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Database: UniProt
Entry: A0A1X7BLK3_9RHOB
LinkDB: A0A1X7BLK3_9RHOB
Original site: A0A1X7BLK3_9RHOB 
ID   A0A1X7BLK3_9RHOB        Unreviewed;       592 AA.
AC   A0A1X7BLK3;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000256|HAMAP-Rule:MF_00044};
DE            EC=6.1.1.23 {ECO:0000256|HAMAP-Rule:MF_00044};
DE   AltName: Full=Aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00044};
DE            Short=AspRS {ECO:0000256|HAMAP-Rule:MF_00044};
DE   AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00044};
DE            Short=ND-AspRS {ECO:0000256|HAMAP-Rule:MF_00044};
GN   Name=aspS {ECO:0000256|HAMAP-Rule:MF_00044,
GN   ECO:0000313|EMBL:SMC10506.1};
GN   ORFNames=ROA7745_00313 {ECO:0000313|EMBL:SMC10506.1};
OS   Roseovarius aestuarii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=475083 {ECO:0000313|EMBL:SMC10506.1, ECO:0000313|Proteomes:UP000193224};
RN   [1] {ECO:0000313|EMBL:SMC10506.1, ECO:0000313|Proteomes:UP000193224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7745 {ECO:0000313|EMBL:SMC10506.1,
RC   ECO:0000313|Proteomes:UP000193224};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Aspartyl-tRNA synthetase with relaxed tRNA specificity since
CC       it is able to aspartylate not only its cognate tRNA(Asp) but also
CC       tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first
CC       activated by ATP to form Asp-AMP and then transferred to the acceptor
CC       end of tRNA(Asp/Asn). {ECO:0000256|HAMAP-Rule:MF_00044}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-
CC         aspartyl-tRNA(Asx); Xref=Rhea:RHEA:18349, Rhea:RHEA-COMP:9710,
CC         Rhea:RHEA-COMP:9711, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC         ChEBI:CHEBI:456215; EC=6.1.1.23; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00044};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00044}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00044}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303, ECO:0000256|HAMAP-
CC       Rule:MF_00044}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00044}.
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DR   EMBL; FWXB01000001; SMC10506.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7BLK3; -.
DR   OrthoDB; 9802326at2; -.
DR   Proteomes; UP000193224; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050560; F:aspartate-tRNA(Asn) ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd04317; EcAspRS_like_N; 1.
DR   Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_00044; Asp_tRNA_synth_type1; 1.
DR   InterPro; IPR004364; Aa-tRNA-synt_II.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004524; Asp-tRNA-ligase_1.
DR   InterPro; IPR047089; Asp-tRNA-ligase_1_N.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR004115; GAD-like_sf.
DR   InterPro; IPR029351; GAD_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   NCBIfam; TIGR00459; aspS_bact; 1.
DR   PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF02938; GAD; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF55261; GAD domain-like; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00044};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00044}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00044};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00044};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00044};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00044}; Reference proteome {ECO:0000313|Proteomes:UP000193224}.
FT   DOMAIN          142..559
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          199..202
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         175
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         221..223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         221
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         453
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         486
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         493
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         538..541
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   SITE            33
FT                   /note="Important for tRNA non-discrimination"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
SQ   SEQUENCE   592 AA;  66458 MW;  49D5216EE0F2A8FD CRC64;
     MHTYRSHSCA ELNKSNVGDT VRLSGWVHRI RDHGGVLFVD LRDHYGITQV LCDGDSAAFA
     ELEGVRSEWC IRIDGEVKAR DESLINPKLP TGEIEVYIRE MEVLGSAGEL PLIVFGDQEY
     PEETRLRYRY LDLRREAMQE NMKLRSDVVA SIRRRMWDTG FREYQTPIIT ASSPEGARDF
     LVPSRLHPGK FYALPQAPQL FKQLIMVSGF DKYFQVAPCF RDEDPRADRS PTDFYQLDME
     MSFVEQQDVF DTIQPVIAGI FEEFGGGRKV DAEWPQISYR DSAMWYGTDK PDLRNPIKMQ
     DVSEHFRGSG FAIFAKLLEQ DGTQIRAIPA PTGGSRKFCD RMNAFAQKEG LPGMGYIFWR
     DQGEGMEAAG PLAKNIGPER TEAIRQQLGL DVGDAAFFLG GKPAAFESVA GKARSVIGEE
     LNLTDKERFA FAWIVDFPMY EADEETGKVD FSHNPFSMPQ GGLEALNGDP LNVLGYQYDL
     ACNGYELVSG AIRNHKLDIM IKAFELAGYG ADEVHKRFGG LVNAFQYGAP PHGGCAAGID
     RIVMLLADEA NIREVIMFPM NQRAEDLMMN APSDPTSDQL MELGLRVIPR ED
//
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