SYV_ANOFW
ID SYV_ANOFW Reviewed; 875 AA.
AC B7GH39;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=Aflv_0614;
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1;
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
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; CP000922; ACJ32995.1; -; Genomic_DNA.
DR AlphaFoldDB; B7GH39; -.
DR SMR; B7GH39; -.
DR STRING; 491915.Aflv_0614; -.
DR PRIDE; B7GH39; -.
DR EnsemblBacteria; ACJ32995; ACJ32995; Aflv_0614.
DR KEGG; afl:Aflv_0614; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_9; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000000742; 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 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..875
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000189240"
FT COILED 804..875
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 44..54
FT /note="'HIGH' region"
FT MOTIF 520..524
FT /note="'KMSKS' region"
FT BINDING 523
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 875 AA; 101444 MW; 03BD0F68834E971E CRC64;
MMLPPKYDHR AVEANRYEWW LKGKFFEATS DETKKPFTIV IPPPNVTGKL HLGHAWDTTL
QDIITRMKRM QGYDVLWLPG MDHAGIATQA KVEEKLRNEG KTRYDLGREK FVEETWKWKE
EYAGHIRSQW AKLGLGLDYT RERFTLDEGL SKAVREVFVS LYKKGLIYRG EYIINWDPVT
KTALSDIEVV YKDVQGALYH MRYPLADGSG YIEVATTRPE TMLGDTAVAV HPEDERYKHL
IGKTVILPIV GREIPIIGDE YVDMSFGSGA VKITPAHDPN DFEIGNRHHL PRILVMNEDG
TMNDNALQYK GLDRFECRKQ IVKDLQEQGV LFKIEEHMHS VGHSERSGAV VEPYLSTQWF
VKMKPLAEAA IEQQKTEGKV NFVPERFEKT YLHWMENIRD WCISRQLWWG HRIPAWYHKE
TGEVYVDHEP PADIENWEQD QDVLDTWFSS ALWPFSTMGW PDKTSADYNR YYPTDVLVTG
YDIIFFWVSR MIFQALEFTG KRPFKDVLIH GLVRDAQGRK MSKSLGNGVD PMDVIDQYGA
DSLRYFLATG SSPGQDLRFS TEKVEATWNF VNKIWNASRF ALMNMEGFTY EDIDLHGEKS
VADHWILTRL NETIETVTKL ADKYEFGEVG RVLYNFIWDD LCDWYIEMAK LPLYGDDEQA
KKTTRSVLAY VLDQTMRLLH PFMPFVTEEI WQQLPHEGES ITVASWPQVR PELSNHEAAE
TMRLLVDIIR AVRNIRAEVN TPLSKPITLY IKAKDEHVKA TLETNRAYIE RFCNPSELVI
DTTIPTVEKA MTAVVTGAEL SLPLEGLINI EEEVKRLEKE LQKLDQEVER VQKKLSNEGF
LAKAPAHVVE EERKKERDYI EKREAVRARL AQLKQ
