ID A0A0E4GEA0_9FIRM Unreviewed; 881 AA.
AC A0A0E4GEA0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02004};
DE EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02004};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02004};
DE Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02004};
GN Name=valS {ECO:0000256|HAMAP-Rule:MF_02004};
GN ORFNames=1925 {ECO:0000313|EMBL:CFX81103.1};
OS Syntrophomonas zehnderi OL-4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=690567 {ECO:0000313|EMBL:CFX81103.1, ECO:0000313|Proteomes:UP000045545};
RN [1] {ECO:0000313|EMBL:CFX81103.1, ECO:0000313|Proteomes:UP000045545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OL-4 {ECO:0000313|EMBL:CFX81103.1,
RC ECO:0000313|Proteomes:UP000045545};
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00001624, ECO:0000256|HAMAP-
CC Rule:MF_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000256|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:0000256|HAMAP-Rule:MF_02004}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02004}.
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DR EMBL; CGIH01000031; CFX81103.1; -; Genomic_DNA.
DR RefSeq; WP_046498202.1; NZ_CGIH01000031.1.
DR AlphaFoldDB; A0A0E4GEA0; -.
DR STRING; 690567.1925; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000045545; Unassembled WGS sequence.
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 CDD; cd00817; ValRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 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 NCBIfam; TIGR00422; valS; 1.
DR PANTHER; PTHR11946:SF93; VALINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 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; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF46589; tRNA-binding arm; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02004};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02004}; Coiled coil {ECO:0000256|HAMAP-Rule:MF_02004};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02004};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02004};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02004};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02004}; Reference proteome {ECO:0000313|Proteomes:UP000045545}.
FT DOMAIN 18..565
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 608..753
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 815..877
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 820..875
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 47..57
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 526..530
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 881 AA; 100841 MW; 23BED7D952D47055 CRC64;
MSINSLPSVY DPKDVEAKWY SFWKSRNYFA PDNDRSKETF TIVMPPPNVT GQLHLGHALD
NTLQDILTRW RRMQGYRTLW LPGTDHAGIA TQAKVEEALA QEGLSRHDLG REKFLDRVWE
WKHLYGGRIT QQLSLMGSSC DWSRERFTMD EACSRAVREV FVNLFEKGLI YQGNYITNWC
PKCQTAISDI EVEHEDSDGY LWHIKYPVED SDEYLVIATT RPETMLGDTG VAVHPDDERY
THLLGKNVVL PLVGRKIPVF ADEYVDREFG TGAVKVTPAH DPNDFDMGLR HHLEQLVVIN
PDGTMSAATG PFAGMDRYAC RKEIVERLKA DGSLLKIDDH RHAVGHCQRC DTVIEPLISK
QWFVKMKPLV KPAVEKVLNG EIRFVPERFT KIYVSWMENI RDWCISRQLW WGHRIPVWYC
QDCGEIICSK ADPDICPACS SSQLQQDEDV LDTWFSSALW PFSTLGWPED TDDMADFYPT
SVLVTGRDII FFWVARMIFS GIEHTGQVPF HEVNIHGLIL DGQGRKMSKS LGNGIDPIEV
IEKYGADTLR FSMITGVTPG NDVRFHWDKV ENSRNFANKI WNASRFVLMN LEGMAAIEIN
ADELTLADRW ILSRFNLKAE ETTRLLERYD LGEAAKGLYE FIWDEYCDWY IELTKPRLTN
SASLREKQVA QKVLRDVHMG ILRLLHPFMP FITEEIYQQL PGHQESIMID PWPLKDEKQI
WPEAVEGMQA IMAVTRALRN IRAEFNISPA ASINTIMLVE NAANWDLFKN YGRYIEAMAK
TQLEMVANMD VKPRQAVSAL TNVAEIYVPL EGVIDVGKEI GRLKKDLKQV EADLARTEGK
LNNSAFLAKA PPDVIAKEKA KAQEAISRKE GIEQRLQIFQ A
//
