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Database: UniProt/TrEMBL
Entry: H6NBB7_9BACL
LinkDB: H6NBB7_9BACL
Original site: H6NBB7_9BACL 
ID   H6NBB7_9BACL            Unreviewed;       432 AA.
AC   H6NBB7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   29-MAY-2013, entry version 10.
DE   RecName: Full=Asparagine--tRNA ligase;
DE            EC=6.1.1.22;
DE   AltName: Full=Asparaginyl-tRNA synthetase;
GN   Name=asnS; ORFNames=PM3016_5385;
OS   Paenibacillus mucilaginosus 3016.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1116391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=3016;
RX   PubMed=22535950; DOI=10.1128/JB.00323-12;
RA   Ma M., Wang Z., Li L., Jiang X., Guan D., Cao F., Chen H., Wang X.,
RA   Shen D., Du B., Li J.;
RT   "Complete Genome Sequence of Paenibacillus mucilaginosus 3016, a
RT   Bacterium Functional as Microbial Fertilizer.";
RL   J. Bacteriol. 194:2777-2778(2012).
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; CP003235; AFC32085.1; -; Genomic_DNA.
DR   RefSeq; YP_005315234.1; NC_016935.1.
DR   EnsemblBacteria; AFC32085; AFC32085; PM3016_5385.
DR   GeneID; 11887376; -.
DR   KEGG; pmq:PM3016_5385; -.
DR   KO; K01893; -.
DR   BioCyc; PMUC1116391:GLI5-5413-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA: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_IIb.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA-helicase.
DR   PANTHER; PTHR22594; PTHR22594; 1.
DR   PANTHER; PTHR22594:SF6; PTHR22594:SF6; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 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; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   432 AA;  49797 MW;  2174C3A4FC8D8DCC CRC64;
     MSRTLCTIRE AGKHVEQPVT IGCWLHNIRS SGKIRFLQLR DGSGFMQGVV VKSEVSEEVW
     ENAGKLTQES SLYITGIVKE DTRSKGGYEL TVTGLEIIQI ASEYPITPKE HGVDFLMDHR
     HLWIRSPRQR AILVVRAQII RAVQEFFDER GFHLVDPPIL TPSSCEGTTN LFHTKYFEED
     AYLTQSGQLY MEAAAMALGR VYSFGPTFRA EKSKTRRHLI EFWMIEPEMA FVTHEENLEI
     QEQFVSHVVQ SVLKNCRKEL ETLERDISKL ENIQAPFPRI TYDEAVEFLK KNGHEFEWGE
     DFGAPHETAI AQSYDKPVFI THYPTEIKAF YMKPDPSRPE VVLCADMIAP EGYGEIIGGS
     QRIDDPELME ERFLQHELSK EAYQWYLDLR KYGSVPHSGF GLGLERTVAW ICGLDHVRET
     IPFPRLLYRL YP
//
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