ID C3YTL2_BRAFL Unreviewed; 519 AA.
AC C3YTL2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE RecName: Full=Aminoacyl-transfer RNA synthetases class-II family profile domain-containing protein {ECO:0000259|PROSITE:PS50862};
DE Flags: Fragment;
GN ORFNames=BRAFLDRAFT_204226 {ECO:0000313|EMBL:EEN56139.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN56139.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN56139.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN56139.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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; GG666552; EEN56139.1; -; Genomic_DNA.
DR RefSeq; XP_002600127.1; XM_002600081.1.
DR AlphaFoldDB; C3YTL2; -.
DR STRING; 7739.C3YTL2; -.
DR eggNOG; KOG2411; Eukaryota.
DR InParanoid; C3YTL2; -.
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; 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 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; 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}.
FT DOMAIN 145..459
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EEN56139.1"
FT NON_TER 519
FT /evidence="ECO:0000313|EMBL:EEN56139.1"
SQ SEQUENCE 519 AA; 59004 MW; AF94721FEAE85D89 CRC64;
DVSSYSLRSH TCGELRAVHA GEDVTLCGWV QFQRKQLFVT LRDSYGVIQL VLPQDKKHAD
MKQTLAHLPP ESVVCVQGIV QLRPIGEANK AMSTGDVEVA VSKVEMVNKS KSLPFQIRDF
FQVNEHLRLK HRYLDLRGSQ LQHNLRLRSQ VIMKMREVNK HLSSQFRFVD VETPTLFRRT
PGGAREFVVP SREKGKFFCL PQSPQQFKQL LMVGGVDRYF QIAKCYRDED LRQDRQPEFT
QVDIEMSFVD QRGVEQLIEE LLQHAWPDGK GALTLPFPRM QYKDAMKKYG SDKPDTRFGM
KLNDVSDIMR SSGVTVFERL LKDNSGNTIQ AINAKQAAPH MKNKDIEKLQ DLAKQMMSKG
LSILQILPGG EMKGAMAKHI SSPCRNALLQ ELQAEEGDML LLAGGEHLKT CELLGRIRVE
CADILETQGV QLRDPDVFNF LWITDFPLFV PKEDGSGLES AHHPFTAPHP DDLDLVYSHP
HKVRSQHYDL VLNGNEIAGG SIRIHDAEVQ RYILEEVLK
//
