ID W5MS75_LEPOC Unreviewed; 661 AA.
AC W5MS75;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Aspartyl-tRNA synthetase 2, mitochondrial {ECO:0000313|Ensembl:ENSLOCP00000011234.1};
GN Name=DARS2 {ECO:0000313|Ensembl:ENSLOCP00000011234.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000011234.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000011234.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AHAT01039651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MS75; -.
DR STRING; 7918.ENSLOCP00000011234; -.
DR Ensembl; ENSLOCT00000011250.1; ENSLOCP00000011234.1; ENSLOCG00000009206.1.
DR eggNOG; KOG2411; Eukaryota.
DR GeneTree; ENSGT01030000234618; -.
DR InParanoid; W5MS75; -.
DR OMA; YQLDVEM; -.
DR Proteomes; UP000018468; Linkage group LG10.
DR Bgee; ENSLOCG00000009206; Expressed in pharyngeal gill and 13 other cell types or tissues.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004815; F:aspartate-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:0006422; P:aspartyl-tRNA aminoacylation; IBA:GO_Central.
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 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:UP000018468}.
FT DOMAIN 200..636
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 661 AA; 74514 MW; 17644A33A2E0091B CRC64;
MSYKAGILIR RILMKGIKWH HSARTNSTAT SYRQCSQRSM TGKYLAVMRP SAILTGHNSF
SSRSHTCGEL RASHAGEQVT LCGWIQYQRQ DLFVILRDFH GLTQLFIPQD ESGAQLKEVL
CDLPLESVVR VTGEVRQRPP GQENKEMPTG DIEVCVRSVE VLNACRRLPF EIKDFVKKSE
SLRMQYRYLD LRSVQMQYNL RLRSQMVMKM REYLCNLHVG FVDVETPTLF KRTPGGAKEF
IVPSREPGRF YSLPQSPQQF KQLLMVGGID RYFQVARCYR DEGSKPDRQP EFTQVDIEMS
FVDQDGIRTL IEGLIQHSWP EDKGQIHVPF PCMTYAEAMK YYGTDKPDTR FEMKLVDISE
AFKHTAIGFL QDALNKPQGC VHAFCVPNGA THFKNKDLEV LRELAKTQFN QEVSAVVVKS
DGIWKSPLSK LLTESEKQQV CQMTHARAGD LVLLSAGQPQ DVCPALGKLR LHCAELLEAR
GVGIRDPSAF HFLWVVDFPL FLPKEDEPGQ LESAHHPFTA PHPLDADLLY SQPHKVRGQH
YDLVLNGCEI GGGSIRIHNA KLQQYVLEET LKEDKGLLSH LIEALESGAP PHGGIALGLD
RLISIIVGAA SIRDVIAFPK SFRGHDLMSN APDFVPAEDL KPYHISTTWP AGAQKNKGQE
P
//
