ID   SYV_SACS2               Reviewed;         842 AA.
AC   Q97ZK9;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02005};
DE            EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02005};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02005};
DE            Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02005};
GN   Name=valS {ECO:0000255|HAMAP-Rule:MF_02005}; OrderedLocusNames=SSO0899;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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. {ECO:0000255|HAMAP-Rule:MF_02005}.
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:0000255|HAMAP-Rule:MF_02005};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02005}.
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. {ECO:0000255|HAMAP-Rule:MF_02005}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02005}.
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; AE006641; AAK41179.1; -; Genomic_DNA.
DR   PIR; D90240; D90240.
DR   RefSeq; WP_009992319.1; NC_002754.1.
DR   AlphaFoldDB; Q97ZK9; -.
DR   SMR; Q97ZK9; -.
DR   STRING; 273057.SSO0899; -.
DR   EnsemblBacteria; AAK41179; AAK41179; SSO0899.
DR   GeneID; 44129827; -.
DR   KEGG; sso:SSO0899; -.
DR   PATRIC; fig|273057.12.peg.900; -.
DR   eggNOG; arCOG00808; Archaea.
DR   HOGENOM; CLU_001493_0_2_2; -.
DR   InParanoid; Q97ZK9; -.
DR   OMA; FATKLWN; -.
DR   PhylomeDB; Q97ZK9; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_02005; Val_tRNA_synth_type2; 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; IPR022874; Valine-tRNA_ligase_type_2.
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..842
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224635"
FT   MOTIF           86..96
FT                   /note="'HIGH' region"
FT   MOTIF           572..576
FT                   /note="'KMSKS' region"
FT   BINDING         575
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   842 AA;  98578 MW;  916108C2583B46D5 CRC64;
     MLFSLRNFIS YSNLYLYKNV CIGGQLLLNQ DEILKKMEEW PKHYNPKEIE EKWQKIWLSE
     EYWRDVFRFR DEDDKAPRFV IDTPPPFTSG ELHMGHAYWV TIADTIGRFK RLEGYNVLLP
     QGWDTQGLPT ELKVQYKLGI PKDNRQLFLQ KCIEWTEEMI KKMKEAMIRL GYRPEWERFE
     YKTYEPKYRK IIQKSLIDMY KMNLIEMREG PVIWCPKCET ALAQSEVGYL EKEGILAYIK
     FPLKEGGEIV IATTRPELLA ATQAIAVNPM DERYKNLVGK IALVPIFNIE VKIISDADVE
     KEFGTGAVMI STYGDPQDIK WQLKYNLPIK VIVDEKGRII NTNGILDGLK IEQARNKMIE
     LLKTKGYLVK VEKIKHNVLS HVERSDCLSP VEFLVKKQIY IKVLDKKQKL LEEYKKMKFK
     PARMSYYLED WIKSIEWDWN ITRQRIYGTP LPFWYCENGH LVPAKEEDLP IDPIKTSPPL
     EKCPLCGSEL KPVTDVADVW IDSSVTVLYL TKFYEDKNVF NRTFPASLRL QGTDIIRTWL
     FYTFFRTLML ANNVPFTTVL VNGQVLGPDG TRMSKSKGNV VSPLDRVNDF GADAIRMALL
     DASIGDDFPF KWDIVKGKKM LLQKLWNASR LVYPFIAKQR LDKPKSLHIV DKWILQEHKK
     FVTKAINAYE NYDFYLVLQE LYNYFWEIVA DEYLEMIKHR LFDDDNSAKY TIQRIIRDII
     ILLHPIAPHI TEEIYSRLFG HKKSVLLEEL PKVDDIEENK RIDELGEVIK KTNSLIRSEK
     IKNRLSMNTP VSVKLYASKQ VIELINEVKD DVMKTLKVTN LELIESNEEK VEIKTANQSM
     GV