ID A0A024GQT5_9STRA Unreviewed; 1024 AA.
AC A0A024GQT5;
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_105470 {ECO:0000313|EMBL:CCI49265.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI49265.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI49265.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI49265.1,
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:CCI49265.1}.
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DR EMBL; CAIX01000284; CCI49265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024GQT5; -.
DR STRING; 65357.A0A024GQT5; -.
DR InParanoid; A0A024GQT5; -.
DR OrthoDB; 5473263at2759; -.
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 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; 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..605
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 715..869
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1024 AA; 117704 MW; 3E0217838CC4FD89 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 RIRYEVVAGH PGTYLEVDTT RPETIFGDVA VAIHPQDARY EAFHRGHVIH
PFTKDRIPIV LDDTLVDMQL GTGVVKVTPS HDANDFECGQ RHELPERPVL DQKGCMYGQV
PSEYLGLDRF KARTQVIEDL ERMNLYVGKV NHPTTIRICS RSGDLIEPLL MPQWFISVHA
MAKRASSNVR EGIVDIEPKH HMSTWFHFLD NAHDWCISRQ LWWGHRIPAY RVQSQRISNA
DHDDAWIVAA SVEEALAQAE KKYKQPFVEA DLVQDEDVLD TWFSSALLPL SSNVGGPYPL
SLMETGSDIL FFWVARMMML CEELSGTIPF KKILLHPMVR DKSGRKMSKS LGNVMDPLHV
IHGATLEQLL HEVKHGNLPD REREIAEKTL RQEFPNGLPH KVDHDFPFLD PFSINIRIPG
RQINIDVNRV ISYRHICNKI WNAVRYALPL LKANDQCLTE RIALEDVRDQ MTISDRWILS
RLVSAAYEIV EACNLGLSTN RFASSVAAIH QFFVQDLCDV YIEFSKSILY QSHTDTSASD
CDAKKRKLCA LTTLLECLEC SMRLLHPFAP FLTEELWQRL NLYKTSETSD LNSILSAAYP
TKENAKFWID VRAETSFEIV LDVLRGLRSL VQTFRKVTGL NTNKMGVILA CKDIEMLRML
QQYKHSIESQ AKVVIHLKLD TEKFADSEAI LTYNATNKCQ VLIPVPKSKD IMGRVAAEAE
RLDKRLGKCK MTIDQLTLQV KQPHYASQVP EDVQAQSSNR LAKLKIELTA LRKSLDAIEF
LRQN
//
