ID E2LIB3_MONPE Unreviewed; 155 AA.
AC E2LIB3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
DE Flags: Fragment;
GN ORFNames=MPER_06285 {ECO:0000313|EMBL:EEB94838.1};
OS Moniliophthora perniciosa (strain FA553 / isolate CP02) (Witches'-broom
OS disease fungus) (Marasmius perniciosus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=554373 {ECO:0000313|EMBL:EEB94838.1, ECO:0000313|Proteomes:UP000000741};
RN [1] {ECO:0000313|EMBL:EEB94838.1, ECO:0000313|Proteomes:UP000000741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FA553 / isolate CP02 {ECO:0000313|Proteomes:UP000000741};
RX PubMed=19019209; DOI=10.1186/1471-2164-9-548;
RA Mondego J.M., Carazzolle M.F., Costa G.G., Formighieri E.F., Parizzi L.P.,
RA Rincones J., Cotomacci C., Carraro D.M., Cunha A.F., Carrer H., Vidal R.O.,
RA Estrela R.C., Garcia O., Thomazella D.P., de Oliveira B.V., Pires A.B.,
RA Rio M.C., Araujo M.R., de Moraes M.H., Castro L.A., Gramacho K.P.,
RA Goncalves M.S., Neto J.P., Neto A.G., Barbosa L.V., Guiltinan M.J.,
RA Bailey B.A., Meinhardt L.W., Cascardo J.C., Pereira G.A.;
RT "A genome survey of Moniliophthora perniciosa gives new insights into
RT Witches' broom disease of cacao.";
RL BMC Genomics 9:548-548(2008).
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:EEB94838.1}.
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DR EMBL; ABRE01010608; EEB94838.1; -; Genomic_DNA.
DR AlphaFoldDB; E2LIB3; -.
DR STRING; 554373.E2LIB3; -.
DR KEGG; mpr:MPER_06285; -.
DR HOGENOM; CLU_1699710_0_0_1; -.
DR InParanoid; E2LIB3; -.
DR OrthoDB; 382728at2759; -.
DR Proteomes; UP000000741; 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:UP000000741}.
FT DOMAIN 25..155
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EEB94838.1"
SQ SEQUENCE 155 AA; 18269 MW; 563E27D7B67ED7DD CRC64;
YFKGNAFLAQ SPQLAKQMCI AADFERVYEI GPVFRAEDSN THRHLTEFMG LDLEMAIEEH
YHEVMELLDG LFISIFRGLR EKYKKEIQVI GKQFPADEFK WREGPEGTLK LKFREAIDLL
HGKRKEAWQN CKGKYDTDYL IIDNFTMSYV RSNYA
//
