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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)

 B3U4L4_9BACT            Unreviewed;       587 AA.
B3U4L4;
02-SEP-2008, integrated into UniProtKB/TrEMBL.
02-SEP-2008, sequence version 1.
28-FEB-2018, entry version 82.
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,
ECO:0000313|EMBL:ACE75581.1};
ORFNames=NIDE1425 {ECO:0000313|EMBL:CBK41174.1};
Nitrospira defluvii.
Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Nitrospira.
NCBI_TaxID=330214 {ECO:0000313|EMBL:ACE75581.1};
[1] {ECO:0000313|EMBL:ACE75581.1}
NUCLEOTIDE SEQUENCE.
PubMed=18459973; DOI=10.1111/j.1462-2920.2008.01646.x;
Maixner F., Wagner M., Lucker S., Pelletier E., Schmitz-Esser S.,
Hace K., Spieck E., Konrat R., Le Paslier D., Daims H.;
"Environmental genomics reveals a functional chlorite dismutase in the
nitrite-oxidizing bacterium 'Candidatus Nitrospira defluvii'.";
Environ. Microbiol. 10:3043-3056(2008).
[2] {ECO:0000313|EMBL:CBK41174.1, ECO:0000313|Proteomes:UP000001660}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.1003860107;
Lucker S., Wagner M., Maixner F., Pelletier E., Koch H., Vacherie B.,
Rattei T., Sinninghe Damste J., Spieck E., Le Paslier D., Daims H.;
"A Nitrospira metagenome illuminates the physiology and evolution of
globally important nitrite-oxidizing bacteria.";
Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2010).
[3] {ECO:0000313|EMBL:CBK41174.1}
NUCLEOTIDE SEQUENCE.
Genoscope - CEA;
Submitted (MAR-2010) 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}.
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EMBL; EU559167; ACE75581.1; -; Genomic_DNA.
EMBL; FP929003; CBK41174.1; -; Genomic_DNA.
RefSeq; WP_013247998.1; NC_014355.1.
STRING; 330214.NIDE1425; -.
EnsemblBacteria; CBK41174; CBK41174; NIDE1425.
KEGG; nde:NIDE1425; -.
eggNOG; ENOG4105C9M; Bacteria.
eggNOG; COG0173; LUCA.
HOGENOM; HOG000275159; -.
KO; K01876; -.
OrthoDB; POG091H021G; -.
BioCyc; CNIT330214:G1GVO-1328-MONOMER; -.
Proteomes; UP000001660; 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: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.
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:ACE75581.1};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651746};
Complete proteome {ECO:0000313|Proteomes:UP000001660};
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:ACE75581.1};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651746};
Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651732};
Reference proteome {ECO:0000313|Proteomes:UP000001660}.
DOMAIN 149 555 AA_TRNA_LIGASE_II.
{ECO:0000259|PROSITE:PS50862}.
NP_BIND 222 224 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}.
NP_BIND 534 537 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}.
REGION 200 203 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
BINDING 176 176 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
BINDING 222 222 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
BINDING 231 231 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}.
BINDING 448 448 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
BINDING 482 482 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}.
BINDING 489 489 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
SITE 32 32 Important for tRNA non-discrimination.
{ECO:0000256|HAMAP-Rule:MF_00044}.
SEQUENCE 587 AA; 65584 MW; 38257367B69E4D1C CRC64;
MKIRTHRCGE LTKAQVGQQV VLNGWVQRRR DHGMVLFIDL RDRTGLTQVV FNAERNAAVH
EAAHTLRSEC VVSVTGQVMA RPDESKNPNL PTGEIEVFAD AVEILNEAKT PPFMIEDDIE
ITESLRLKYR YLDLRRPRMQ RLLGLRHGIM QAVRTFLNAE QFLEVETPVL TKSTPEGARD
YLVPSRVNPG MFYALPQSPQ LFKQVLMVSG VDRYYQIARC FRDEDLRNDR QPEFTQIDLE
MSFVDREQVM SLMERMIVSV FKDAGGVQLP TPFPRMTYAD AMGRYGSDKP DLRFDLPLHD
VTAFAAKSDF KVFKEAATKG GLVKALVVSG GASIARSRID ALGETAKSFG AKGLAWLKIT
ADGQLESVIA KFLDAKAFAE ALPEAKPGDL VLFGADKPAI VHDVLGRIRL LLGEELNLID
KTAWKPLWVT EFPLLDYSPE EKRYIFMHNP FAAPMDEDLP FLDTEPLRAR AKAYDMVLNG
SEIGGGSIRN HRSDIQFRIL DLLGIGKEQA QAKFGFLLEA LEYGAPPHGG IAFGLDRLIM
LLGGADSIRD VIAFPKTQRA QCPLTEAPSG VSADQLKELR IKLDLVE


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