SPNE_DROYA
ID SPNE_DROYA Reviewed; 1436 AA.
AC B4PRJ9;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=GE24344;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01;
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; CM000160; EDW97399.1; -; Genomic_DNA.
DR RefSeq; XP_002097687.1; XM_002097651.2.
DR AlphaFoldDB; B4PRJ9; -.
DR SMR; B4PRJ9; -.
DR STRING; 7245.FBpp0269354; -.
DR PRIDE; B4PRJ9; -.
DR EnsemblMetazoa; FBtr0270862; FBpp0269354; FBgn0241465.
DR GeneID; 6537126; -.
DR KEGG; dya:Dyak_GE24344; -.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_002601_1_0_1; -.
DR OMA; DPCRTVY; -.
DR OrthoDB; 278674at2759; -.
DR PhylomeDB; B4PRJ9; -.
DR Proteomes; UP000002282; Chromosome 3R.
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..1436
FT /note="Probable ATP-dependent RNA helicase spindle-E"
FT /id="PRO_0000391923"
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 940..1003
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 1436 AA; 164992 MW; 8D1769B06F2FE29F CRC64;
MDQDVMDFFD FSKEFKREVA PQGYISSDPK MMATDSIDSK VPKREVIGTE YVTEIVAKEK
GLLNRTLRDE CPQSKRKHTL DDLDTDDEEE ETEIRRDDEY YKKYRFNLNR DKNLPIYAKR
EEILAAINAN PVVILKGETG CGKTTQVPQY ILDEGYKSGK YCNIVVTQPR RIAAISIANR
VCQEREWQQD TVCSYQVGLH RPTSLEDTRL LYCTTGVLLN NLIRNKTLTH YTHIVLDEVH
ERDQDMDFLL IVVRRLLATN SRHVKIILMS ATIDARELSD YFTTTNSIPP VISASHGRKH
SIEKFYRDQM GSIKWKEEED DQLVPQINDH GYRAAVKIIM VIDNMEREGA IHSRMSYDEA
LRYGAVLIFL PGIYEIDTMA ENITLMLEND RNVKVFIVRC FSLMTPENQR DVFHPPPPGF
RKIILTTNIA ESSITVPDVS YVIDFCLTKV LVTDTATNFS SLRLTWASKA NCRQRAGRVG
RLRSGRVYRM VNKSFYQREM SEFGIPEMLR LPLQNSVLRA KELEMGSPVE ILALALSPPN
LSDIQNTILL LKEVGALFLT VDGVYNAMDG DVTYWGTIMS RLPLDPRLSR LIILGYVFNL
LEEAIIMAAG LSMRGLYVHE GSSSRSTRAQ FDSFWMHYIF ADGSGSDLVA IWRVYLTYLN
MVEIGHEQES AIRWANRFHV SLRSLKEMHL LVQELRVRCT NLGLIPFSVN PSQIMDDREK
SFILKVIIAG AFYPNYFTRS KEMWNEHDRH IYQTISGHDP CRTVYFTNFG PSCMGELYTR
RIKDFFHDAR IPPENMDVTF QPGSEKVFVT FKQDDCVADS SKLVSVPGRV QSEVYKAVRM
RLSCMQRIIR IMRPKQFMNY VQERGIGDVI EGRWIPPTKP LNVELLALPS VFSKTITGLI
TGIINCGKFY FQPLSLAECI RNMSEIFNAP QQLRKYVVDA CDISKGMMVL AKRDSNFQRA
TVIRPENQSN RQPMFYVRFI DYGDCALLPM QQLRFMSEEL IQQYGDLPPR VFECRLALVQ
PSSMVHGNYS WPTAANDLLQ FVAKCGRIDI EVYSLFNNVA AVLIHMRNGT INDKLVAQKL
CRRSDEDYMS RKDHDFRLRS QESGRYLSSA ERQQINEEYL RSCQLPQDFD LPPPPQDLCG
TNVRLKGPYS PLECSMQSII RVGSSKRVNI DSASVNAVLL DTDPQDHHDH LIVAHATVES
PNGQTLTARG TTLMPNVQGY GALMVMLFCP TMQLKCNEEG TSYVSILAGL GCDPVTGEPY
YAEHDVLINL DVNILEDDLV LINQIRYYID SVFFNFKEEN YPAVSVNERE SIYTQLRSLI
KRLLSKDRSY IGKNMSNSDF VWETNPELPM PNEPFGKRAI FPMHSLTELK EDDMGRLMNL
RENCSMLHKW RNFEGTLPHM TCKLCNQLLE SVPQLRLHLL TILHRDREKQ IDFCNQ
