ID C9S0P0_GEOSY Unreviewed; 431 AA.
AC C9S0P0;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 01-MAY-2013, entry version 31.
DE RecName: Full=Asparagine--tRNA ligase;
DE EC=6.1.1.22;
DE AltName: Full=Asparaginyl-tRNA synthetase;
GN Name=asnS; OrderedLocusNames=GYMC61_0508;
OS Geobacillus sp. (strain Y412MC61).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=544556;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y412MC61;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Brumm P., Mead D.;
RT "Complete sequence of chromosome of Geobacillus sp. Y412MC61.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001794; ACX77190.1; -; Genomic_DNA.
DR RefSeq; YP_003251672.1; NC_013411.1.
DR STRING; 544556.GYMC61_0508; -.
DR EnsemblBacteria; ACX77190; ACX77190; GYMC61_0508.
DR GeneID; 8524314; -.
DR KEGG; gyc:GYMC61_0508; -.
DR PATRIC; 32162479; VBIGeoSp85804_0540.
DR eggNOG; COG0017; -.
DR HOGENOM; HOG000226034; -.
DR KO; K01893; -.
DR OMA; HEQGFYW; -.
DR BioCyc; GSP544556:GI3L-583-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:HAMAP.
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 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; Complete proteome; Cytoplasm;
KW Ligase; Nucleotide-binding; Protein biosynthesis.
SQ SEQUENCE 431 AA; 49649 MW; F376274DDF21B8EB CRC64;
MKTTTIAEVN QYAGQQVTIG AWLANKRSSG KIVFLQLRDG TGFIQGVVEK ANVSEEVFQR
AKTLTQETSL YVTGTVRIDE RSPFGYELSV ADLQVIQEAV DYPITPKEHG VEFLMDHRHL
WLRSRRQHAI MKIRNEIIRA TYEFFNDRGF VKVDAPILTG SAPEGTTELF HTKYFDEDAY
LSQSGQLYME AAAMALGKVF SFGPTFRAEK SKTRRHLIEF WMVEPEMAFY EFEDNLRLQE
EYVSYLVQSV LERCRLELGR LGRDVSKLEL VKPPFPRLTY DEAIKLLHEK GLTDIEWGDD
FGAPHETAIA ESFDKPVFIT HYPTSLKPFY MQPDPNRPDV VLCADLIAPE GYGEIIGGSE
RIHDYELLKR RLEEHHLPLE AYEWYLDLRK YGSVPHSGFG LGLERTVAWI CGVEHVRETI
PFPRLLNRLY P
//
