SYV_BLOPB
ID SYV_BLOPB Reviewed; 957 AA.
AC Q493Z9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=BPEN_033;
OS Blochmannia pennsylvanicus (strain BPEN).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX NCBI_TaxID=291272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPEN;
RX PubMed=16077009; DOI=10.1101/gr.3771305;
RA Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT evolutionary trends among bacterial mutualists of insects.";
RL Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ40682.1; -; Genomic_DNA.
DR AlphaFoldDB; Q493Z9; -.
DR SMR; Q493Z9; -.
DR STRING; 291272.BPEN_033; -.
DR EnsemblBacteria; AAZ40682; AAZ40682; BPEN_033.
DR KEGG; bpn:BPEN_033; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000007794; 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 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 PANTHER; PTHR11946; PTHR11946; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 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..957
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224444"
FT COILED 889..918
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 47..57
FT /note="'HIGH' region"
FT MOTIF 558..562
FT /note="'KMSKS' region"
FT BINDING 561
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 957 AA; 112037 MW; 80ADDA20B51C1C70 CRC64;
MSNYIVEKIY NPKNIEEPIY KFWEYGDYFS PHGNTSQESY CIMMPPPNIT GQLHLGHAFQ
QTIMDVLIRY QRMQGKNTLW QTGTDHAGIA TQMLVEHKIY NNTGKTRHDY TRDELIKNIW
AWKSQSEQFI TYQMKRLGNS VDWKRQRFTM DTEMSYAVTE AFIRLYRKNL IYRGKRLVNW
DCKLQTAISD LEVINKKTKG SIWYIYYKLD NATISSNSHH LIVATTRPET MLGDTAVAVH
PEDTRYKNYI GQYVIAPITN RRIPIISDKN VDMFKGTGCL KITPAHDFND YIIGKRHGLP
MINIFSLNGK ILKKLEVFNS SGQLTDQLYC KIPQIFHNLD SDNARKKIIS ECNALKLLHN
IEPHDLTIPY SDRTGTIIEP MLTDQWYIRV KHLTQHAIDA VNLNIINFVP KQYKNMYFSW
MNNLQDWCIS RQIWWGHKIP AWYDDNNTIY VGYCEKDIRI KNKLNNNVIL HREKDVLDTW
FSSSLWTFAA LGWPKNTNLL NVFHPTNIII SGFDIIFFWI ARMIMLTMHF IKNDNGSAQI
PFKTVYITGL IRDELGQKMS KSKGNIIDPI DIIDGISIEN LLKKRTKNML QPQLSKHIIN
NTIKQFPNGI KPHGTDALRF TLVALASSGR DIHWDMQRLT GYRNFCNKLW HASRFVLMHT
KNQDCGISIN INEKSFSLAD RWIITKFHQT VQIFHKKLEI YRFDEIANIL HEFIWHQFCD
WYLELTKPIL YHGNALELRG TRYTLITLLE SLLRLTHPII PFITEKIWQE VKTVTGNNGT
TIMLQPFPKY DESVIDMKSV IDIEWIKNAV LAIRTARVNM NISYNIPLQI VFRDTSSEVK
KRITENSKIL CHIAQLKSIH FISKGTIYPK SMTMPLDSSE LLIRIPDTFN KENEINRLKK
ESELINRKIE TIQKLLDDNN FINQAPKSVI KDKQALLNYY ELIQNKLIDQ CAIMKKL
