ID A0AAD5KWJ3_9CRUS Unreviewed; 991 AA.
AC A0AAD5KWJ3;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 7.
DE RecName: Full=Valine--tRNA ligase {ECO:0000256|ARBA:ARBA00024407};
DE EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
GN ORFNames=GHT06_002302 {ECO:0000313|EMBL:KAI9551276.1};
OS Daphnia sinensis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia;
OC Daphnia similis group.
OX NCBI_TaxID=1820382 {ECO:0000313|EMBL:KAI9551276.1, ECO:0000313|Proteomes:UP000820818};
RN [1] {ECO:0000313|EMBL:KAI9551276.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WSL {ECO:0000313|EMBL:KAI9551276.1};
RA Jia J.;
RT "A multi-omics perspective on studying reproductive biology in Daphnia
RT sinensis.";
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tRNA(Val) + L-valine + ATP = L-valyl-tRNA(Val) + AMP +
CC diphosphate; 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:ARBA00047552};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KAI9551276.1}.
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DR EMBL; WJBH02000021; KAI9551276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAD5KWJ3; -.
DR Proteomes; UP000820818; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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 FunFam; 3.40.50.620:FF:000020; Valine--tRNA ligase, mitochondrial; 1.
DR FunFam; 3.40.50.620:FF:000078; Valine--tRNA ligase, mitochondrial; 1.
DR FunFam; 3.90.740.10:FF:000005; Valine--tRNA ligase, mitochondrial; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
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 HAMAP; MF_02004; Val_tRNA_synth_type1; 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; NF004349; PRK05729.1; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000820818}.
FT DOMAIN 45..649
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 708..862
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT COILED 926..956
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 991 AA; 113720 MW; DF02458F2EF5E6A1 CRC64;
MLKVARRRIL LLSSRPLTTA KLQLPKNVKD EMPKAYSPAI VEINWYEWWE GNSFFSHHKP
QPSTKKFSMV LPPPNITGTL HIGHALTCAI QDSLVCWNRM KGKDTHWFPG CDHAGIATQV
IVEKNLKSQN MTREQLGRKR FEEEVWKWKD EKEKTIYQQL KALGATLNWE KAVFTMDPKM
CYAVNEAFIQ LHRKGKIYRK ESLVNWSCQL RSAISDIEVD HQLVDGPKGI LVPGYDKPVT
FGYIYQFEYK LWDSTERIMV STTRPETIIG DMAVAVHPED MRYKQYIGRS VIHPVLHTKL
PVIADPEVDQ QFGTGALKVT PAHDPKDYEI AKRHGLEMFS IFDDRGISNK NCNQFHGLPR
FELREKMINF LRDNDLLRGI MPHQMSVPVC SRSGDIIEPL LRPQWFVDTQ EMAQKAMEAV
QSGKLKIYPP QFERVWFEWL GNIKDWCISR QLWWGHRVPA YNIAGPKETA IWIAAHNTEK
AVEHAKNQGF DFSAVHQDED VLDTWFSSSL FPFSVCGWPE DTADLRKLFP LDLMETGHDI
LFFWVARMVM MSLELTGELP FKEILLHGII CDSQGRKMSK SLGNVIDPLD IVYGASLKCM
EDKLESSFQK KHLSSKEFEK AIAEKRTAFP SGIPQTGADA LRFTLCSYNV KSHFINLDMA
ILKRNRLFCN KIWQATRFLF RLLDDIPPKT GSDSFSWLNE PNNSSLVNQW IMNGLAEMVN
QIDGAMTRYD FHQATDALYN FLYGNLCDVY LEAIKPLIGK DRQESALVLV VCLDTALRCL
VPFMPFLSEE LYQRLHSKLA DLGIPSSRSV SVLVAEYPSK DEFALWRNEE LEKTIDSVLR
AVTELRNMKL EYGLAKSKPD AVFVCPSERV LSQVDQYSKL MSTIAGLNVT IYGDICLTNS
SEKAWVSRTV ENCSVHLNLA GMIDRNMELK KNQEKLKKLV ENLARLEANM STASYRSSAP
AHVQETHRLK VAFLQTEICQ LKEYAKELDK M
//
