SYV_LATSS
ID SYV_LATSS Reviewed; 882 AA.
AC Q38XD1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=LCA_0849;
OS Latilactobacillus sakei subsp. sakei (strain 23K) (Lactobacillus sakei
OS subsp. sakei).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Latilactobacillus.
OX NCBI_TaxID=314315;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=23K;
RX PubMed=16273110; DOI=10.1038/nbt1160;
RA Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M.,
RA Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R., Loux V.,
RA Zagorec M.;
RT "The complete genome sequence of the meat-borne lactic acid bacterium
RT Lactobacillus sakei 23K.";
RL Nat. Biotechnol. 23:1527-1533(2005).
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; CR936503; CAI55150.1; -; Genomic_DNA.
DR RefSeq; WP_011374552.1; NC_007576.1.
DR AlphaFoldDB; Q38XD1; -.
DR SMR; Q38XD1; -.
DR STRING; 314315.LCA_0849; -.
DR EnsemblBacteria; CAI55150; CAI55150; LCA_0849.
DR KEGG; lsa:LCA_0849; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_9; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002707; 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..882
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224492"
FT REGION 844..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 809..882
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT MOTIF 524..528
FT /note="'KMSKS' region"
FT COMPBIAS 845..866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 527
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 882 AA; 101295 MW; F9D538F86AF9F9CF CRC64;
MTDHKEMSTK YDPNQVEDGR YQDWLKEDLF KPNANPDAKP YSIVIPPPNV TGKLHLGHAW
DTTLQDMLIR QKRMQGYDVL WLPGMDHAGI ATQAKVEAKL AEQGISRYDL GREKFIDQVW
EWKDEYAATI HDQWAKMGLS LDYSRERFTL DDGLSDAVRK VFVNLYNKGL IYRGEYIINW
DPKARTALSD IEVLHQDDEG AFYHVSYPLT DGSGSIEIAT TRPETLPGDT AIAVHPDDER
YADLVGKTVT LPLMNREIPI IADHYVDKDF GTGALKITPA HDPNDFEVGN RHDLPRINVM
NEDASMNESA GKYNGMDRFE ARKAIVADLK EQGFLIKVDP MTHSVGHSER TGVQVEARLS
TQWFVKMKPL AEMALKNQET DQKVNFVPER FENTFTQWME NVHDWVISRQ LWWGHQIPAW
YHKQTGEMYV GEEAPEDIEN WTQDSDVLDT WFSSALWPFS TMGWPNTEAP DFKRYFPTNT
LVTGYDIIFF WVSRMIFQSL EFTEQRPFEH VLIHGLIRDE QGRKMSKSLG NGIDPMEVIE
KYGADALRWF LTSGSTPGQD VRFSYTKMDA AWNFINKIWN ASRFVIMNLE DTPAPTKVPE
AANLDLTDKW ILSQLNQTVA DVTRLYEGFE FGEAGRTLYN FIWNDFCDWY IEMAKEVLYG
DDQEAIANKR YNLAYVLDQT LRLLHPVMPF VTEEIWQSMP HTGESIMTAS YPEVHAELDD
QEATTQMNAL IDLIRSVRNI RSEANAPLSK PIDILINIQD TPLMAIFKQN QDFIERFVHP
KSLEIAEGLT APALAKTAII SGAEVYVPLA ELLDLDEEIT RLEGELKRLN GEIKRAQGKL
ANKGFTDRAP EKVVQEERDK QADYEQQYQS VEKRLAELKA AR
