SPNE_DROGR
ID SPNE_DROGR Reviewed; 1434 AA.
AC B4JT42;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=GH23451;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00;
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; CH916373; EDV94932.1; -; Genomic_DNA.
DR RefSeq; XP_001994196.1; XM_001994160.1.
DR AlphaFoldDB; B4JT42; -.
DR SMR; B4JT42; -.
DR STRING; 7222.FBpp0157357; -.
DR PRIDE; B4JT42; -.
DR EnsemblMetazoa; FBtr0158865; FBpp0157357; FBgn0130908.
DR GeneID; 6567215; -.
DR KEGG; dgr:6567215; -.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_002601_1_0_1; -.
DR InParanoid; B4JT42; -.
DR OMA; DPCRTVY; -.
DR OrthoDB; 278674at2759; -.
DR PhylomeDB; B4JT42; -.
DR Proteomes; UP000001070; 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 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 SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 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_0000391915"
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 938..1001
FT /note="Tudor"
FT REGION 66..86
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 1434 AA; 164881 MW; CF07CB2D44702AD9 CRC64;
MDDLMDFFDS SKNFKRGTLP RGCISGDPNA YTSESSDSKP IKREIIGTKD VNEIVQKEQQ
LMNQLVGGPS NTKRTKTLDE LESDDDDKME LNEAPTVRSD EAFYEKYHFD LNRNRSLPIY
AQREQIMKAI KENPVVILKG ETGCGKTTQV PQYILDEAFK KREFCNIVVT QPRRIAAISI
ANRVCQERRW QPGTVCSYQV GLHKQSNSAD TRLLYCTTGV LLNNLIRLKT LTHYTHIVLD
EVHDRDQDMD FLLIVVRRLL ALNSRHVKVI LMSATIDTRE FCKYFASCKS MPPVVAASHG
RKYPLVKYYR DQLKNINWKT EPQQREPGIT HEGYRDAVKI LLVIDNMERK AEGQSEQSYE
EAKRTGSVLI FLPGVNEIDT MAEHIEHVMN ESPNIKITIV RCHSLMSSDS QEDVFQPPLS
GHRKVILTTN IAESSITVTD VSYVIDFCLA KVMHIDTASN FSCLCLEWAS KVNCRQRAGR
VGRTRSGRVY RMVTKAFYME EMQEFGIPEM LRSPLQSSVL KAKELDMGGP SEILALAMSP
PNLTDIHNTV LLLKEVGALY TTVDGVYEQL DGDLTYWGTI MSRFPLDVRL SRLIILGYIF
NCLDEAIIIA AGMSVRSLYL SGQRQRTSDA FWMHYIFADG SGSDLVGFWR VYKIYVNMCQ
NLPMKDSEVQ WARRYNVSLR SLKEMYLLVQ ELQKRCAALN LVSLPVGASH MWHDREKSII
LKVIIAGAFY PNYFTRNNKT IPDYDRDVYH SICGNDPCRT VYFTQFVPRY MGELYTRRVK
ELFLEARIPP EKIDVTFQQG SEKIFVTFKG DDDDYMNSTD VVQVPGRVTT EVYKAIRMRM
NNPNRSLRVM DQNSALKYVQ QRNIGVVQDS KWVPPSKQWN VELLTLPSVF DKKITGLITY
IVNCGKFYFQ PRSLAERIAS MTEIFNAPEQ LSYHVRNASA ITKGLQLLAR RGSKFQRAVV
LKVEPQSNAI PQFLVRFIDY GDWALLAMDQ LRLMRHELRR DLEELPPRMF ECRLALVQPS
SVTSYSNRWP QKANEMLSKL ASCGPLELEV YSLVNNVAAV LIHMRDGVLN DKLVEHQLAR
RADEDYMSRK DHDFRIRKQK MKRYVPAAEQ QQVNEEYLRF NQLPQDADLE PPPLDKCHTS
IRLKGPYSPL ENSMNSMLRI GMYKSVAIEK ESVNAVLLDA DPQDRHDQMI VAASVTESDG
NDKLVARGTT LMPNIHGFGA LMAMLFCPTM QIKCNPERTK YVCLLAGLGF NPDTLEPYFQ
EHDMVINLDV GILKDDIRII NQMRYNIDSM FFNFDANELP AVGVEGRLVI FNQLRNLLTR
LLGKDRSFIE RHVWNSKYVW EDMSDLEPPS EPYGKRAIFP MHGSYDLESE DMGNLLALQE
NCSELYDWQN FDGVMQPRNC RLCNETLESV TQLRLHLLTQ LHRDREKQVG WKQQ
