ID A0A024GRA1_9STRA Unreviewed; 1019 AA.
AC A0A024GRA1;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=BN9_105450 {ECO:0000313|EMBL:CCI49263.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI49263.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI49263.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI49263.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00005594, 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:CCI49263.1}.
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DR EMBL; CAIX01000284; CCI49263.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024GRA1; -.
DR STRING; 65357.A0A024GRA1; -.
DR InParanoid; A0A024GRA1; -.
DR Proteomes; UP000053237; 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 Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal 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; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR NCBIfam; TIGR00422; valS; 1.
DR PANTHER; PTHR11946:SF109; VALINE--TRNA LIGASE; 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.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053237}.
FT DOMAIN 53..600
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 710..864
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1019 AA; 117221 MW; 060D888ED21086CC CRC64;
MQWCRRATCW RLKEPTRFHR SLFSLPDSIY ERVRRKPLAA NYDPIAVESG WTQFWQQELS
DSGKQKTSQR LFSLLLPPPN ITGSLHIGHA LTVTIQDALI RWHRMQGKNV SWIPGLDHAG
IATQSVVERN LLKKDVKRHD LGREEFIQNT WSWKKRFGSR ILDQMEQLGT RLDRQKLYFT
LDEKRSHAVK MAFVQLYEKG LIFRQRRMIN WCPFLNTALS DVEVELKSIE KPTRILLPGS
MTSVEFGVIY RIRYEVAGHP GTYLEVDTTR PETIFGDVAV AIHPQDARYE AFHRGHVIHP
FTKDRIPIVL DDTLVDMQLG TVTPSHDAND FECGQRHELP ERPVLDQKGC MYGQVPSEYL
GLDRFKARTQ VIEDLERMNL YVGKVNHPTT IRICSRSGDL IEPLLMPQWF ISVHAMAKRA
SSNVREGIVD IEPKHHMSTW FHFLDNAHDW CISRQLWWGH RIPAYRVQSQ RISNADHDDA
WIVAASVEEA LAQAEKKYKQ PFVEADLVQD EDVLDTWFSS ALLPLSSNVG GPYPLSLMET
GSDILFFWVA RMMMLCEELS GTIPFKKILL HPMVRDKSGR KMSKSLGNVM DPLHVIHGAT
LEQLLHEVKH GNLPDREREI AEKTLRQEFP NGLPHKVDHD FPFLDPFSIN IRIPGRQINI
DVNRVISYRH ICNKIWNAVR YALPLLKAND QCLTERIALE DVRDQMTISD RWILSRLVSA
AYEIVEACNL GLSTNRFASS VAAIHQFFVQ DLCDVYIEFS KSILYQSHTD TSASDCDAKK
RKLCALTTLL ECLECSMRLL HPFAPFLTEE LWQRLNLYKT SETSDLNSIL SAAYPTKENA
KFWIDVRAET SFEIVLDVLR GLRSLVQTFR KVTGLNTNKM GVILACKDIE MLRMLQQYKH
SIESQAKVVI HLKLDTEKFA DSEAILTYNA TNKCQVLIPV PKSKDIMGRV AAEAERLDKR
LGKCKMTIDQ LTLQVKQPHY ASQVPEDVQA QSSNRLAKLK IELTALRKSL DAIEFLRQN
//
