SYV_METMA
ID SYV_METMA Reviewed; 869 AA.
AC Q8Q024;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=MM_0314;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(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; AE008384; AAM30010.1; -; Genomic_DNA.
DR RefSeq; WP_011032268.1; NC_003901.1.
DR AlphaFoldDB; Q8Q024; -.
DR SMR; Q8Q024; -.
DR STRING; 192952.MM_0314; -.
DR EnsemblBacteria; AAM30010; AAM30010; MM_0314.
DR GeneID; 24877164; -.
DR KEGG; mma:MM_0314; -.
DR PATRIC; fig|192952.21.peg.386; -.
DR eggNOG; arCOG00808; Archaea.
DR HOGENOM; CLU_001493_0_2_2; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000000595; 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..869
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224627"
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; 99130 MW; DF543E9395D48AC9 CRC64;
MTESEIPKEY NANEVEKKWM EKWNLSMYHF NWGEDTRPQY IIDTPPPYPT GNFHIGNALN
WCYIDFVARY KRMRGYNVMF PQGWDCHGLP TEVKVEETHG ITKNQVPRAE FRRMCRELTA
GNIDKMRQTM LRLGFSVDWS NEFVTMEPSY FVKTQKSFVR MYNNGHIYHE DHPVNWCPRC
ETAIAFAEVE YDQGQTKLNF VHFDKVDIAT TRPELMAACV AVAVNPEDER YSQYIGKEIE
VPLFGQKVTL IADEAVEPEF GTGAVMICTF GDKQDVRWWA KYGLPLIKAI DKQGRMTKAA
GKYEGMSIPE CRQAVISDLR DAGFLYNQKP LEQNVGLCWR CDTPIEILSE PQWFVKINHE
GILKAADEIN WYPEYMKVRL QNWTGTMEWD WCISRQRIFA TPIPIWYCKK CGEVMIAEES
WLPIDPNENV PKKACACGST EFEPETDVLD TWMDSSITAL HVSGWESEHD LRLPAQIRPQ
GHDIIRTWAF YTILRSLALE GKRPWDSIVI NGMVLGPDGH KMSKSLGNVI SPEEVTTQYS
ADAFRQWGAV GGSTGSDVMF RWKDVVSASR FLQKMWSIYR FSMSHLKDFD PADAENFPPD
SLYTIDRWLL SKLNRLVEST TKELDGYQFD STFKAIRGFA WEVLADNYLE LVKGRLYGEN
KEGRKAAQYV LYTTTRTLSL LLAPFIPFFA EEMYSRFDSA SVHTRAWPAV NESLMSEEAE
AAGEMIKDIT GEVRRYKSDL GMALNAPLKK IEIYNTQIDT GDIAGATNSE VELMEGAPSF
DYVPVEVKPN MGILGPRFRK DAGAIVKALK AEDPASVEAQ IASGRITVTV NGEKIELEPE
AVEIRKEVIS GGREVDVLDI KGAVVVIVR
