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SPNE_DROPE
ID   SPNE_DROPE              Reviewed;        1434 AA.
AC   B4GEU5;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Probable ATP-dependent RNA helicase spindle-E;
DE            EC=3.6.4.13;
DE   AltName: Full=Homeless;
GN   Name=spn-E; Synonyms=hls; ORFNames=GL22075;
OS   Drosophila persimilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSH-3 / Tucson 14011-0111.49;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Probable ATP-binding RNA helicase which plays a central role
CC       during spermatogenesis and oogenesis by repressing transposable
CC       elements and preventing their mobilization, which is essential for the
CC       germline integrity. Acts via the piRNA metabolic process, which
CC       mediates the repression of transposable elements during meiosis by
CC       forming complexes composed of piRNAs and Piwi and govern the
CC       methylation and subsequent repression of transposons. Involved in the
CC       repression of LTR retrotransposon copia. Also involved in telomere
CC       regulation by repressing specialized telomeric retroelements HeT-A,
CC       TAHRE, and TART; Drosophila telomeres being maintained by transposition
CC       of specialized telomeric retroelements. Involved in telomeric trans-
CC       silencing, a repression mechanism by which a transposon or a transgene
CC       inserted in subtelomeric heterochromatin has the capacity to repress in
CC       trans in the female germline, a homologous transposon, or transgene
CC       located in euchromatin. Involved in the repression of testis-expressed
CC       Stellate genes by the homologous Su(Ste) repeats. Required for
CC       anteroposterior and dorsoventral axis formation during oogenesis (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Component of the
CC       nuage, also named P granule, a germ-cell-specific organelle required to
CC       repress transposon during meiosis. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CH479182; EDW34130.1; -; Genomic_DNA.
DR   RefSeq; XP_002017030.1; XM_002016994.1.
DR   AlphaFoldDB; B4GEU5; -.
DR   SMR; B4GEU5; -.
DR   STRING; 7234.FBpp0186182; -.
DR   EnsemblMetazoa; FBtr0187690; FBpp0186182; FBgn0159667.
DR   GeneID; 6592096; -.
DR   KEGG; dpe:6592096; -.
DR   eggNOG; KOG0920; Eukaryota.
DR   HOGENOM; CLU_002601_1_0_1; -.
DR   OMA; DPCRTVY; -.
DR   PhylomeDB; B4GEU5; -.
DR   Proteomes; UP000008744; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblMetazoa.
DR   GO; GO:0043186; C:P granule; IEA:EnsemblMetazoa.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046843; P:dorsal appendage formation; IEA:EnsemblMetazoa.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0007294; P:germarium-derived oocyte fate determination; IEA:EnsemblMetazoa.
DR   GO; GO:0098795; P:global gene silencing by mRNA cleavage; IEA:EnsemblMetazoa.
DR   GO; GO:0031507; P:heterochromatin assembly; IEA:EnsemblMetazoa.
DR   GO; GO:0008298; P:intracellular mRNA localization; IEA:EnsemblMetazoa.
DR   GO; GO:0007076; P:mitotic chromosome condensation; IEA:EnsemblMetazoa.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:EnsemblMetazoa.
DR   GO; GO:0000335; P:negative regulation of transposition, DNA-mediated; IEA:EnsemblMetazoa.
DR   GO; GO:0030717; P:oocyte karyosome formation; IEA:EnsemblMetazoa.
DR   GO; GO:0030720; P:oocyte localization involved in germarium-derived egg chamber formation; IEA:EnsemblMetazoa.
DR   GO; GO:0001556; P:oocyte maturation; IEA:EnsemblMetazoa.
DR   GO; GO:0009949; P:polarity specification of anterior/posterior axis; IEA:EnsemblMetazoa.
DR   GO; GO:0009951; P:polarity specification of dorsal/ventral axis; IEA:EnsemblMetazoa.
DR   GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IEA:EnsemblMetazoa.
DR   GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IEA:EnsemblMetazoa.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   CDD; cd04508; TUDOR; 1.
