SYV_FERNB
ID SYV_FERNB Reviewed; 867 AA.
AC A7HJX5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Fnod_0343;
OS Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=381764;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Fervidobacterium nodosum Rt17-B1.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000771; ABS60208.1; -; Genomic_DNA.
DR AlphaFoldDB; A7HJX5; -.
DR SMR; A7HJX5; -.
DR STRING; 381764.Fnod_0343; -.
DR EnsemblBacteria; ABS60208; ABS60208; Fnod_0343.
DR KEGG; fno:Fnod_0343; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_0; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000002415; 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; 1.10.287.380; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
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..867
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000073714"
FT COILED 794..867
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 42..52
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_02004"
SQ SEQUENCE 867 AA; 101498 MW; 9FFCAF48E17EA203 CRC64;
MEIGTRYDPK NIEMKWYKHW LEKKYFTPRG AGPKYSIVIP PPNITGKIHM GHALNITIQD
ILSRYKRMKG FDVLWLPGED HAGIATQTAV ERYLSTQGKS RRDFSRDEFL NIVWNWANKY
RQEIKNQIMS IGASVDWTRE RFTLDEGLSK AVRKVFVDMY KKGLIYKGKY IVNWCHRCGT
VLSDEEVDYH EEEGALYHIK YPIKGEDDYI IIATTRPETM LGDTAVAVHP SDERYRKYVG
KIAILPLVGR EIPVIADNYV DPSFGTGALK VTPAHDTNDY LIGQRHNLPF VDIFDENIVI
NENGGKFKGM TAEQARKAVV EELEAQGYLV KIEKMKHSVG RCYRCDTVVE PRLMDQWFVS
MKPLAKRAIE AVENGEVTFI PDRWKKVYLN WMYEIRDWCI SRQLWWGHRI PVWQCQDCGH
YNVSENEPVK CEKCGSTNLK QDEDVLDTWF SSALWPFSTM GWPEKTPDLE RYYPTDVLVT
GFDIIFFWVA RMIMMGYEFM DEKPFKEVYI HQLVRDKYGR KMSKSLGNGI DPLEVIDEYG
ADPMRFTLAI LAAQGRDLKL DVRFFDTYKK FANKIWNATR FVLMNLEDFE KVDIKLSKLK
LSDKWILSRL QKTIQKISEA LDSYDFNIAA NEIYNFFWDE LCDWYIEAVK NRLKTEERKV
VQNVLVYVLD MSLRLLHPFM PFLTEELWTK LPTSGESIVV AQWPEIEENF IDENSEKRFM
QLMNIIRGIR NIRAEVNVPQ STKVKTFVKG TLTDEEQEYI KFLGNVESIE FVEKRPELSA
TAYISLENEV YVSLGTLIDV KSEVERLRKK VEKLKSDMEK FAKKLEDENF LKNAPEDIVE
ETKEKQRLFQ EQIARIEQII SDLEAKA
