TDRD1_DANRE
ID TDRD1_DANRE Reviewed; 1175 AA.
AC Q58EK5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Tudor domain-containing protein 1;
GN Name=tdrd1; ORFNames=im:7155161;
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 [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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 691-1175.
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a central role during spermatogenesis by participating
CC in the repression 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. Required for the localization of Piwi
CC proteins to the meiotic nuage. Involved in the piRNA metabolic process
CC by ensuring the entry of correct transcripts into the normal piRNA pool
CC and limiting the entry of cellular transcripts into the piRNA pathway.
CC May act by allowing the recruitment of piRNA biogenesis or loading
CC factors that ensure the correct entry of transcripts and piRNAs into
CC Piwi proteins (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q58EK5; Q8UVX0: piwil1; NbExp=3; IntAct=EBI-7011788, EBI-7011759;
CC Q58EK5; A2CEI6: piwil2; NbExp=9; IntAct=EBI-7011788, EBI-7011808;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Component of the
CC meiotic nuage, also named P granule, a germ-cell-specific organelle
CC required to repress transposon activity during meiosis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TDRD1 family. {ECO:0000305}.
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DR EMBL; CR932360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC091863; AAH91863.1; -; mRNA.
DR AlphaFoldDB; Q58EK5; -.
DR SMR; Q58EK5; -.
DR IntAct; Q58EK5; 95.
DR MINT; Q58EK5; -.
DR STRING; 7955.ENSDARP00000127267; -.
DR PaxDb; Q58EK5; -.
DR ZFIN; ZDB-GENE-070803-1; tdrd1.
DR eggNOG; KOG2039; Eukaryota.
DR InParanoid; Q58EK5; -.
DR PhylomeDB; Q58EK5; -.
DR PRO; PR:Q58EK5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0043186; C:P granule; ISS:UniProtKB.
DR GO; GO:0071546; C:pi-body; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034584; F:piRNA binding; IDA:ZFIN.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
DR GO; GO:0007281; P:germ cell development; ISS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030719; P:P granule organization; IMP:ZFIN.
DR GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR CDD; cd04508; TUDOR; 4.
DR Gene3D; 2.40.50.90; -; 3.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR002893; Znf_MYND.
DR Pfam; PF00567; TUDOR; 4.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00333; TUDOR; 4.
DR PROSITE; PS50304; TUDOR; 4.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Differentiation; Meiosis; Metal-binding;
KW Reference proteome; Repeat; RNA-mediated gene silencing; Zinc; Zinc-finger.
FT CHAIN 1..1175
FT /note="Tudor domain-containing protein 1"
FT /id="PRO_0000367315"
FT DOMAIN 222..282
FT /note="Tudor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 453..512
FT /note="Tudor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 674..733
FT /note="Tudor 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 925..983
FT /note="Tudor 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT ZN_FING 83..119
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT CONFLICT 691
FT /note="W -> G (in Ref. 2; AAH91863)"
FT /evidence="ECO:0000305"
FT CONFLICT 748
FT /note="V -> M (in Ref. 2; AAH91863)"
FT /evidence="ECO:0000305"
FT CONFLICT 836
FT /note="P -> Q (in Ref. 2; AAH91863)"
FT /evidence="ECO:0000305"
FT CONFLICT 1132
FT /note="S -> P (in Ref. 2; AAH91863)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1175 AA; 129042 MW; 6DD18C1D98CAB859 CRC64;
MNPAFAQPMM RPNLPLRRPA TGPSSLSPRG PAPAIYEERL LASDVLDGPK IDTMRKDISQ
NCGDVLSSPQ TAVSMMGQVV KLCNYCSHQG NLRCTRCKKT CYCSVACQTQ DWIAHRHVCK
PSIPEVTSEK PKESKAVPYA NGLGGTQAKE ISVDAQPKRI YRRDLHKKVV SKGSEIKGTV
IDLRNPGMFS IHCQCEEMIE SLKKITQQLQ KTYCSSFAQE YKPEVGELCA VKFSLDQNWY
RAEIQAVDVA RKTAGVFYID FGNEENVALD HIRPLSENID AVPPFALQCC IAGVKPLTGS
WTGECCIAVR QLIAGKSLTF TVLDIMNDGD LLAVDSLVST LGKHVSTFLI DQSYAIKEDV
PVKTQTEHSI SSLLTASFEN FKRFSGGKNE NSEARPPEPL TQGVGDSFTA VVTHLQSPSE
ILCQKLENAS IIQQLQMNLR VHCSNTAASD DFRPAPGTVC CSLFSEDNQW YRAKVLAYSS
EDRVCVGYID FGNSEEVELN RLRPISKELL ALATQAIPCS LAGIKSLTDT WSDEAVLMLK
HLVCNRFIRV EILGKKDGRA LVSMIDESSD PQASVTELLV NMGFAAIESV ETKKNEPDPA
TSTEIPLSQP VVEKLEWTGA ELPFDGQKVE LVISTLKSLD EFYCYNYSKT DEHTLTEMSF
ELMKHCESER APFTPIVGEP CCALFTGDAR WYRAMVLEVC GEGKARVCFV DYGNSCEVDA
AHLKAITQSL LKLPFQAIRC WLAGVEPVEG QWKKEAMLRF QALCAGQPLS GKVLSITEKG
YGMELESAGQ TVASVLISEH LAKPYGQVRQ PPQIQPAKPA SQIEDLPSLK PIDQNPSVEE
PLKVSSKGAA TTPEDLPVSS GCFPLNWKTL ELSCSGTFQP RVAAVISPSL FYIMNPGQVN
VEGLKAVMTD VAKYCSKQPV PNQCHPLPGA SCCAQFSGDK NWYRAVVLEV TTKHAHVIYS
DYGNMETVPL SSILPITKEL LQHPFQIVRC ALTGKEHFPV VWPTEVLELF GIQLSGGVLA
SFQGFDGTSN LLTLTQQSGQ SDRDINSIIL GALQKGQIKP SSKLPANVNE EKKDVEQKQT
QPISSNKAVE QTLSTNVEKP ALDDQTLPLS VSLKHEEPEN MSKTKTAEEC TSTPDTVSSI
ESSHAAQSCC CQELKQKMDR IEELVLLLVK QVGSR
