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Database: UniProt
Entry: A0A0M0JUS9_9EUKA
LinkDB: A0A0M0JUS9_9EUKA
Original site: A0A0M0JUS9_9EUKA 
ID   A0A0M0JUS9_9EUKA        Unreviewed;       575 AA.
AC   A0A0M0JUS9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=asparagine--tRNA ligase {ECO:0000256|ARBA:ARBA00012816};
DE            EC=6.1.1.22 {ECO:0000256|ARBA:ARBA00012816};
GN   ORFNames=Ctob_014277 {ECO:0000313|EMBL:KOO30082.1};
OS   Chrysochromulina tobinii.
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC   Chrysochromulinaceae; Chrysochromulina.
OX   NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO30082.1, ECO:0000313|Proteomes:UP000037460};
RN   [1] {ECO:0000313|Proteomes:UP000037460}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX   PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA   Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA   Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA   Cattolico R.A.;
RT   "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT   Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT   Prymnesiales (Haptophyceae).";
RL   PLoS Genet. 11:e1005469-e1005469(2015).
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:KOO30082.1}.
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DR   EMBL; JWZX01002297; KOO30082.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M0JUS9; -.
DR   OrthoDB; 2786597at2759; -.
DR   Proteomes; UP000037460; Unassembled WGS sequence.
DR   GO; GO:0004816; F:asparagine-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:0006421; P:asparaginyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd04318; EcAsnRS_like_N; 1.
DR   CDD; cd01200; WHEPGMRS_RNA; 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_00534; Asn_tRNA_synth; 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; IPR004522; Asn-tRNA-ligase.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR   InterPro; IPR000738; WHEP-TRS_dom.
DR   NCBIfam; TIGR00457; asnS; 1.
DR   PANTHER; PTHR22594:SF34; ASPARAGINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00152; tRNA-synt_2; 2.
DR   Pfam; PF01336; tRNA_anti-codon; 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   ECO:0000313|EMBL:KOO30082.1}; 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:UP000037460};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..575
FT                   /note="asparagine--tRNA ligase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005602104"
FT   DOMAIN          249..309
FT                   /note="WHEP-TRS"
FT                   /evidence="ECO:0000259|PROSITE:PS51185"
FT   DOMAIN          346..567
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   575 AA;  61853 MW;  C0A855C3556A91E5 CRC64;
     MLRLLACSTM LMGVSGVRSA TRIWQQRGSS LAVSPDFAGL VGRQRSRMLC ASSIETPAPV
     AAAMAATPAL KRRKVGSLLA EGESAIGTQV LLKGWVRTVR NQKTFSFVEL NDGSSLAGLQ
     VVAPSEIGTY ATVEALTTGA AVSVVGKVVA SQGKGQALEV QAQSVELVGD CPADTYPLQK
     KRHSIEFLRS IAHLRPRSNL FGAVSRVRSA LAQATHAFFA SEGFKYVQTP LITASDCEGA
     GEMFRVTTLP LTLEGEIASQ GVKVRDLKAA AKEGNAEKSD VEAAVAKLLE LKAKAAAPPP
     AAAAAPAPPN MGSSDPYAAD FFGRAAYLTV SGQLSAETYA CALGDVYTFG PTFRAENSNT
     ARHLAEFWMI EPEMAFADLA ADMNNAEAFV KYVVRHVLEH CAEDMAYFSS LDKELAGRLE
     RLVRDDFARV SYTRAIDLLQ AEIAKDPKQW ENPEVVFGTD LATEHERWLA EKHFGTATFV
     YNYPKAIKAF YMRDNDGCEP GKETVAAMDL LVPGIGELIG GSQREERLDK LLSKMAGVPH
     AGYGLGFERL VCYVTGVTNI RDAIAFPRFP GSCEF
//
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