ID   SYV_CERS1               Reviewed;         987 AA.
AC   A3PHJ6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Rsph17029_0699;
OS   Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=349101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17029 / ATH 2.4.9;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.,
RA   Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC 17029.";
RL   Submitted (FEB-2007) 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: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; CP000577; ABN75812.1; -; Genomic_DNA.
DR   RefSeq; WP_011840547.1; NC_009049.1.
DR   AlphaFoldDB; A3PHJ6; -.
DR   SMR; A3PHJ6; -.
DR   EnsemblBacteria; ABN75812; ABN75812; Rsph17029_0699.
DR   GeneID; 57469385; -.
DR   KEGG; rsh:Rsph17029_0699; -.
DR   HOGENOM; CLU_001493_0_2_5; -.
DR   OMA; FATKLWN; -.
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   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..987
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_1000022172"
FT   COILED          917..985
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;  110523 MW;  3F77AA0C915483A3 CRC64;
     MPMDKTFNAA EAEARLYDAW EKAGAFRAGA NASRPETFCI MIPPPNVTGS LHMGHAFNNT
     LQDILTRWHR MRGFDTLWQP GQDHAGIATQ MVVERELARA GNPGRREMGR EAFLEKVWEW
     KEQSGGTIVN QLKRLGASCD WSRNAFTMDP NFQRAVLKVF VDLYEKGFIY RGKRLVNWDP
     HFETAISDLE VEQVEVNGNM WRLRYQLADG ATYRHPVAFD EEGRPTEWEE RDYLTVATTR
     PETMLGDTGI AVNPSDERYA HLIGKEVVLP LVGRRIPIVA DDYADPSKGT GAVKITPAHD
     FNDWGVGQRT GLRAINVMSG RATMFLIENP DFTEGCAPSE EALALDGLDR YEARKRVVAL
     AEEQGWLDGI DQDRHMVPHG DRSKVAIEPM LTDQWFVDTA QIVQPAIDAV RTGRTEILPE
     RDAKTYFHWL ENIEPWCISR QLWWGHQIPV WYGLDIWPAR FEDDGDDTLD EVEIFELLED
     GAFNHADPTH HCAFDFEGVS EKFLDDLASL PHPLNNARVV EVASRAEAID RLAQALADYN
     LNEDPTHLVY PVWRDPDVLD TWFSSGLWPI GTLGWPEETP ELARYFPTNV LITGFDIIFF
     WVARMMMMQL AVVNEVPFKT VYVHALVRDE KGKKMSKSLG NVLDPLELID EFGADAVRFT
     LTAMAAMGRD LKLSTARIQG YRNFGTKLWN ACRFAEMNGV WEGHGTQAAP PAATATVNRW
     IIGETGRVRE EVDAALAAYR FDSAANALYA FVWGKVCDWY VEFSKPLFDT EAAAETRATM
     GWVLDQCMVL LHPIMPFITE DLWATTGSRT KMLVHTDWPS FGAELVDPAA DREMSWVISL
     IEEIRSARAQ VHVPAGLKLP VVQLALDAAG REALARNEAL ILRLARLEGF TEAASAPKGA
     LTIAVEGGSF AIPLEGVIDI GAEKARLAKT LEKLEKDMAG LRGRLGNPNF VASAPEEVVD
     EARTRLEQGE EEGAKLSAAL ARLSEIA