DR   Gene3D; 2.40.50.90; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR035437; SNase_OB-fold_sf.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00567; TUDOR; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00333; TUDOR; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50304; TUDOR; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Developmental protein; Differentiation; Helicase;
KW   Hydrolase; Meiosis; Nucleotide-binding; Oogenesis; Reference proteome;
KW   RNA-mediated gene silencing; Spermatogenesis.
FT   CHAIN           1..1434
FT                   /note="Probable ATP-dependent RNA helicase spindle-E"
FT                   /id="PRO_0000391918"
FT   DOMAIN          126..295
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          356..527
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          936..999
FT                   /note="Tudor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT   MOTIF           241..244
FT                   /note="DEAH box"
FT   BINDING         139..146
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1434 AA;  164380 MW;  98B8B07DCF85C273 CRC64;
     MDQELMDFFD FSKEFVRKQA PRGHVSSNVH AFVTESDELE KPIKREIVGK DYVKSFVEKE
     KKRMNGIFSS DEMASRRNKS LDDMDSDEEY EASPEIRTDA EFYEKYYFNL NRDKSLPIYA
     KREEIINAIN ENPVVIVKGE TGCGKTTQVP PILFWMMVSK AKQYCNIVVT QPRRIAAISI
     ANRVCQERQW QPGTVCGYQV GLHRQLERFA DTRLLYCTTG VLLNILVNNK TLTHYTHIVL
     DEVHERGQEM DFLLIVIRRL LATNSRHVKV ILMSATINPR ELSDYFANES SAPPVIAASY
     GRNFTVEKYY RDQLQSINWE GHQEDINSPG ITQEGYRSAI KTILVIDNME RNERGTGKSY
     NQSLREGSIL IFLPGVGEIN NMSDMLKDMA NHDPIMKFNM VRCHSLMTSE DQREIFQPSP
     PGYRKIIMAT NVAESSITVP DVSYIIDFCL EKVLVTDTST NFSSLRLAWA SKTNCRQRAG
     RVGRLRNGRV YRMVTKSFYQ RELSEYSVPE MLRSPLQNCV LKAKELKMGT PVEMLALALS
     PPNLSDICNT ILMLKEVGAL FPTMDGTYDP RDGDITYWGT IMSKLPLDTH LSRLIILGYV
     FNLVDEAIII AAGLTVRGIY IDSARLGADN YWMHYVFADG SGSDLVGIWR VYLTYLNMCE
     NGLQKDASIQ WAKRFHLSLR ALSEMHLLVQ DLRLRCEKLS LLPLNFPTHR ISDDREKAIM
     LKVIIAGSFY PNYFVQSKST SGDDRNMFSV ISGLDPCRTV YFTSFTDRTM GELYTRKVKQ
     LFPEAQIPPE NMDVTFGQGS EKIFVTFKND IYKPEGTTYV HVPGRIKAEV YKALRLRTYC
     NQHSLRVMEP MNALKYVKDK KIGKIVEGRW IPPSKPVAVE LLALPSLFDK IIIGRITNIV
     SCGKFFFQPE SFENCIANMS EHFNNPQQLQ NCVRNAGAIT KGLMLLAKRQ GKYQRATVVR
     VDTQDSRNVR FYVRFVDYGD IERLPMAQLR LMSQDLLRHY RDLPPRLFEC RLALVQPASM
     VSTYNAWPQK ADDMLHALAK GGRVQLEIYS LVQNVAAVMI HLREGNLNEL LVKEKLARRT
     DEDYMSRVDH DFRMRKQECR GYVSQQERQQ VNEEYLRSKQ LPQDMDLSPP PPEECNSLIT
     LKGPFSTLES RVFSTMRSGM SKTVRIDPCS VNFVLLDTEP QDQHAKMVVA ASISAAGRHN
     DVLTLRSTSI MPNIPGFAAI MTLIFCPRAQ LKANTANSRY VSILAGIGYH PQTMQSYYED
     HDLVINLDVN IDEHDVLLIN QIRYMIDSAF FNLEGELHPT AGHADRVLIH NTIYPALNRL
     LSKNRNFIEC NPNSSDYVWQ DMEESGEPDP QPYGRRSIFP MHTIPELHEE KMDTVLDLIA
     NCKEMYDYRN FEGSFDPMTC SLCKQYLESV AELRLHLLTQ LHLDREKEVG YPID
 
 
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