ID   SYVC_ENCCU              Reviewed;         921 AA.
AC   Q8SS27;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Probable valine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.9;
DE   AltName: Full=Valyl-tRNA synthetase;
DE            Short=ValRS;
GN   OrderedLocusNames=ECU04_1140;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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}.
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DR   EMBL; AL590444; CAD25302.1; -; Genomic_DNA.
DR   RefSeq; NP_584798.1; NM_001041148.1.
DR   AlphaFoldDB; Q8SS27; -.
DR   SMR; Q8SS27; -.
DR   STRING; 284813.Q8SS27; -.
DR   GeneID; 858946; -.
DR   KEGG; ecu:ECU04_1140; -.
DR   VEuPathDB; MicrosporidiaDB:ECU04_1140; -.
DR   HOGENOM; CLU_001493_0_1_1; -.
DR   InParanoid; Q8SS27; -.
DR   OMA; RQWYIRN; -.
DR   OrthoDB; 229591at2759; -.
DR   Proteomes; UP000000819; Chromosome IV.
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..921
FT                   /note="Probable valine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000388386"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           84..94
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           602..606
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   BINDING         605
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   921 AA;  104983 MW;  7BB10989295F652A CRC64;
     MDSSKEALKE RKKMAKDEKK RQKLEKFLAK KTLEIGVSKP RKEYRKEGYD PLQVEGKWYK
     LWEEQGLFKP VEGGARYVVP IPPPNVTGSL HIGHAMMVSI QDAVCRYKRM CGYEVLYIPG
     TDHAGIATQN VVSKQLAREG IVVDREGFLK KAWEWKDRHG SRIYEQLKRL GTSVDFGRER
     FTLDPGMSRA VADAFVKLYE KGLIYREPKI VNWCSRLLTT ISDLEVNHEE VMPNTYLQVD
     GGKYEFGVIY HFKYPITADK GFSGDHLSLP TIEVATTRPE TILGDTAVCV NGRDCRFSPE
     GIKEMLGDVP HGCRIYGVNP LTRDVIPVIF DDYADMSFGT GVVKITPAHD ANDFEVSKRH
     GLPCKVVFDE QNRVVVEGEF KGLKRFEARK AVVSKLRDVG LFVSKKGHPQ VIPRCSRSDD
     VIEPIIKSQW WLNCKEMARK AIEAVEDGRI SILPEGAEKQ WYKWLGNIRD WCLSRQLWWG
     HRVPAYKAPS GKWYVGRTKE DAFLKMRSEC MGSDCDLSEL EQDEDVLDTW FSSGLWPFAT
     LGWPEETEDF LKYYPNTLLE TGSDILFFWV ARMVMLGLEL TGKVPFSQVL LHGIVRDAHG
     RKMSKSLGNV IDPIFVIDGC SLEKLISTMR SGNLDEREVK RAEAVLRQDF PNGISRCGAD
     ALRFALLSYT SGMKDINLDV LRVEGYRRFC NKIWNAHKFV KTMVDELAGK NGNGPVCKDD
     YGKYIVSSAE LPGPSEEGPV EWILRRRNET VEEIRRTLDS FNFMGATQAI HQFFIYDLCD
     VFIEVVKKSK NEKYIRVLFR VFIDSMKMLH PFMPFITEEV FSNYFNGSIS VSPYPETDGS
     EHESKFSVTL QITRHIRAKA ESNGWSKAVV EIAPGGDVNH ADLRFIRSLC RKIVELKIIS
     DAEDGPYEKV GGSRVLVRQT E