ID   SYV_AERPE               Reviewed;         823 AA.
AC   Q9YAZ0;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 3.
DT   03-AUG-2022, entry version 113.
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=APE_1805.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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; BA000002; BAA80808.2; -; Genomic_DNA.
DR   PIR; C72565; C72565.
DR   AlphaFoldDB; Q9YAZ0; -.
DR   SMR; Q9YAZ0; -.
DR   STRING; 272557.APE_1805.1; -.
DR   PRIDE; Q9YAZ0; -.
DR   EnsemblBacteria; BAA80808; BAA80808; APE_1805.1.
DR   KEGG; ape:APE_1805.1; -.
DR   PATRIC; fig|272557.25.peg.1210; -.
DR   eggNOG; arCOG00808; Archaea.
DR   Proteomes; UP000002518; 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..823
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000106247"
FT   BINDING         547
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   823 AA;  95247 MW;  A98A47A49073F8C2 CRC64;
     MGEEFKPAIQ EKRWDIGEEE KLLSLWDAED LHKSTLDPDD PREIVVIDTP PPYPSGKWHV
     GGAAHYTQID MIARYFRLKG YNVVAPFYAD RNGLPVEVQV EKTYGVVAHE MARTTEGRER
     FLALCSEFLD KVESEIVQLW RRLGCGFDYW REGTDSPRYR SMTQATFIDL WRRGLIYEAE
     RPVRWCPRCK TTLAEAEIEH KEDEDFIYYV KYRLEEDGRD LVVATTRPEL LAGCAALAYH
     PEDERYKGLA GKTAIAPLYG HRVKIVEHPA VKKDFGTGLM MICSYGDEED VRLFLELDLK
     PKVLIDENGV MNENAGPIAG LPVKEARRRI AEILEREGLL VKKERIVHSV PVCWRCKTPL
     QIIHRRELFL RQLDFKDAVK QAAAKMDFKP EMHRKKLYDW IDSIKMDWPI SRERFYGTEI
     PLWTCEKCGA KLVPEPGRYY RPWAEEPPWD SCPRCGAPRR YLKGETRVFD TWFDSSISPL
     YVTRWMWDKR FYERASRNVL RPQGQDIIRT WLYYSILRVL QLTGKPAFRW VRITGLGLDP
     KGRPMHKSLG NVIDPEPIIA KYGGDAFRFW AAIAAKLGYD YRFDENKVKT GRNFATKLWN
     LARFVSSFPR PEGSPLEKAT EVDKAFLALA DEYLEAADKA YGELDVYEPA NLIYELAWDI
     FASHYVELVK ERSYNRSGLF TREEQEAAWA TLHELLRRIL VALSPIMPFV TDAIHRRLYG
     SSVHRQRWPD PLFTPEERRE LAGKARLIVS VNKAVWNLKR SMGKKLYEPL DTVEVLVPSG
     IESARRDLEA LHKAAIRTYT GAPPEGSEEA IPGSSVYYIA KKS