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Aspartate--tRNA(Asp/Asn) ligase (EC 6.1.1.23) (Aspartyl-tRNA synthetase) (AspRS) (Non-discriminating aspartyl-tRNA synthetase) (ND-AspRS)

 SYDND_CHLT2             Reviewed;         582 AA.
B0B8B6;
24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 1.
22-NOV-2017, entry version 73.
RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000255|HAMAP-Rule:MF_00044};
EC=6.1.1.23 {ECO:0000255|HAMAP-Rule:MF_00044};
AltName: Full=Aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044};
Short=AspRS {ECO:0000255|HAMAP-Rule:MF_00044};
AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044};
Short=ND-AspRS {ECO:0000255|HAMAP-Rule:MF_00044};
Name=aspS {ECO:0000255|HAMAP-Rule:MF_00044};
OrderedLocusNames=CTL0804;
Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
Chlamydia/Chlamydophila group; Chlamydia.
NCBI_TaxID=471472;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=434/Bu / ATCC VR-902B;
PubMed=18032721; DOI=10.1101/gr.7020108;
Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J.,
Marsh P., Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H.,
Harris B., Ormond D., Rance R., Quail M.A., Parkhill J.,
Stephens R.S., Clarke I.N.;
"Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
venereum isolates.";
Genome Res. 18:161-171(2008).
-!- FUNCTION: Aspartyl-tRNA synthetase with relaxed tRNA specificity
since it is able to aspartylate not only its cognate tRNA(Asp) but
also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is
first activated by ATP to form Asp-AMP and then transferred to the
acceptor end of tRNA(Asp/Asn). {ECO:0000255|HAMAP-Rule:MF_00044}.
-!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asx) = AMP +
diphosphate + L-aspartyl-tRNA(Asx). {ECO:0000255|HAMAP-
Rule:MF_00044}.
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00044}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00044}.
-!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
family. Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00044}.
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EMBL; AM884176; CAP04242.1; -; Genomic_DNA.
RefSeq; WP_009873886.1; NC_010287.1.
RefSeq; YP_001654875.1; NC_010287.1.
ProteinModelPortal; B0B8B6; -.
SMR; B0B8B6; -.
EnsemblBacteria; CAP04242; CAP04242; CTL0804.
GeneID; 5858582; -.
KEGG; ctb:CTL0804; -.
PATRIC; fig|471472.4.peg.861; -.
HOGENOM; HOG000275160; -.
KO; K01876; -.
OMA; YQLDVEM; -.
Proteomes; UP000000795; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0050560; F:aspartate-tRNA(Asn) ligase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
HAMAP; MF_00044; Asp_tRNA_synth_type1; 1.
InterPro; IPR004364; aa-tRNA-synt_II.
InterPro; IPR006195; aa-tRNA-synth_II.
InterPro; IPR004524; Asp-tRNA-ligase_1.
InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
InterPro; IPR004115; GAD-like_sf.
InterPro; IPR029351; GAD_dom.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR004365; NA-bd_OB_tRNA.
PANTHER; PTHR22594:SF5; PTHR22594:SF5; 1.
Pfam; PF02938; GAD; 1.
Pfam; PF00152; tRNA-synt_2; 1.
Pfam; PF01336; tRNA_anti-codon; 1.
PRINTS; PR01042; TRNASYNTHASP.
SUPFAM; SSF50249; SSF50249; 1.
SUPFAM; SSF55261; SSF55261; 1.
TIGRFAMs; TIGR00459; aspS_bact; 1.
PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
3: Inferred from homology;
Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
Ligase; Nucleotide-binding; Protein biosynthesis.
CHAIN 1 582 Aspartate--tRNA(Asp/Asn) ligase.
/FTId=PRO_1000090978.
NP_BIND 223 225 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}.
NP_BIND 533 536 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}.
REGION 201 204 Aspartate. {ECO:0000255|HAMAP-
Rule:MF_00044}.
BINDING 177 177 Aspartate. {ECO:0000255|HAMAP-
Rule:MF_00044}.
BINDING 223 223 Aspartate. {ECO:0000255|HAMAP-
Rule:MF_00044}.
BINDING 232 232 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}.
BINDING 447 447 Aspartate. {ECO:0000255|HAMAP-
Rule:MF_00044}.
BINDING 481 481 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}.
BINDING 488 488 Aspartate. {ECO:0000255|HAMAP-
Rule:MF_00044}.
SITE 32 32 Important for tRNA non-discrimination.
{ECO:0000255|HAMAP-Rule:MF_00044}.
SITE 84 84 Important for tRNA non-discrimination.
{ECO:0000255|HAMAP-Rule:MF_00044}.
SEQUENCE 582 AA; 66272 MW; 2938ADD5BF0EC1B1 CRC64;
MKYRTHKCNE LSLDHVGEHV RLSGWVHRYR NHGGVVFIDL RDRFGITQIV CRQEENPELH
QLMDQVRSEW VLCVEGLVCA RLEGMENPNL VTGSIEVEVS SLEVLSRAQN LPFSISDEHI
NVNEELRLTY RYLDMRRGDI LDRLMCRHKV MLACRQYLDE QGFTEVVTPI LGKSTPEGAR
DYLVPSRIYP GNFYALPQSP QLFKQILMVG GLDRYFQIAT CFRDEDLRAD RQPEFTQIDM
EMSFGGPEDL FPVVEELVTR LFAVKGIELK APFLRMTYQE AKDSYGTDKP DLRFGLRLKN
CCEYARKFTF SIFLDQLAHG GTVKGFCVPG GADMSRKQLD IYTDFVKRYG SMGLVWIKKQ
DGGVSSNVAK FASEDVFQEM FEAFEAKDQD ILLLIAAPEA VANQALDHLR RLIAKERQLY
DSTQYNFVWI TDFPLFAKEE GELCPEHHPF TAPLDEDISL LDSDPFAVRS SSYDLVLNGY
EIASGSQRIH NPDLQNKIFA LLKLSQESVK EKFGFFIDAL SFGTPPHLGI ALGLDRIMMV
LTGAETIREV IAFPKTQKAG DLMMSAPSEI LPIQLKELGL KL


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