GenomeNet

Database: UniProt
Entry: B3M383
LinkDB: B3M383
Original site: B3M383 
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   31-JUL-2019, entry version 62.
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;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; 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
CC       role during spermatogenesis and oogenesis by repressing
CC       transposable elements and preventing their mobilization, which is
CC       essential for the germline integrity. Acts via the piRNA metabolic
CC       process, which mediates the repression of transposable elements
CC       during meiosis by forming complexes composed of piRNAs and Piwi
CC       and govern the methylation and subsequent repression of
CC       transposons. Involved in the repression of LTR retrotransposon
CC       copia. Also involved in telomere regulation by repressing
CC       specialized telomeric retroelements HeT-A, TAHRE, and TART;
CC       Drosophila telomeres being maintained by transposition of
CC       specialized telomeric retroelements. Involved in telomeric trans-
CC       silencing, a repression mechanism by which a transposon or a
CC       transgene inserted in subtelomeric heterochromatin has the
CC       capacity to repress in trans in the female germline, a homologous
CC       transposon, or transgene located in euchromatin. Involved in the
CC       repression of testis-expressed Stellate genes by the homologous
CC       Su(Ste) repeats. Required for anteroposterior and dorsoventral
CC       axis formation during oogenesis (By 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
CC       the nuage, also named P granule, a germ-cell-specific organelle
CC       required to repress transposon during meiosis. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. {ECO:0000305}.
DR   EMBL; CH902617; EDV43544.1; -; Genomic_DNA.
DR   RefSeq; XP_001954983.2; XM_001954947.2.
DR   SMR; B3M383; -.
DR   STRING; 7217.FBpp0121739; -.
DR   GeneID; 6501320; -.
DR   KEGG; dan:Dana_GF18547; -.
DR   FlyBase; FBgn0095565; Dana\GF18547.
DR   eggNOG; KOG0920; Eukaryota.
DR   eggNOG; COG1643; LUCA.
DR   InParanoid; B3M383; -.
DR   KO; K18408; -.
DR   OMA; DPCRTVY; -.
DR   OrthoDB; 278674at2759; -.
DR   PhylomeDB; B3M383; -.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   Bgee; FBgn0095565; Expressed in 1 organ(s), highest expression level in adult organism.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0007275; P:multicellular organism development; 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   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; Complete proteome; Cytoplasm; Developmental protein;
KW   Differentiation; Helicase; Hydrolase; Meiosis; Nucleotide-binding;
KW   Oogenesis; Reference proteome; RNA-mediated gene silencing;
KW   Spermatogenesis.
FT   CHAIN         1   1429       Probable ATP-dependent RNA helicase
FT                                spindle-E.
FT                                /FTId=PRO_0000391913.
FT   DOMAIN      121    288       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      349    521       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      933    996       Tudor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00211}.
FT   NP_BIND     134    141       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       234    237       DEAH box.
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
//
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