ID   SYV_EHRRW               Reviewed;         810 AA.
AC   Q5HC99; Q5FCN8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02005};
DE            EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02005};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02005};
DE            Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02005};
GN   Name=valS {ECO:0000255|HAMAP-Rule:MF_02005};
GN   OrderedLocusNames=Erum0780, ERWE_CDS_00710;
OS   Ehrlichia ruminantium (strain Welgevonden).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=254945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Welgevonden;
RX   PubMed=15637156; DOI=10.1073/pnas.0406633102;
RA   Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E.,
RA   Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M.,
RA   Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C.,
RA   Berthier D., Botha M., Joubert F., Corton C.H., Thomson N.R., Allsopp M.T.,
RA   Allsopp B.A.;
RT   "The genome of the heartwater agent Ehrlichia ruminantium contains multiple
RT   tandem repeats of actively variable copy number.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Welgevonden;
RX   PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA   Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA   Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT   "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT   reveals an active process of genome size plasticity.";
RL   J. Bacteriol. 188:2533-2542(2006).
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_02005}.
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_02005};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02005}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02005}.
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_02005}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02005}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI26565.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR767821; CAH57790.1; -; Genomic_DNA.
DR   EMBL; CR925678; CAI26565.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011154761.1; NC_006832.1.
DR   AlphaFoldDB; Q5HC99; -.
DR   SMR; Q5HC99; -.
DR   STRING; 254945.Erum0780; -.
DR   EnsemblBacteria; CAI26565; CAI26565; ERWE_CDS_00710.
DR   KEGG; eru:Erum0780; -.
DR   KEGG; erw:ERWE_CDS_00710; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_5; -.
DR   BioCyc; ERUM254945:ERUM_RS00435-MON; -.
DR   Proteomes; UP000001021; 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; 3.40.50.620; -; 2.
DR   HAMAP; MF_02005; Val_tRNA_synth_type2; 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR022874; Valine-tRNA_ligase_type_2.
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; 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; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..810
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224610"
FT   MOTIF           45..55
FT                   /note="'HIGH' region"
FT   MOTIF           534..538
FT                   /note="'KMSKS' region"
FT   BINDING         537
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   810 AA;  93855 MW;  6702A8B59CD39580 CRC64;
     MQSLFSNKYK FKDTEEKLNA YWDKIKLYKW KNLQGKQFII DTPPPTISGQ LHIGHVFSYC
     HTDFIARYQR MLGKDVLYPI GFDDNGLPTE RLVEKIKKVR AADIDRKEFK ALCNEVSAKF
     RMEFKILFQS LGISYDWDLE YHTISEEIQK LSQMSFIALY NMGKIYRKLQ PIFWDCADRT
     AIARVEVEEK EMSSFMSTIA FSTEAGELIN IATTRPELMP ACVALFFNPL DIRYQHLQGQ
     YAIVPIFGNK VPILSDEQVK IDKGTGLVMC CTFGDELDVY WWNKHNLNTQ IIISKSGTLD
     LKHNIAETDT LSGKLHGVSI VEARKLVLET LSKCNLLIKK EEILHNVKCA ERSGMPIEIL
     LSNQWFIKVV EIKHELLEQV RKINWYPQSM RKQIEMWIDG LNWDWCISRQ RYFGIPFPVW
     YSKRDNEEII IPDVNELPID PTETLPQGYS KEEVEADVDV MDTWATSSLS PQFNSIHTGI
     NSIPLIPASL RAQSHEIIRS WAFYTILQAY YHHNSIPWEN IMVSGWCLAA DKSKMSKSKG
     NALIPNQLLQ EYGADVIRYW AANSRLGSDT VFSDEVLQLG KRLVTKLWNA SKFVSMFVSQ
     CQIPDLNCVT ETMDKWVLTK LYKVIVKATE SFNVFEYCVA LDYIESFFWK DFCDNYLELV
     KKRAYGESVT NKENLSAVNT LSFVLMALLK MLAPFMPYIT EEIYSTLYNN GSIHDHDNWP
     VVNTSLCNEM DEQLGEDFIE ILNQVRKIKA NAQLSVKCKI YKLIINSENY DFPTSWENDL
     KAVCNAEHIV QDKRTSYYND KFLISVQFAN