SYV_THEMA
ID SYV_THEMA Reviewed; 865 AA.
AC Q9X2D7;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02004}; OrderedLocusNames=TM_1817;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(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. {ECO:0000255|HAMAP-Rule:MF_02004}.
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_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}.
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_02004}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
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DR EMBL; AE000512; AAD36880.1; -; Genomic_DNA.
DR PIR; D72206; D72206.
DR RefSeq; NP_229614.1; NC_000853.1.
DR RefSeq; WP_004082363.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9X2D7; -.
DR SMR; Q9X2D7; -.
DR STRING; 243274.THEMA_05110; -.
DR EnsemblBacteria; AAD36880; AAD36880; TM_1817.
DR KEGG; tma:TM1817; -.
DR eggNOG; COG0525; Bacteria.
DR InParanoid; Q9X2D7; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000008183; 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; 1.10.287.380; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_02004; Val_tRNA_synth_type1; 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; IPR010978; tRNA-bd_arm.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR019499; Val-tRNA_synth_tRNA-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 Pfam; PF10458; Val_tRNA-synt_C; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF46589; SSF46589; 1.
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; Coiled coil; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..865
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106238"
FT COILED 797..865
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 523..527
FT /note="'KMSKS' region"
FT BINDING 526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 865 AA; 101809 MW; 0D4F16060E94648F CRC64;
MAELSTRYNP AEIETKWYRY WEEKGYFTPK GVGEKFSIVI PPPNITGRIH MGHALNITLQ
DIVVRYKRMK GYDVLWVPGE DHAGIATQNA VEKFLLQTQG KTREEIGREK FLEITWEWAN
KYRREIREQI KALGASVDWT RERFTLDEGL SRAVRKVFVE LYRKGLIYRG KYIVNWCPRC
KTVLSDEEVE HKEHKSKLYY VKYPVKDSDE YIVVATTRPE TMLGDTAVAV HPEDERYKNF
VGKTLILPLV GREIPVVADK YVDPKFGTGA VKVTPAHDPN DYLIAQRHNL PMIEIFDDNA
RINENGGKYK GLDRYEAREK IVKDLEEQGF LVKIEDYTHS VGHCYRCDTV IEPKLSDQWF
VSTKPLAKRA IEAVENGEIR FFPERWTKVY LNWMYEIRDW CISRQLWWGH RIPVWYCQDC
GHLNVSEEDV EKCEKCGSTN LKQDEDVLDT WFSSALWPFS TLGWPEETED LKRYYPTDLL
VTGFDIIFFW VARMIMMGYE FMNDKPFSHV YIHQLVRDKY GRKMSKSLGN GIDPLEVIDE
YGADPMRFTL AILAAQGRDI KLDPRYFDAY KKFANKIWNA TRFVLMNLED YKEVPLENLK
TVDKWILTRL NKTVEEVTNA LENYDFNIAA RTIYNFFWDD FCDWYIEASK PRLKTEERNL
VQTVLVKVLD ASLRLLHPFM PFLTEELWQK LPVAGESITI AKWPEIEREL IDETAEKEFT
RLMNMVRGVR NVRAEMNLPQ SQRVKVYIKG YEVTEEEELL LKTLGNIEEV SFVNEKPPKT
ATAYVEEEIE AYVDLGGLID FEKEKERLKQ IMEKIQKEID RLEKKLANKD FVEKAPEEVV
EETKEKLNTN RERLARLESI LRDLE
