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Database: UniProt/SWISS-PROT
Entry: SYN_LACJO
LinkDB: SYN_LACJO
Original site: SYN_LACJO 
ID   SYN_LACJO               Reviewed;         432 AA.
AC   Q74JA9;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   01-OCT-2014, entry version 73.
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};
GN   OrderedLocusNames=LJ_1200;
OS   Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=257314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNCM I-1225 / La1 / NCC 533;
RX   PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA   Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA   Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA   Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT   "The genome sequence of the probiotic intestinal bacterium
RT   Lactobacillus johnsonii NCC 533.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + L-asparagine + tRNA(Asn) = AMP +
CC       diphosphate + L-asparaginyl-tRNA(Asn). {ECO:0000255|HAMAP-
CC       Rule:MF_00534}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00534}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00534}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00534}.
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DR   EMBL; AE017198; AAS09021.1; -; Genomic_DNA.
DR   RefSeq; NP_965055.1; NC_005362.1.
DR   ProteinModelPortal; Q74JA9; -.
DR   STRING; 257314.LJ1200; -.
DR   EnsemblBacteria; AAS09021; AAS09021; LJ_1200.
DR   GeneID; 2742535; -.
DR   KEGG; ljo:LJ1200; -.
DR   PATRIC; 22238777; VBILacJoh1832_1066.
DR   eggNOG; COG0017; -.
DR   KO; K01893; -.
DR   OMA; KIGAWVA; -.
DR   OrthoDB; EOG6ZSP6X; -.
DR   BioCyc; LJOH257314:GJN3-1064-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_00534; Asn_tRNA_synth; 1.
DR   InterPro; IPR004364; aa-tRNA-synt_II.
DR   InterPro; IPR018150; aa-tRNA-synt_II-like.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
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   PANTHER; PTHR22594; PTHR22594; 1.
DR   PANTHER; PTHR22594:SF16; PTHR22594:SF16; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00457; asnS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    432       Asparagine--tRNA ligase.
FT                                /FTId=PRO_0000176416.
SQ   SEQUENCE   432 AA;  50260 MW;  228CCF8DA2AE6A7A CRC64;
     MTELISIKDS SKHVDQEVKM HVWLTDKRSS GKIIFLQLRD GTAFFQGVIR KNDVSEEVFE
     AAKSLRQEAS FYITGTVHED KRSHFGYEIQ ISDLEIVSNN EGYPIGNKEH GVDFLLDNRH
     LWLRSKRPFA IMQIRNTMFK ATVDFFEKEG FIKFDAPIFM HSAPEGTTQL FHVEYFNNDA
     YLSQSGQLYG EAGAMAYGKI FTFGPTFRAE ESKGRRHMTE FWMMEPEMAW MHQDESLDIQ
     ERYLAYMVKQ VLENNEYELK ILGRDPEKLR PTTEGNFTRL SYDDAIKMLQ EAGRDIKWGD
     DFGAPDEGYI SEQFDRPVFI VNYPTTIKPF YMKKNPDNPK EYLCADVIAP EGYGEIFGGS
     EREGNYEILK QQIEEAGLNL EDYQWYLDLR KFGGVPHSGF GMGFERTIAW ICKLDHIREA
     IPFPRLINRM QP
//
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