ID   SYV_EHRCJ               Reviewed;         802 AA.
AC   Q3YT16;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Valyl-tRNA synthetase;
DE            EC=6.1.1.9;
DE   AltName: Full=Valine--tRNA ligase;
DE            Short=ValRS;
GN   Name=valS; OrderedLocusNames=Ecaj_0088;
OS   Ehrlichia canis (strain Jake).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=269484;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16707693; DOI=10.1128/JB.01837-05;
RA   Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P.,
RA   Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C.,
RA   Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W.,
RA   Kyrpides N.C.;
RT   "The genome of the obligately intracellular bacterium Ehrlichia canis
RT   reveals themes of complex membrane structure and immune evasion
RT   strategies.";
RL   J. Bacteriol. 188:4015-4023(2006).
CC   -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As
CC       ValRS can inadvertently accommodate and process structurally
CC       similar amino acids such as threonine, to avoid such errors, it
CC       has a "posttransfer" editing activity that hydrolyzes mischarged
CC       Thr-tRNA(Val) in a tRNA-dependent manner (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate
CC       + L-valyl-tRNA(Val).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DOMAIN: ValRS has two distinct active sites: one for
CC       aminoacylation and one for editing. The misactivated threonine is
CC       translocated from the active site to the editing site (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. ValS type 2 subfamily.
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DR   EMBL; CP000107; AAZ68139.1; -; Genomic_DNA.
DR   RefSeq; YP_302737.1; -.
DR   GeneID; 3618413; -.
DR   GenomeReviews; CP000107_GR; Ecaj_0088.
DR   KEGG; ecn:Ecaj_0088; -.
DR   HOGENOM; Q3YT16; -.
DR   OMA; Q3YT16; SGWILDP.
DR   BioCyc; ECAN269484:ECAJ_0088-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_02005; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd.
DR   InterPro; IPR002303; Val-tRNA_synth_Ia.
DR   InterPro; IPR019754; Val-tRNA_synth_Ia_N.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR11946:SF5; tRNA-synt_val; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   TIGRFAMs; TIGR00422; valS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    802       Valyl-tRNA synthetase.
FT                                /FTId=PRO_0000224608.
FT   MOTIF        45     55       "HIGH" region.
FT   MOTIF       524    528       "KMSKS" region.
FT   BINDING     527    527       ATP (By similarity).
SQ   SEQUENCE   802 AA;  93049 MW;  4B1A79DFF931A674 CRC64;
     MQSIFNNKYQ FKNIETKYNT LWDTTKLYKW KNSGTNQFVI DTPPPTISGQ LHIGHVFSYC
     HTDFIARYQR MLGKDVFYPI GFDDNGLPTE RLVEKTKKIR ATDISRKEFK TICTQVSHEF
     RIQFKQLFQS IGISYDWDLE YHTISKDIQK ISQTSFINLY NKGKLYRKLQ PIFWDCIDKT
     AIARAEVEEN ELSSFMNTIA FSTEAGKAIN IATTRPELMP ACVAVFFNPS DIRYQDLLGQ
     NAIVPIFGNK VKILSDDQVK IDKGTGLVMC CTFGDEMDVY WWNKHNLDTK IIISKSGTID
     HLNTLQGQDV CKQLHGLSIT EARALIIEIL ERNNLLIQKQ EITHNVKCAE RSGAPIEILL
     SHQWFIKVVD IKHELLKQVQ KINWHPQSMR KQIEIWIEGL NWDWCISRQR YFGVPFPVWY
     SKDGKIILPD INKLPIDPTN DLPEGYQDTE IEVETDVMDT WATSSLSTQF HNISATPADL
     RAQSHEIIRS WAFYTILQAY YHNNDIPWKN IMISGWCLAE DKTKMSKSKG NVLTPNKLLD
     EYGADVVRYW TANSKLGADT TFSNEILKLG KRFTTKLWNA SKFVSMFIDQ YSEPDLQYIT
     ETMDKWILSK LYKVIVKATE SFNSFEYCIA LDCIESFFWK DFCDNYLELS KKRAYGELIS
     KQEHLSAVNT LSFVLRELLK MLAPFMPYVT EEIYRTLYSS NNSIHSHNTW PAADVNLYNE
     SDELLGETFI EILNQVRKVK ASAQLSVKYK INKLIINKHF PVSLENDLKA VCNADCIVYD
     NRQNDNKEQL LVSVEFENVQ IT
//