ID A8BPC2_GIAIC Unreviewed; 555 AA.
AC A8BPC2;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
GN ORFNames=GL50803_10870 {ECO:0000313|EMBL:EDO78048.1};
OS Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=184922 {ECO:0000313|EMBL:EDO78048.1};
RN [1] {ECO:0000313|EMBL:EDO78048.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB C6 {ECO:0000313|EMBL:EDO78048.1};
RX PubMed=17901334; DOI=10.1126/science.1143837;
RA Morrison H.G., McArthur A.G., Gillin F.D., Aley S.B., Adam R.D.,
RA Olsen G.J., Best A.A., Cande W.Z., Chen F., Cipriano M.J., Davids B.J.,
RA Dawson S.C., Elmendorf H.G., Hehl A.B., Holder M.E., Huse S.M., Kim U.U.,
RA Lasek-Nesselquist E., Manning G., Nigam A., Nixon J.E., Palm D.,
RA Passamaneck N.E., Prabhu A., Reich C.I., Reiner D.S., Samuelson J.,
RA Svard S.G., Sogin M.L.;
RT "Genomic minimalism in the early diverging intestinal parasite Giardia
RT lamblia.";
RL Science 317:1921-1926(2007).
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:EDO78048.1}.
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DR EMBL; AACB02000030; EDO78048.1; -; Genomic_DNA.
DR RefSeq; XP_001705722.1; XM_001705670.1.
DR AlphaFoldDB; A8BPC2; -.
DR STRING; 184922.A8BPC2; -.
DR EnsemblProtists; EDO78048; EDO78048; GL50803_10870.
DR GeneID; 5698613; -.
DR KEGG; gla:GL50803_0010870; -.
DR VEuPathDB; GiardiaDB:GL50803_10870; -.
DR HOGENOM; CLU_004553_2_1_1; -.
DR OMA; WVHEIRD; -.
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:EDO78048.1};
KW Ligase {ECO:0000313|EMBL:EDO78048.1}.
FT DOMAIN 247..555
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 555 AA; 62600 MW; 62266E5C574AB37D CRC64;
MRIKMADPAP QQPAELSKKA LKKAAKEAEK QAKRAENKSK QAGVDFAEAY IPPVLTTAQF
RRLRFGDAPL HMSQPELSSF RKLTDIDRPL THLVGHKVWV RARIHTVRAT GKSAFLMLRG
KMAILQACCF VPGKSEGSAE KVDEYRAMIK YINSLPPESV VEVCGALSSV DAPIKTASAE
HRDYELQLEK IYAISRAASQ MPLQVDDAMR PDSVYQAPDS QYVRPGKDTK QDYRVIDLRT
PTNQAIMRVR SAIAHEFRSF LDKAGFIEIN TPKIVAGTSE GGAAVFNVNY FNTKACLAQS
PQLYKQMCIS SGFGRVYEVG PVFRAEHSHT HRHLCEFIGL DLEMEIYESY TEILVLLGDL
MKHIFKAVEA RCSKEMSIVR TQYDLTAPEP LVWADETVIV TFCDGIKMLQ EAGYEASPLD
DLSTENERAL GKLIKEKYNT DFYILDKFPL NARPFYTMPD PHDGRYSNSY DMFIRGEEIC
SGAQRVHDPE LLEKQCRERN VDPESLRSYI DAFRYGCAPH GGAGLGLERI VMLMLGIENC
RQTCLFPRTQ ERLTP
//
