SPNE_DROPS
ID SPNE_DROPS Reviewed; 1433 AA.
AC Q296Q5;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 94.
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=GA16329;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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; CM000070; EAL28403.2; -; Genomic_DNA.
DR RefSeq; XP_001359258.2; XM_001359221.3.
DR AlphaFoldDB; Q296Q5; -.
DR SMR; Q296Q5; -.
DR STRING; 7237.FBpp0284335; -.
DR PRIDE; Q296Q5; -.
DR EnsemblMetazoa; FBtr0285897; FBpp0284335; FBgn0076345.
DR GeneID; 4802318; -.
DR KEGG; dpo:Dpse_GA16329; -.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_002601_1_0_1; -.
DR InParanoid; Q296Q5; -.
DR OMA; DPCRTVY; -.
DR Proteomes; UP000001819; Chromosome 2.
DR Bgee; FBgn0076345; Expressed in female reproductive system and 3 other tissues.
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..1433
FT /note="Probable ATP-dependent RNA helicase spindle-E"
FT /id="PRO_0000391919"
FT DOMAIN 126..294
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 355..526
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 935..998
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT MOTIF 240..243
FT /note="DEAH box"
FT BINDING 139..146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1433 AA; 164469 MW; B29FBEF73448C369 CRC64;
MDQELMDFFD FSKEFVRKQA PRGHVSSNVH AFVTESEELE KPIKREIVGK DYVKSFVEKE
KERMNGIFSS DEMAPMRNKS LDDMDSDEEY EASPEIRTDA EFYEKYYFNL NRDKSLPIYA
KREEIINAIN ENPVVIVKGE TGCGKTTQVP QYILDEGFKS KQYCNIVVTQ PRRIAAISIA
NRVCQERQWQ RGTVCGYQVG LHRQLERFAD TRLLYCTTGV LLNILVNNKT LTHYTHIVLD
EVHERGQEMD FLLIVIRRLL ATNSRHVKVI LMSATINPRE LSDYFANERS APPVIDASYG
RNFTVEKYYR DQLQTINWEG HQEDINSPGI TQEGYRSAIK TILVIDNMER NERSTGKSYN
QSLREGSILI FLPGVGEINN MSDMLKDMAN HDSIMKFNMV RCHSLMSSDD QREIFQPSPP
GYRKIIMATN VAESSITVPD VSYIIDFCLE KVLFTDTFTN FSSLRLVWAS KTNCRQRAGR
VGRLRNGRVY RMVTKSFYQR ELSEYSVPEM LRSPLQNCVL KAKELKMGTP VEMLALALSP
PNLSDICNTI LLLKEVGALF PTVDGTYDPC DGDITYWGTI MSKLPLDTRL SRLIILGYIF
NLLDEAIIIA AGLTVRGIFV DSTRLGSDNY WMHYVFADGS GSDLVGIWRV YLTYLNMCEN
GLQKDASIQW AKRFHLSLRA LSEMNLLVLD LRLRCEKLSL LPLNFPISRI SDDSEKAIML
KVIIAGSFYP NYFVQSKSTS GDDRNMFSVI SGLDPCRTVY FTSFTDRTMG ELYTRKVKQL
FPETQIPPEN MDVTFGQGSE KIFVTFKNDI YKPEGTTYVH VPGRIKAEVY KALRLRTYCN
HHSLRVMEPM SALKYVKDKK IGKVVEGRWI PPSKPVAVEL LALPSVFDKI IVGRITNIVS
CGKFFFQPES FENCIANMSE HFNNPQQLQN CVRNAGAITK GLMLLAKRQG KYQRATVVRV
DTQNSSNVRF YVRFVDYGDI ERLPMTQLRL MSQDLLRHYR DLPPRLFECR LALVQPASMV
STYNAWPQKA DDMLHALAKG GRVQLEIYSL VQNVAAVMIH LREGNLNELL VKEKLARRTN
EDYMSRVDHD FRMRKQECRG YVSQQERQQV NEEYLRSKQL PQDMDLSPPP PQECKSLIIL
KGPFSTLEST VFSTMQSGMS KTVRIDPCSV NFVLLDTEPQ DQHAKMVVAA SISSAGRHND
VLTLRSTSIM PNIPGFAAIM TLIFCPRAQL NANTANSRYV SILAGLGYHP QTMKSYYEDH
DLVINLDVNI DEHDVLLINQ IRYMMDSVFF NLEGELRPIA GHADRVLIHD TIYRALNRLL
SKNRNFIVCN PKSSDYVWQD MEESGEPDPQ PYGRRSIFPM HTIPELHEEN MDTVLDLIAN
CKEMYDYRNF EGSFDPMTCR LCKQYLESVS ELRLHLLTQL HLDREKEVGY PMD
