Legends: 1, BINDING Aspartate. {ECO:0000255|HAMAP- Rule:MF_00044}; 2, BINDING ATP. {ECO:0000255|HAMAP-Rule:MF_00044}; 3, SITE Important for tRNA non-discrimination. {ECO:0000255|HAMAP-Rule:MF_00044}; 4, NP_BIND ATP. {ECO:0000255|HAMAP-Rule:MF_00044}; 5, REGION Aspartate. {ECO:0000255|HAMAP- Rule:MF_00044}; 6, ipfam:tRNA_anti-codon [T]; 7, ipfam:GAD [T].
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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 30-NOV-2016, entry version 82.
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). {ECO:0000255|HAMAP-Rule:MF_00044}.
CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asx) = AMP +
CC diphosphate + L-aspartyl-tRNA(Asx). {ECO:0000255|HAMAP-
CC Rule:MF_00044}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00044}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00044}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family. Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00044}.
DR EMBL; AP007255; BAE51640.1; -; Genomic_DNA.
DR ProteinModelPortal; Q2W3D5; -.
DR STRING; 342108.amb2837; -.
DR EnsemblBacteria; BAE51640; BAE51640; amb2837.
DR KEGG; mag:amb2837; -.
DR PATRIC; 22439930; VBIMagMag129836_2801.
DR eggNOG; ENOG4105C9M; Bacteria.
DR eggNOG; COG0173; LUCA.
DR HOGENOM; HOG000275160; -.
DR KO; K01876; -.
DR OMA; NDWAREN; -.
DR OrthoDB; POG091H021G; -.
DR Proteomes; UP000007058; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050560; F:aspartate-tRNA(Asn) 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:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR Gene3D; 3.30.1360.30; -; 1.
DR HAMAP; MF_00044; Asp_tRNA_synth_type1; 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_bac/mit.
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; 2.
DR PANTHER; PTHR22594:SF5; PTHR22594:SF5; 2.
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:0000255|HAMAP-Rule:MF_00044}.
FT NP_BIND 815 818 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}.
FT REGION 1 278 Unknown.
FT REGION 279 876 Aspartyl-tRNA synthetase.
FT REGION 477 480 Aspartate. {ECO:0000255|HAMAP-
FT Rule:MF_00044}.
FT BINDING 453 453 Aspartate. {ECO:0000255|HAMAP-
FT Rule:MF_00044}.
FT BINDING 499 499 Aspartate. {ECO:0000255|HAMAP-
FT Rule:MF_00044}.
FT BINDING 729 729 Aspartate. {ECO:0000255|HAMAP-
FT Rule:MF_00044}.
FT BINDING 763 763 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}.
FT BINDING 770 770 Aspartate. {ECO:0000255|HAMAP-
FT Rule:MF_00044}.
FT SITE 311 311 Important for tRNA non-discrimination.
FT {ECO:0000255|HAMAP-Rule:MF_00044}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 301 381 ipfam:tRNA_anti-codon [T]
FT MYHIT 593 679 ipfam:GAD [T]
FT MYHIT 282 865 ihamap:Asp_tRNA_synth_type1 [T]
FT MYHIT 422 836 iprf:AA_TRNA_LIGASE_II [T]
FT MYHIT 400 838 ipfam:tRNA-synt_2 [T]
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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