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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)

 A0A2G7GSH9_9DEIO        Unreviewed;       584 AA.
A0A2G7GSH9;
31-JAN-2018, integrated into UniProtKB/TrEMBL.
31-JAN-2018, sequence version 1.
25-APR-2018, entry version 4.
RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000256|HAMAP-Rule:MF_00044};
EC=6.1.1.23 {ECO:0000256|HAMAP-Rule:MF_00044};
AltName: Full=Aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00044};
Short=AspRS {ECO:0000256|HAMAP-Rule:MF_00044};
AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00044};
Short=ND-AspRS {ECO:0000256|HAMAP-Rule:MF_00044};
Name=aspS {ECO:0000256|HAMAP-Rule:MF_00044};
ORFNames=AMD26_019640 {ECO:0000313|EMBL:PIG95768.1};
Deinococcus sp. UR1.
Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
Deinococcaceae; Deinococcus.
NCBI_TaxID=1704277 {ECO:0000313|EMBL:PIG95768.1, ECO:0000313|Proteomes:UP000051726};
[1] {ECO:0000313|Proteomes:UP000051726}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=UR1 {ECO:0000313|Proteomes:UP000051726};
Perry B.J., Steve J., Yost C.K.;
"A Deinococcus species isolated from a roadside stainless steel
surface.";
Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:PIG95768.1, ECO:0000313|Proteomes:UP000051726}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=UR1 {ECO:0000313|EMBL:PIG95768.1,
ECO:0000313|Proteomes:UP000051726};
Banno H., Chua N.-H.;
Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|Proteomes:UP000051726}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=UR1 {ECO:0000313|Proteomes:UP000051726};
Suchan D.M., Steve J., Pierce A.J., Olshefsky S.C., Kirzinger M.W.B.,
Cameron A.D.S., Yost C.K.;
"Whole-Genome Sequence and Annotation of Deinococcus sp. UR1.";
Submitted (NOV-2017) 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_00044}.
-!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asx) = AMP +
diphosphate + L-aspartyl-tRNA(Asx). {ECO:0000256|HAMAP-
Rule:MF_00044}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651735}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651743}.
-!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
family. Type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00667367}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00044}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:PIG95768.1}.
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EMBL; LIYN02000038; PIG95768.1; -; Genomic_DNA.
Proteomes; UP000051726; Unassembled WGS sequence.
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:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
Gene3D; 3.30.1360.30; -; 1.
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 {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651728};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651746};
Complete proteome {ECO:0000313|Proteomes:UP000051726};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651756};
Ligase {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651728};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651746};
Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651732}.
DOMAIN 138 558 AA_TRNA_LIGASE_II.
{ECO:0000259|PROSITE:PS50862}.
NP_BIND 217 219 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}.
NP_BIND 524 527 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}.
REGION 195 198 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
BINDING 171 171 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
BINDING 217 217 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
BINDING 226 226 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}.
BINDING 437 437 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
BINDING 472 472 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}.
BINDING 479 479 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
SITE 81 81 Important for tRNA non-discrimination.
{ECO:0000256|HAMAP-Rule:MF_00044}.
SEQUENCE 584 AA; 64844 MW; B2A52EC7144C0BD1 CRC64;
MKRTALIGHL NDTHAHQTVT LQGWVNRRRD LGGLIFLELR DRSGLVQVQV EPDSAAFAEA
DRLRAEYVAE IEGTYQPRPE GQRKGGAADF EVIATRVRVL NTARTPPFEL DKGDSVAEDI
RLKFRYLDLR RPEMQRNLML RSRAVAAVTA YLDREGFVQV ETPMLTKSTP EGARDFLVPS
RQNPGEFYAL PQSPQLFKQM LMIAGYDRYY QLARCFRDED LRADRQPDFT QLDMEMSFVE
QDDVLAIQEG LMAHVFRETL GVELPVPFPR LPYFDAMNDY GSDKPDLRFD HKFVDVTDLF
QGGEFKAFAE AQTVKVIAAP ELTRKQIDEL ERIAKQNGAR GLAWLKRDGD GFTGGVSKFV
TAQAPELLAR TGVGQGGTLL FAAGDWKKAV TALGAVRLAL RDLFDLTAGG PQFHISWVTD
FPQLEFDEDS GTWTYMHHPF TAPHPDDLAL FGTDRQGDIR AQAYDLVLNG FEIGGGSVRI
HDPAVQAKMF AAIGFTEEQA RDKFGFFLDA LEYGTPPHGG IAWGFDRLIM VMSGASSIRE
VIAFPKNNRG VDLMAQAPSP VDAAQLAEVG LEVALPAAEA PAAG


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