ID   SYN_THET8               Reviewed;         438 AA.
AC   P54263; Q5SKD5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 2.
DT   03-NOV-2009, entry version 66.
DE   RecName: Full=Asparaginyl-tRNA synthetase;
DE            EC=6.1.1.22;
DE   AltName: Full=Asparagine--tRNA ligase;
DE            Short=AsnRS;
GN   Name=asnS; OrderedLocusNames=TTHA0708;
OS   Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CRYSTALLIZATION.
RX   MEDLINE=96314511; PubMed=8706760;
RX   DOI=10.1111/j.1432-1033.1996.0501u.x;
RA   Seignovert L., Haertlein M., Leberman R.;
RT   "Asparaginyl-tRNA synthetase from Thermus thermophilus HB8. Sequence
RT   of the gene and crystallization of the enzyme expressed in Escherichia
RT   coli.";
RL   Eur. J. Biochem. 239:501-508(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y.,
RA   Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   MEDLINE=98250666; PubMed=9582288; DOI=10.1093/emboj/17.10.2947;
RA   Berthet-Colominas C., Seignovert L., Haertlein M., Grotli M.,
RA   Cusack S., Leberman R.;
RT   "The crystal structure of asparaginyl-tRNA synthetase from Thermus
RT   thermophilus and its complexes with ATP and asparaginyl-adenylate: the
RT   mechanism of discrimination between asparagine and aspartic acid.";
RL   EMBO J. 17:2947-2960(1998).
CC   -!- CATALYTIC ACTIVITY: ATP + L-asparagine + tRNA(Asn) = AMP +
CC       diphosphate + L-asparaginyl-tRNA(Asn).
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; X91009; CAA62491.1; -; Genomic_DNA.
DR   EMBL; AP008226; BAD70531.1; -; Genomic_DNA.
DR   RefSeq; YP_143974.1; -.
DR   HSSP; Q9LCY8; 1N9W.
DR   STRING; P54263; -.
DR   GeneID; 3168522; -.
DR   GenomeReviews; AP008226_GR; TTHA0708.
DR   KEGG; ttj:TTHA0708; -.
DR   NMPDR; fig|300852.3.peg.713; -.
DR   HOGENOM; P54263; -.
DR   OMA; LQKKRHS; -.
DR   BioCyc; TTHE300852:TTHA0708-MON; -.
DR   BRENDA; 6.1.1.22; 245.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IDA:UniProtKB.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:HAMAP.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IDA:UniProtKB.
DR   HAMAP; MF_00534; -; 1.
DR   InterPro; IPR004364; aa-tRNA-synt_II.
DR   InterPro; IPR018150; aa-tRNA-synt_II-like.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR004522; Asn-tRNA-synth_IIb.
DR   InterPro; IPR002312; Asp-tRNA-synth_IIb.
DR   InterPro; IPR004365; NA_bd_OB_tRNA-helicase.
DR   PANTHER; PTHR22594; aa-tRNA-synt_II; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   TIGRFAMs; TIGR00457; asnS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    438       Asparaginyl-tRNA synthetase.
FT                                /FTId=PRO_0000176470.
FT   CONFLICT    355    355       A -> R (in Ref. 1; CAA62491).
SQ   SEQUENCE   438 AA;  50785 MW;  B6A22A7D08F3D496 CRC64;
     MRVFIDEIAR HVDQEVELRG WLYQRRSKGK IHFLILRDGT GFLQATVVQG EVPEAVFREA
     DHLPQETALR VWGRVREDRR APGGFELAVR DLQVVSRPQG EYPIGPKEHG IDFLMDHRHL
     WLRHRRPFAV MRIRDELERA IHEFFGERGF LRFDAPILTP SAVEGTTELF EVELFDGEKA
     YLSQSGQLYA EAGALAFAKV YTFGPTFRAE RSKTRRHLLE FWMVEPEVAF MTHEENMALQ
     EELVSFLVAR VLERRSRELE MLGRDPKALE PAAEGHYPRL TYKEAVALVN RIAQEDPEVP
     PLPYGEDFGA PHEAALSRRF DRPVFVERYP ARIKAFYMEP DPEDPELVLN DDLLAPEGYG
     EIIGGSQRIH DLELLRRKIQ EFGLPEEVYD WYLDLRRFGS VPHSGFGLGL ERTVAWICGL
     AHVREAIPFP RMYTRMRP
//