ID A0A024VK28_PLAFA Unreviewed; 795 AA.
AC A0A024VK28;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=PFFCH_04408 {ECO:0000313|EMBL:ETW28251.1};
OS Plasmodium falciparum FCH/4.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=1036724 {ECO:0000313|EMBL:ETW28251.1, ECO:0000313|Proteomes:UP000030656};
RN [1] {ECO:0000313|EMBL:ETW28251.1, ECO:0000313|Proteomes:UP000030656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FCH/4 {ECO:0000313|EMBL:ETW28251.1,
RC ECO:0000313|Proteomes:UP000030656};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Annotation of Plasmodium falciparum FCH/4.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETW28251.1, ECO:0000313|Proteomes:UP000030656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FCH/4 {ECO:0000313|EMBL:ETW28251.1,
RC ECO:0000313|Proteomes:UP000030656};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum FCH/4.";
RL Submitted (FEB-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}.
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DR EMBL; KI928026; ETW28251.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024VK28; -.
DR EnsemblProtists; ETW28251; ETW28251; PFFCH_04408.
DR Proteomes; UP000030656; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Gene3D; 1.25.40.270; Vacuolar protein sorting-associated protein vta1; 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 InterPro; IPR039431; Vta1/CALS_N.
DR InterPro; IPR023175; Vta1/CALS_N_sf.
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 Pfam; PF04652; Vta1; 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 Ligase {ECO:0000313|EMBL:ETW28251.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000030656}.
FT DOMAIN 483..795
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 85..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 795 AA; 93310 MW; 839E1987094950D3 CRC64;
MRPSFGSLDY NVLSNFCEKL FLAADKNDRN EVITKKTLQM FFTSKIFYEI LNHFKNLSTE
ENKKYVYAKY KTIYLKKCFD NNITPEPGSP KNEDAVSEVD NKIDDEDKEE EEQITNDKYE
HYEENNNDYY KGREKIGTQS KGTEDSVDFN LSLKHAQYAV NGIIKIIYIM INCLLQLNGR
LNYLKKYLLL INLFNLKNKD INFILVRKGL FVCGLRKMEK DDVVSSTPAA TEEAVMNDKK
KEKKAKKLAE KELKLAKKLE RENLKNEAAK VLDYVCEDIN KDNYGYIKVS TLQKYADSIM
ELYNLEDIYN FFVKSEDCEN EKREICVDKN VGDVKDTYNE ENLLGKKKIW VRGRIHDIRS
KGSIAFIILR HKLYSLQCIL DIKNNNNDKN MMKWVSNLSL ECIVDIYGEI KKPEIPIDST
NIKYEIHINK IFCLSKTMKE LPFLLKDANM KETNDEITIK VNQDNRLNNR CFDLRTYANY
SIFSLQSVIC HIFRTFLLQH NFVEIHTPKL LGESSEGGAN AFKINYFNQN GYLAQSPQLY
KQMCINSGFD KVFEVGPVFR AENSNTYRHL CEYVSLDIEM TYKFDYMENV HFYDSMFKHI
FKELTNNEKN KTFIKTIKNQ YPSDDFVWLD KTPIFTYEEA IKILIKNGKL FLKEEDILTY
DLTTDLEKEL GKLIKLSHNT DYYIIINFPS SLRPFYTMYK EDDPKISNSY DFFMRGEEIL
SGSQRISDMK LLLENIKLFN LDPNKLNFYI DSFAYSSYPH SGCGIGLERV LMLFLGLNNI
RKTSLFPRDP KRLIP
//
