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Database: UniProt
Entry: C6LS14_GIAIB
LinkDB: C6LS14_GIAIB
Original site: C6LS14_GIAIB 
ID   C6LS14_GIAIB            Unreviewed;       555 AA.
AC   C6LS14;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE            EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
GN   ORFNames=GL50581_1550 {ECO:0000313|EMBL:EET01155.1};
OS   Giardia intestinalis (strain ATCC 50581 / GS clone H7) (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=598745 {ECO:0000313|EMBL:EET01155.1, ECO:0000313|Proteomes:UP000002488};
RN   [1] {ECO:0000313|EMBL:EET01155.1, ECO:0000313|Proteomes:UP000002488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50581 / GS clone H7 {ECO:0000313|Proteomes:UP000002488};
RX   PubMed=19696920; DOI=10.1371/journal.ppat.1000560;
RA   Franzen O., Jerlstrom-Hultqvist J., Castro E., Sherwood E., Ankarklev J.,
RA   Reiner D.S., Palm D., Andersson J.O., Andersson B., Svard S.G.;
RT   "Draft genome sequencing of giardia intestinalis assemblage B isolate GS:
RT   is human giardiasis caused by two different species?";
RL   PLoS Pathog. 5:E1000560-E1000560(2009).
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:EET01155.1}.
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DR   EMBL; ACGJ01002166; EET01155.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6LS14; -.
DR   EnsemblProtists; EET01155; EET01155; GL50581_1550.
DR   VEuPathDB; GiardiaDB:GL50581_1550; -.
DR   OMA; WVHEIRD; -.
DR   OrthoDB; 382728at2759; -.
DR   Proteomes; UP000002488; 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   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   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   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:EET01155.1};
KW   Ligase {ECO:0000313|EMBL:EET01155.1}.
FT   DOMAIN          247..555
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   555 AA;  62571 MW;  87858BD0BDB46092 CRC64;
     MQIKMTDPTS QQPAELSKKA LKKAAKEAEK QAKKAENKNK QAEAEASEVY VPPVLTTAQF
     RRLRFGDAPL HMSQPELSSF RKLTEIDKPL THLIGRKIWV RARIHTVRAT GKSAFLMLRG
     KMAILQACCF VPGKAENSTE KIDEYRAMIK YINSLPPESV VEIYGAVSSV DSPIKTASAE
     HRGYELQLER IYAISRAASQ MPLQVDDAMR PDSVYQAPDS QYVHPGKDTK LDYRVIDLRT
     PANQAIMRVR SAIAHEFRSF LDNAGFIEIN TPKIIAGTSE GGAAVFNVNY FNTKACLAQS
     PQLYKQMCIS SGFGRVYEIG PVFRAENSHT HRHLCEFTGL DLEMEIYESY SEVLTLLGDL
     MKHIFKTVEA KCAKEISVIR AQYDLTVPEP LVWADETVIV NFCDGIKMLQ EAGYDASPLD
     DLNTENERAL GKLIKEKYNT DFYILDKFPL SARPFYTMPD PQDGRYSNSY DMFVRGEEIC
     SGAQRVHNPE LLEKQCRERN VDPESLKSYI DAFKYGCAPH GGAGLGLERI VMLMLGIENC
     RQTCLFPRTQ ERLTP
//
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