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Database: UniProt
Entry: A0A915A9X0_PARUN
LinkDB: A0A915A9X0_PARUN
Original site: A0A915A9X0_PARUN 
ID   A0A915A9X0_PARUN        Unreviewed;      1001 AA.
AC   A0A915A9X0;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   28-JAN-2026, entry version 11.
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};
OS   Parascaris univalens (Nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Parascaris.
OX   NCBI_TaxID=6257 {ECO:0000313|Proteomes:UP000887569, ECO:0000313|WBParaSite:PgR002_g282_t01};
RN   [1] {ECO:0000313|WBParaSite:PgR002_g282_t01}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2022) to UniProtKB.
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   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR   AlphaFoldDB; A0A915A9X0; -.
DR   WBParaSite; PgR002_g282_t01; PgR002_g282_t01; PgR002_g282.
DR   Proteomes; UP000887569; Unplaced.
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:000119; Putative valine--tRNA ligase-like; 1.
DR   FunFam; 1.10.730.10:FF:000009; Valine--tRNA ligase, mitochondrial; 1.
DR   FunFam; 3.40.50.620:FF:000020; 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   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:UP000887569}.
FT   DOMAIN          43..671
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          716..869
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   COILED          931..958
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1001 AA;  113996 MW;  1975641C8AB4D6E8 CRC64;
     EREAKKPKVD VVEYKGTTKI GEKKDTSMEI PNAYSPKYVE AAWYDWWEKE GFFRPEYDGR
     DLRKPNPKGS FTIVIPPPNV TGTLHLGHAL ATSVEDTLCR WHRMKGKTVL FNPGCDHAGI
     ATQVVVEKRL KKERGLTRHD LGREKFIEEV WKWKDEKGVI IYDQLRKMGA GVDWERACFM
     MDPKMMRAVT HAFVDMHDRG VIYRSNRLVN WSCTLRSAIS DIEVDKIELS GRTLLSVPGY
     SKKVEFGVLV SFAYPVEGSD EEVVVATTRV ETMLGDTAIA VHPDDDRYEH LIGKFCKHPF
     VDRRLPIVAD SFVEKEFGTG AVKITPAHDH NDYGVGVRHN LPFITIFTDD GEMNDKCGEF
     KGMKRFEARE AVLEALKKKG LYRDVKDNPM IVPICSRSKD VIEPILKSQW YVRCDMMAER
     AKEAVARGEL VIIPDYHVAT WNRWLDSMRD WCISRQLWWG HRIPAYFVTV DDPSVPAGDS
     DDNNYWVSAH NEGEAIEKAA KKFNVPKEKI SVKWDEDVLD TWFSSGMWPF TIFGWPEKTS
     DLRNFFPGSV LETGHDILFF WVARMVFMSQ ELTGQLPFKE IYLHAMIRDA HGRKMSKSLG
     NVIDPIDVIH GISLAQLNKQ LESGNLDAKE LKTAKEGQAR DYPNGIPECG TDALRFALMV
     YTSQGRDINL DVLRVQGYRF FCNKIWQASK FTLMQLGNDF KPLAEFKLSG SESTLDKWIL
     SRLSFAVETC NAAMSSYTFH QATSAMYNFW LYDFCDIYIE GSKPVLLNGG ANVVSTTRQI
     LYTCVDTGLR LISPIMPFIS EELWQRLPRR PSAHKQPLSI CVAEYPEVEE YKYRNELLEN
     RVSRVMDIVK TVRSLRSDYD LTAKVKADLY VTFMEKEEAD AVGDLVTLIS TLTSSQMVSI
     LTGDQDSEIP KGCAQITVSA RCKASLALQD IIDVAKELAK LGEKKTKLES QLDKLDEIMS
     KRDYEQKVPL GVRTNNAEKK DSLCIELKHI NEAIAALEAS E
//
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