ID A0A067D1D8_SAPPC Unreviewed; 620 AA.
AC A0A067D1D8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Aspartyl-tRNA synthetase {ECO:0000313|EMBL:KDO32847.1};
GN ORFNames=SPRG_02540 {ECO:0000313|EMBL:KDO32847.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO32847.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO32847.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO32847.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303}.
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DR EMBL; KK583194; KDO32847.1; -; Genomic_DNA.
DR RefSeq; XP_012196501.1; XM_012341111.1.
DR AlphaFoldDB; A0A067D1D8; -.
DR STRING; 695850.A0A067D1D8; -.
DR EnsemblProtists; KDO32847; KDO32847; SPRG_02540.
DR GeneID; 24125090; -.
DR KEGG; spar:SPRG_02540; -.
DR VEuPathDB; FungiDB:SPRG_02540; -.
DR OMA; YQLDVEM; -.
DR OrthoDB; 1046261at2759; -.
DR Proteomes; UP000030745; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR CDD; cd00777; AspRS_core; 1.
DR CDD; cd04317; EcAspRS_like_N; 1.
DR Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_00044; Asp_tRNA_synth_type1; 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; IPR004524; Asp-tRNA-ligase_1.
DR InterPro; IPR047089; Asp-tRNA-ligase_1_N.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR047090; AspRS_core.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR029351; GAD_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR NCBIfam; TIGR00459; aspS_bact; 1.
DR PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02938; GAD; 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; SSF55261; GAD domain-like; 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 ECO:0000313|EMBL:KDO32847.1}; 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:UP000030745}.
FT DOMAIN 151..585
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 620 AA; 68051 MW; 3D78EBA8784C3331 CRC64;
MASSSDATLA TQDFRTHTCG GLREGDVGSS IKLSGWVDAV RAFGPLTFVS LRDRHGTTQL
VFSDERVEAA NQLKPESVIR VTGAVRERPD TMRNANMATG AIEVVVDSVE TLNTCAQLPM
QVSTGSDVAT EETRLRHRYL DLRRASLQQN LAVRSKVAMT ARNYLCDNGF LEIETPTLFK
STPEGAREFL VPTRTKNQFY ALTQSPQQYK QLLMVGGLDR YFQLARCYRD EGGRADRQPE
FTQIDLEMSF VNQHDIMGMI EGMVKQIWHG ANASIDMSTP FPIMSFDEAM DRFGVDKPDT
RYGLEMRDIL AHMPKDVVGD APVVRAINAK QLGLHGFSRK DIGELEALSK RLSVDGKGAF
VVKVDEGQAW KSSLAKKLSN DQLAALNMQL EVDAGDVLLI ASGSYASVCT LLGRMRIQCA
QMLYAKGFLQ KELDPFNYHH LWVVDFPMFE LDEGGNGLSA THHPFTAPQA AHLPTLQALL
STGQNAWEDE AMQTALLNIK AQHFDLVCNG WELGGGSIRL HSVDLQNAVL QQVLNLPEVQ
KKSFEHLLNA LGHGAPPHGG IALGLDRLVA ILCGASSLRD VIAFPKSTTG NELMTGSPGP
VTPEQLLEYH IAVNQATTTA
//
