GenomeNet

Database: UniProt
Entry: B3P3W1
LinkDB: B3P3W1
Original site: B3P3W1 
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   18-SEP-2019, entry version 60.
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;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; 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
CC       role during spermatogenesis and oogenesis by repressing
CC       transposable elements and preventing their mobilization, which is
CC       essential for the germline integrity. Acts via the piRNA metabolic
CC       process, which mediates the repression of transposable elements
CC       during meiosis by forming complexes composed of piRNAs and Piwi
CC       and govern the methylation and subsequent repression of
CC       transposons. Involved in the repression of LTR retrotransposon
CC       copia. Also involved in telomere regulation by repressing
CC       specialized telomeric retroelements HeT-A, TAHRE, and TART;
CC       Drosophila telomeres being maintained by transposition of
CC       specialized telomeric retroelements. Involved in telomeric trans-
CC       silencing, a repression mechanism by which a transposon or a
CC       transgene inserted in subtelomeric heterochromatin has the
CC       capacity to repress in trans in the female germline, a homologous
CC       transposon, or transgene located in euchromatin. Involved in the
CC       repression of testis-expressed Stellate genes by the homologous
CC       Su(Ste) repeats. Required for anteroposterior and dorsoventral
CC       axis formation during oogenesis (By 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
CC       the nuage, also named P granule, a germ-cell-specific organelle
CC       required to repress transposon during meiosis. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. {ECO:0000305}.
DR   EMBL; CH954181; EDV49067.1; -; Genomic_DNA.
DR   RefSeq; XP_001980109.1; XM_001980073.2.
DR   SMR; B3P3W1; -.
DR   STRING; 7220.FBpp0135504; -.
DR   PRIDE; B3P3W1; -.
DR   EnsemblMetazoa; FBtr0137012; FBpp0135504; FBgn0109186.
DR   GeneID; 6553090; -.
DR   KEGG; der:6553090; -.
DR   KO; K18408; -.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006342; P:chromatin silencing; IEA:EnsemblMetazoa.
DR   GO; GO:0046843; P:dorsal appendage formation; IEA:EnsemblMetazoa.
DR   GO; GO:0007294; P:germarium-derived oocyte fate determination; 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: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   GO; GO:0030423; P:targeting of mRNA for destruction involved in RNA interference; IEA:EnsemblMetazoa.
DR   Gene3D; 2.40.50.90; -; 1.
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; Complete proteome; Cytoplasm; Developmental protein;
KW   Differentiation; Helicase; Hydrolase; Meiosis; Nucleotide-binding;
KW   Oogenesis; RNA-mediated gene silencing; Spermatogenesis.
FT   CHAIN         1   1432       Probable ATP-dependent RNA helicase
FT                                spindle-E.
FT                                /FTId=PRO_0000391914.
FT   DOMAIN      124    291       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      337    524       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      936    999       Tudor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00211}.
FT   NP_BIND     137    144       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       237    240       DEAH box.
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
//
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