SYV_PARD8
ID SYV_PARD8 Reviewed; 873 AA.
AC A6LIG7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=BDI_3795;
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000140; ABR45481.1; -; Genomic_DNA.
DR RefSeq; WP_009017033.1; NC_009615.1.
DR AlphaFoldDB; A6LIG7; -.
DR SMR; A6LIG7; -.
DR STRING; 435591.BDI_3795; -.
DR PRIDE; A6LIG7; -.
DR EnsemblBacteria; ABR45481; ABR45481; BDI_3795.
DR KEGG; pdi:BDI_3795; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_10; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR BioCyc; PDIS435591:G1G5A-3892-MON; -.
DR Proteomes; UP000000566; 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; 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..873
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000022171"
FT COILED 802..873
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 532..536
FT /note="'KMSKS' region"
FT BINDING 535
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 873 AA; 99787 MW; 1A37F717C2DC3ADD CRC64;
MEIASKYNPA EVEGKWYQYW LDNGFFKSKP DGREPYTIVI PPPNVTGVLH MGHMLNNTIQ
DILVRRARMM GKNACWVPGT DHASIATEAK VVNRLAGQGI KKTDLTRDEF LRHAWEWKEE
HGGIILKQLR KLGASCDWDR TAFTMDEKRS ESVIKVFVDL YKKGLIYRGV RMVNWDPKAL
TALSDEEVIY KEEHSKLYYL RYKIVGEEGY AVVATTRPET IMGDTAMCIN PNDPKNQHLR
GKKVIVPLVG REIPVIEDDY VDIEFGTGCL KVTPAHDVND YMLGEKYNLP SIDIFNDNGT
LSEAAGLYVG MDRFDVRKQI EEDLRNAGLL EKVEAYENKV GFSERTNVPI EPKLSMQWFL
KMEHLAQIAL EPVMKDDIKF YPPKFKNTYR HWMENIKDWC ISRQLWWGHR IPAYFLPEGG
YVVAETEEKA LELAKEKCGN PNLTMSDLRQ DEDVLDTWFS SWLWPISLFD GINNPDNEEI
NYYYPTSDLV TGPDIIFFWV ARMIMAGYEY RGKMPFKSVY FTGIVRDKLG RKMSKSLGNS
PDPLQLIEQY GADGVRMGLM LAAPAGNDIP FDDALCEQGR NFNNKIWNAF RLVKGWTVDD
TIAQPEASAI AVKWFKMQLD KTIAEVDDSF SKYRLSEAMM AVYKLFWDEF SSWYLEMVKP
GYQQPIDKAT YEATLGFFDA LLRLLHPFMP FITEELWQAL EPRKEGESLM VAQMPEIAVI
DSAYLDAFEI VKEIVGGVRT IRLQKNIPNK DALELQIVGE HNEAFNAVIA KMCNLSSISK
VEEKAAGAVS FLVRTTEYAV PLGNLINVEE ELAKLQEELK YQKGFLASVM KKLGNENFVS
KAPAKVIEME KKKQADAESK IKSIEESIAA LTK
