SYV_METMP
ID SYV_METMP Reviewed; 886 AA.
AC Q6LZP0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=MMP0584;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
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; BX950229; CAF30140.1; -; Genomic_DNA.
DR RefSeq; WP_011170528.1; NC_005791.1.
DR AlphaFoldDB; Q6LZP0; -.
DR SMR; Q6LZP0; -.
DR STRING; 267377.MMP0584; -.
DR EnsemblBacteria; CAF30140; CAF30140; MMP0584.
DR GeneID; 2761076; -.
DR KEGG; mmp:MMP0584; -.
DR PATRIC; fig|267377.15.peg.597; -.
DR eggNOG; arCOG00808; Archaea.
DR HOGENOM; CLU_001493_0_2_2; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 4914at2157; -.
DR BioCyc; MMAR267377:MMP_RS03075-MON; -.
DR Proteomes; UP000000590; 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-UniRule.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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..886
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224623"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 528..532
FT /note="'KMSKS' region"
FT BINDING 531
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ SEQUENCE 886 AA; 102046 MW; 561C2A487DB2BC7C CRC64;
MEIKEEYSIE LEKKVQEKWE DEKTFKFLDD EKRPPYIIDT PPPYPTGRMH LGHGLNWTYM
DIIARFKRMN GYDVLFPQGW DCHGLPTEVK VEELNNITKS DIDRHEFRRL CVELTDENVE
KMRGQVRSLG ISIDWDREYI TMNPDYVRKS QTAFLKMYEK GLIYRGKHPV NWCPRCETAI
AFAEVEYQGR TSKLNYIKFP YAENSGKYLE IATSRPELMA ACVGIVVHPE DERYSDVVGK
TVKVPLFDQE VNVYPDSDVE KEFGTGVVMV CTFGDKTDVT WVNRHKLEVK KAINEKGQLT
EICGKYAGKK SDDARKEIIS DLISENYMIK QEPLEQNVGS CWRCKTPIEI IVGDQWFVNV
TKLLTEVENA ANEISWVPEH MKARLMKWIE DMGWDWCISR QRLFATPIPV WYCKDCGEII
VAKPEDLPID PTKESPYTCK CGNSNLVAET DVLDTWMDSS ITPLVIAGWL EDEEFFKKHY
PVQLRPQGHD IIRTWAFYTM VRSLAITGEK PWDEIVINGM VFGEDGFKMS KSRGNVVEPG
EITKTYGADA LRLWASNSTI GKDVPFAWKE VEYGGRFLRK IWNACKFAKM NISDETISEL
KSLNSISIEN PVDLWILSKL NNLISKVSDD LGNYKINTVV EIQKFLWHEF CDNYIEMVKH
RLYNKEESES AQQEKLMAQY TLYKVITESV KLLTPFTPHF AEIVGEIYEI DDLHTSWPVS
DERLISLENE FVGEVVKNTV ASIRRYKSNK GMPLNAELNK VEMYVSDEKD FNAVSKASED
VKKSLKIKEL EINLGKPSLE QKISEVTPNK SKIGPEFKKD AGKVMAFIKE ADADTIEKML
SEGIETEFGI LNKEHIKEVK RAIYNKGEIV ETADIDSLID TIAIIQ
