ID V4ZGI5_TOXGV Unreviewed; 773 AA.
AC V4ZGI5; A0A0F7UZA1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033155};
GN ORFNames=BN1205_046930 {ECO:0000313|EMBL:CEL73888.1}, TGVEG_202530
GN {ECO:0000313|EMBL:ESS32976.1};
OS Toxoplasma gondii (strain ATCC 50861 / VEG).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=432359 {ECO:0000313|EMBL:ESS32976.1, ECO:0000313|Proteomes:UP000002226};
RN [1] {ECO:0000313|EMBL:ESS32976.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:ESS32976.1};
RA Paulsen I.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50861 / VEG {ECO:0000313|Proteomes:UP000002226};
RA Lorenzi H., Inman J., Amedeo P., Brunk B., Roos D., Caler E.;
RT "Annotation of Toxoplasma gondii VEG.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ESS32976.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:ESS32976.1};
RA Sibley D., Venepally P., Karamycheva S., Hadjithomas M., Khan A., Brunk B.,
RA Roos D., Caler E., Lorenzi H.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:CEL73888.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:CEL73888.1};
RX PubMed=25875305; DOI=10.1371/journal.pone.0124473;
RA Ramaprasad A., Mourier T., Naeem R., Malas T.B., Moussa E., Panigrahi A.,
RA Vermont S.J., Otto T.D., Wastling J., Pain A.;
RT "Comprehensive Evaluation of Toxoplasma gondii VEG and Neospora caninum LIV
RT Genomes with Tachyzoite Stage Transcriptome and Proteome Defines Novel
RT Transcript Features.";
RL PLoS ONE 10:e0124473-e0124473(2015).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LN714496; CEL73888.1; -; Genomic_DNA.
DR EMBL; AAYL02000119; ESS32976.1; -; Genomic_DNA.
DR AlphaFoldDB; V4ZGI5; -.
DR STRING; 432359.V4ZGI5; -.
DR PaxDb; 5811-TGME49_002530; -.
DR EnsemblProtists; ESS32976; ESS32976; TGVEG_202530.
DR VEuPathDB; ToxoDB:TGVEG_202530; -.
DR eggNOG; KOG0556; Eukaryota.
DR OMA; WVHEIRD; -.
DR Proteomes; UP000002226; Partially assembled 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:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd04320; AspRS_cyto_N; 1.
DR CDD; cd00776; AsxRS_core; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_02075; Asp_tRNA_synth_type2; 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; IPR004523; Asp-tRNA_synthase_2.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR NCBIfam; TIGR00458; aspS_nondisc; 1.
DR PANTHER; PTHR43450:SF1; ASPARTATE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR43450; ASPARTYL-TRNA SYNTHETASE; 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; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:CEL73888.1};
KW Coiled coil {ECO:0000256|SAM:Coils}; Ligase {ECO:0000313|EMBL:ESS32976.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002226}.
FT DOMAIN 464..773
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 227..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 255..289
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 773 AA; 86762 MW; 73E8F029D7D60373 CRC64;
MERDGLCSLC MRFPPFRFAP ILFIFSLFLI DTEEVFLPQQ RPASRFFLST SAPFSPLRSS
GVSELSSSPP SAPLVPWPSS LSASFLSSCA ACRRSPFRSS AFAAAEPGDR CFGRNKENWR
MRVLPSSSLC FTSVSPSSAR APVTSRCFSS LPTKALKPSV SFIRVSRFRS SSALLKPRSL
PLSSARCSSL AGHSAEVDRR MPSAVSVSSS PTTPSLLRAF SCLSSLPPAM PEETPKREEA
APSVAEVAEA PVSKKAQKKA EKEAAKEAAK AAKREALEAE QRAAQAVMNK QVEDLEKDAF
GYLPVIDSRM RTNREWIPVD QLRNHVGKTV WVRGRIQESR GKGSVGFLML RERQETVQGV
LDAKRGNTKD MIKWTMSLPL ESVVDLQGTV VEPEVEIQST SQKGVELLVT KIFCVSKAAQ
ELPFQLRDAM RPEDGSEGGI RVNMDTRLDN RILDLRTPVN QAIFRIQSET LQLFREFLLS
RNFVELHSPK LIGGASEGGA SCFTLKYFNR DACLAQSPQL YKQMAMCADF ERVFEIGPVF
RAENSNTHRH LCEFTGLDLE MTFKEHYSEV LDLLDDLFKF IFKGLSERCK KEIDLFHQQH
PAEPFTWIEE TPRLSFEEGV QMLREAGCPN IPEDLSEFDL STEQEKMLGR LVKEKYHTDF
YMLLQYPLKV RPFYTMPDPH NKMYSNSYDF FMRNEEITSG AQRVHDADLL TQRCLECGVP
PSSIQTYIDS FRLGTAPHGG AGIGLERVVM LFLGAKNIRQ VSLFPRDPKR LTP
//
