SYV_BUCBP
ID SYV_BUCBP Reviewed; 956 AA.
AC Q89AG3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=bbp_331;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27052.1; -; Genomic_DNA.
DR AlphaFoldDB; Q89AG3; -.
DR SMR; Q89AG3; -.
DR STRING; 224915.bbp_331; -.
DR PRIDE; Q89AG3; -.
DR EnsemblBacteria; AAO27052; AAO27052; bbp_331.
DR KEGG; bab:bbp_331; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000000601; 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..956
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106218"
FT COILED 889..920
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 556..560
FT /note="'KMSKS' region"
FT BINDING 559
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 956 AA; 112418 MW; 4FDB5E97B96C5D02 CRC64;
MIKKYFDPLR MEKSLYEFWE KNGYFKPQNN KGKPNFCIVM PPPNITGNLH IGHAFQQTIM
DILIRYNRMI GKNTFWQVGT DHAGIATQIV VEKKILKEEN KTVQQLGKKE FLERIWKWKN
TSKNVITSQM RRLGISVDWT HEKFTLDPQI SFAVRKVFMT LYDECLIYKR KKLVNWDPVL
KTVISDLEVK NRNVIGNMWY IKYYLVKNHS IKISQEYYLV IATTRPETLF GDTAIAVHPN
DSRYKKYIGC YALVPIINRI IPIISDEFVD VNKGTGCVKI TPAHDFNDYE IAMRHNLSII
NVFTRNGKIT DVIEEYDISG EKSCIYKQNV PLRFHHLDRF IARKIIVKEL IALKLLIKIQ
KHNLAIPYGE RSGSVIEPLL TDQWYLRVEP LAKIAVEAVK SGKIIFIPKK YEKIYYSWMN
NIKDWCISRQ LLWGHRMPIW YDKKNNIYVG LDEKHIREKY HISDDIFLIQ ETDVLDTWFS
SSLWMFSSLG WPNNKDLFKN FYSTDVVVSG FDIIFFWIAR MIMLSMHLIK DHNGNGRVPF
KKVYITGLIC DEHGKKMSKS KGNVVDPLDM IDGISLDALI QKRIKSTVFS THSKKIITQI
QSLYPNGINS SGVDALRFTC AALSTPTRYI KWNINRLYGY RNFCNKLWNA SRFILMNLTH
EVEPVKLILI KPMSLSDRWI VAEFHNLVKR YRTALDNYRF DIAANVLYEF VWNKFCDFYI
ELVKSFINSC SMLELKSTRC TLVYILDSVL RLAHPIIPFI TEEIWQKLQV FVKKNDKNTI
MLQSFPKYDV KLVNKTILED MDWIKNIFII IRSFRMDLKI SHTTLISISF KNVSSKIHKL
IEEHKDYIKK IAYLDNVSII LSNVDSMLFF KSYIVLGAEL LIPYSKIFPK EKELKNLNKE
ISKIQLAINK LQQRLSNEEF IGKAPIHVVK KYKNQLQIYI EHKTQLCHKK LTMLRD
