SYN_THET8
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 25-MAY-2022, entry version 139.
DE RecName: Full=Asparagine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00534};
DE EC=6.1.1.22 {ECO:0000255|HAMAP-Rule:MF_00534};
DE AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00534};
DE Short=AsnRS {ECO:0000255|HAMAP-Rule:MF_00534};
GN Name=asnS {ECO:0000255|HAMAP-Rule:MF_00534}; OrderedLocusNames=TTHA0708;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CRYSTALLIZATION.
RX PubMed=8706760; 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 of the
RT gene and crystallization of the enzyme expressed in Escherichia coli.";
RL Eur. J. Biochem. 239:501-508(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA 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 PubMed=9582288; DOI=10.1093/emboj/17.10.2947;
RA Berthet-Colominas C., Seignovert L., Haertlein M., Grotli M., Cusack S.,
RA 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:
CC Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-
CC asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659,
CC Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00534};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00534}.
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DR EMBL; X91009; CAA62491.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70531.1; -; Genomic_DNA.
DR RefSeq; WP_011228137.1; NC_006461.1.
DR RefSeq; YP_143974.1; NC_006461.1.
DR PDB; 5ZG8; X-ray; 2.40 A; A=1-438.
DR PDBsum; 5ZG8; -.
DR AlphaFoldDB; P54263; -.
DR SMR; P54263; -.
DR STRING; 300852.55772090; -.
DR EnsemblBacteria; BAD70531; BAD70531; BAD70531.
DR GeneID; 3168522; -.
DR KEGG; ttj:TTHA0708; -.
DR PATRIC; fig|300852.9.peg.702; -.
DR eggNOG; COG0017; Bacteria.
DR HOGENOM; CLU_004553_2_0_0; -.
DR OMA; DNMDLAE; -.
DR PhylomeDB; P54263; -.
DR BRENDA; 6.1.1.22; 2305.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0004816; F:asparagine-tRNA ligase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IDA:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00534; Asn_tRNA_synth; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004522; Asn-tRNA-ligase.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00457; asnS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..438
FT /note="Asparagine--tRNA ligase"
FT /id="PRO_0000176470"
FT CONFLICT 355
FT /note="A -> R (in Ref. 1; CAA62491)"
FT /evidence="ECO:0000305"
FT HELIX 5..11
FT /evidence="ECO:0007829|PDB:5ZG8"
FT STRAND 14..28
FT /evidence="ECO:0007829|PDB:5ZG8"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:5ZG8"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:5ZG8"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:5ZG8"
FT STRAND 68..77
FT /evidence="ECO:0007829|PDB:5ZG8"
FT STRAND 84..96
FT /evidence="ECO:0007829|PDB:5ZG8"
FT HELIX 111..116
FT /evidence="ECO:0007829|PDB:5ZG8"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:5ZG8"
FT HELIX 125..147
FT /evidence="ECO:0007829|PDB:5ZG8"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:5ZG8"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:5ZG8"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:5ZG8"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:5ZG8"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:5ZG8"
FT STRAND 218..229
FT /evidence="ECO:0007829|PDB:5ZG8"
FT HELIX 233..254
FT /evidence="ECO:0007829|PDB:5ZG8"
FT HELIX 256..262
FT /evidence="ECO:0007829|PDB:5ZG8"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:5ZG8"
FT HELIX 270..274
FT /evidence="ECO:0007829|PDB:5ZG8"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:5ZG8"
FT HELIX 282..295
FT /evidence="ECO:0007829|PDB:5ZG8"
FT HELIX 310..317
FT /evidence="ECO:0007829|PDB:5ZG8"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:5ZG8"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:5ZG8"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:5ZG8"
FT STRAND 344..355
FT /evidence="ECO:0007829|PDB:5ZG8"
FT TURN 356..359
FT /evidence="ECO:0007829|PDB:5ZG8"
FT STRAND 360..368
FT /evidence="ECO:0007829|PDB:5ZG8"
FT HELIX 372..381
FT /evidence="ECO:0007829|PDB:5ZG8"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:5ZG8"
FT HELIX 390..397
FT /evidence="ECO:0007829|PDB:5ZG8"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:5ZG8"
FT HELIX 410..418
FT /evidence="ECO:0007829|PDB:5ZG8"
FT HELIX 423..426
FT /evidence="ECO:0007829|PDB:5ZG8"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:5ZG8"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:5ZG8"
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
