ID A0A0V1MJS4_9BILA Unreviewed; 1045 AA.
AC A0A0V1MJS4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 Name=VARS {ECO:0000313|EMBL:KRZ71820.1};
GN ORFNames=T10_6498 {ECO:0000313|EMBL:KRZ71820.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ71820.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ71820.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ71820.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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}.
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:KRZ71820.1}.
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DR EMBL; JYDO01000089; KRZ71820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1MJS4; -.
DR STRING; 268474.A0A0V1MJS4; -.
DR Proteomes; UP000054843; 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; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
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; 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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KRZ71820.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000054843}.
FT DOMAIN 97..716
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 761..911
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1045 AA; 119600 MW; 9C3ABE178447E9ED CRC64;
MVNPDQANSL HSEATSNKKE KDKIKDAKKQ AKLEKFQQKQ QMLAQKLEMA KSKSDVPIKE
KTKEIITYDM PTLAGEKKDV SCEMPKSYSP KYVEACWYDW WEKSGFFKPE FEHKNKRRQS
EKFVMVIPPP NVTGTCHLGH ALTISIEDAV TRRTVLWNPG CDHAGIATQV VVEKKIWRES
KQTRHHLGRE AFLKQVWSWK NEKGDTIYKQ LKVLGSSLDW DRACFTMDEK MCHAVTEAFV
RLHETGNIYR SVRLVNWSCV LRSAISDIEV VDKIELTGRT MLTVPGYDEQ VEFGVLVHFA
YPVINSDERI VVATTRVETM LGDVAIAVHP DDIRYKHLVG KECQHPFLDR KLPIVSHSFV
DMSFGTGAVK ITPAHDQNDY EVGQRLNLPF ISCINDEGLM EAWCGRFAGM KRFHARKAVL
QELKAIGLFV TMAENPMVVP VCNRSKDIVE PLLKAQWYVK CDEMAQNAAA AVQNGDMRII
PNIHEKTWYK WMSGIRDWCI SRQLWWGHRI PAYFVSIKGR EKGNDACDDS WVVARTEAEA
MQKAIKKFNV AQSEITLHQD EDVLDTWFSS ALFPISIFGW PNQTKDLKEF YPGTLLETGY
DILFFWVAKM VFLCQNLTGK LPFTDIYLHS VIRDAHGRKM SKSLGNVIDP LDVINGISLE
KLHNKLLSSN LDPAEVQRAK EGQKRDYPNG IPECGTDALR FALCAYAAQG RDINLDVLRI
QGYRHFCNKI WNACRFVMMT LGKDFEAEPE FKVNKMATEV DLWILSRLST AVRLCNDAFE
NYEFSKATTA CYNFWLYELC DVYLECIKPV MRDADPEVQS ATKRVLCFCV DSALRLIAPF
MPFIAEELWQ RLPAGGHDKR LSICVAPYPE SEQYNWADIT VDNRIQFAMS VVKAVRSLRA
SFDLTAKTKL DCIYVLSNDS EMADDLKRCA EMIAVLSTCN SVKINSNEYP LKGCVRFPVS
DKCRIILPIE GVVDISKELK KLSVKKQKIQ VQMEQLLEQM KGEDYLKTPE HIRYANEQKY
LEFDNALEEI IATESALRVS AEDAE
//
