ID A0A0G1YL55_9BACT Unreviewed; 913 AA.
AC A0A0G1YL55;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=UY56_C0027G0004 {ECO:0000313|EMBL:KKW15737.1};
OS Parcubacteria group bacterium GW2011_GWA1_50_14.
OC Bacteria.
OX NCBI_TaxID=1618798 {ECO:0000313|EMBL:KKW15737.1, ECO:0000313|Proteomes:UP000034143};
RN [1] {ECO:0000313|EMBL:KKW15737.1, ECO:0000313|Proteomes:UP000034143}
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:KKW15737.1}.
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; LCQL01000027; KKW15737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1YL55; -.
DR PATRIC; fig|1618798.3.peg.473; -.
DR Proteomes; UP000034143; 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; 3.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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; IPR015947; PUA-like_sf.
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 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; SSF88697; PUA domain-like; 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 36..482
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 620..752
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 806..910
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 913 AA; 105845 MW; 371E83A9FCFF0D6D CRC64;
MPEQLEPRYD HLKTEEKIYR LWEESGFFDP DRLEKAYSKW HKANKKNQNK KPSAIGHKPF
AIIMPPPNAN GSLHIGHAVG ITLEDIMVRF ARMRGKRTLW LPGADHAGFE TQVVFDKKLD
KEGRNSDALH GRSSDTEGRR SRFTMNREEL WEEIWEFTQK NKKVMENQLR KLGASCDWSR
EKFTLDPDII KTVYETFEQL YKDGLVYRDL KVVNWCPKHK TALSDLEVKY VEREDPLYYI
KYGPLTLATV RPETKFGDTA LAVNPKDKRY QKYIGKEIEA QGVLGPLKFK VIADDAIDPK
FGTGVVKVTP AHDPLDFEIW QRHKSEIPGP KIIIDESGRL TGEVGEFKGL KVPEAREKVA
ERMKELGILE KVDQNYNHQV ATCYKCGNTL EPLPKPQWFI AMTKPLRNQK SKIKNQKSGK
SLRDLGVDAV KSGKIKIYPK RTEKVYMHWL KNIRDWNISR QIVWGIRIPA WFRNKQKTKI
WDLKTYDGEK IFEALKNGKK RVETRAGKPD GAEKDWRNFK IGDVINFSLV EEGTERVLSS
EVITKEIVSI HHFQTIDKLL LRFDVNEIHP YHPNEYRNWW ESRPVFKERI KKYGIWAFEL
QDINEKTQEV YVGIAPPSGE GWTQDPDVFD TWFSSGQWPY ATLMSHASSK SQAPNSRQKS
DFEEFYPTDV METGYDILFF WVARMIMLGL YRTGKVPFKN VYLHGLVRDK DRQKMSKSKG
NVVDPLGVAE MYGVDALRMA LVVGNTPGND IVISEDKIRG YRNFATKIWN ASRFVLMNSP
SQILGKTWEG KPAKLSTKDK KNIAGAKKMK AAVAKHIEKF EFHLAAEKAY HYFWHTFADK
IIEETKLRLQ NGTPEEKAAA YSGLETILRE SLKMLHPFMP FITEEIYQKL PPSLISKETN
EGKRTKLLLV EKW
//
