ID SYNC_MACFA Reviewed; 558 AA. AC Q4R4Z1; DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 16-JUN-2009, entry version 31. DE RecName: Full=Asparaginyl-tRNA synthetase, cytoplasmic; DE EC=6.1.1.22; DE AltName: Full=Asparagine--tRNA ligase; DE Short=AsnRS; GN Name=NARS; ORFNames=QnpA-18508; OS Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Parietal cortex; RG International consortium for macaque cDNA sequencing and analysis; RT "DNA sequences of macaque genes expressed in brain or testis and its RT evolutionary implications."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-asparagine + tRNA(Asn) = AMP + CC diphosphate + L-asparaginyl-tRNA(Asn). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). 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; AB169753; BAE01834.1; -; mRNA. DR HOVERGEN; Q4R4Z1; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:EC. DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:InterPro. 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 GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:InterPro. 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 2: Evidence at transcript level; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis. FT CHAIN 1 558 Asparaginyl-tRNA synthetase, cytoplasmic. FT /FTId=PRO_0000341690. FT MOD_RES 71 71 Phosphoserine (By similarity). SQ SEQUENCE 558 AA; 63839 MW; B484626B81020D17 CRC64; MSLEVTRATA GMVLELYVSD REGSDATGDG TKEKPFKTGL KALMTVGKEP FPTIYVDSQK ENERWNVISK SQLKNIKKMW HREQMKSESR EKKEAEDSLR REKNLEEAKK ITIKNDPALP EPKCVKISAL EGYRGQRVKV FGWVHRLRRQ GKNLMFLVLR DGTGYLQCVL ADELCQCYNG VLLSTESSVA VYGMLNLTPK GKQAPGGHEL SCDFWELIGL APAGGADNLI NEESDVDVQL NNRHMMIRGE NMSKILKARS MITRCFRDHF FDRGYHEITP PSLVQTQVEG GATLFKLNYF GEEAFLTQSS QLYLETCLPA LGDVFCIAQS YRAEQSRTRR HLAEYTHVEA ECPLLTFDDL LNRLEDLVCD VVDRILKSPA GSIVYELNPN FQPPKRPFKR MNYSDAIIWL KEHDIKKEDG TFYEFGEDIP EAPERLMTDT INEPILLCRF PVEIKSFYMQ RCPEDSCLTE SVDVLMPNVG EIVGGSMRTS DAEEILAGYK REGIDPAPYY WYTDQRKYGT CPHGGYGLGL ERFLTWILNR YHIRDVCLYP RFVQRCTP //