SYV_ACTP7
ID SYV_ACTP7 Reviewed; 954 AA.
AC B3GYI3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=APP7_1562;
OS Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=537457;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP76;
RA Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA Tegetmeyer H., Singh M., Gerlach G.F.;
RT "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL Submitted (JUN-2008) 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: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; CP001091; ACE62214.1; -; Genomic_DNA.
DR RefSeq; WP_005617986.1; NC_010939.1.
DR AlphaFoldDB; B3GYI3; -.
DR SMR; B3GYI3; -.
DR EnsemblBacteria; ACE62214; ACE62214; APP7_1562.
DR KEGG; apa:APP7_1562; -.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR BioCyc; APLE537457:APP7_RS08045-MON; -.
DR Proteomes; UP000001226; 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; -; 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.
FT CHAIN 1..954
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000189237"
FT COILED 883..954
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT MOTIF 560..564
FT /note="'KMSKS' region"
FT BINDING 563
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 954 AA; 108798 MW; 3A9E32FA16BBE359 CRC64;
MTQNLQMADR FDSSAVEQAL YKHWEEQGYF KPTENPSLPS YCIAIPPPNV TGSLHMGHAF
QQTLMDTLIR FNRMEGNNTL WQTGTDHAGI ATQMVVERKI AAEEGKTRHD YGREAFINKI
WDWKAYSGGT ISQQMRRLGN SIDWDREHFT MDEGLSNAVK EVFVRLHEEG LIYRGKRLVN
WDPKLHTAIS DLEVENKESK GSLWHFRYPL ANGAKTADGK DYLVVATTRP ETVLGDTAVA
VHPEDERYQS LIGKTVVLPL ANREIPIVAD EYVDREFGTG VVKITPAHDF NDYEVGKRHG
LPMVNVMTMN ADIRAEAEII GTDGKPLTTY EAKIPADYQG LERFAARKKV VADFEALGLL
DEIKPHDLKV PYGDRGGVPI EPMLTDQWYV SVKPLAEVAT KAVEDGEIQF VPKQYENLYF
SWMRDIQDWC ISRQLWWGHR IPAWYDEAGN VYVARSEEEV RQKHNLPADL ALRQDEDVLD
TWFSSGLWTF STLGWPEQTK ELKMFHPTDV LITGFDIIFF WVARMIMFTM HFVKDENGKP
QVPFKTVYVT GLIRDEQGQK MSKSKGNVLD PIDMIDGISL EDLLEKRTGN MMQPQLAEKI
AKATRKEFEN GIAAHGTDAL RFTLAALASN GRDINWDMKR LEGYRNFCNK LWNASRFVLT
NDKLDLSAGE VEYSLADRWI ESKFNRTVGE FREALSQYRF DLAANAIYDF TWNEFCDWYL
ELTKPVFANG TEAQKRGASQ TLVRVLEKLL RLAHPIMPFI TEEIWQKVKG FAGIDADTIM
LQPFPKVVKS ELDESAEMQI GWIKELIIAV RNIRAESNIA PSKGLEFLVR NVSDEQRKIL
AENDRLLKAM AKLDSVQVLS ADENAPLSVA KLVGNVEVLI PMAGFINKEA ELARLTKEIE
KMRGEITRIE NKLGNEAFVA KAPEAVIAKE REKMQEYQNG LEKLQTQYQA IENL
