ID   TDRD5_XENLA             Reviewed;         963 AA.
AC   A1L1H3;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Tudor domain-containing protein 5;
GN   Name=tdrd5;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required during spermiogenesis to participate in the
CC       repression transposable elements and prevent their mobilization, which
CC       is essential for the germline integrity. Probably acts via the piRNA
CC       metabolic process, which mediates the repression of transposable
CC       elements during meiosis by forming complexes composed of piRNAs and
CC       Piwi proteins and govern the methylation and subsequent repression of
CC       transposons (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localizes to
CC       chromatoid body (CB) and pi-body (also called intermitochondrial
CC       cementin), 2 cytoplasmic ribonucleoprotein granules involved in RNA
CC       processing for spermatogenesis. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TDRD5 family. {ECO:0000305}.
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DR   EMBL; BC129060; AAI29061.1; -; mRNA.
DR   RefSeq; NP_001090599.1; NM_001097130.1.
DR   AlphaFoldDB; A1L1H3; -.
DR   SMR; A1L1H3; -.
DR   PRIDE; A1L1H3; -.
DR   DNASU; 100036842; -.
DR   GeneID; 100036842; -.
DR   KEGG; xla:100036842; -.
DR   CTD; 100036842; -.
DR   Xenbase; XB-GENE-5884063; tdrd5.L.
DR   OrthoDB; 1115068at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 100036842; Expressed in testis and 8 other tissues.
DR   GO; GO:0033391; C:chromatoid body; ISS:UniProtKB.
DR   GO; GO:0071546; C:pi-body; ISS:UniProtKB.
DR   GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR   GO; GO:0030719; P:P granule organization; ISS:UniProtKB.
DR   GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR   CDD; cd09975; LOTUS_2_TDRD5; 1.
DR   CDD; cd04508; TUDOR; 1.
DR   Gene3D; 2.40.50.90; -; 1.
DR   Gene3D; 3.30.420.610; -; 3.
DR   InterPro; IPR041966; LOTUS-like.
DR   InterPro; IPR025605; OST-HTH/LOTUS_dom.
DR   InterPro; IPR035437; SNase_OB-fold_sf.
DR   InterPro; IPR037982; TDRD5_LOTUS_2.
DR   InterPro; IPR002999; Tudor.
DR   Pfam; PF12872; OST-HTH; 3.
DR   Pfam; PF00567; TUDOR; 1.
DR   PROSITE; PS51644; HTH_OST; 3.
DR   PROSITE; PS50304; TUDOR; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Developmental protein; Differentiation; Reference proteome;
KW   Repeat; Spermatogenesis.
FT   CHAIN           1..963
FT                   /note="Tudor domain-containing protein 5"
FT                   /id="PRO_0000408349"
FT   DOMAIN          6..79
FT                   /note="HTH OST-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT   DOMAIN          122..197
FT                   /note="HTH OST-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT   DOMAIN          375..449
FT                   /note="HTH OST-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT   DOMAIN          586..645
FT                   /note="Tudor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT   REGION          232..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          739..763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          803..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          864..891
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        803..819
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   963 AA;  108146 MW;  4ECEC0157026F17A CRC64;
     MEQERIMQRV QKDVRSLLIA SKNGLSIQEL EQDYRMMIGS QIPLRSLGYK STMELLLDMP
     NVVQIHTQMD GTVNLSAVVD EATRKIADLV SCQKDRSTAR SRNRRRNIRP RCPVDLVRRG
     RVSPVLPATV KSDLRDLLSL SPLLLSELEK AFFSRFGRSF QYTRYGFYSM LEVLRSISDI
     VEVKQTRTGS LLVLRKSETG HISASLCVKK SLDCQPAAVP NKTSCVFEKC LNEPQRPEKK
     PSEPATSLKI SPPEFQKFSS QEPQSITSSR SFLHSSSNKE PDVNRNVSLG ESKKSIENKT
     SPAVPSNNVV LNNSLVKNSE TFESLFTRMS KPVSHVEADH ANASEPNSSD LNWLEKKLEK
     ELKLCLARKG AGGSVSDDLR SDIKHVVNQH SNGLNISLLP TAFKSFTGKD LPFKELGFMS
     VMELVGSLGD ILCLESTDEG KDWKLFGAKK EDLVDEFSAG LRSTNSSLSS WNSTRQSTAP
     LKPVGTIFSK VDEKLWWGPL ELKVCSTEQI DIPPDAVRNQ KLHCLPRIKH SLMIGVYVES
     IESPSQFYVR CCGKDTSEKL EDMMIEMRHC YSNECVSERY IVPDNCISVG QIYALRVPGD
     VWWYRVIVHS IKNSELLDVF YPDFGNVATV KKSWLRFLKN CYMKVPAQAV PSSLPFVTST
     EAQWSTQAIK RFRQLCSCLP LVGLVLQYVQ DVLVIFLCDT SSAEDVYLHQ LLIAQGLAKM
     EPEHACKKVS RNTFMHYLTP SQEKPQEESS KSSVPSESSQ SEVLCTKETI LQVIDEVDPE
     MPYLEAFPTD TDVWDENWVF SDGAGGSNTT PTIPKVETQK QENKISKEQK QPFKFCMDSG
     DASVVHRPLE EFYISLIKSS KSQESTDIQQ SSHTEEQHLA EKSHRCTAEQ LQGGSSSSML
     CEKKLYYENK DLTYCQQQSK CSFSPLIGFQ KLQIPRSATP AALGPAARLA TAGRLLYWAS
     DSH