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Database: UniProt
Entry: A0A061J856_TRYRA
LinkDB: A0A061J856_TRYRA
Original site: A0A061J856_TRYRA 
ID   A0A061J856_TRYRA        Unreviewed;       336 AA.
AC   A0A061J856;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE            EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
GN   ORFNames=TRSC58_01959 {ECO:0000313|EMBL:ESL10311.1};
OS   Trypanosoma rangeli SC58.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Herpetosoma.
OX   NCBI_TaxID=429131 {ECO:0000313|EMBL:ESL10311.1, ECO:0000313|Proteomes:UP000031737};
RN   [1] {ECO:0000313|EMBL:ESL10311.1, ECO:0000313|Proteomes:UP000031737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC58 {ECO:0000313|EMBL:ESL10311.1,
RC   ECO:0000313|Proteomes:UP000031737};
RA   Stoco P.H., Wagner G., Gerber A., Zaha A., Thompson C., Bartholomeu D.C.,
RA   Luckemeyer D.D., Bahia D., Loreto E., Prestes E.B., Lima F.M.,
RA   Rodrigues-Luiz G., Vallejo G.A., Filho J.F., Monteiro K.M., Tyler K.M.,
RA   de Almeida L.G., Ortiz M.F., Siervo M.A., de Moraes M.H., Cunha O.L.,
RA   Mendonca-Neto R., Silva R., Teixeira S.M., Murta S.M., Sincero T.C.,
RA   Mendes T.A., Urmenyi T.P., Silva V.G., da Rocha W.D., Andersson B.,
RA   Romanha A.J., Steindel M., de Vasconcelos A.T., Grisard E.C.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC         aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC         Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC         ChEBI:CHEBI:456215; EC=6.1.1.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00000225};
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type 2 subfamily. {ECO:0000256|ARBA:ARBA00005312}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESL10311.1}.
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DR   EMBL; AUPL01001959; ESL10311.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061J856; -.
DR   EnsemblProtists; ESL10311; ESL10311; TRSC58_01959.
DR   VEuPathDB; TriTrypDB:TRSC58_01959; -.
DR   OrthoDB; 382728at2759; -.
DR   Proteomes; UP000031737; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:InterPro.
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; IPR004523; Asp-tRNA_synthase_2.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   PANTHER; PTHR43450:SF1; ASPARTATE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR43450; ASPARTYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000031737}.
FT   DOMAIN          1..336
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   336 AA;  38727 MW;  55522C6A11EEF6D2 CRC64;
     MQSRVGQYFR QFLLDNDFVE IHSPKIISAA SEGGANVFKV DYFNRNAYLA QSPQLYKQMA
     LQGDFKRVFE VGPVFRAENS NTHRHLTEFV GLDVEMRINE HYYEVLDTAE ELFSYMFANL
     AEHTAELDAI YQQYPFASLL WQLTPETIKT LGVGIIEDDV EPTDVYKARV RNMGMRMLRI
     NYPYCIELLN TVLEEKLSPT DDINTANEKL LGKLVKERYG VDFFISDRFP SVVRPFYTMP
     CPDDERFTNS YDMFIRGEEI SSGAQRIHDS SLLLQRAKTL GVDLSPIRDY VDSFRLGAWP
     HGGFGVGLER VVMLYLGLHN VRLVSLFPRD PQRVTP
//
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