ID   SPNE_DROMO              Reviewed;        1431 AA.
AC   B4K5R2;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=GI22949;
OS   Drosophila mojavensis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15081-1352.22;
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; CH933806; EDW15124.1; -; Genomic_DNA.
DR   RefSeq; XP_001999663.1; XM_001999627.2.
DR   AlphaFoldDB; B4K5R2; -.
DR   SMR; B4K5R2; -.
DR   STRING; 7230.FBpp0172166; -.
DR   PRIDE; B4K5R2; -.
DR   EnsemblMetazoa; FBtr0173674; FBpp0172166; FBgn0145676.
DR   GeneID; 6573595; -.
DR   KEGG; dmo:Dmoj_GI22949; -.
DR   eggNOG; KOG0920; Eukaryota.
DR   HOGENOM; CLU_002601_1_0_1; -.
DR   InParanoid; B4K5R2; -.
DR   OMA; DPCRTVY; -.
DR   OrthoDB; 278674at2759; -.
DR   PhylomeDB; B4K5R2; -.
DR   Proteomes; UP000009192; 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   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..1431
FT                   /note="Probable ATP-dependent RNA helicase spindle-E"
FT                   /id="PRO_0000391917"
FT   DOMAIN          127..294
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          354..526
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          937..1000
FT                   /note="Tudor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT   MOTIF           240..243
FT                   /note="DEAH box"
FT   BINDING         140..147
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1431 AA;  165000 MW;  E768189B3336487F CRC64;
     MDSDLMDFFD FSKQFSRAPA PKGYITGDPT AFATETIDSK PIKRELIGKD YVHEVVEKEK
     HLMKKLADGY NTSKNRRTLD ELDSDDDEVL MKELPSVRSD EEYYKKYRFD LNRNKNLPIY
     EQREDILAAI RENPVVILKG ETGCGKTTQV PQYILDEAFK RREFCNIVVT QPRRIAAISI
     ANRVCHERKW QPGTVCSYQV GLHRQSNLED TRLLYCTTGV LLNNLVRVKT LTQYTHIILD
     EVHERDQDMD FLLLVVRRLL ALNSRHVKVI LMSATIDTRE FSKYFAMSSS LPPVVTASHG
     RKFPLVKFYR DQLKNIHWKD EPQRTTPGIG PEGYSDAIKL LLVIDNMERK ADNQSQQSYE
     EAKRTGAVLI FLPGIHEIDT MAEHIGRIVD ENPNFKISIV RCHSLMSPDS QEEVFLPPPL
     GHRKVILTTN ISESSITVPD VSYVIDFCLT KVLHTDTASN FSSLRLEWAS KVNCRQRAGR
     VGRLRSGRVY RMVTKDFYMN HMNEFGIPEM LRSPLQNSVL KAKELEMGNP SEILALAMSP
     PNLSDIQNTV LLLKEVGALY TTVDGVYEEL DGDLSFWGKI MSKFPLDVRL SRLIILGYVF
     NCLDEAIVIA AGMTVRSLYV TGSRGQMNEA FWMHYIFADG SGSDMIGIWR VYRIYLNMCQ
     DRMLKESAQQ WARRFNVNLR SLKEMHLMVQ DLRQRCASLN IQPLPYGACH MWDDREKSII
     LKVIIAGAFY PNYFMRSNKA NADYDRSLFQ TICGNDPCRT VYFTNFEPRY MGELYTRRIK
     ELFLEAKIPP ENIDVTFQHG SEKVFVTFKP DDEDIDTTKV VQVPGRVMTE VYKAVRMRLE
     NQNRPLRVMD QNSAFKYVEQ NRIGVISDCT WVPPSNQWPV ELLTLPSVFD KTIFGLITHV
     ANCGKFYFQP QALAERIASM SEIFNRSLEL SCYVQNAKAV TKGLQLLAKR GNLYQRAVVL
     KVETQINGYP RFRVRFIDYG DVAVVPIDKL RLMSPQLKRD FERLPPRMFE CRLALVQPSS
     VASSYNQWPQ HANEMLISVA KSGRVELEIY SLVNNVAAVL IHTRGGVLND MLVDRQLARR
     ADEDYMSRKD HDLRLRKQET KRNVSITDQR LINEEYLRFA QLPKDTDLEP PPLNKCNLSI
     RLKGPYSPLE ASLNSLLRIG MYKSVYIDKE SVNSVLLDSD PQDRHDQMVV AASVTEAFDN
     LTVRGTTLMP NIHGFGALMA MLFCPTMQIK CNKDRTKYVS ILAGLGYNPD TMQPHFEEHD
     MVINLDVAIL KDDIRIINQM RYNIDSMFYN FDVNEMPSVG TEDRVVIFNQ LRSLLIRLLG
     KDRSFIERHV SNFEYLWEDM SDLEPPSEPY GKRAIFPMHS SYDFESENMG NLLSLQANCK
     ELYSWRNFEG TMQPMKCRLC NDTLESVAEL RLHLLTQLHR DREKQVGWKQ N