
     MAGELEKNFE PKGVEEKIYS LWEKENVFTP KIDKKKKPFT IILPLPNAND PMHMGHGMFV
     IEDILTRYHI MKGDPTLWLP GADHAGIETQ FVFEKKLAKE GKSRFDFDRE TLFEKLKEFV
     EENRLTNKDQ LKRLGFALDW SRYHYSMEPE IVERVLETFM KLHKDGLIYR GERVVHYCTK
     CGTSFSDLEV LYEEREDKLY YLDYGPIIIA TTRPETIFAD VAVAINPKHK KIKELKGAEA
     IIPLINKKIP VIQDELVDLE FGTGALKITP GHDAVDFEIG SKHRLKTISV VDRSGKMVNV
     PEKYLGLKVL KAREETIKDL KAAGKLVKEE PLKHSVGTCY RCGTVIEPMV FPQWFVKTKP
     LAEPAIKAVK NGETKIFPQK RFEKMYFDWM ENIKDWNISR QIVWGPRIPA WYCLDCNDSI
     RINFLNKKKE VVSGPYKEIK QSYSFEEIKS GLQSLFSTGD ATYQLKDGSC QKCGGPNVIQ
     ETDTFDTWFL SGQWPVNTLK ANPGDLEYFY PTSVLDTLWD ILFFWAGRMM MVGLYLTGKV
     PFRVIHLHAR VVDKFGKKMS KSKGNVIDPL VMVNQYGADA LRLALVLGVG PASDVSLSDE
     KVRGMRNFTN KLWNIGRFII MSSKEQGFQR FEPGMPGLEE VDRAIIESLN KLVKQTTKML
     DNYRFGQASE ELFQFIWHEF ADVYIEQSKQ RIKSGDKTVL AVLFHVYSVC LKLLHPFMPF
     ITEAVWQKMF AKNNSLLIKE SWPS
//
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