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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)

 I3R2A4_HALMT            Unreviewed;       434 AA.
I3R2A4; M0IZR0;
05-SEP-2012, integrated into UniProtKB/TrEMBL.
03-SEP-2014, sequence version 2.
23-MAY-2018, entry version 49.
RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000256|HAMAP-Rule:MF_02075};
EC=6.1.1.23 {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=Non-discriminating aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02075};
Short=ND-AspRS {ECO:0000256|HAMAP-Rule:MF_02075};
Name=aspS {ECO:0000256|HAMAP-Rule:MF_02075,
ECO:0000313|EMBL:AFK18364.2};
Synonyms=aspC {ECO:0000313|EMBL:AHZ22239.1};
OrderedLocusNames=HFX_0640 {ECO:0000313|EMBL:AFK18364.2};
ORFNames=BM92_06040 {ECO:0000313|EMBL:AHZ22239.1},
C439_07265 {ECO:0000313|EMBL:EMA02362.1};
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
Archaea; Euryarchaeota; Halobacteria; Haloferacales; Haloferacaceae;
Haloferax.
NCBI_TaxID=523841 {ECO:0000313|EMBL:AFK18364.2, ECO:0000313|Proteomes:UP000006469};
[1] {ECO:0000313|EMBL:AFK18364.2}
NUCLEOTIDE SEQUENCE.
STRAIN=CGMCC 1.2087;
PubMed=22247127; DOI=10.1128/AEM.07114-11;
Cai S., Cai L., Liu H., Liu X., Han J., Zhou J., Xiang H.;
"Identification of the haloarchaeal phasin (PhaP) that functions in
polyhydroxyalkanoate accumulation and granule formation in Haloferax
mediterranei.";
Appl. Environ. Microbiol. 78:1946-1952(2012).
[2] {ECO:0000313|EMBL:AFK18364.2, ECO:0000313|Proteomes:UP000006469}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
R-4 {ECO:0000313|Proteomes:UP000006469}, and
CGMCC 1.2087 {ECO:0000313|EMBL:AFK18364.2};
PubMed=22843593; DOI=10.1128/JB.00880-12;
Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B.,
Chen Y., Zhou J., Hu S., Xiang H.;
"Complete genome sequence of the metabolically versatile halophilic
archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
hydroxyvalerate) producer.";
J. Bacteriol. 194:4463-4464(2012).
[3] {ECO:0000313|Proteomes:UP000011603}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
R-4 {ECO:0000313|Proteomes:UP000011603};
Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D.,
Darling A., Eisen J.A., Facciotti M.T.;
Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|EMBL:EMA02362.1}
NUCLEOTIDE SEQUENCE.
STRAIN=ATCC 33500 {ECO:0000313|EMBL:EMA02362.1};
PubMed=25393412;
Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I.,
Wu D., Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
"Phylogenetically driven sequencing of extremely halophilic archaea
reveals strategies for static and dynamic osmo-response.";
PLoS Genet. 10:E1004784-E1004784(2014).
[5] {ECO:0000313|EMBL:AHZ22239.1, ECO:0000313|Proteomes:UP000027075}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33500 {ECO:0000313|EMBL:AHZ22239.1}, and
ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
{ECO:0000313|Proteomes:UP000027075};
Bautista V.;
"Transcriptional profiles of Haloferax mediterranei on the basis of
nitrogen availability.";
Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000313|EMBL:AFK18364.2}
NUCLEOTIDE SEQUENCE.
STRAIN=CGMCC 1.2087;
Wang L., Yang H., Xiang H.;
Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
-!- 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:0000256|HAMAP-Rule:MF_02075}.
-!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asx) = AMP +
diphosphate + L-aspartyl-tRNA(Asx). {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; CP001868; AFK18364.2; -; Genomic_DNA.
EMBL; CP007551; AHZ22239.1; -; Genomic_DNA.
EMBL; AOLO01000007; EMA02362.1; -; Genomic_DNA.
RefSeq; WP_004057587.1; NZ_CP007551.1.
EnsemblBacteria; AFK18364; AFK18364; HFX_0640.
EnsemblBacteria; AHZ22239; AHZ22239; BM92_06040.
EnsemblBacteria; EMA02362; EMA02362; C439_07265.
GeneID; 13026809; -.
KEGG; hme:HFX_0640; -.
PATRIC; fig|523841.21.peg.1469; -.
KO; K09759; -.
OrthoDB; POG093Z02FK; -.
BioCyc; HMED523841:G1HBL-627-MONOMER; -.
Proteomes; UP000006469; Chromosome.
Proteomes; UP000011603; Unassembled WGS sequence.
Proteomes; UP000027075; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0050560; F:aspartate-tRNA(Asn) ligase activity; IEA:UniProtKB-EC.
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:AFK18364.2};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_02075};
Complete proteome {ECO:0000313|Proteomes:UP000006469};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02075};
Ligase {ECO:0000256|HAMAP-Rule:MF_02075, ECO:0000313|EMBL:AFK18364.2};
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};
Reference proteome {ECO:0000313|Proteomes:UP000006469}.
DOMAIN 134 434 AA_TRNA_LIGASE_II.
{ECO:0000259|PROSITE:PS50862}.
NP_BIND 211 213 ATP. {ECO:0000256|HAMAP-Rule:MF_02075}.
NP_BIND 219 221 ATP. {ECO:0000256|HAMAP-Rule:MF_02075}.
NP_BIND 405 408 ATP. {ECO:0000256|HAMAP-Rule:MF_02075}.
REGION 189 192 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_02075}.
METAL 357 357 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_02075}.
METAL 357 357 Magnesium 3. {ECO:0000256|HAMAP-
Rule:MF_02075}.
METAL 360 360 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_02075}.
BINDING 167 167 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_02075}.
BINDING 211 211 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_02075}.
BINDING 357 357 ATP. {ECO:0000256|HAMAP-Rule:MF_02075}.
BINDING 360 360 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_02075}.
BINDING 364 364 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_02075}.
SITE 82 82 Important for tRNA non-discrimination.
{ECO:0000256|HAMAP-Rule:MF_02075}.
SEQUENCE 434 AA; 48650 MW; FAB1CE1F8654F4FC CRC64;
MRNRTYTADA EPGDTVTVAG WVHEVRDLGG IAFLILRDTS GKIQVKFEKD EMDDDLVETG
LGVHRESVIS VTGEVAEEPR APTGVEVTPE SLDVIAEAEA QLPLDPSGKV DAELSTRLDN
RTLDLRKDEV KAIFEIRAEV QRAVRDEFRN LRATEINTPK IVATGTEGGT ELFPITYFGQ
EAFMNQSPQL FKQLMVGSGL ERVFEVGPIF RAEEHNTPRH LNEATSIDFE SAFIDHTEAM
DVCEAVVKAA YEAVEENCQD ELEALGLAEE FEAPSGEFPR LTYEEAIQRI NATGELDEQL
VWGDDLPTEG EKALGEDVGE HYFITDWPSE IKPFYIKDHD DDETLSTGFD MMHPNMELVS
GGQREHRFDH LVAGFEQQGL DPDAFEYYTK MFKYGMPPHA GFGLGGERLI MTMLGLENIR
EAVLFPRDRQ RLSP


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