ID   SYV_METAC               Reviewed;         869 AA.
AC   Q8TLI4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, 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=MA_3052;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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}.
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DR   EMBL; AE010299; AAM06425.1; -; Genomic_DNA.
DR   RefSeq; WP_011022991.1; NC_003552.1.
DR   AlphaFoldDB; Q8TLI4; -.
DR   SMR; Q8TLI4; -.
DR   STRING; 188937.MA_3052; -.
DR   EnsemblBacteria; AAM06425; AAM06425; MA_3052.
DR   GeneID; 1474946; -.
DR   KEGG; mac:MA_3052; -.
DR   HOGENOM; CLU_001493_0_2_2; -.
DR   InParanoid; Q8TLI4; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 4914at2157; -.
DR   PhylomeDB; Q8TLI4; -.
DR   Proteomes; UP000002487; 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..869
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224625"
FT   MOTIF           47..57
FT                   /note="'HIGH' region"
FT   MOTIF           521..525
FT                   /note="'KMSKS' region"
FT   BINDING         524
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   869 AA;  98945 MW;  056D948AB5719AA0 CRC64;
     MTESEIPKEY NANEVEEKWM EKWNLSMYHF NWGEDPRPQY IIDTPPPYPT GNFHIGNALN
     WCYIDYIARY KRMRGYNVMF PQGWDCHGLP TEVKVEEIHG ITKNQVPRAE FRKMCRELTA
     GNIEKMRKTM LRLGFSVDWS NEFVTMEPSY FVKTQKSFVR MYNDGHIYHE DHPVNWCPRC
     ETAIAFAEVE YESRQTKLNF VHFDKVDIAT TRPELMAACV AVAVNPKDER YSQHIGKEIT
     VPIFGQKVTL IADEAVEPEF GTGAVMICTF GDKQDVRWWV KYGLPLVKAL DKQGRMTKAA
     GKYEGMTLAE CREAVIADLK AAGFLYDQKS LEQNVGLCWR CDTPIEILSE PQWFVKINHE
     GILKAADEIK WYPEYMKVRL QNWTGTMEWD WCISRQRIFA TPIPIWYCKK CGEVMIAEES
     WLPIDPNENT PKKACACGST EFEPETDVLD TWMDSSITAL HVSGWESEHE MRLPTQIRPQ
     GHDIIRTWAF YTILRSLALE GKRPWDSIVI NGMVLGPDGH KMSKSLGNVI SPEEVTTQYS
     ADAFRQWGAV GGSTGSDVMF RWKDVVSASR FLQKMWSIYR FSMSHLKDFE PADAENFPPD
     ALLTIDRWLL SKLNKLVDTA TKELDGYQFD STFKAIRGFA WEVLADNYLE LVKGRLYGED
     PEGRKAAQYV LYTTTRTLSL LLAPFIPFFA EEMYSRFSEE SVHTQTWPAV NEKLISEEAE
     AAGEMIKEIT GEVRRYKSDL GMALNAPLKK IEIYNAEIDT GDIAGATNSE VELMAGAPSF
     EYVPVEVKPN MGFLGPRFRK EAGAVVKALQ AEDPAAIEAQ AASGKITITV NGEAVKLEPE
     AVEIRKEVIS GGREVDVLDV KGAVVVIVR