SYV_LEPIN
ID SYV_LEPIN Reviewed; 882 AA.
AC Q8EZT8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 108.
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=LA_3763;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
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; AE010300; AAN50961.2; -; Genomic_DNA.
DR RefSeq; NP_713943.2; NC_004342.2.
DR RefSeq; WP_000744010.1; NC_004342.2.
DR AlphaFoldDB; Q8EZT8; -.
DR SMR; Q8EZT8; -.
DR STRING; 189518.LA_3763; -.
DR EnsemblBacteria; AAN50961; AAN50961; LA_3763.
DR KEGG; lil:LA_3763; -.
DR PATRIC; fig|189518.3.peg.3736; -.
DR HOGENOM; CLU_001493_0_2_12; -.
DR InParanoid; Q8EZT8; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000001408; Chromosome I.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 1.10.287.380; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
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_0000224497"
FT COILED 812..881
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 45..55
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 882 AA; 101059 MW; 79A257FAD72751A6 CRC64;
MKKQIGDRYE PKDVENKWIS LWEKKKSFAP NSNARESFSI VIPPPNVTGS LHIGHALNHT
IQDILVRIER KKGKSTLWLP GMDHAGIATQ MVVERELAKE SKKRTDFTRE EFIHKVWEWK
NHSGGMITKQ QKLLGESVDW SRERFTLDEG LSKAVFKVFK SLYDEGLIYR GERIINWCPA
SQTAISDLEV EFRETKGKLY HIKYPIHGKK DQFLVVATTR PETMLGDVAV CANPEDERYT
SLKDVVLDLP LTNRQIPLLF DSFVDKEFGS GLVKITPAHD ANDFEAGQRL GLKPLLVMNP
NGTMNENAGI YQGLDRFEAR KKVLADLEAK GLIEKIEDHI HAVGHNSRGG AVIEPYLSTQ
WFVKIKPLAD LAVQAVQSGQ VEFIPKMWEK TFFEWMNNIR DWCISRQLWW GHRIPAYHCK
KCKHFEVSET AVTVCTSCGS QEVEPDPDVL DTWFSSQLWP FSTLGWPDQT EDLKRYYPTS
VLVTGFDIIF FWVSRMIMMG MKFMQAPPFH KVLIHGLVRD KDGKKFSKSV GNVIDPLVMM
DKYGTDSFRF FLAATLPEGK DILFDESRLD GYRSFCNKIW NSSRFILMNL EESFVPIGIT
PDIEKDLEPM DQWILSRFNH CLEEYNKAHS KFHFYEMAAA IYEFIWGDFC DWYIELVKPR
AYGKVSPRSA EVAKQVLSDV LIRALGLLHP FMPFLTEEVH SVFSDQYIVT TPFPESYPVA
SDSLGVQKLN LLQEIVTKIR VMRSENGVAP DRKCKAIVKS SDNLSSSTIL ENEVSLLQLA
RLESIRIDTL YEIQKTDSVS HFTKGEIVLP LEGLIDVAKE KTRLEKELQK SELEKEKLEI
KLSNPGFLSK AAPEVVEKER DKLKTLIDKV EVLKKGIQNL AG
