ID B8C1D1_THAPS Unreviewed; 487 AA.
AC B8C1D1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=asparagine--tRNA ligase {ECO:0000256|ARBA:ARBA00012816};
DE EC=6.1.1.22 {ECO:0000256|ARBA:ARBA00012816};
GN ORFNames=THAPSDRAFT_26191 {ECO:0000313|EMBL:EED93221.1};
OS Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC Thalassiosiraceae; Thalassiosira.
OX NCBI_TaxID=35128 {ECO:0000313|EMBL:EED93221.1, ECO:0000313|Proteomes:UP000001449};
RN [1] {ECO:0000313|EMBL:EED93221.1, ECO:0000313|Proteomes:UP000001449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED93221.1};
RX PubMed=15459382; DOI=10.1126/science.1101156;
RA Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D.,
RA Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., Brzezinski M.A.,
RA Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., Detter J.C.,
RA Glavina T., Goodstein D., Hadi M.Z., Hellsten U., Hildebrand M.,
RA Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., Lau W.W., Lane T.W.,
RA Larimer F.W., Lippmeier J.C., Lucas S., Medina M., Montsant A., Obornik M.,
RA Parker M.S., Palenik B., Pazour G.J., Richardson P.M., Rynearson T.A.,
RA Saito M.A., Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A.,
RA Wilkerson F.P., Rokhsar D.S.;
RT "The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and
RT metabolism.";
RL Science 306:79-86(2004).
RN [2] {ECO:0000313|EMBL:EED93221.1, ECO:0000313|Proteomes:UP000001449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED93221.1};
RX PubMed=18923393; DOI=10.1038/nature07410;
RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA Grigoriev I.V.;
RT "The Phaeodactylum genome reveals the evolutionary history of diatom
RT genomes.";
RL Nature 456:239-244(2008).
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229}.
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DR EMBL; CM000641; EED93221.1; -; Genomic_DNA.
DR RefSeq; XP_002289684.1; XM_002289648.1.
DR AlphaFoldDB; B8C1D1; -.
DR STRING; 35128.B8C1D1; -.
DR PaxDb; 35128-Thaps26191; -.
DR EnsemblProtists; EED93221; EED93221; THAPSDRAFT_26191.
DR GeneID; 7447475; -.
DR KEGG; tps:THAPSDRAFT_26191; -.
DR eggNOG; KOG0554; Eukaryota.
DR HOGENOM; CLU_004553_2_0_1; -.
DR InParanoid; B8C1D1; -.
DR OMA; DNMDLAE; -.
DR Proteomes; UP000001449; Chromosome 4.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004816; F:asparagine-tRNA ligase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR CDD; cd00776; AsxRS_core; 1.
DR CDD; cd04318; EcAsnRS_like_N; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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 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; 1.
DR Pfam; PF01336; tRNA_anti-codon; 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: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:UP000001449}.
FT DOMAIN 144..479
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"
SQ SEQUENCE 487 AA; 53919 MW; BF5A3354830F509B CRC64;
MTNSDATVSP PRVKTAEAQV SEDPVSVKGW VKTVRKQKTL AFVEVNDGSN MGGIQCVVPF
DGVDEDTLAA IDNLTTGCSV HATGLIVNSQ GGKQSVELSA SSLRVVGTCP GETFPLAKKR
HSLEYLRTIA HLRPRTNTIA AVARVRSTLA GSIHSFFQGE GFQYVQTPLI TASDCEGAGE
MFRVTTLNTD DVSSLPRAKD EDGKELPGVD YTEDFFGKAA FLTVSGQLGG ETYACALGDV
YTFGPTFRAE NSQTARHLAE FWMVEPEMAF ADLTSAMDNA ESMLKSVVGE VLEKCDEDLT
FFANFFDKGL KNRLKKVVEK PFVRVAYRDA IGYLQEEIAK DPSKWQFPEV EFGTDLATEH
ERWLAETKFE SAVFVYNYPK KIKAFYMRDN DEDGGETVNA MDLLVPGVGE LVGGSQREER
LDVLIEKMKE LGLNEEDYWW YLDLRRFGSV PHAGYGLGFE RLVTYVCGIE NIRDAIAYPR
YPGNAEF
//
