ID A0A024GRQ9_9STRA Unreviewed; 1010 AA.
AC A0A024GRQ9;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, 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=BN9_105410 {ECO:0000313|EMBL:CCI49259.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI49259.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI49259.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI49259.1,
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:CCI49259.1}.
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; CAIX01000284; CCI49259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024GRQ9; -.
DR STRING; 65357.A0A024GRQ9; -.
DR InParanoid; A0A024GRQ9; -.
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..656
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 705..855
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1010 AA; 116119 MW; 343F9020B2986480 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 ALLPLSSNGP YPLSLMETGS
DILFFWVARM MMLCEELSGT IPFKKILLHP MVRDKSGRKM SKSLGNVMDP LHVIHGATLE
QLLHEVKHGN LPDREREIAE KTLRQEFPNG LPQCGADALR LTLTSYLQQG RQINIDVNRV
ISYRHICNKI WNAVRYALPL LKANDQCLTE RIALEDVRDQ MTISDRWILS RLARSVEACN
LGLSTNRFAS SVAAIHQFFV QDLCDVYIEF SKSILYQSHT DTSASDCDAK KRKLCALTTL
LECLECSMRL LHPFAPFLTE ELWQRLNLYK TSETSDLNSI LSAAYPTKEN AKFWIDVRAE
TSFEIVLDVL RGLRSLVQTF RKVTGLNTNK MGVILACKDI EMLRMLQQYK HSIESQAKVV
IHLKLDTEKF ADSEAILTYN ATNKCQVLIP VPKSKDIMGR VAAEAERLDK RLGKCKMTID
QLTLQVKQPH YASQVPEDVQ AQSSNRLAKL KIELTALRKS LDAIEFLRQN
//
