SPNE_DROER
ID SPNE_DROER Reviewed; 1432 AA.
AC B3P3W1;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=GG16958;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01;
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; CH954181; EDV49067.1; -; Genomic_DNA.
DR RefSeq; XP_001980109.1; XM_001980073.2.
DR AlphaFoldDB; B3P3W1; -.
DR SMR; B3P3W1; -.
DR STRING; 7220.FBpp0135504; -.
DR PRIDE; B3P3W1; -.
DR EnsemblMetazoa; FBtr0137012; FBpp0135504; FBgn0109186.
DR GeneID; 6553090; -.
DR KEGG; der:6553090; -.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_002601_1_0_1; -.
DR OMA; DPCRTVY; -.
DR OrthoDB; 278674at2759; -.
DR PhylomeDB; B3P3W1; -.
DR Proteomes; UP000008711; 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;
KW RNA-mediated gene silencing; Spermatogenesis.
FT CHAIN 1..1432
FT /note="Probable ATP-dependent RNA helicase spindle-E"
FT /id="PRO_0000391914"
FT DOMAIN 124..291
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 337..524
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 237..240
FT /note="DEAH box"
FT BINDING 137..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1432 AA; 164345 MW; FB0A4D821A84CF1A CRC64;
MDQEVMDFFD FSKEFKREAA PQGYISSDPS IMATETNESK VPKREVIGTD YVPEIVAKEK
CLLDRTLRDD CPQSKRNRTL DDLDTDDEGE ETEIRRDDEY YKRYRFNLNR DKNLPIYAKR
EEILAAINAH PVVILKGQTG CGKTTQVPQY ILDEGYKSGK YCNIVVTQPR RIAAISIANR
VCQEREWQQD TVCSYQVGLH RPTSLEDTRL LYCTTGVLLN NLINKKTLTH YTHIVLDEVH
ERDQDMDFLL IVVRRLLATN SRHVKIILMS ATIDARELAD YFTTTNSVPP VITASHGRKH
AIEKFYRDQM GSIRWKEEED DQLVPQINDH GYRAAVKIIM VIDNMEREAA IQSRLSYDEA
LRYGAVLIFL PGIDEIDTMA ENITSMLQSD RNIKVFIVRC FSLMTPENQR DVFHPPPPGF
RKIILTTNIA ESSITVPDVS YVIDFCLTKV LVTDTATSFS SLRLTWASKA NCRQRAGRVG
RLRSGRVYRM VNKSFYQREM AEFGIPEMLR MPLQNSVLRA KELEMGSPIE ILALALSPPN
LSDIQNTILL LKEVGALFLT VDGVYNAMDG DITYWGTIMS RLPLDTRLSR LIILGYVFNL
LEEAIIIAAG LSMRGLYVNE GRRTQGADSF WMHYIFADGS GSDLVAIWRV YLTYLNMVEI
AHEQESAIRW AKRFHVSLRS LKEMHLLVQE LRWRCTNLGL IPFAVNPSQM MGDREKSIIL
KVIIAGAFYP NYFTRSKESC AEPDRNIYQT ISGHDPCRTV YFTNFKPAYM GELYTRRIKE
LFQEARIPPE NIDVTFQQGS QKVFVTFKQD DWLADSSKFV SVSGRVQSEV YKAVRMRLDR
IQRPIRIMTQ NNFMNYVQQR GIGDVIEGRW IPPTKPLNVE LLALPSVFSK TITGLITCII
SCGKFFFQPQ SFAECIRNMS EIFNAPQQLR NYVINAGAIT KGMMVLAKRD SNFQRATVIR
PENQSNRQPM FYVRFIDYGD CALLSMQQLR LMPKELIQQY GDLPPRVFEC RLAHVQPSSV
VSGNNRWPTA ANDLLKSVAK CGRIDIEVYS LFNNVAAVLI PMKDGIINDM LVELKLSRRS
DEDYMSRKDH DFRLRRQESA RYLTLTERQQ INEEYLRSCQ LPQDLDLPPP PLDKCNTIVM
LKGPSSPLEC SMQSIIRVGS SKRVNIDNAS VNAVLLDADP QDHHDHLIVA HATVESTNGQ
TLTARGTTLM PNVQGFGALM VMLFCPTMQL KCNNEGTSYV SILAGLGCDP VTGEPYYAEH
DVLINLDVNI LEDDVVLINQ IRYYIDSVFF NFKEEKDPAV SINERVSIYT QLRSLINRLL
CKDRSYMQRN MSNSDFEWES NPELPMPNEP FGKRAIFPMH SLTELQEEDM GRLMHLRENC
SMLHKWRNFE GTLPHMTCKL CNQLLESVPQ LRLHLLTVLH RDREKQIDYC NQ
