ID   A0A183SLP7_SCHSO        Unreviewed;       925 AA.
AC   A0A183SLP7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=SSLN_LOCUS5145 {ECO:0000313|EMBL:VDL91530.1};
OS   Schistocephalus solidus (Tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Diphyllobothriidea; Diphyllobothriidae; Schistocephalus.
OX   NCBI_TaxID=70667 {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0000530801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SSLN_0000530801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDL91530.1, ECO:0000313|Proteomes:UP000275846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NST_G2 {ECO:0000313|EMBL:VDL91530.1,
RC   ECO:0000313|Proteomes:UP000275846};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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}.
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DR   EMBL; UYSU01033132; VDL91530.1; -; Genomic_DNA.
DR   STRING; 70667.A0A183SLP7; -.
DR   WBParaSite; SSLN_0000530801-mRNA-1; SSLN_0000530801-mRNA-1; SSLN_0000530801.
DR   Proteomes; UP000050788; Unplaced.
DR   Proteomes; UP000275846; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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   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; 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:UP000275846}.
FT   DOMAIN          58..674
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          717..868
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   925 AA;  106112 MW;  584FE4506F0EE7A1 CRC64;
     MDGVGKSEKQ LRNEAKKLEK LAKFNAKKEK LANKNVEKVY VSGSMPESYS PKYVEAIWYQ
     WWEKCGFFSP EYWVNPQKPR KKFVMVIPPP NVTGNLHLGH ALTNSLEDAI TRWHRMRGEI
     TVWVPGCDHA GIATQVVVEK KLWREKQLMR QDIGREAFLK EVWKWKEEKG ENIYHQLKSL
     GSSCDWSRAA FTMDPNLSHA VTEAFVRMYE GGLIYRGVRL VNWCCALQSA ISDIEVEKRE
     LTGRTSITVP GYAKPVIFGI LSSFAYPLID SPNGEELVVA TTRLETMVGD TGVAVHPEDP
     RYSHLIGRFV QHPFIPERRM PIVGDTFVER EFGTGAVKLT PAHDHTDYEV GMRHNLPFIT
     VIDDKGYMTK EAGPFAGMKR FEARWAIRKA LEEKGLFRGE VDNPMVVPIC SRTKDVIEPL
     LKPQWYIRCQ ELADRAVKEV ADGNLKIMPR MYVRTWNNWL RDCHDWCISR QLWWGHRVPA
     YQPRQQPHSE NDSWVVGRDE KEALATAAER FKRPIDEIRL IQDEDVLDTW FSSQLFPMSV
     FGWPNTESSD FRSFYPGTLL ETGHDILFFW VARMVMCGLF FTDRLPFKEV YLHAMIRDAH
     GKKMSKSLGN AIDPVDVING ISLPELQAKL LVGNLDPSEL TRATAAQAKD YPKGIPECGT
     DALRFALCSY RTRGWSINLN IQRVQGYRFF CNKLWNAWPR IAPKSSPFEK HDLSGTDQWI
     LSCLAHAVQE CNAGFKEYKF PRATTACFNF WLYEFCDVYL EYSKPLVKLE PGCSPAALKR
     AETVRHVVYT CLDLGLRMLH PFMPFVTEEL YQRLPRRDPL NDPPSICVAP YPDDGEENPV
     VTISFRLAFS LVHRLRSFYA TCNISKTTAF PEAVLVAPES TLEGLRAGKF LVDIVQTLGK
     CRLTDLTTDK SLGKRCYIDI RVREI
//