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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)

 A0A0R1PKQ6_9LACO        Unreviewed;       589 AA.
A0A0R1PKQ6;
20-JAN-2016, integrated into UniProtKB/TrEMBL.
20-JAN-2016, sequence version 1.
25-OCT-2017, entry version 17.
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=FD33_GL001007 {ECO:0000313|EMBL:KRL29320.1};
Lactobacillus paralimentarius DSM 13238 = JCM 10415.
Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
Lactobacillus.
NCBI_TaxID=1122151 {ECO:0000313|EMBL:KRL29320.1, ECO:0000313|Proteomes:UP000051908};
[1] {ECO:0000313|EMBL:KRL29320.1, ECO:0000313|Proteomes:UP000051908}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 13238 {ECO:0000313|EMBL:KRL29320.1,
ECO:0000313|Proteomes:UP000051908};
PubMed=26415554; DOI=10.1038/ncomms9322;
Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O.,
Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E.,
Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R.,
Caufield P.W., Cui Y., Zhang H., O'Toole P.W.;
"Expanding the biotechnology potential of lactobacilli through
comparative genomics of 213 strains and associated genera.";
Nat. Commun. 6:8322-8322(2015).
-!- 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:KRL29320.1}.
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EMBL; AZES01000129; KRL29320.1; -; Genomic_DNA.
RefSeq; WP_025086124.1; NZ_BAMH01000101.1.
EnsemblBacteria; KRL29320; KRL29320; FD33_GL001007.
PATRIC; fig|1122151.5.peg.1044; -.
Proteomes; UP000051908; 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.
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.
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, ECO:0000313|EMBL:KRL29320.1};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651746};
Complete proteome {ECO:0000313|Proteomes:UP000051908};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651756};
Ligase {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651728, ECO:0000313|EMBL:KRL29320.1};
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 142 565 AA_TRNA_LIGASE_II.
{ECO:0000259|PROSITE:PS50862}.
NP_BIND 221 223 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}.
NP_BIND 536 539 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}.
REGION 199 202 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
BINDING 175 175 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
BINDING 221 221 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
BINDING 230 230 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}.
BINDING 448 448 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
BINDING 484 484 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}.
BINDING 491 491 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
SITE 83 83 Important for tRNA non-discrimination.
{ECO:0000256|HAMAP-Rule:MF_00044}.
SEQUENCE 589 AA; 67606 MW; 8499E03ABC5D5588 CRC64;
MEERTDYCGN ITEKYVGQKV SLDGWVQRRR DLGGLVFVDL RDYKGIVQLV FNTDHQDVLD
VAETLRSEYV INVIGTVRLR GEGATNDEMT TGKVEVVVEK VEILNKSLTP PFEIKDDIDS
SEETKLKYRY LDLRRPEMQK AIRTRAQIKH SVNEYLYDNG FIDIETPNLT PSTPEGARDY
LVPSRVYPGR FFALPQSPQL FKQLLMVGGF DRYFQLAHCF RDEDLRGDRQ PEFTQIDIET
SFMNKKEIQT VTEGLIARVM KDEKGIEVKT PFPRIDWDDA MDRYGSDKPD VRFGMELQNL
NDVLKDTEFK VFKNTIDNGG QVKAIVVKNA ADKYSRKNIE SYQEYIKRFG AKGLAWFKYN
DDDMTGGVSK FIKDHKDALV DRLGLENNDL VLFVADKKKV VADALGYLRK AIAKEQHLYD
PNEFAFIWVV NWPLFEYDEG IKRWTAAHHP FTMPNEEDVH YLNDGEDPHK AYAQSYDIVL
NGYELGGGSI RIHDYKIQEK MLKALNFTKE KAYEQFGFLL DALQYGCPPH GGLAIGLDRF
AMLLSGKDNI RDVIAFPKNS NATEPMTHAP LEVAKQQLDD LGIEVSKKD


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