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LOCUS XP_017015962 1250 aa linear INV 09-DEC-2024 ACCESSION XP_017015962 VERSION XP_017015962.2 DBLINK BioProject: PRJNA1194641 DBSOURCE REFSEQ: accession XM_017160473.3 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_017015962.1. ##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..1250 /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..1250 /product="copper-transporting ATPase 1" /calculated_mol_wt=135421 Region 13..75 /region_name="HMA" /note="Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain...; cd00371" /db_xref="CDD:238219" Site order(18..20,23) /site_type="metal-binding" /note="metal-binding site [ion binding]" /db_xref="CDD:238219" Region 94..156 /region_name="HMA" /note="Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain...; cd00371" /db_xref="CDD:238219" Site order(99..101,104) /site_type="metal-binding" /note="metal-binding site [ion binding]" /db_xref="CDD:238219" Region 207..271 /region_name="chaper_CopZ_Eh" /note="copper chaperone CopZ; NF033794" /db_xref="CDD:411374" Region 282..345 /region_name="HMA" /note="Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain...; cd00371" /db_xref="CDD:238219" Site order(288..290,293) /site_type="metal-binding" /note="metal-binding site [ion binding]" /db_xref="CDD:238219" Region 371..1125 /region_name="P-type_ATPase_Cu-like" /note="P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A and ATP7B; cd02094" /db_xref="CDD:319783" Site order(697,699,1096) /site_type="other" /note="putative Cu binding site [ion binding]" /db_xref="CDD:319783" Site order(741..743,817,913..915,945,985..987,1007,1010,1013, 1032,1035) /site_type="other" /note="putative ATP binding site [chemical binding]" /db_xref="CDD:319783" CDS 1..1250 /gene="ATP7" /coded_by="XM_017160473.3:303..4055" /db_xref="GeneID:108070129" ORIGIN 1 mqrssedmst vrlpivgmtc qscvrniqeq igqkpgiitv rvvleeqagy fdydprqtdp 61 sriasdiddm gfecsyptdt qqsssssssa wtnirvvgmt cqscvrnieg nigtkpgihs 121 ievqlaakna rvqydpaqhd paqiaelidd mgfeasvqpa dwettsksks pspaassprk 181 retppaaqng savaipieqe lltkcflhir gmtcascvaa iekhckkiyg ldtilvalla 241 akaevkfnan vvtaeniaks itelgfptel idepdngeae veleimgmtc ascvnkiesh 301 vlkikgvtsa svtlltkrgk fryitedtgp rsiceaiegl gfeaklmtgr dkmahnyleh 361 keeirkwrna flvslifggp cmvamiyfml emsdkghanm cclvpglsme nlvmfllstp 421 vqffggfhfy vqsyraikhg ttnmdvlism vttisyvysv avviaavlle qnsspltffd 481 tppmllifis lgrwlehiak gktsealskl lslkaadall veispdfdiv sekvisvdyv 541 qrgdilkvip gakvpvdgkv lyghsscdes litgesmpva krkgsvvigg sinqngvllv 601 eathtgentt laqivrlvee aqtskapiqq ladriagyfv pfvvvvssit liawiiigfa 661 npnlvpvame hkmhmdqnti ivsyafkcal svlaiacpca lglatptavm vatgtgaing 721 vlvkgatale nahkvktvvf dktgtithgt pmtskvtlfv raqvcslara ltivgaaeqn 781 sehpiasaiv hfakdmlnvg sspqggsfgk sshfqavpgc girvtvsnye qtlrqacnae 841 riinyenlhr nsplesvpvd ngasiehllp qhsvrksmel nnqqllsdlv leteeqlttd 901 qplidgpeil vlignrewmq rngievplei sdcmtheerk ghtavlcaln gqlvcmfavs 961 dmvkpeahla vytlkrmgid vvlltgdnkn taasiarevg irtvyaevlp shkvakiqri 1021 qasgirvamv gdgvndspal aqadvgitia agtdvaaeas divlmrndll dvvacldlsr 1081 ctvrrirynf ffasmynllg iplasglfap ygftllpwma svamaassvs vvcsslllkm 1141 yrkptaktlr taeyeaqlaa eraggsefel dklslhrgld dlpekggrla fkrssnslis 1201 rifmqgnggi sspnakheeg lldpeeqydg rtkivrsryh asdstelqkl