ID   SYVC_NOSCE              Reviewed;         883 AA.
AC   C4V924;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Probable valine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.9;
DE   AltName: Full=Valyl-tRNA synthetase;
DE            Short=ValRS;
GN   ORFNames=NCER_101032;
OS   Nosema ceranae (strain BRL01) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae; Nosema.
OX   NCBI_TaxID=578460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRL01;
RX   PubMed=19503607; DOI=10.1371/journal.ppat.1000466;
RA   Cornman R.S., Chen Y.P., Schatz M.C., Street C., Zhao Y., Desany B.,
RA   Egholm M., Hutchison S., Pettis J.S., Lipkin W.I., Evans J.D.;
RT   "Genomic analyses of the microsporidian Nosema ceranae, an emergent
RT   pathogen of honey bees.";
RL   PLoS Pathog. 5:E1000466-E1000466(2009).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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; ACOL01000081; EEQ82274.1; -; Genomic_DNA.
DR   RefSeq; XP_002995945.1; XM_002995899.1.
DR   AlphaFoldDB; C4V924; -.
DR   SMR; C4V924; -.
DR   STRING; 578460.C4V924; -.
DR   EnsemblFungi; EEQ82274; EEQ82274; NCER_101032.
DR   KEGG; nce:NCER_101032; -.
DR   VEuPathDB; MicrosporidiaDB:NCER_101032; -.
DR   HOGENOM; CLU_001493_0_0_1; -.
DR   InParanoid; C4V924; -.
DR   OMA; RQWYIRN; -.
DR   Proteomes; UP000009082; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; 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   Gene3D; 3.40.50.620; -; 2.
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   PANTHER; PTHR11946; PTHR11946; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00422; valS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..883
FT                   /note="Probable valine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000388387"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           82..92
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           586..590
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         589
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   883 AA;  102513 MW;  AB09ECD71DED875F CRC64;
     MTLKMDRKAL KEEKKKQKLE KFLNKKTTQS KISKAPKPAK NKSSSGYDPM PVEQKWNNYW
     LSNNLFEPQE RSNKFVMCMP PPNITGSLHI GHSMMIAIQD AICRYMRLIN YEVLYLPGTD
     HAGIATQTVV MKQLEKEKKT YNRESFLEAT WKWKENYGSR ILDQFKRLGT SADFSRQKFT
     MDAGMNKAVT EAFCSLYEKG LIYRDNKIVN WCCKLQTTLS DIEIDYLSVG KNTILKIDGR
     DYEFGVIYVF KYPVKFVKDG YESEGHIEVA TTRPETILGD VALCANPKDA RYTKYDKIIP
     RNPITEEELS FVFDEAAEMD LESGVLKITP AHDPIDFEIG KKNNLKNIKI FDNQNKIIIE
     GNYYKLKRLD ARDLVVQTLK NKNLFVEKKP YEQVLPMCSR SSDLLEPVIK EQWWCSCSEM
     AKKAIDAVKT EQIKIYPEES KDDWYRWFEN PRDWCLSRQL WWGHRIPAYK TPDGVWTIAR
     NKEQAIQSYK KNNPLNVHYQ ESDFVQDEDV LDTWFSSGLW PFATLGWPNK NQDLDKYFPT
     SLLETGKDIL FFWVGRMVMM SLELTGKVPF KKVLLHGIVR DAYGRKMSKS LGNVIDPIHV
     IDGASIETLL DALKLGNLTK ENLINAESAV KKDFINGITV CGADALRFTL LSYMNGINDI
     KLDIERVKGN RKFCNKIWNA ALFVKKIVDE IISSDSLSYQ DLLNLDLSNE DDKLLVWLIQ
     ERNKVISTTH KAFKEYKFMS AVQSIHQFFL YDFCDVYIEI VKKIKTKKYI QACFMVLIDS
     IKIFSPYMPF ITEEIYSQFF DNSLMYTSYP EIIHNKFSTN FKSTLSKIKA IRADIEKYGK
     EKVDVILDGC ECFDKIDIQF ISILIPNINT IKFGEGYEVK KVN