SYV_CERSK
ID SYV_CERSK Reviewed; 987 AA.
AC B9KMT9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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};
GN OrderedLocusNames=RSKD131_0291;
OS Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=557760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KD131 / KCTC 12085;
RX PubMed=19028901; DOI=10.1128/jb.01565-08;
RA Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL J. Bacteriol. 191:1118-1119(2009).
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; CP001150; ACM00151.1; -; Genomic_DNA.
DR RefSeq; WP_012643613.1; NC_011963.1.
DR AlphaFoldDB; B9KMT9; -.
DR SMR; B9KMT9; -.
DR EnsemblBacteria; ACM00151; ACM00151; RSKD131_0291.
DR GeneID; 67445770; -.
DR KEGG; rsk:RSKD131_0291; -.
DR HOGENOM; CLU_001493_0_2_5; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000001597; Chromosome 1.
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; -; 3.
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; 2.
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 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..987
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000189243"
FT COILED 917..987
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT MOTIF 634..638
FT /note="'KMSKS' region"
FT BINDING 637
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 987 AA; 110778 MW; 3827264B62149193 CRC64;
MPMDKTFNAA EAEARLYDAW EKAGAFRAGA NASRPETFCI MIPPPNVTGS LHMGHAFNNT
LQDILTRWHR MRGFDTLWQP GQDHAGIATQ MVVERELARA GNPGRREMGR EAFLEKVWEW
KEQSGGTIVN QLKRLGASCD WSRNAFTMDP NFQRAVLKVF VDLYEKGFIY RGKRLVNWDP
HFETAISDLE VEQVEVNGNM WRLRYRLADG ATYRHPVAFD EEGRPTDWEE RDYLTVATTR
PETMLGDTGI AVNPSDERYA HLIGKEVVLP LVGRRIPIVA DDYADPSKGT GAVKITPAHD
FNDWGVGQRT GLRAINVMTG RATMFLIENP DFTEGCAPSE EALALDGLDR YEARKRVVAL
AEEQGWLDGI DQDRHMVPHG DRSKVAIEPM LTDQWFVDTA QIIQPAIDAV RTGRTEILPE
RDAKTYFHWL ENIEPWCISR QLWWGHQIPV WYGLDIWPAR FEDDGDDTLD EVEIFELLED
GAFNHADPTH HCAFDFEGVS EKFLDDLASL PHPLNNARVI EVASRAEAID RLAQALADYN
LNEDPTHLVY PVWRDPDVLD TWFSSGLWPI GTLGWPEETP ELARYFPTNV LITGFDIIFF
WVARMMMMQL AVVNEVPFKT VYVHALVRDE KGKKMSKSLG NVLDPLELID EFGADAVRFT
LTAMAAMGRD LKLSTARIQG YRNFGTKLWN ACRFAEMNGV WEGHATQAAP PAATATVNRW
IIGETGRVRE EVDAALAAYR FDSAANALYA FVWGKVCDWY VEFSKPLFDT EAAAETRATM
GWVLDQCMVL LHPIMPFITE DLWATTGSRT KMLVHTDWPS FGAELVDPAA DREMSWVISL
IEEIRSARAQ VHVPAGLKLP VVQLALDAVG REALARNEAL ILRLARLEGF TEAASAPKGA
LTIAVEGGSF AIPLEGVIDI GAEKARLAKT LEKLEKDMAG LRGRLNNPNF VASAPEEVVD
EARTRLEQGE EERAKLSAAL ARLSEIA
