ID F4A285_MAHA5 Unreviewed; 595 AA.
AC F4A285;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 03-APR-2013, entry version 15.
DE RecName: Full=Aspartate--tRNA ligase;
DE EC=6.1.1.12;
DE AltName: Full=Aspartyl-tRNA synthetase;
GN Name=aspS; OrderedLocusNames=Mahau_0934;
OS Mahella australiensis (strain DSM 15567 / CIP 107919 / 50-1 BON).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family IV. Incertae Sedis; Mahella.
OX NCBI_TaxID=697281;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15567 / CIP 107919 / 50-1 BON;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Teshima H.,
RA Brettin T., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA Pukall R., Steenblock K., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Mahella australiensis DSM 15567.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asp) = AMP +
CC diphosphate + L-aspartyl-tRNA(Asp).
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; CP002360; AEE96132.1; -; Genomic_DNA.
DR RefSeq; YP_004462954.1; NC_015520.1.
DR EnsemblBacteria; AEE96132; AEE96132; Mahau_0934.
DR GeneID; 10607683; -.
DR KEGG; mas:Mahau_0934; -.
DR PATRIC; 54630507; VBIMahAus157719_0958.
DR KO; K01876; -.
DR BioCyc; MAUS697281:GH33-967-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004815; F:aspartate-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:0006422; P:aspartyl-tRNA aminoacylation; IEA:HAMAP.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1360.30; -; 1.
DR HAMAP; MF_00044_B; Asp_tRNA_synth_B; 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; IPR004524; Asp-tRNA-ligase_IIb_bac/mt.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR004115; GAD_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA-helicase.
DR PANTHER; PTHR22594; PTHR22594; 1.
DR PANTHER; PTHR22594:SF5; PTHR22594:SF5; 1.
DR Pfam; PF02938; GAD; 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 SUPFAM; SSF55261; SSF55261; 1.
DR TIGRFAMs; TIGR00459; aspS_bact; 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 595 AA; 67722 MW; 9AF505B9E42662D3 CRC64;
MDELLGGLKR THMCGQLRLS DVDTSAVVMG WVQRRRDLGG VIFIDLRDRT GIVQVVFNEI
FDADAFDKAQ ALRNEYVIAV VGDVVRRSED TVNPKINTGE IEIRARQLKV LGRSETPPFP
VEDDINVSEI LRLKYRYLDL RRPDMQRNLM LRHKVSKITR DFLSDEGFIE VETPMLTKST
PEGARDYLVP SRLHPGSFYA LPQSPQLFKQ LLMISGFDKY FQIARCFRDE DLRADRQPEF
TQIDLEMSFV DVEDVIALNE QLIARIFKDA IGMDISLPLK RLTYKEAMER YGSDKPDTRF
GLELKDISDI VRSSQFKVFA DAVAHGGSVR GINVIDGADK FARRELDALV DFVKTFGAKG
LAWITITADE LKSPITKFLS QDEIDGILGR MDAKAGDLLL FVADKDEVVF DSLGQLRLEL
GKRLNLIDDS RYDLLWVTEF PLLEYSEEEK RYVAKHHPFT SPMDEDISLL NSEPWKARAK
AYDMVLNGNE IGGGSIRIHS TELQQKMFEV LGFSKEDAWE RFGFLLKAFE YGAPPHGGMA
YGLDRLVMLL AGLDTIRDVI AFPKVQNASC PLTEAPTPVD EKQLRELHIR VRQQQ
//
