ID   SYV_ANAMM               Reviewed;         823 AA.
AC   Q5P9M8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   16-JUN-2009, entry version 33.
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=AM1170;
OS   Anaplasma marginale (strain St. Maries).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma.
OX   NCBI_TaxID=234826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15618402; DOI=10.1073/pnas.0406656102;
RA   Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L.,
RA   Palmer G.H., McGuire T.C., Knowles D.P. Jr.;
RT   "Complete genome sequencing of Anaplasma marginale reveals that the
RT   surface is skewed to two superfamilies of outer membrane proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:844-849(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   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. ValS type 2 subfamily.
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DR   EMBL; CP000030; AAV87002.1; -; Genomic_DNA.
DR   RefSeq; YP_154257.1; -.
DR   GeneID; 3171649; -.
DR   GenomeReviews; CP000030_GR; AM1170.
DR   KEGG; ama:AM1170; -.
DR   HOGENOM; Q5P9M8; -.
DR   OMA; Q5P9M8; SGWILDP.
DR   BioCyc; AMAR234826:AM1170-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_02005; -; 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; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    823       Valyl-tRNA synthetase.
FT                                /FTId=PRO_0000224606.
FT   MOTIF        52     62       "HIGH" region.
FT   MOTIF       549    553       "KMSKS" region.
FT   BINDING     552    552       ATP (By similarity).
SQ   SEQUENCE   823 AA;  94004 MW;  C8F916707C698F84 CRC64;
     MNVRVRHFMQ SLDSRYQHKT VEEECNAAWD EHKIYKWKGN VAQSFVIDTP PPTVSGVLHM
     GHVFSYCHTD FIARYQRMAG KDVFYPIGFD DNGLPTERLV EKIKKLRAVQ LERAEFTKMC
     REVSHEFRTK FRNLFRRLGI SYDWALEYHT VSEEVQRLSQ ASFLDLYAKD KLYRKQQPIL
     WDTVDCTAIA HAEVEELDLH SHLNTISFHT VGGEKIDIAT TRPELIPACV ALFFNPEDDR
     YTHLHGQFAV VPVGGHKVKI LPDDKVRIDK GTGLVMCCTF GDETDVYWWR THNLDTKTIV
     SRTGHIVDLA EDTPDAKIPA AQFDGMHVQK ARKAVCDALE GAGLLVSQEP IVHTVKCAER
     SGAPIEILLS HQWFVRVMEH KHELLEQVQK VQWHPDSMRK RMEIWIENLN WDWCISRQRY
     FGVPFPVWYS KREGEVGKVL LPDVRDLPVD PLRDLPSGYG RDEVEPDVDV MDTWATSSIS
     PQFLTKSVGQ VLRNENLEPL FPTDLRAQSH EIIRSWAFYT MLKSYYHNGE IPWQNIMISG
     WCLAEDKTKM SKSKGNAMDP ESTLDLYGAD SVRYWAAKSR LGADTVFSEE VLKTGRRLTT
     KLWNASKFVA TFFLRDNPPA GTTAAPTDLW ILSKLHKAVA HNTENLKLFE YCAALNRTEE
     FFWKDFCDNY LELVKHRAYN HGSAHGHASA VSTLHHTLKT LLLLFAPFLP YVTEAVYGTL
     FSGCIHAQEW PNADEIPYNA SLEQHGDALI KIVEEVRKAK THAQVSVKYP VELITIGGLA
     TDFPESMLED LKHMCCAEQI KLTAPDSTEL EVAVTLAPTV SSN
//