SYV_STRT2
ID SYV_STRT2 Reviewed; 883 AA.
AC Q5M5J8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 114.
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=stu0477;
OS Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=264199;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-250 / LMG 18311;
RX PubMed=15543133; DOI=10.1038/nbt1034;
RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT "Complete sequence and comparative genome analysis of the dairy bacterium
RT Streptococcus thermophilus.";
RL Nat. Biotechnol. 22:1554-1558(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV60187.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000023; AAV60187.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011225592.1; NC_006448.1.
DR AlphaFoldDB; Q5M5J8; -.
DR SMR; Q5M5J8; -.
DR STRING; 264199.stu0477; -.
DR EnsemblBacteria; AAV60187; AAV60187; stu0477.
DR KEGG; stl:stu0477; -.
DR PATRIC; fig|264199.4.peg.480; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_9; -.
DR Proteomes; UP000001170; 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; 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; Reference proteome.
FT CHAIN 1..883
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224581"
FT COILED 809..844
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 46..56
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 883 AA; 101274 MW; 676774EFF42C63D4 CRC64;
MSKELSPKYN PAEVEAGRYQ KWLDEDVFKP SGDKKAKPYS IVIPPPNVTG KLHLGHAWDT
TLQDIIIRQK RMQGFDTLWL PGMDHAGIAT QAKVEARLAE SGISRYDLGR EKFLDKVWEW
KDEYAATIKE QWGKMGLSVD YSRERFTLDE GLSKAVRKVF VELYKKGWIY RGEFIINWDP
KARTALSDIE VIHKDVEGAF YHMNYMLEDG SRALEVATTR PETMFGDTAV AVNPNDDRYK
DLIGKNVILP ILNKPIPIVG DEHADPEFGT GVVKITPAHD PNDFLVGQRH NLPQVNVMND
DGTMNELAGE FNGMDRFEAR KAIVKKLEEI GALVEIEKMT HSVGHSERTG VPVEPRLSTQ
WFVKMDQLAK NAIANQDTDD KVDFYPPRFN DTFLQWMENV HDWVISRQLW WGHQIPAWYN
AEGEIYVGEE APEGDGWKQD EDVLDTWFSS ALWPFSTMGW PDVDSEDFKR YFPTSTLVTG
YDIIFFWVSR MIFQSLEFTG RQPFKNVLIH GLIRDEQGRK MSKSLGNGID PMDVIEKYGA
DALRWFLSNG SAPGQDVRFS YEKMDASWNF INKIWNISRY ILMNNEGLTL DVARENVAKV
AAGQAGNVTD RWILHNLNET IRKVTENFDK FEFGVAGHIL YNFIWDEFAD WYVELTKEVL
YSDNEDEKVI TRSVLLYTLD QILRLLHPIM PFVTEEIFGQ ISEGSIVTAE YPVARPEFEN
EEAAAGVEAL KDVIRSVRNS RAEVNVAPSK PITILIKTSD SKLDAFFNDN INYIKRFTNP
EHLEIAADVE VPDLVMSSII TGAEIYLPLA DLLNVEEELA RLEKELAKWQ KELDMVGKKL
SNERFVANAK PEVVQKERDK QKDYQAKYDA IVVRIDEMKK LVK
