SPNE_DROVI
ID SPNE_DROVI Reviewed; 1433 AA.
AC B4LX81;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=GJ23765;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87;
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; CH940650; EDW66733.1; -; Genomic_DNA.
DR RefSeq; XP_002053213.1; XM_002053177.2.
DR AlphaFoldDB; B4LX81; -.
DR SMR; B4LX81; -.
DR STRING; 7244.FBpp0238182; -.
DR EnsemblMetazoa; FBtr0239690; FBpp0238182; FBgn0210862.
DR GeneID; 6631068; -.
DR KEGG; dvi:6631068; -.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_002601_1_0_1; -.
DR InParanoid; B4LX81; -.
DR OMA; DPCRTVY; -.
DR OrthoDB; 278674at2759; -.
DR PhylomeDB; B4LX81; -.
DR Proteomes; UP000008792; 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..1433
FT /note="Probable ATP-dependent RNA helicase spindle-E"
FT /id="PRO_0000391921"
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 REGION 76..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 1433 AA; 165312 MW; 24ADB3A8D883F841 CRC64;
MDSDLMDFFD FSKQFKRGTA LKGCITGDPN ALTTESRDSK PIKREKIGTD YVNEIVEKEK
QLMNKLVDGQ SVAKRNRTLD ELDSDDEEEN MQEQPSVRSD EAYYEKYRFD LNRNKNLPIY
AQREQIMKAI RENPVVILKG ETGCGKTTQV PQYILDEACK RREFCNIVVT QPRRIAAISI
ANRVCQERQW QPGTVCSYQV GLHRQSNVED TRLLYCTTGV LLNNLIRLKT LTHYTHIVLD
EVHERDQDMD FLLIVVRRLL ALNSRHVKVI LMSATIDTRE FSKYFATSSA FPPVVTASHG
RKYPLVKYYR DQLKNIHWKD EPQERAPGIG PEGYADAIKI LLVIDNMERK AVGQSLQSYE
EAKRTGSVLI FLPGINEIDT MADHITSVME ENPTMIITIV RCHSLMSPDS QEEVFQPPLP
GHRKIILTTN IAESSITVPD VSYVIDFCLT KVLHTDTATN YSCLRLEWAS KVNCRQRAGR
VGRLRSGRVY RMVSKAFYLE EMKEFGIPEM LRSPLQNSVL KAKELEMGRP SEILALAMSP
PNLSDIQNTV LLLKEVGALY TTVDGVYEEL DGDLTYWGTI MSRFPLDVRL SRLIILGYVF
NCLEEVIVIA AGMTVRSLYL TGKRRQVNDA FWMHYIFADG SGSDMVAIWR VYRIYLNMCQ
DRMLKESAEQ WARRFNVNLR SLKEMHLMVQ ELRQRCASVN LQPLPYGTCQ MWDDREKSII
LKVIIAGAFY PNYFMRSNKS NADYDRSLFQ SICGNDPCRT VFFTHYEPRY MGELYTRRIK
ELFLEVKIPP ENMDVTFLHG SEKVFVTFKS DDEDMDTAKV VQVPGRVMTE VYKAVRMRLE
NQNRPLRVMD QNSALRYVQD RKIGVVTEGT WFPPSNQWNV ELLTLPSVFA KNITGLVTYI
VSCGKFYFQP RALAESIASM SEIFNGPQQL SCHVRNASAV TKGLQLLAKR GHLFQRAVVL
RIETQTNGHP RFRVRFIDYG DMAVLPMDQL RLMPHELKRD FDQLPPRMFE CRLALVQPSM
VTSSYNRWPK AANDMLISVA QCGRLELEVY SLVNNVAAVL IHMRDGVLND RLVERQLARR
ADEDYMSRKD HDLRIRKQEA KRNISVAEQE RINEEYLRFA QLPKDMDLEP PPLDKCNLSI
RLRGPFSPLE SSMNSMLRIG MYKSVTIDKD SVNAVLLDTD PQDRHDQMVV AASVTETDNT
ERLTARGTTL MPNIHGFGAL MAMLFCPTMQ IKCNKDRTKY VCLLAGLGFD PETLEPYFAE
HDMVINLDVT ILRDDIRIIN QMRYNIDSMF YNFDANEMPS VGTEDRVVIF NQLRSLLTRL
LGKDRSFIER HVSNSEYLWE DMSDLEPPSE PYGKRAIFPM HSSYDLENDN LSNLLELQAN
CKQLYDWRNF EGNLQTQVCR LCNESLESVA ELRLHLLTQL HRDREKQVGY KQQ
