ID   SYV_DEHSC               Reviewed;         880 AA.
AC   Q3ZZG9;
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=cbdbA384;
OS   Dehalococcoides sp. (strain CBDB1).
OC   Bacteria; Chloroflexi; Dehalococcoidetes; Dehalococcoides.
OX   NCBI_TaxID=255470;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16116419; DOI=10.1038/nbt1131;
RA   Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.;
RT   "Genome sequence of the chlorinated compound-respiring bacterium
RT   Dehalococcoides species strain CBDB1.";
RL   Nat. Biotechnol. 23:1269-1273(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.
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DR   EMBL; AJ965256; CAI82595.1; -; Genomic_DNA.
DR   RefSeq; YP_307511.1; -.
DR   GeneID; 3623827; -.
DR   GenomeReviews; AJ965256_GR; cbdbA384.
DR   KEGG; deh:cbdb_A384; -.
DR   NMPDR; fig|255470.3.peg.768; -.
DR   HOGENOM; Q3ZZG9; -.
DR   OMA; Q3ZZG9; TDQWYVS.
DR   BioCyc; DSP255470:CBDBA384-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_0000224472.
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;  100189 MW;  E0A6F24298F69053 CRC64;
     MAQCSDLPEM AKAYEAAEVE KKWYQYWMEK SYFKPNPNSD KKPFVIIMPP PNVTGELHLG
     HALTATLEDI MIRWHRMQGE PTLWLPGVDH AGIAAQVVVE RELAKQGKTR QQLGRELFLE
     KMWEWVNPCR EKIRHQHMRL GASCDWDRET FTLDAGPVKA VREIFTNLYE KGLIYKGERI
     INWCPRCGTA VSDLEVDHKD LAGHIWHLRY PLEDGSGFVT VATTRPETMQ GDTAVAIHPD
     DTRYAGMVGK NVVLPIMNRR IPVIADEAVD MAFGTGAVKV TPAHDPNDFE MGLRHNLPMI
     TIQNRDTTMN ENAGPCSGMT AKACREYVVS EMKSLGLLLR IEDYIHSVGH CQRCSAVIEP
     MVSKQWFVKM EPLAKPALEA VNSGRIQILP ERFNKVYQNW MENIRDWCIS RQLWWGHRIP
     VWYCPCGEMI VAKVDPTVCP KCGGTELEQD PDVLDTWFSS GLWPHSTLGW PDQTEDLKRF
     YPGTVMETAY DIIFFWVARM IVMGMEDMNE VPFRTVYLHG LIRDDKGEKM SKTKGNVIDP
     LKVIDQYGTD ALRFAVTFGT SPGNDSKLGQ TKLEAARNFA NKLWNASRFV IMNLGEAKEL
     TPEAELPLED RWIISRMNRV TADVTRLMEE FQFGEAQRVL QDFIWGEFCD WYIELAKVRL
     RDEASVSPRP VLVRVLSSIL RLLHPYMPFI TEELWSYLRP YLPESLRETD IIVAPYPAAD
     KTCFDEQAES VMGSLVEIVR SLRNLRAEHN VEISRYIQAN IYAGDMASVL GNYLGAVETL
     SRARPVNILP GHYSGASTAT EVVLVLTGIE VVVPMSTMVD LEVEAKRVKA EISELEIQIE
     RLSTRLSDEQ FLAKAPQAVV DKERIKLEGY IEKVSRLKSA
//