SYV_BUCAI
ID SYV_BUCAI Reviewed; 955 AA.
AC P57447;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=BU366;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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; BA000003; BAB13070.1; -; Genomic_DNA.
DR RefSeq; NP_240184.1; NC_002528.1.
DR RefSeq; WP_010896088.1; NC_002528.1.
DR AlphaFoldDB; P57447; -.
DR SMR; P57447; -.
DR STRING; 107806.10039036; -.
DR EnsemblBacteria; BAB13070; BAB13070; BAB13070.
DR KEGG; buc:BU366; -.
DR PATRIC; fig|107806.10.peg.380; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000001806; 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; 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; Reference proteome.
FT CHAIN 1..955
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106216"
FT COILED 926..946
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 41..51
FT /note="'HIGH' region"
FT MOTIF 554..558
FT /note="'KMSKS' region"
FT BINDING 557
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 955 AA; 112990 MW; E7511B1E3BF86706 CRC64;
MEKIYNPKHI EESLYFFWEK NGFFKPNHLE KSTFCIMMPP PNITGSLHMG HAFQQTIMDI
LIRYHRMQGK NTFWQVGTDH AGIATQILVE RQIFEKEQKT KKDYSRDDFI KKIWEWKKQS
SNIITKQMRR LGISVDWDYE KFTLDPDISN SVREAFIILY KNNLIYQKKK LVHWDSKLET
VISDLEVEHR LIKGKKWFIR YPIIENDMSL RSKVKYLIVS TTRPETLLGD TAIAVNPEDY
KYNQFIGNHV SCPLTNRIIP IIKDRYADLE KGTGCVKITP AHDFNDYKVG LHHKLPMINI
FTFDGRIKST AEVYNYKGEK SNQYSTCIPM QFQHLDILSA RIEIIKEITK LGFLEKIEEC
NVTVPYSERS GVIIEPMLTN QWYLKTSTLA KVALNAVKDK KIKFIPQQYE SMYSSWMNNI
EDWCISRQLW WGHRIPVWYD DQKNIYIGQN EKEIRQAYSI SENVLLKQEN DVLDTWFSSG
LWTFSSLGWP KKTTFLKTFH PTNVLVSGFD IIFFWIARMI MLTMYFMKDK HNNPEVPFKN
IYITGLIRDE FGKKMSKSKG NVIDPLDMID GISLSELIKK RTNNLLQPNL SDKIIQRTIK
QFPEGIKSTG TDALRFTFSA LASSTRDIQW DMNRLKGYRN FCNKLWNASR FVLINTQDHN
FSKFDVKRKM LLINKWILIE FNNTVKLYRE SLDTYRFDIA ANILYDFIWN IFCDWYLEFV
KIVIKLGSSK EVYCTKNVLV YVLELLLKLA HPIMPFITET IWQRIKLIQN ISEKTIMLQD
FPEYNHKLFD KKILVQMNWM KKIIVFLRNI RTNMNVSSTK LLPLFLYNIN SEQEKVIKEN
ISLIKNISFL DKITILSEKY DKDLCIKEII DGAEIIIPIL KLVDTKVELK RLVKEQKKTE
LNIFKIKTKI LNKDFLSYAP TKIVTQEKNK LLKLNEINLK LSEQIKIFRN MSYKK
