TDRD9_DANRE
ID TDRD9_DANRE Reviewed; 1342 AA.
AC B8A4F4; B5A7D9;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=ATP-dependent RNA helicase TDRD9 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q14BI7};
DE AltName: Full=Tudor domain-containing protein 9 {ECO:0000305};
GN Name=tdrd9 {ECO:0000250|UniProtKB:Q14BI7}; ORFNames=si:dkey-15f17.9;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AB;
RA Honda J., Beh L., Wong Q.Y., Orban L., Kai T.;
RT "Expression and localization of zebrafish spindle-E.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: ATP-binding RNA helicase which plays a central role during
CC spermatogenesis by repressing transposable elements and preventing
CC their mobilization, which is essential for the germline integrity. Acts
CC via 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. Acts downstream of piRNA biogenesis:
CC exclusively required for transposon silencing in the nucleus,
CC suggesting that it acts as a nuclear effector in the nucleus together
CC with piwil4. {ECO:0000250|UniProtKB:Q14BI7}.
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:Q14BI7};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14BI7}. Nucleus
CC {ECO:0000250|UniProtKB:Q14BI7}. Note=Component of the nuage, also named
CC P granule, a germ-cell-specific organelle required to repress
CC transposon activity during meiosis. Specifically localizes to piP-
CC bodies, a subset of the nuage which contains secondary piRNAs. PIWIL2
CC is required for its localization to piP-bodies.
CC {ECO:0000250|UniProtKB:Q14BI7}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; EU817488; ACF35262.1; -; mRNA.
DR EMBL; BX072537; CAX14617.1; -; Genomic_DNA.
DR RefSeq; NP_001123984.1; NM_001130512.1.
DR AlphaFoldDB; B8A4F4; -.
DR SMR; B8A4F4; -.
DR IntAct; B8A4F4; 2.
DR MINT; B8A4F4; -.
DR STRING; 7955.ENSDARP00000104975; -.
DR PaxDb; B8A4F4; -.
DR PeptideAtlas; B8A4F4; -.
DR Ensembl; ENSDART00000019202; ENSDARP00000011360; ENSDARG00000013453.
DR GeneID; 553222; -.
DR KEGG; dre:553222; -.
DR CTD; 122402; -.
DR ZFIN; ZDB-GENE-090313-193; tdrd9.
DR eggNOG; KOG0920; Eukaryota.
DR GeneTree; ENSGT00940000157035; -.
DR InParanoid; B8A4F4; -.
DR OMA; DPCRTVY; -.
DR OrthoDB; 278674at2759; -.
DR PhylomeDB; B8A4F4; -.
DR PRO; PR:B8A4F4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 13.
DR Bgee; ENSDARG00000013453; Expressed in testis and 13 other tissues.
DR GO; GO:0005634; C:nucleus; 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:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0009566; P:fertilization; 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:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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 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; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50304; TUDOR; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Developmental protein; Differentiation; Helicase;
KW Hydrolase; Meiosis; Nucleotide-binding; Nucleus; Reference proteome;
KW RNA-mediated gene silencing; Spermatogenesis.
FT CHAIN 1..1342
FT /note="ATP-dependent RNA helicase TDRD9"
FT /id="PRO_0000391909"
FT DOMAIN 99..265
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 317..503
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 901..962
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 31..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 211..214
FT /note="DEAH box"
FT /evidence="ECO:0000250|UniProtKB:Q14BI7"
FT COMPBIAS 31..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 151
FT /note="S -> G (in Ref. 1; ACF35262)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1342 AA; 150811 MW; 81DEAD7A788CDC97 CRC64;
MHQAITSAQI AHWFTVGAQF ANIRITNEAK KAEAEDNATE VRSDKAFSEL SSPEKEKSDD
GNQRRKRAQL PTGPGTSPPS LASYEYPILP ITKNRQELVS LIENNSVVII RGATGSGKTT
QLPQFILDHY AERNIPCNLV VTQPRKIGAT SIARWVARER KCTLGSLVGY QVGLEKMATE
HTKLIYVTTG VLLQKLVSSK TLTEYSHIFI DEVHERSEEL DFLLLVVRKL LRSNSRYVKV
ILMSATINCI EFAEYFGSPI RNQMNPAYVF EVEGAPYAVE EYYLDELKTM LPVGVNLDLT
LPQDPYITEE MYNVAVSLIQ SFDEMEAKDH RRSEQTGSTT HPERGSVLVF LPGLAEIQYM
KEALSKLVRK RLQVYPLHST VTLEEQNGVF LVPVPGYRKI ILSTNIAESS VTVPDVKYVI
DFCLVRQLAC DKETNYRCLR ITWASKTSCN QRRGRAGRVS KGFCYRLVTR HFWENEIPNF
SIPEMLRSPL ASTLLKVKLL DMGDPRSVLS TALTPPILGD IERTVLQLKQ IGALSVQSNS
QRQFDGDLTF LGRVLAQLPV DLQLGKLIVL GHVFGCLEEC LIIAASLSLK SFFAMPSLQQ
LAGYRSKLSF AQNVPSDFIA YVNAFKAWYT SRAKGELRHP KDELEWGKEN CIQIKRIREV
AELFEDLKKR VSRFNMHISS SSNPTDYTSL HKQRFILQVV IAGALFPNYF SQGEIDEQLA
SKELSGNDPK TTILIRNLPP FAFLCYKQLQ SLFRQCGQVK SIAFDGSRAY VEFHRSCVRE
SGVLHEVLLA LLRSRHTPAL HLQVHHADEV EFHAKGKPIA HLRYTRVNVD VQSHTVSPVG
VLSSSVNPEK LPTSRDFVIN ITEVIDVGHF WGFQTDENSV EKQCQLTAAL NMRDLRPLSV
SLYPNLLCVA PFKDGQQMAK YYRAKVLHIL GSNVEVFFVD FGNTTVVPSS SLRELPSDLM
TPAFQAQEFC IARMAPSAQS LILGDRWSSR ARNRFKTLTS GRSAIVSLFS ILHGVMRVDL
HISTETGDVS VADLLVQEGH ACHTPESFES QQSHEVLISL YEDMASGRFT PSFASGSLNS
RMEEDKQLIN QLLLHFCSSG SSAPKCKAVV HGPSSPHKVN FHSMSKVSNF RSVNIERDSI
NCVMVNENPQ DWHERMLVAA SVSLSASGSR ILLKETSLMP HIHGLPSLVT MLFTPVMELR
TNEDRTCFTG ALCGLGWNSV SQEAVLPEHD IEIAFDVKFE IEDITEINAL RGTVNRLVCD
GPNGLLNLSQ EKISSLQEEA RERLIRLFIK TPSRPECTPV YHDKFKKWNL VDRSQQMEIQ
EKDDGKSKGV LFQLHPITLL NM
