SPNE_DROAN
ID SPNE_DROAN Reviewed; 1429 AA.
AC B3M383;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=GF18547;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13;
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; CH902617; EDV43544.1; -; Genomic_DNA.
DR RefSeq; XP_001954983.2; XM_001954947.2.
DR AlphaFoldDB; B3M383; -.
DR SMR; B3M383; -.
DR STRING; 7217.FBpp0121739; -.
DR EnsemblMetazoa; FBtr0123247; FBpp0121739; FBgn0095565.
DR GeneID; 6501320; -.
DR KEGG; dan:6501320; -.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_002601_1_0_1; -.
DR InParanoid; B3M383; -.
DR OMA; DPCRTVY; -.
DR OrthoDB; 278674at2759; -.
DR PhylomeDB; B3M383; -.
DR Proteomes; UP000007801; 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; Reference proteome;
KW RNA-mediated gene silencing; Spermatogenesis.
FT CHAIN 1..1429
FT /note="Probable ATP-dependent RNA helicase spindle-E"
FT /id="PRO_0000391913"
FT DOMAIN 121..288
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 349..521
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 933..996
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT MOTIF 234..237
FT /note="DEAH box"
FT BINDING 134..141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1429 AA; 164179 MW; 11EC2DA83952B48D CRC64;
MDFFDFTKDF RREEAPSGFI SSDPSSMATE MFESKPIKRE VIGTDYVAEI AAKEKLLMSG
QLKAEIPGQY SGGMDDLDSN DDMDDEEISK IRLDEEYYKK YRFNLNRDKN LPIYAKREVI
VNAINTHQVV ILKGETGCGK TTQVPQYILD EGFKSGQYCN IVVTQPRRIG AISIANRVSQ
ERMWEPDTVC SYQVGLHRKQ HLEDTRLLYC TTGVLLNSLI RNKTLTHYTH IVLDEVHERD
QDMDFLLIVV RRLLATNSRH VKVILMSATI DTREFCDYFS TKVSVPPVIS ASHGRKHSIE
KFYRDQLGSI NWKDDPDDGY QARIPDEAYK AAVKIILVVD NMERQAANQS EQSYDDAKSQ
GAVLIFLPGI YEIDNMAESL GNMTKEEPSM KLFIVRCFSL MTPDAQRDVF SPPPSGFRKI
ILATNIAESS ITVPDVSYVI DFCLTKVLVT DTATNFSSLR LTWASKANCR QRAGRVGRLR
SGRVYRMVHK LFYKTNMTEF GVPEMLRLPL QNSVLKAKLL DIAPPIEMLA LALSPPNLSD
IQNTILLLKE VGALFPTVDG EYCEVDGDIT FWGIIMSRLP LDTRLSRLII LGYVFNLLEE
AIVIAAGLSM RGLSTEAGRG RLTSDAYWMN YVFADGSGSD LVAIWRIYRT YENMVANGMH
QESAEPWARR YHVSLRALKE MHLLVQELKS RCSQLGMISF NLSSSDMPDD LEKAILLKVI
IAGAFYPNYF LRSKKTTLEQ ERDIFHVISG RDPCRTVYFT NFKPAYMGEL YTRRIKDLFQ
ELKIPPESIE VTFQPGSQKV FVTFKSDECD TNCTRLINVP GQVLTEVYKS IRMRLYQSNR
TFRVMDHNNA LNYVQRHGIG TLKEGHWTPP SRPLNVEMLA LPSVYEKNMT GLITHVDHCG
KFFFQPKSFA RCIQNMSEII NTPMHLQYEI QNAGVLTKGM MVLAKRKGTF ERAIIVRPET
QNNRQPKFFV RFVDYGNTDL MYIEQLRLMT KELLSQYGDL PPRVFECRLA LVQPSTMSNT
LSRWSRDAKD MLISASKNNI VEIEIYSLVY NVAAVMVHTR DGLLNDKLVE HNLARRADEN
FMSRQDHDFR IRKQESARYI SGPERQQVNE EYLRSCQMPE DLDLTPPPLD KCNMIVMLKG
PYSPLETSMF STIRVGVWKT VKIDNSSVNA VLLDSDPQDN HDQLVVSHST VESSNGDVLT
ARGTTLMPNI HGFGPLMTML FCPTMQIKCN KDCTKYVSIL AGLGFDKETM KPYFEEHDMV
MNLDVNLYED DVRMINQMRY NIDTMFFNFE GEELPSLNMN DRVTIYKELR KLVNRLLSKD
RSYIELNASN SDFNWEKEDR IEPQPEPFGK RCIFPMHVIP ELLEEDIGRR LYLIDNCKKL
YKWRNFEGAL DILNCKLCNM SLETTPQLRL HLLTQLHRDR EKQIGFKNE
