ID A0A172WDQ0_BUCSC Unreviewed; 953 AA.
AC A0A172WDQ0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=XW81_01675 {ECO:0000313|EMBL:ANF17106.1};
OS Buchnera aphidicola subsp. Schlechtendalia chinensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=118110 {ECO:0000313|EMBL:ANF17106.1, ECO:0000313|Proteomes:UP000077654};
RN [1] {ECO:0000313|EMBL:ANF17106.1, ECO:0000313|Proteomes:UP000077654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC {ECO:0000313|EMBL:ANF17106.1,
RC ECO:0000313|Proteomes:UP000077654};
RA Zhang Y.;
RT "Buchnera aphidicola assembly.";
RL Submitted (APR-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; CP011299; ANF17106.1; -; Genomic_DNA.
DR RefSeq; WP_075474228.1; NZ_CP011299.1.
DR AlphaFoldDB; A0A172WDQ0; -.
DR STRING; 118110.XW81_01675; -.
DR PATRIC; fig|118110.3.peg.337; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000077654; 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 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 Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing 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; 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 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:UP000077654}.
FT DOMAIN 13..634
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 677..823
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 558..562
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 561
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 953 AA; 112313 MW; A9C19015A460AEA1 CRC64;
MKKYFNPIDI EEKLYDFWEK NGYFKPDFSC NKSNFCIILP PPNITGNLHI GHAFQYTIMD
ILVRYHRMQG KNTLWQVGTD HAGIATQIVL EKKILLKEEK TLKEYGKEKF IKKAWEWKKK
SIHKITYQMR RLGISVDWTR QKFTLDPEIS YAVKQAFIIL FNQKLIYKRK KLVNWDPILK
TVVSDLEVQN RNSIGKMWYI RYTVINNNSD IDNDDISNEY LTIATTRPET LFGDAAVAVH
PEDKRYKKFI GRNVLVPLIN RVVPIIGDYY VQMDKGTGCV KVTPAHDFND FAIGVRHNLP
IINIFTLDGD ISDTVQEYCL DGKPSNIYDK EIPLKYRKIN KFLARKLIIN ELIENNQLEK
VENYNLTIPY GDRSNAIIEP LLTNQWYLSV SSLSKKALDS VKNGDIEFIP RSYENIYFSW
MSKIEDWCIS RQLWWGHQIP IWYDKKGNMY AGHCERHVRK TYSLSKEVEL IQDDDVLDTW
FSSGLWVLAS LGWPKDISFL KKFYSTDVIV SGFDIIFFWI SRMIMLSMHF MTDKQKKLTV
PFKKVYITGL ICDENGRKMS KSEGNVIDPI DMIDGITLES LIKKRTKDML CSKLEIQIQK
RTKIMFPNGI NATGTDALRF TCAALASPTR YINWNVNRLF GYRNFCNKLW NASRFLLLNI
DIAMKFHDDK KVLSIADKWI LLKFNTTVKE YRYALDTYRF DLASSVLYEF VWNIFCDFYI
ELVKPFIVSC SDLELVGTKH TLLYVLESIL RLAHPIIPFI TEEIWQKIRI FLNTKDVNTI
MLCSFPKYKK NFNDNNVLKD MKRIRSIIEI VRQYRNNIKL TYKTLIPIYF YNTSLKINML
IESHKEYLKK VLYLKDITIL FDNKNRSSYL SYSFFGSEIL IPILGNFSKN MEFERISKEI
LKTTLKIKKI KNQLFNKNFL KNAPQEIIKN VKKQFKDLNM NLEKLLLKKD QLL
//
