ID   SYV_DECAR               Reviewed;         943 AA.
AC   Q47BG6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=Daro_3085;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Dechloromonas.
OX   NCBI_TaxID=159087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S., Kellar K.,
RA   Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.;
RT   "Complete sequence of Dechloromonas aromatica RCB.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for
CC       aminoacylation activity (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. ValS type 1 subfamily.
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DR   EMBL; CP000089; AAZ47815.1; -; Genomic_DNA.
DR   RefSeq; YP_286285.1; -.
DR   GeneID; 3566514; -.
DR   GenomeReviews; CP000089_GR; Daro_3085.
DR   KEGG; dar:Daro_3085; -.
DR   NMPDR; fig|159087.4.peg.3070; -.
DR   HOGENOM; Q47BG6; -.
DR   OMA; Q47BG6; WPDETPE.
DR   BioCyc; DARO159087:DARO_3085-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_02004; -; 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   InterPro; IPR019499; Val-tRNA_synth_Ia_tRNA-bd.
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   Pfam; PF10458; Val_tRNA-synt_C; 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; Coiled coil;
KW   Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN         1    943       Valyl-tRNA synthetase.
FT                                /FTId=PRO_0000224470.
FT   COILED      875    934       Potential.
FT   MOTIF        45     55       "HIGH" region.
FT   MOTIF       541    545       "KMSKS" region.
FT   BINDING     544    544       ATP (By similarity).
SQ   SEQUENCE   943 AA;  106500 MW;  9CB7A2DAC73D3442 CRC64;
     MELAKAFEPA DIERRWYPEW ETQNYFAAGV DASKADNFCI LLPPPNVTGT LHMGHGFNQT
     IMDALTRYYR MRGHNTLWQP GTDHAGIATQ IVVERQLDAQ GISRHDLGRE KFLEKVWEWK
     EYSGNTITKQ MRRMGTSPDW KRERFTMDAG LNKVVTETFV RLFNEGLIYR GKRLVNWDPK
     LNTAVSDLEV VQEEEDGFMW HIRYPLADGS DSLVVATTRP ETMLGDTAVM VHPEDERYKH
     MIGQMVKLPL TDREIPIIAD SYVDLEFGTG CVKVTPAHDF NDYAVGQRHG LPMISILTLD
     AKVNENAPEK YRGLDRFDAR KAVVADLEAL GILEKTDKHK LKVPRGDRTN VVIEPMLTDQ
     WFVAMSKPGD DGKSITEKAL DVVHSGEIKF YPENWVNTYN QWLNNIQDWC ISRQLWWGHQ
     IPAWYGDNGQ IFVAHSEAEA KAEAAKQGYT GTLKRDEDVL DTWFSSALWP FSTLDWTGDE
     AIDAANPLLK QYLPSSVLVT GFDIIFFWVA RMVMMTKQIT GQIPFKHVYV HGLIRDGEGQ
     KMSKSKGNVL DPIDLIDGIG LEALIEKRTT GLMNPKQAES IAKKTKKEFP EGIASFGTDA
     LRFTFASLAS PGRDIKFDLN RCDGYRNFCN KLWNATRFVL MNVEGHDLAL EHQQNGPACG
     GSAPLEFSFA DRWIVSQLQR VEQEVEQHFT DYRFDLIAQA IYKFIWDEFC DWYLEIAKVE
     IQTGNDAQQR GARRTLVRTL EAVLRLAHPL IPFITEELWQ TVAPIAGRKT HDSIMLAAYP
     RAEEYKIDAA SEAKVERLKA LAYACRNLRG EMNVSPALRM PLLVAGGGAE ISEFAAILQA
     LGKLSEVQIV DDMPADAMAP VAVVGETRLM LKVEIDVAAE RIRLAKEIEK LEKQISIAQG
     KLANEGFVAR APAAVIDQEK QRVADFTATL EQLKPQLAKL GQA
//