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
