ID   SYV_NANEQ               Reviewed;         751 AA.
AC   Q74NF3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Valine--tRNA ligase;
DE            EC=6.1.1.9;
DE   AltName: Full=Valyl-tRNA synthetase;
DE            Short=ValRS;
GN   Name=valS; OrderedLocusNames=NEQ252;
OS   Nanoarchaeum equitans (strain Kin4-M).
OC   Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC   Nanoarchaeaceae; Nanoarchaeum.
OX   NCBI_TaxID=228908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kin4-M;
RX   PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA   Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA   Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA   Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA   Stetter K.O., Short J.M., Noorderwier M.;
RT   "The genome of Nanoarchaeum equitans: insights into early archaeal
RT   evolution and derived parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
CC   -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can
CC       inadvertently accommodate and process structurally similar amino acids
CC       such as threonine, to avoid such errors, it has a 'posttransfer'
CC       editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-
CC       dependent manner (By similarity). {ECO:0000250}.
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   -!- DOMAIN: ValRS has two distinct active sites: one for aminoacylation and
CC       one for editing. The misactivated threonine is translocated from the
CC       active site to the editing site (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 2 subfamily. {ECO:0000305}.
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DR   EMBL; AE017199; AAR39104.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q74NF3; -.
DR   SMR; Q74NF3; -.
DR   STRING; 228908.NEQ252; -.
DR   EnsemblBacteria; AAR39104; AAR39104; NEQ252.
DR   KEGG; neq:NEQ252; -.
DR   PATRIC; fig|228908.8.peg.256; -.
DR   HOGENOM; CLU_001493_0_2_2; -.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000000578; Chromosome.
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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..751
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224628"
FT   BINDING         520
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   751 AA;  89618 MW;  790A1BFF847BBEBC CRC64;
     MPYNPKEIEQ WYKENYKYFF GEGDKILIID TPPPYPAPLW HIGAALSYAL QDFIARGFRK
     LGYKVIFPEG FDGNGIPIEM YLEKYEKIPF GSIDREEYIK KCRQILDSWR EKMDKILKDL
     LLSMDFEHRY NTDDPEYRAL TQKTFAELWE KGLIYEAEYP INYCPHCKTA IADAEIERKI
     KKTKLVYIKF KIKDSDDYIT VATTRPELLG ACKAIIVHPD DERYKKYHNK IAIVPYYNRE
     IPIIPHKMAD PNFGTGAVMI CSYGDWVDVQ IFRELQLKPE KIIDENGRLT IEPVKGLTTK
     EGREKMIEVL KQLGVVEKIE EIEHSVPVHE RCETEIEIIP MKEFYLKQLP FKEEIKKLSK
     EIEFIPERYR KNLENWIDSI TIDWPISRRR WYATEIPLWY CPKCGYIHVA KDGKYHQPWK
     EEMVCPRCNT KMVGETRVLD TWMDSSITIY YLIKKYSKIL GIDEEGLFNN YTLRPQGYEI
     IRTWLYYTLL RVYQLTGKKA FDFVVINGMG LDKHGRKMSK RYGNVIEPET LLEKYGADTL
     RYWFAMEISI GEDYRINEQK IAGIMKFMNK VWNIANYISQ YQYRETQNLK PTDEWIINYV
     KYLENKAIEY IRNFEFNKLA RELYRFVWDV FANHYIELTK KRAKNNDDSA IYALYFVFER
     VLNMLSIFSP GIAKYLAKKL YNKDIEKEKL KYWGKVRLDL LYKGEKLIEF NNYVWKLKTS
     QGKKLKDPIS IEIPKELEIF KEDLILLHNI Q