ID   SYV_BLOPB               Reviewed;         957 AA.
AC   Q493Z9;
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=BPEN_033;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(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; CP000016; AAZ40682.1; -; Genomic_DNA.
DR   RefSeq; YP_277554.1; -.
DR   GeneID; 3562918; -.
DR   GenomeReviews; CP000016_GR; BPEN_033.
DR   KEGG; bpn:BPEN_033; -.
DR   HOGENOM; Q493Z9; -.
DR   OMA; Q493Z9; WPDETPE.
DR   BioCyc; CBLO291272:BPEN_033-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   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; Coiled coil;
KW   Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN         1    957       Valyl-tRNA synthetase.
FT                                /FTId=PRO_0000224444.
FT   COILED      889    918       Potential.
FT   MOTIF        47     57       "HIGH" region.
FT   MOTIF       558    562       "KMSKS" region.
FT   BINDING     561    561       ATP (By similarity).
SQ   SEQUENCE   957 AA;  112037 MW;  80ADDA20B51C1C70 CRC64;
     MSNYIVEKIY NPKNIEEPIY KFWEYGDYFS PHGNTSQESY CIMMPPPNIT GQLHLGHAFQ
     QTIMDVLIRY QRMQGKNTLW QTGTDHAGIA TQMLVEHKIY NNTGKTRHDY TRDELIKNIW
     AWKSQSEQFI TYQMKRLGNS VDWKRQRFTM DTEMSYAVTE AFIRLYRKNL IYRGKRLVNW
     DCKLQTAISD LEVINKKTKG SIWYIYYKLD NATISSNSHH LIVATTRPET MLGDTAVAVH
     PEDTRYKNYI GQYVIAPITN RRIPIISDKN VDMFKGTGCL KITPAHDFND YIIGKRHGLP
     MINIFSLNGK ILKKLEVFNS SGQLTDQLYC KIPQIFHNLD SDNARKKIIS ECNALKLLHN
     IEPHDLTIPY SDRTGTIIEP MLTDQWYIRV KHLTQHAIDA VNLNIINFVP KQYKNMYFSW
     MNNLQDWCIS RQIWWGHKIP AWYDDNNTIY VGYCEKDIRI KNKLNNNVIL HREKDVLDTW
     FSSSLWTFAA LGWPKNTNLL NVFHPTNIII SGFDIIFFWI ARMIMLTMHF IKNDNGSAQI
     PFKTVYITGL IRDELGQKMS KSKGNIIDPI DIIDGISIEN LLKKRTKNML QPQLSKHIIN
     NTIKQFPNGI KPHGTDALRF TLVALASSGR DIHWDMQRLT GYRNFCNKLW HASRFVLMHT
     KNQDCGISIN INEKSFSLAD RWIITKFHQT VQIFHKKLEI YRFDEIANIL HEFIWHQFCD
     WYLELTKPIL YHGNALELRG TRYTLITLLE SLLRLTHPII PFITEKIWQE VKTVTGNNGT
     TIMLQPFPKY DESVIDMKSV IDIEWIKNAV LAIRTARVNM NISYNIPLQI VFRDTSSEVK
     KRITENSKIL CHIAQLKSIH FISKGTIYPK SMTMPLDSSE LLIRIPDTFN KENEINRLKK
     ESELINRKIE TIQKLLDDNN FINQAPKSVI KDKQALLNYY ELIQNKLIDQ CAIMKKL
//