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Database: UniProt/TrEMBL
Entry: E3E4Q2_PAEPS
LinkDB: E3E4Q2_PAEPS
Original site: E3E4Q2_PAEPS 
ID   E3E4Q2_PAEPS            Unreviewed;       431 AA.
AC   E3E4Q2;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   14-MAY-2014, entry version 26.
DE   RecName: Full=Asparagine--tRNA ligase;
DE            EC=6.1.1.22;
DE   AltName: Full=Asparaginyl-tRNA synthetase;
GN   Name=asnS; OrderedLocusNames=PPSC2_c3070;
OS   Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=886882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2;
RX   PubMed=21037012; DOI=10.1128/JB.01234-10;
RA   Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA   Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J.,
RA   Du B.;
RT   "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of
RT   plant growth-promoting Rhizobacterium with broad-spectrum
RT   antimicrobial activity.";
RL   J. Bacteriol. 193:311-312(2011).
CC   -!- CATALYTIC ACTIVITY: ATP + L-asparagine + tRNA(Asn) = AMP +
CC       diphosphate + L-asparaginyl-tRNA(Asn).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP002213; ADO57030.1; -; Genomic_DNA.
DR   RefSeq; YP_003947271.1; NC_014622.1.
DR   EnsemblBacteria; ADO57030; ADO57030; PPSC2_c3070.
DR   GeneID; 9851369; -.
DR   KEGG; ppm:PPSC2_c3070; -.
DR   PATRIC; 42509314; VBIPaePol172748_2933.
DR   HOGENOM; HOG000226034; -.
DR   KO; K01893; -.
DR   OMA; KIGAWVA; -.
DR   BioCyc; PPOL886882:GBY1-3163-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.
SQ   SEQUENCE   431 AA;  49136 MW;  16C6740F17FBB563 CRC64;
     MTNKSTIAQV GRHVGETVTI GAWVNNKRSS GKIQFLQLRD GSGYIQGVIV KSEVSEDIWN
     DAKSLTQESS LYVTGIVREE PRSQSGYELT VTGIEIIHLT ENYPITPKEH GVDFLMDHRH
     LWLRSAKQRA VLIIRAEIIR AIQEFFNGNG FTKVDPPILT PSSAEGTTEL FHIKYFDEDA
     YLTQSGQLYM EAAAMALGKV YSFGPTFRAE KSKTRRHLIE FWMIEPEMAF VDHEESLRVQ
     EQFVSHIVQS VLKNCAKELE AIGRDVSKLE QIQGEFPRIT YDEAIAFLQG EGFDIPWGED
     FGAPHETAIA ERYNKPVFIT HWPTHIKAFY MKPDPARPEV VLCADMIAPE GYGEIIGGSQ
     RIDDPALMEE RFNEHNLARE AYQWYMDLRT YGSVPHSGFG LGLERTVAWI CGLDHVRETI
     PFPRMLYRLY P
//
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