ID A0A024GR56_9STRA Unreviewed; 1020 AA.
AC A0A024GR56;
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_105540 {ECO:0000313|EMBL:CCI49272.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI49272.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI49272.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI49272.1,
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:CCI49272.1}.
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; CCI49272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024GR56; -.
DR STRING; 65357.A0A024GR56; -.
DR InParanoid; A0A024GR56; -.
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..865
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1020 AA; 117284 MW; 0F4A7DA81D74FB18 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
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
//
