SYV_LACCA
ID SYV_LACCA Reviewed; 883 AA.
AC P36420;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 113.
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};
OS Lactobacillus casei.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1582;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8468307; DOI=10.1128/jb.175.8.2475-2478.1993;
RA Taylor B.V., Toy J., Sit T.L., Bognar A.L.;
RT "Cloning and sequence determination of the valS gene, encoding valyl-tRNA
RT synthetase in Lactobacillus casei.";
RL J. Bacteriol. 175:2475-2478(1993).
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=AAA57558.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L08854; AAA57558.1; ALT_INIT; Genomic_DNA.
DR PIR; A49856; A49856.
DR AlphaFoldDB; P36420; -.
DR SMR; P36420; -.
DR STRING; 1582.AAW28_03910; -.
DR eggNOG; COG0525; Bacteria.
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.
FT CHAIN 1..883
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106229"
FT REGION 859..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 811..883
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 50..60
FT /note="'HIGH' region"
FT MOTIF 527..531
FT /note="'KMSKS' region"
FT BINDING 530
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 883 AA; 100962 MW; 679887435CACED9A CRC64;
MEPVSDETLA PKYDHKAVEE GRYQEWLDED VFKPSGDKKA KPYSIVIPPP NVTGKLHMGH
AWDTTLQDIV IRQKRIEGFD TLWLPGMDHA GIATQAKVEA KLRKEGISRY DLGREKFVQK
VWEWKDEFAK TIHGQWAKMG LSLDYSRERF TLDKGLNQAV RRVFVDLYNQ GLIYRGEYIV
NWDPQARTAL SDIEVIHKDD KGAFYHVKYP FADGSGYIEI ATTRPETMMG DTAVAVHPGD
ERYKDMVGTE LILPLANRKI PIIEDAYVDP EFGTGAVKIT PAHDPNDFQV GNRHDLKRIN
TMNDDGTMNE NAGKYQGMDR FEARKAMVAD LDKAGLLLKV EPIVHSVGHS ERTGVQVEAR
LSTQWFVKMK PLAEAAIKAQ QEPDKKVTFV PERFEHTYLQ WMENIHDWVI SRQLWWGHQI
PAWYNKQTGE TYVGMEAPKD IENWKQDPDV LDTWFSSALW PFSTMGWPNT DAPDYKRYYP
TDTLVTGYDI IPFWVARMIF QGLHFTHQRP FQYTLIHGLM RDEQGRKMSK SLGNGIDPMD
VIEKYGADAL RWFLITGNKP GQDTRFSYKQ VEAAWNFINK IWNISRFVMM NLGDLDTPQQ
PDPSTFDLSD KWLFAQLNET IKQVMDLSAR FEFGEMGRTL YNFTWNVLAD WYVEMSKEVL
YGDDEQAKAA KRVNLAYALD QILRLLHPVM PFVHGKLWLA LPHTGKSIVT ASYPVANTAF
ENADATSAMD AIIALIRGVR GIRKEAGAPL KTKVDILVKL TDPALKPIFE QNFDFIDRFV
NSKAFTVGTD VAEPKMAGSA VITGATIFVP LNELIDLDEE KAKLTKDAKK LEQEIARIDK
KLNNQGFLSK APEAVVAEQR TKRSDFEDQL TSTKQRLEQL QRA
