ID   SYV_DEHE1               Reviewed;         880 AA.
AC   Q3Z9C5;
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=DET0430;
OS   Dehalococcoides ethenogenes (strain 195).
OC   Bacteria; Chloroflexi; Dehalococcoidetes; Dehalococcoides.
OX   NCBI_TaxID=243164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15637277; DOI=10.1126/science.1102226;
RA   Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M.,
RA   Methe B.A., Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M.,
RA   Kolonay J.F., Dodson R.J., Daugherty S.C., Brinkac L.M.,
RA   Sullivan S.A., Madupu R., Nelson K.E., Kang K.H., Impraim M., Tran K.,
RA   Robinson J.M., Forberger H.A., Fraser C.M., Zinder S.H.,
RA   Heidelberg J.F.;
RT   "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT   ethenogenes.";
RL   Science 307:105-108(2005).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000027; AAW40282.1; -; Genomic_DNA.
DR   RefSeq; YP_181174.1; -.
DR   GeneID; 3230246; -.
DR   GenomeReviews; CP000027_GR; DET0430.
DR   KEGG; det:DET0430; -.
DR   NMPDR; fig|243164.3.peg.566; -.
DR   TIGR; DET0430; -.
DR   HOGENOM; Q3Z9C5; -.
DR   OMA; Q3Z9C5; TDQWYVS.
DR   BioCyc; DETH243164:DET_0430-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    880       Valyl-tRNA synthetase.
FT                                /FTId=PRO_0000224471.
FT   COILED      815    854       Potential.
FT   MOTIF        51     61       "HIGH" region.
FT   MOTIF       529    533       "KMSKS" region.
FT   BINDING     532    532       ATP (By similarity).
SQ   SEQUENCE   880 AA;  99965 MW;  91B19D29BDDE3605 CRC64;
     MAQCSGLPEM AKAYEAAEVE KKWYQYWMEK GYFKPNPDSD KKPFVIIMPP PNVTGELHLG
     HALTATLEDI MIRWHRMLGE PALWLPGADH AGIAAQVVVE RMLAKQGKTR QELGRELFLE
     KMWEWVNPCR ERIRHQHMRL GASCDWDRET FTLDPGPVKA VREIFTNLYQ KGLIYRGERI
     INWCPRCATA VSDLEVDHKD LAGHIWHLRY PLEDGSGFVT VATTRPETML GDTAVAVHPD
     DARYTGMVGK NVLLPIMNRR IPVIADEAVD MAFGTGAVKV TPAHDPNDFE MGLRHSLPMI
     TIQNRDTTMN ENAGPCSGMT AKACREYVVS ELKSLGLLLK IEDYTHSVGH CQRCSAVIEP
     MVSKQWFVKM EPLAKPALEA VNSGRIQILP ERFTKVYQNW MENIRDWCIS RQLWWGHRIP
     VWYCPCGEMI VSKEDPTACP KCGSTKLEQD PDVLDTWFSS GLWPHSTLGW PDQTEDLKRF
     YPGSVLETAY DIIFFWVARM IVMGIEDMKE VPFRTVYLHG LIRDDKGEKM SKTKGNVIDP
     LKVIDQYGTD ALRFAVTFGT SPGNDSKLGQ TKLEAARNFV NKLWNASRFV IMNLGEEKEL
     LPEAGLPLED RWILSRMNRV TADVIRLMEE FQFGEAQRVL QDFVWGEFCD WYIELAKVRL
     RDEASVSPRP VLVKVLSTIL RLLHPYMPFI TEELWSYLRP YLPKSLGETD IIVAPFPQAD
     ETCFDEQAES IMGSLVEVVR SLRNLRAEHN VEISRYIQAN IYAGDMAEVL SNYLGAVETL
     SRSRPVNILP GHYSGASTAT EVVLVLNGIE VVVPMSTMVD LEAEAKRVEA EIAELETQIE
     RLSARLSDTQ FLAKAPQAVV DKERTKLEGY IEKVSRLKAV
//