ID   SYV_CORJK               Reviewed;         932 AA.
AC   Q4JWU8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 30.
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=jk0550;
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=306537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B.,
RA   Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T.,
RA   Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P.,
RA   Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant
RT   nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring
RT   bacterium of the human skin flora.";
RL   J. Bacteriol. 187:4671-4682(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; CR931997; CAI36709.1; -; Genomic_DNA.
DR   RefSeq; YP_250327.1; -.
DR   GeneID; 3433539; -.
DR   GenomeReviews; CR931997_GR; jk0550.
DR   KEGG; cjk:jk0550; -.
DR   NMPDR; fig|306537.3.peg.546; -.
DR   HOGENOM; Q4JWU8; -.
DR   OMA; Q4JWU8; TDQWYVS.
DR   BioCyc; CJEI306537:JK0550-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    932       Valyl-tRNA synthetase.
FT                                /FTId=PRO_0000224468.
FT   COILED      863    929       Potential.
FT   MOTIF        75     85       "HIGH" region.
FT   MOTIF       568    572       "KMSKS" region.
FT   BINDING     571    571       ATP (By similarity).
SQ   SEQUENCE   932 AA;  104813 MW;  E67C2E72F2147002 CRC64;
     MPCLARLLDL ADVSDSSSKA NGSNPIGADR SAQLPAAWDP AAVEENLYQG WVDSGYFKAD
     PSSDKPPFSI VLPPPNVTGQ LHMGHALDHT LMDAMARRKR MQGFEVLWLP GSDHAGIATQ
     TKVEANLKET EGKDRFDYGR DAFVGKVWEW KDRYGGVIQR QMRAIGDSVD WSRERFTLDD
     GLSRAVQTMF KELFDAGLIY RANRMVNWSP VLQTAISDIE VVYSDDEGEL VSIRYGSLED
     SEPHVVVATT RVETMLGDVA VAVHPEDERY TDLVGKSLPH PFLPDRQMIV VADDYVDPEF
     GTGAVKITPA HDPNDFAMGQ RHDLPMPVIM DETGHIANTG TEFDGMERYE AREKIRLALE
     EQGRIVARKF PYVHSVGHSE RSKEAVEPRL SEQWFVKVEE LAKMSGDAIR SGDSVIHPSS
     QEPRWFDWVD DMHDWCISRQ LWWGHRIPIW YGPNGEIVCC GPDDEAPTGE GWYQDEDVLD
     TWFSSALWPF STMGWPEKTP ELEKFYPTSV LVTGYDILFF WVARMMMFAT FASKHTPEIL
     GTGKDGRPQI PFNDIFLHGL VRDEHGRKMS KSLGNGIDPM DWVRDYGADA LRFTLARGAN
     PGSDLPVGED AAQSSRNFAT KLYNATKFAL MNGARVGELP ARETLTDADR WILDRLEEVR
     QLVDDALDRY EFSLANENLY RFAWGEFCDW YLEIAKVQIP RDWDSATEEQ VQRGIRTQIV
     LGRVLDSVLR LLHPAMPFVT ETLWKALTDG EEGYSESLVT ADWPTADLTN GGAQTDADAV
     RRMADVDKLV TELRRFRSDQ GVKPSQKVPA KLDFAAADLA NFEEAVRSLV RLETPEEDFA
     ETASIEVRLS QATIAVQLDT SGTVDVAAER KRLEKDLAAA QKELDNAAKK LGNENFLAKA
     PEKVVEGIRE RQRVAQEEFE RITARLEGLP KA
//