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LOCUS XP_017007273 476 aa linear INV 09-DEC-2024 takahashii]. ACCESSION XP_017007273 VERSION XP_017007273.2 DBLINK BioProject: PRJNA1194641 DBSOURCE REFSEQ: accession XM_017151784.3 KEYWORDS RefSeq. SOURCE Drosophila takahashii ORGANISM Drosophila takahashii Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora. COMMENT MODEL REFSEQ: This record is predicted by automated computational analysis. This record is derived from a genomic sequence (NC_091683) annotated using gene prediction method: Gnomon. Also see: Documentation of NCBI's Annotation Process On Oct 18, 2021 this sequence version replaced XP_017007273.1. ##Genome-Annotation-Data-START## Annotation Provider :: NCBI RefSeq Annotation Status :: Full annotation Annotation Name :: GCF_030179915.1-RS_2024_12 Annotation Pipeline :: NCBI eukaryotic genome annotation pipeline Annotation Software Version :: 10.3 Annotation Method :: Gnomon; cmsearch; tRNAscan-SE Features Annotated :: Gene; mRNA; CDS; ncRNA Annotation Date :: 12/07/2024 ##Genome-Annotation-Data-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..476 /organism="Drosophila takahashii" /strain="IR98-3 E-12201" /db_xref="taxon:29030" /chromosome="X" /sex="female" /tissue_type="Whole fly" /dev_stage="Adult fly" /collected_by="Originally obtained from EHIME-Fly" Protein 1..476 /product="tRNA-dihydrouridine(20) synthase [NAD(P)+]-like" /calculated_mol_wt=52861 Region 30..271 /region_name="DUS_like_FMN" /note="Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also...; cd02801" /db_xref="CDD:239200" Site order(34..36,60,105,131,173,201,232,234,259..260) /site_type="other" /note="FMN binding site [chemical binding]" /db_xref="CDD:239200" Site order(105,134..135,173,175,200..201,203..204,233..234,260) /site_type="active" /db_xref="CDD:239200" Site order(134,175,201,203) /site_type="active" /note="catalytic residues [active]" /db_xref="CDD:239200" Site order(135,173,200,204,233..234) /site_type="other" /note="substrate binding site [chemical binding]" /db_xref="CDD:239200" Region 397..461 /region_name="DSRM_DUS2L" /note="double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) and similar proteins; cd19871" /db_xref="CDD:380700" Site order(397,399..400,403..404,407..408,413..414,421, 422..423,425,443..446,449..450) /site_type="other" /note="putative RNA binding site [nucleotide binding]" /db_xref="CDD:380700" CDS 1..476 /gene="Dus2" /coded_by="XM_017151784.3:85..1515" /db_xref="GeneID:108064304" ORIGIN 1 mqsmrlpiqi larslgismk trqrldyrdk lilapmvrvg tlpmrllale mgadivytee 61 lvdlkliksi rrpnaalgtv dfvdpsdgti vfrtcaqets rlvlqlgtsd pnralavgql 121 lqrdiagldi nmgcpkefsi kggmgaalls dpakaalilr tlcsgldipv tckirilpdv 181 aqtidlvqql aatgiaaigi hartrderpq hpahpevlra vaqavdipii anggsksmhc 241 hedlrkfqad cgaasvmvar aaqinvsifr kegllpmdel ierylrlcvd ydnaphnaky 301 cvqsilrelq etprgkrflq cqtlqqmcei wqlgdycrrr qrelrtlgns graeveppea 361 qakrqkleei ssgdeysnvi crnmpflrst ypsdnhlpkt qlyvhaareg ksppayetqq 421 cdklfrsics fdgqrfsssf weknkkqaeq gaalvallhl gqleaqvlrd ngslln