ID SYN_BLOPB Reviewed; 470 AA. AC Q492P3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 16-JUN-2009, entry version 31. 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=BPEN_433; OS Blochmannia pennsylvanicus (strain BPEN). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia. OX NCBI_TaxID=291272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16077009; DOI=10.1101/gr.3771305; RA Degnan P.H., Lazarus A.B., Wernegreen J.J.; RT "Genome sequence of Blochmannia pennsylvanicus indicates parallel RT evolutionary trends among bacterial mutualists of insects."; RL Genome Res. 15:1023-1033(2005). CC -!- CATALYTIC ACTIVITY: ATP + L-asparagine + tRNA(Asn) = AMP + CC diphosphate + L-asparaginyl-tRNA(Asn). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000016; AAZ41052.1; -; Genomic_DNA. DR RefSeq; YP_277928.1; -. DR GeneID; 3562743; -. DR GenomeReviews; CP000016_GR; BPEN_433. DR KEGG; bpn:BPEN_433; -. DR HOGENOM; Q492P3; -. DR OMA; Q492P3; LQKKRHS. DR BioCyc; CBLO291272:BPEN_433-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:HAMAP. 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; IEA:InterPro. 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; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA_bd_OB_tRNA-helicase. DR Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1. 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 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis. FT CHAIN 1 470 Asparaginyl-tRNA synthetase. FT /FTId=PRO_1000051381. SQ SEQUENCE 470 AA; 54210 MW; 0237418B9E940552 CRC64; MNVVSVVDIL SGHVSKNTEI TIQGWIRTRR DSKAKISFLD LYDGSCINSL QIIAYDKLHN YKNEILRLTS GCSVIIVGII VKSIGIKQHV EVIAKNIKIL GWIEDPSTYP ITAKKHTMEY LREVSHLRPR TNTIGAVARI RDTLSQAIHN FLHKQGFIWI PTPIITACDT EGSSKMFCVS TSETQKILNN PNEKLHHTHD TTYDFFSKKA FLTVSGQLNA EAYACALSKV YTFGPTFRAE YSNTNRHLAE FWMIEPEAAF MTLDDIIILA ESLLKNIIRI LLEKRSDDIK YLVDKINKNI ITILENFSEI KFNHIEYTEA IKLLEICNRK FNNPIHWGTD LFSEHEKYLS EEYFKSPVII KNFPKNIKAF YMRLNDDNKT VASMDILVPG IGEIIGGSQR EERLSKLDQR LQENCLTQEN YWWYRDLRRY GTVPHSGFGL GFERLMIYVT GIKNIRDVIP FPRTSKNINF //