ID K0TKC7_THAOC Unreviewed; 631 AA.
AC K0TKC7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
GN ORFNames=THAOC_03817 {ECO:0000313|EMBL:EJK74501.1};
OS Thalassiosira oceanica (Marine diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC Thalassiosiraceae; Thalassiosira.
OX NCBI_TaxID=159749 {ECO:0000313|EMBL:EJK74501.1, ECO:0000313|Proteomes:UP000266841};
RN [1] {ECO:0000313|EMBL:EJK74501.1, ECO:0000313|Proteomes:UP000266841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK74501.1,
RC ECO:0000313|Proteomes:UP000266841};
RX PubMed=22835381; DOI=10.1186/gb-2012-13-7-r66;
RA Lommer M., Specht M., Roy A.S., Kraemer L., Andreson R., Gutowska M.A.,
RA Wolf J., Bergner S.V., Schilhabel M.B., Klostermeier U.C., Beiko R.G.,
RA Rosenstiel P., Hippler M., Laroche J.;
RT "Genome and low-iron response of an oceanic diatom adapted to chronic iron
RT limitation.";
RL Genome Biol. 13:R66-R66(2012).
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229}.
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:EJK74501.1}.
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DR EMBL; AGNL01003610; EJK74501.1; -; Genomic_DNA.
DR AlphaFoldDB; K0TKC7; -.
DR EnsemblProtists; EJK74501; EJK74501; THAOC_03817.
DR eggNOG; KOG0556; Eukaryota.
DR OMA; WVHEIRD; -.
DR Proteomes; UP000266841; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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: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; 1.10.287.10; S15/NS1, RNA-binding; 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; IPR009068; uS15_NS1_RNA-bd_sf.
DR InterPro; IPR000738; WHEP-TRS_dom.
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; PF00458; WHEP-TRS; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SMART; SM00991; WHEP-TRS; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000266841}.
FT DOMAIN 15..71
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 325..623
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 631 AA; 70964 MW; EDE850922F1B07E9 CRC64;
MSEENGEGTT TPNPEIVELT NQISGLGAQI ADAKKAKQPK EEWDPLLQQM LALKLTYKEK
TGEDYHAAKP KAESKKPKGP VNQVASEKNA EKRKKKAEEK RLKEEKKRKQ REERERRERE
KLEKLKAAAD EDWSAVFGDM PMIQSASKSP EGIDKWTKIG DLGKGLAGKK VTVRGFLHTS
RGVGKGAFVV LRSSLYTVQC VAFEAKASGD RGEIPQSMIK YMTGQPVESV VDVEGVVTVP
EKPVEGASQS DVEIQVSKFH CVHKSVAAMP FQMEDACRPD TTRETDVGAY DPEANSTTEL
GRVGQENRLD NRWIDLRTPA NQSIFRVQSM VCTLFREYLL SKDFIEIHTP KLLSGASEGG
ADVFTLDYFG RPACLSMSPQ LHKQMASACG GFERVFEIGP VFRAENSNTR RHLCEFTGMD
LEMAIVEHYD EVLDVIGELF VHIFDGLKQR SSAEIERVRE QHPFEDLQYL PKTLKIDYAT
GCKMLREAGV DQGDYEDLST ENEKKLGDLV KEKYNTDFYI MDKYPLSVRP FYTMPDPNNP
KLSNSYDIFI RGQEILSGAQ RVHEPEFIEK RAKEWGLDVS TITSYIDSFR NGALPHGGGG
IGLERVVMLY LGLPNIRKTS MFPRDPKRIS P
//
