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Aspartate--tRNA(Asp) ligase (EC 6.1.1.12) (Aspartyl-tRNA synthetase) (AspRS) (Discriminating aspartyl-tRNA synthetase) (D-AspRS)

 B7R3A3_9EURY            Unreviewed;       438 AA.
B7R3A3;
10-FEB-2009, integrated into UniProtKB/TrEMBL.
10-FEB-2009, sequence version 1.
31-JAN-2018, entry version 60.
RecName: Full=Aspartate--tRNA(Asp) ligase {ECO:0000256|HAMAP-Rule:MF_02075};
EC=6.1.1.12 {ECO:0000256|HAMAP-Rule:MF_02075};
AltName: Full=Aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02075};
Short=AspRS {ECO:0000256|HAMAP-Rule:MF_02075};
AltName: Full=Discriminating aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02075};
Short=D-AspRS {ECO:0000256|HAMAP-Rule:MF_02075};
Name=aspS {ECO:0000256|HAMAP-Rule:MF_02075};
ORFNames=TAM4_289 {ECO:0000313|EMBL:EEB74001.1};
Thermococcus sp. AM4.
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
Thermococcus.
NCBI_TaxID=246969 {ECO:0000313|EMBL:EEB74001.1, ECO:0000313|Proteomes:UP000009277};
[1] {ECO:0000313|EMBL:EEB74001.1, ECO:0000313|Proteomes:UP000009277}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AM4 {ECO:0000313|EMBL:EEB74001.1};
PubMed=22123768; DOI=10.1128/JB.06259-11;
Oger P., Sokolova T.G., Kozhevnikova D.A., Chernyh N.A.,
Bartlett D.H., Bonch-Osmolovskaya E.A., Lebedinsky A.V.;
"Complete Genome Sequence of the Hyperthermophilic Archaeon
Thermococcus sp. Strain AM4, Capable of Organotrophic Growth and
Growth at the Expense of Hydrogenogenic or Sulfidogenic Oxidation of
Carbon Monoxide.";
J. Bacteriol. 193:7019-7020(2011).
-!- FUNCTION: Catalyzes the attachment of L-aspartate to tRNA(Asp) in
a two-step reaction: L-aspartate is first activated by ATP to form
Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
{ECO:0000256|HAMAP-Rule:MF_02075}.
-!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asp) = AMP +
diphosphate + L-aspartyl-tRNA(Asp). {ECO:0000256|HAMAP-
Rule:MF_02075}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_02075};
Note=Binds 3 Mg(2+) cations per subunit. The strongest magnesium
site (Mg1) is bound to the beta- and gamma-phosphates of ATP and
four water molecules complete its coordination sphere.
{ECO:0000256|HAMAP-Rule:MF_02075};
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02075}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02075}.
-!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
family. Type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02075}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02075}.
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EMBL; CP002952; EEB74001.1; -; Genomic_DNA.
RefSeq; WP_014122359.1; NC_016051.1.
STRING; 246969.TAM4_289; -.
EnsemblBacteria; EEB74001; EEB74001; TAM4_289.
GeneID; 7419080; -.
KEGG; tha:TAM4_289; -.
eggNOG; arCOG00406; Archaea.
eggNOG; COG0017; LUCA.
KO; K01876; -.
OrthoDB; POG093Z02FK; -.
BioCyc; TSP246969:GJBA-1201-MONOMER; -.
Proteomes; UP000009277; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
HAMAP; MF_02075; Asp_tRNA_synth_type2; 1.
InterPro; IPR004364; aa-tRNA-synt_II.
InterPro; IPR006195; aa-tRNA-synth_II.
InterPro; IPR004523; Asp-tRNA_synthase_2.
InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR004365; NA-bd_OB_tRNA.
PANTHER; PTHR43450; PTHR43450; 1.
Pfam; PF00152; tRNA-synt_2; 1.
Pfam; PF01336; tRNA_anti-codon; 1.
PRINTS; PR01042; TRNASYNTHASP.
SUPFAM; SSF50249; SSF50249; 1.
TIGRFAMs; TIGR00458; aspS_nondisc; 1.
PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
3: Inferred from homology;
Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02075,
ECO:0000313|EMBL:EEB74001.1};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_02075};
Complete proteome {ECO:0000313|Proteomes:UP000009277};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02075};
Ligase {ECO:0000256|HAMAP-Rule:MF_02075, ECO:0000313|EMBL:EEB74001.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_02075};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_02075};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02075};
Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02075}.
DOMAIN 137 438 AA_TRNA_LIGASE_II.
{ECO:0000259|PROSITE:PS50862}.
NP_BIND 214 216 ATP. {ECO:0000256|HAMAP-Rule:MF_02075}.
NP_BIND 222 224 ATP. {ECO:0000256|HAMAP-Rule:MF_02075}.
NP_BIND 409 412 ATP. {ECO:0000256|HAMAP-Rule:MF_02075}.
REGION 192 195 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_02075}.
METAL 361 361 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_02075}.
METAL 361 361 Magnesium 3. {ECO:0000256|HAMAP-
Rule:MF_02075}.
METAL 364 364 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_02075}.
BINDING 170 170 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_02075}.
BINDING 214 214 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_02075}.
BINDING 361 361 ATP. {ECO:0000256|HAMAP-Rule:MF_02075}.
BINDING 364 364 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_02075}.
BINDING 368 368 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_02075}.
SITE 85 85 Important for tRNA discrimination.
{ECO:0000256|HAMAP-Rule:MF_02075}.
SEQUENCE 438 AA; 50828 MW; B3C6009E813CE5F1 CRC64;
MYRTHYSSEI TEELNGQRVK VAGWVWEVKD LGGIKFLWLR DREGIVQITA PKKKVDPEIF
KLIPKLNSED VVAVEGTVNF TPKAKLGFEI LPEKLEILSR AEAPLPLDPT GKVKAELDTR
LDNRFMDVRR PEVMAIFKIR SSVFKAIRDF FHENGFIEIH TPKIIATATE GGTELFPMKY
FEKDAFLAQS PQLYKQIMMA SGLDRVYEIA PIFRAEEHNT TRHLNEAWSV DAEMAFIESE
EEVMALLERL VAYTINYVRE HNAKELETLN FELEEPKLPF PRLSYDKALE ILADLGKTIE
WGEDIDTEGE RLLGKYMMEN EEAPLYFLYK YPSEAKPFYI MKYDDKPEIC RAFDLEYRGV
EITSGGQREH RVDVLVEQIK EKGLNPESFE FYLKAFRYGM PPHGGFGLGA ERLIKQMLDL
PNIREVILFP RDRKRLVP


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