ID   SPNE_DROWI              Reviewed;        1432 AA.
AC   B4NBB0;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=GK11214;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24;
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; CH964232; EDW81074.1; -; Genomic_DNA.
DR   RefSeq; XP_002070088.1; XM_002070052.2.
DR   AlphaFoldDB; B4NBB0; -.
DR   SMR; B4NBB0; -.
DR   STRING; 7260.FBpp0240357; -.
DR   EnsemblMetazoa; FBtr0241865; FBpp0240357; FBgn0213225.
DR   GeneID; 6647243; -.
DR   KEGG; dwi:6647243; -.
DR   eggNOG; KOG0920; Eukaryota.
DR   HOGENOM; CLU_002601_1_0_1; -.
DR   InParanoid; B4NBB0; -.
DR   OMA; DPCRTVY; -.
DR   OrthoDB; 278674at2759; -.
DR   PhylomeDB; B4NBB0; -.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
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   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..1432
FT                   /note="Probable ATP-dependent RNA helicase spindle-E"
FT                   /id="PRO_0000391922"
FT   DOMAIN          125..292
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          342..525
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           238..241
FT                   /note="DEAH box"
FT   BINDING         138..145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1432 AA;  164853 MW;  3A9EE76328B3A9AE CRC64;
     MDEDLMGFFD FSKEFKRTEA PKGCISSNFV GLGTEKEKTK PPKQENLGTE YVKEIVDREK
     QNLESLGIGG SAAKRNRTLD DIDSDNEECY EAPDLRLDEE FYSKYYFDLN RDKTLPIYTQ
     RDQIMKAIRE NTVVILKGET GCGKTTQVPQ YIIDEAYQNR QYCNIVVTQP RRIAAISIAN
     RVSQERHWEP GTVCSYQVGL HRQSGSEDAR LLYCTTGVLL NFLINHKTLT HYTHIVLDEV
     HERDQEMDFL LIVVRRLLAT NSRHVKVILM SATIDSREFV QYFATKNGIP PVINASHGRK
     YPLVKFYRDQ LKNMQWQEDQ PNPDEPGMGS HGYSAAIKIL LVIDNMERRT EGQSQRSYEE
     NLKTGSVLIF LPGINEIDNM AESIDHVMQE NPALKVSIIR CHSLMTPDSQ RDVFASPPVG
     YRKIILTTNI AESSITVPDV SYVIDFCLAK VLVTDTATNF SSLRLVWASK SNCRQRAGRV
     GRLRSGRVYR MVPKSFYMKH MLEFGVPEML RSPLESSVLK AKELNMGPPI EMLALALSPP
     KLSDIRNTIL LLKEVGALYP TVDGNYVELD GDLTPWGSIM TRLPLDIRLS RLVLLGYVFN
     CLDEAIVMAA GLSVRGLYLQ EAGFQSYEAY WMHYVFADGS SSDLVAIWRF YKTYLNMCEN
     RIMQESAAQW ARRYHISLRS LKEMHLLVQE LQYRCNKLRL HPVQLQSCQI KDDRERALIL
     KILIAGAFYP NYFIRSNKFN PDYGRNTYQV LGGYDPCRTV YFTHFEPRYM GELYTRRIKD
     LFSEAKIPPE NMDVNFQVGS EKIFVTFKQT EDEMDQLNLI QVPGRILTDV YKAVRLRIGK
     QYRPIRVMEL PHAIQYVQEN KIGTVIEGQW HPPSKPFNAG LMALPSVYDK NMIGYITHIV
     SCGKFFFQPL ELADSITNMS EHINSPKNLS HYVVDAGSIT KNLKLLAKRV DDFQRAQVIR
     VETHSHQYPK FRVRFIDYGD IAVVPMDQLR FMSNQLKREY DDLPPRCFEC RLALVQPAAL
     TSNYNRWPIK ANEMVRKIAM DGRVEMEIYS LVNNVAAVFI KMREGVLNDK LVEKNYARRS
     DEDFASIQDH DFRLRKQERS FHVPRAERKQ VNEEYLRVSR LPQDADLSPP PMHKCQTVVR
     LKGPYSPLEA SMFSTIRASA CKTVRIDPLS VNSVLLDSNP QDRHDQLIVS ASVTTSNNNQ
     VLTVRGSTVM PNTHGFGALM ALIFCPTVQI KCNKECTKFV SLLAGLGYNP ETMEPYYEDH
     DVVMNLDVNL LEDDVRLINQ MRYNIDTIFF KYEGEDAPAV SEGDRSIVFN QLRCLLSRLL
     SKDRCYIEPH SSNLDNVWEK LDNLEPQSEP YGKRAIFPMH TIPELQNEDT TARLVLQENC
     KRLYSWRTFD GVLQPLDCKL CNQRLETVSQ LRLHLLSQLH RDREKQIGFQ DN