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Database: UniProt
Entry: Q2W3D5
LinkDB: Q2W3D5
Original site: Q2W3D5 
ID   SYDND_MAGSA             Reviewed;         876 AA.
AC   Q2W3D5;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   01-OCT-2014, entry version 69.
DE   RecName: Full=Aspartate--tRNA(Asp/Asn) ligase;
DE            EC=6.1.1.23;
DE   AltName: Full=Aspartyl-tRNA synthetase;
DE            Short=AspRS;
DE   AltName: Full=Non-discriminating aspartyl-tRNA synthetase;
DE            Short=ND-AspRS;
GN   Name=aspS; OrderedLocusNames=amb2837;
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=342108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y.,
RA   Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
CC   -!- FUNCTION: Aspartyl-tRNA synthetase with relaxed tRNA specificity
CC       since it is able to aspartylate not only its cognate tRNA(Asp) but
CC       also tRNA(Asn). Reaction proceeds in two steps: aspartate is first
CC       activated by ATP to form Asp-AMP and then transferred to the
CC       acceptor end of tRNA(Asp/Asn) (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asx) = AMP +
CC       diphosphate + L-aspartyl-tRNA(Asx).
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the class-II
CC       aminoacyl-tRNA synthetase family. {ECO:0000305}.
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DR   EMBL; AP007255; BAE51640.1; -; Genomic_DNA.
DR   RefSeq; YP_422199.2; NC_007626.1.
DR   ProteinModelPortal; Q2W3D5; -.
DR   STRING; 342108.amb2837; -.
DR   EnsemblBacteria; BAE51640; BAE51640; amb2837.
DR   GeneID; 3802624; -.
DR   KEGG; mag:amb2837; -.
DR   PATRIC; 22439930; VBIMagMag129836_2801.
DR   eggNOG; COG0173; -.
DR   HOGENOM; HOG000275160; -.
DR   KO; K01876; -.
DR   OMA; FVEQNDV; -.
DR   OrthoDB; EOG68Q0NX; -.
DR   BioCyc; MMAG342108:GJNU-2868-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0050560; F:aspartate-tRNA(Asn) ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.1360.30; -; 1.
DR   HAMAP; MF_00044; Asp_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; IPR004524; Asp-tRNA-ligase_IIb_bac/mt.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR004115; GAD-like.
DR   InterPro; IPR029351; GAD_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
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-codon; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF50249; SSF50249; 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; Reference proteome.
FT   CHAIN         1    876       Aspartate--tRNA(Asp/Asn) ligase.
FT                                /FTId=PRO_0000235533.
FT   NP_BIND     499    501       ATP. {ECO:0000250}.
FT   NP_BIND     815    818       ATP. {ECO:0000250}.
FT   REGION        1    278       Unknown.
FT   REGION      279    876       Aspartyl-tRNA synthetase.
FT   REGION      477    480       Aspartate. {ECO:0000250}.
FT   BINDING     453    453       Aspartate. {ECO:0000250}.
FT   BINDING     499    499       Aspartate. {ECO:0000250}.
FT   BINDING     729    729       Aspartate. {ECO:0000250}.
FT   BINDING     763    763       ATP. {ECO:0000250}.
FT   BINDING     766    766       Aspartate. {ECO:0000250}.
FT   BINDING     770    770       Aspartate. {ECO:0000250}.
FT   SITE        311    311       Important for tRNA non-discrimination.
FT                                {ECO:0000250}.
SQ   SEQUENCE   876 AA;  97040 MW;  0352C2B2DEEF5B74 CRC64;
     MAATDTPWRP FRQAGALRRP MIDPAFVQGH PAYPDAFAQF FAGHGRYGHF AERVGNRNSR
     NGWRRRALAP GPAVGAEIVA RHHEAAAQAG QGGDAARHQH RVDRLGQHHV RAAFEQVGRH
     FRLRGRSEHD RHRKGIVGAD SPAHPPHQIA RLLHAEIRVH HQKVDHFRPE VVFGIVAVVK
     AQQIPASQHA KGAGDDITAA EVEIAQQGAH TWGVVGHGLP SWQERTTFWP PAFRSPSDRS
     ATSEFVAGLV NIGLSRLDKI WPGMPSSRFG FKRAYEGFMH VYRSHTCGQL KAADAGIQAR
     LSGWVHRKRD HGNLLFVDLR DHYGITQCVI DVSSPVFAAL DKARPESVIT VTGKVVKRSA
     ETINPRLPTG EIELQVAEVE IQSIADVLPI QVAGDQEYPE DMRLRYRFLD LRREDVHANM
     MLRSRVIAYL RQAMIGQGFT EFQTPILTAS SPEGARDYLV PSRIHPGKFY ALPQAPQQFK
     QLLMVAGFDK YFQIAPCFRD EAGRADRSPG EFYQLDFEMS YVTQDDVFAA IEPVLEGVFK
     EFGKGRAVTP APFPRITYAD SMLKYGSDKP DLRNPIIIAD VTEPFRGSGF GLFAKLVDKG
     AVVRAIPAPG AAGQPRSWFD KLNDWARENG AGGLGYIQFA ADGPKGPIAK NLEPARVEAI
     KAAANLKDGD AVFFACDKAL PAAKFAGLVR TKIGNELDLL EKDVFKFCWT VDFPMYEINE
     ETGLVEFSHN PFSMPQGGMD ALLNQDPLTI NAYQYDIVCN GVELSSGAIR NHRPDIMYKA
     FEIAGYSAAH VEEHFGGMLN AFKFGAPPHG GSAPGVDRIV MLLADQPNIR EIILFPMNQQ
     AQDLLMQAPA EIAMERLREL HIKVDLPKPK KEVKEG
//
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