SPNE_DROSE
ID SPNE_DROSE Reviewed; 1434 AA.
AC B4HLH4;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=GM24265;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25;
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; CH480815; EDW41994.1; -; Genomic_DNA.
DR RefSeq; XP_002031008.1; XM_002030972.1.
DR AlphaFoldDB; B4HLH4; -.
DR SMR; B4HLH4; -.
DR STRING; 7238.B4HLH4; -.
DR PRIDE; B4HLH4; -.
DR EnsemblMetazoa; FBtr0207250; FBpp0205742; FBgn0179129.
DR GeneID; 6606200; -.
DR KEGG; dse:6606200; -.
DR HOGENOM; CLU_002601_1_0_1; -.
DR OMA; DPCRTVY; -.
DR PhylomeDB; B4HLH4; -.
DR Proteomes; UP000001292; 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..1434
FT /note="Probable ATP-dependent RNA helicase spindle-E"
FT /id="PRO_0000391920"
FT DOMAIN 125..292
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 339..526
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 938..1001
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT MOTIF 238..241
FT /note="DEAH box"
FT BINDING 138..145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1434 AA; 164578 MW; 1A220F676C1EAE23 CRC64;
MDQEVMDFFD FSKELNRVPG APQGYISSDP WLMATESKSS EVPNRETIGT DYVTKIVAKE
KCRLNRTLLE YQPQGKRNRT LDDLDTDDEA EETEIRRDDE YYKKFRFNLN RDKNLSIYAK
REEILAAINA HPVIIIKGET GCGKTTQVPQ YILDEAYKSG KYCNIVVTQP RRIAAISIAN
RVCQEREWQQ NTVCSFQVGL HRPNSLEDTR LLYCTTGVLL NNLINNKTLT HYTHIVLDEV
HERDQNMDFL LIVVRRLLAT NSRHVKIILM SATIDAKELS DYFATTNSIP PVITTNHGRK
HSIEKFYRDQ LGSIIWNEED VGDQHVPEIN KHGYRAAVKI IVIIDNMERK AAIQSRLSYD
ETLRYGAVLI FLPGIYEIDT MAENITCMLE NDRNIKVLIV RCFSLMTPEN QRDVFNPPPP
GFRKIILATN IAESSITVPD VSYVIDFCLT KVKVTDTASS FSSLRLTWAS KANCRQRAGR
VGRLRSGRVY RMVNKHFYQR EMAEFGIPEM LRLPLQNSVL KAKVLNMGSP MEILALALSP
PNLSDIQNTI LLLKEVGALY LTVDGVYDAL DGDLTYWGTI MARLPLDTRQ SRLIILGYIF
NMLEEAIIIA AGLSTNGLFA HDGGRTQLGD SFWMHYIFAD GSGSDLVAIW RVYLTYLSLV
EIGHDQESAI RWAKRFHVSL RSLKEIHLLV QELRVRCMHL GLIPFSVNPS QMMDDREKAI
MLKVIIAGAF YPNYFTRSKD TCADTDRNIY QTISGHDPCR TVYFTNFKPA YMGELYTRRI
KELFQEVRIP PENMDVTFQE GSQKVFVTFK QDDWIADSSK FVPVSGRVQS EVYKAVMMRQ
NRLERPIHIM NPSAFMSYVQ QRGIGDVIEG RWIPPTKPLN VELLALPSVF DKTISGLITC
IVSCGKFFFQ PQSFAECIGN MSEIFNAPQQ LRNYVNNAGD ITKGMMVLAK RDSYFQRATV
IRPENQSNRQ PMFYVRFIDY GDCALLSMQQ MRLMPRELTE QYGDLPPRVF ECRLAMVQPS
SMVSGNNRWS TAANDMLRSV AKSGLIDIEV YSLFNNVAAV LIYMRDGIIN DKLVELMLCR
RSDEDYMSRK DHDFRLRRQE SARYLSSAQR QQINEEYMRS CQLPEDHDLR PPPPEKCKTV
VILKGPYSPL ECTMQCITRV GSSKRVNIDH LSVNALLLDA DPQDHHDHLI VAHEIAENRN
GHTLTARGTT LMPNVQGFGA LMVMLFSPTM QLKCNREGTS YVSVLGGLGC DPETNEPYFP
EHDVLINLDV NILEDDVILI NQIRYYIDSV FFNFKDENNP AVSANERVSI YTQLRSIINR
LLCKDRRYIE RNMSNADFEW ETHPDLPPPN EPFGKRAIFP MHSLTELQEE DTGRLVQLRE
NCSMLHKWRN VEGTLPHMTC KLCNQLLDSV PQLRLHLLTI LHRDREKQID YCNQ
