SYV_STRPM
ID SYV_STRPM Reviewed; 882 AA.
AC Q48SA4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=M28_Spy1296;
OS Streptococcus pyogenes serotype M28 (strain MGAS6180).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=319701;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS6180;
RX PubMed=16088825; DOI=10.1086/430618;
RA Green N.M., Zhang S., Porcella S.F., Nagiec M.J., Barbian K.D., Beres S.B.,
RA Lefebvre R.B., Musser J.M.;
RT "Genome sequence of a serotype M28 strain of group A Streptococcus:
RT potential new insights into puerperal sepsis and bacterial disease
RT specificity.";
RL J. Infect. Dis. 192:760-770(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; CP000056; AAX72406.1; -; Genomic_DNA.
DR RefSeq; WP_011284987.1; NC_007296.2.
DR AlphaFoldDB; Q48SA4; -.
DR SMR; Q48SA4; -.
DR EnsemblBacteria; AAX72406; AAX72406; M28_Spy1296.
DR KEGG; spb:M28_Spy1296; -.
DR HOGENOM; CLU_001493_0_2_9; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000009292; 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; 2.
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.
FT CHAIN 1..882
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224578"
FT COILED 808..882
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT MOTIF 519..523
FT /note="'KMSKS' region"
FT BINDING 522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 882 AA; 100990 MW; D16C8BB40E2E26B2 CRC64;
MTELSPKYNP AEVEAGRYQK WLDADVFKPS GDQKAKPYSI VIPPPNVTGK LHLGHAWDTT
LQDIIIRQKR MQGFDTLWLP GMDHAGIATQ AKVEERLREQ GISRYDLGRD KFLDKVWEWK
DEYATTIKEQ WGKMGLSVDY SRERFTLDEG LSKAVRKVFV DLYKKGWIYR GEFIINWDPA
ARTALSDIEV IHKDVEGAFY HMNYMLEDGS RALQVATTRP ETMFGDVAVA VNPEDPRYKD
LIGKNVILPI VNKLIPIVGD EHADPEFGTG VVKITPAHDP NDFEVGQRHN LPQVNVMNDD
GTMNELAGDF AGMDRFEARQ ATVAKLEELG ALVNIEKRVH SVGHSERSGA VVEPRLSTQW
FVKMDELAKQ AMDNQETDNR VDFYPPRFND TFLQWMENVH DWVISRQLWW GHQIPAWYNA
EGEIYVGEEA PEGDGWTQDE DVLDTWFSSA LWPFSTMGWP DTDVEDFKRY FPTSTLVTGY
DIIFFWVSRM IFQSLEFTGR QPFQNVLIHG LIRDEEGRKM SKSLGNGIDP MDVIEKYGAD
SLRWFLSNGS APGQDVRFSY EKMDASWNFI NKIWNISRYI LMNNEGLTLE EAESNVAKVA
ASEAGNVTDQ WILHNLNETI AKVTENFDKF EFGVAGHILY NFIWEEFANW YVELTKEVLY
SDNEAEKVIT RSVLLYTLDK IVRLLHPIMP FVTEEIYAQY AQGSIVTVDY PVVRPAFENE
AAHKGVERLK DLIRAVRNAR AEVNVAPSKP ITILVKTADS ELEDFFTSNV NYIKRFTNPE
KLEISSAIAA PELAMTSIIT GAEIYLPLAD LLNVEEELAR LDKELAKWQK ELDMVGKKLG
NERFVANAKP EVIQKEKDKQ ADYQAKYDAT QERIAEMKKI KS
