DDX4_PELLE
ID DDX4_PELLE Reviewed; 724 AA.
AC Q3MSQ8;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX4;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q61496};
DE AltName: Full=DEAD box protein 4;
DE AltName: Full=Vasa homolog;
GN Name=ddx4 {ECO:0000250|UniProtKB:Q64060};
GN Synonyms=vlg {ECO:0000312|EMBL:CAH56439.1};
OS Pelophylax lessonae (Pool frog) (Rana lessonae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX NCBI_TaxID=45623;
RN [1] {ECO:0000312|EMBL:CAH56439.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:CAH56439.1};
RA Marracci S., Casola C., Ragghianti M., Bucci S., Ogielska M., Mancino G.;
RT "Characterization of vasa-like genes in the hybridogenetic Rana esculenta
RT complex.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable ATP-dependent RNA helicase required during
CC spermatogenesis to repress transposable elements and preventing their
CC mobilization, which is essential for the germline integrity. Acts via
CC the piRNA metabolic process, which mediates the repression of
CC transposable elements during meiosis by forming complexes composed of
CC piRNAs and Piwi proteins and governs the methylation and subsequent
CC repression of transposons. Involved in the secondary piRNAs metabolic
CC process, the production of piRNAs in fetal male germ cells through a
CC ping-pong amplification cycle. {ECO:0000250|UniProtKB:Q61496}.
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 Evidence={ECO:0000250|UniProtKB:Q61496};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q61496}.
CC Note=Component of the meiotic nuage, also named P granule, a germ-cell-
CC specific organelle required to repress transposon activity during
CC meiosis. {ECO:0000250|UniProtKB:Q61496}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX4/VASA
CC subfamily. {ECO:0000250|UniProtKB:Q64060}.
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DR EMBL; AJ841700; CAH56439.1; -; mRNA.
DR AlphaFoldDB; Q3MSQ8; -.
DR SMR; Q3MSQ8; -.
DR PRIDE; Q3MSQ8; -.
DR GO; GO:0071546; C:pi-body; ISS:UniProtKB.
DR GO; GO:0071547; C:piP-body; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0007141; P:male meiosis I; ISS:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:0010529; P:negative regulation of transposition; ISS:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:1990511; P:piRNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Developmental protein; Differentiation; Helicase;
KW Hydrolase; Meiosis; Nucleotide-binding; Oogenesis; Repeat;
KW RNA-mediated gene silencing; Spermatogenesis.
FT CHAIN 1..724
FT /note="Probable ATP-dependent RNA helicase DDX4"
FT /id="PRO_0000248852"
FT DOMAIN 317..500
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 512..675
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 286..314
FT /note="Q motif"
FT MOTIF 444..447
FT /note="DEAD box"
FT /evidence="ECO:0000250|UniProtKB:Q61496"
FT COMPBIAS 37..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 330..337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 724 AA; 79780 MW; 99DF0C59155F512C CRC64;
MSGQEDWESE IDNPPACVPN LSNSEPAFKA SNQNYFSSNN AFNRTTERGF GNRKASDDCN
QNFEFSERGF GKQRAGSDAN QNFESSERGF GNRRGKGRGG FGTFGKDSNG KQESGDFTND
DNRTIDDNRR RGGFQRRGGF NDETSGRGRR GVRGGTSFSG FGREDGNEQS GFTSNDGFNN
ETSGFGSGRR GSRGDSSFSG DRESDRGRGF GRGGFRGRNE DIGVESGKGQ EGFERSEQGP
RVTYIPPPPP AEESDIFKHY QTGINFDKYD DIVVEVSGSD VPPAILTFEE ANLCDSLAKN
VCKSGYVKLT PIQKHSIPII VAGRDLMACA QTGSGKTAAF LLPILAHLMV KGVESSAFQT
LKEPEAIIVA PTRELINQIY LDARKFSYGT CVRPVVIYGG TQMFHSLKQI SEGCNILCAT
PGRLLDVIRK EKIGLTKLRY LVLDEADRML DMGFREDIEN LLKSSGMPSK EERQTLMFSA
TFPSSIQSLA REILKPDYLF VVVGQVGGAC SDVEQMVIEV DEFGKKDKLM EILQEIGSER
TMVFVKTKKK ADFIATFLCQ EKVPSTSIHG DREQKERETA LRDFRTGQCP VIVATSVAAR
GLDIENVSYV INFDIPDDID EYVHRIGRTG RCGNTGRAIS FFDKRGDDEQ RIARSLVKVL
SDAHQEVPAW LEEVAFSAHG SSAYNPRSNK FASTDDRKRG DSRGDYSTSG FSPSAAQAEE
EDWG
