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SYV_GEOKA
ID   SYV_GEOKA               Reviewed;         880 AA.
AC   Q5KWL3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=GK2638;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(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_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; BA000043; BAD76923.1; -; Genomic_DNA.
DR   RefSeq; WP_011232114.1; NC_006510.1.
DR   AlphaFoldDB; Q5KWL3; -.
DR   SMR; Q5KWL3; -.
DR   STRING; 235909.GK2638; -.
DR   EnsemblBacteria; BAD76923; BAD76923; GK2638.
DR   KEGG; gka:GK2638; -.
DR   PATRIC; fig|235909.7.peg.2818; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_9; -.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000001172; 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; -; 3.
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..880
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224481"
FT   COILED          809..880
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           49..59
FT                   /note="'HIGH' region"
FT   MOTIF           525..529
FT                   /note="'KMSKS' region"
FT   BINDING         528
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   880 AA;  101882 MW;  85D32680AB057994 CRC64;
     MAQHEVSMPP KYDHRAVEAG RYEWWLKGKF FEATGDPNKR PFTIVIPPPN VTGKLHLGHA
     WDTTLQDIIT RMKRMQGYDV LWLPGMDHAG IATQAKVEEK LRQQGLSRYD LGREKFLEET
     WKWKEEYAGH IRSQWAKLGL GLDYTRERFT LDEGLSKAVR EVFVSLYRKG LIYRGEYIIN
     WDPVTKTALS DIEVVYKEVK GALYHLRYPL ADGSGCIEVA TTRPETMLGD TAVAVHPDDE
     RYKHLIGKMV KLPIVGREIP IIADEYVDME FGSGAVKITP AHDPNDFEIG NRHNLPRILV
     MNEDGTMNEN AMQYQGLDRF ECRKQIVRDL QEQGVLFKIE EHVHSVGHSE RSGAVVEPYL
     STQWFVKMKP LAEAAIKLQQ TDEKVQFVPD RFEKTYLHWL ENIRDWCISR QLWWGHRIPA
     WYHKETGEIY VDHEPPKDIE NWEQDPDVLD TWFSSALWPF STMGWPDTES PDYKRYYPTD
     VLVTGYDIIF FWVSRMIFQG LEFTGKRPFK DVLIHGLVRD AQGRKMSKSL GNGVDPMDVI
     DQYGADALRY FLATGSSPGQ DLRFSTEKVE ATWNFANKIW NASRFALMNM GGMTYEELDL
     SGEKTVADHW ILTRLNETIE TVTKLAEKYE FGEVGRTLYN FIWDDLCDWY IEMAKLPLYG
     ADEAAKKTTR SVLAYVLDNT MRLLHPFMPF ITEEIWQNLP HEGESITVAP WPQVRPELSN
     EEAAEEMRLL VDIIRAVRSV RAEVNTPPSK PIALYIKVKD EQVRAALMKN RAYLERFCNP
     SELLIDTNVP APDKAMTAVV TGAELIMPLE GLINIEEEIK RLEKELDKWN KEVERVEKKL
     ANEGFLAKAP AHVVEEERRK RQDYIEKREA VKARLAELKR
 
 
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