ID   TDRD7_XENTR             Reviewed;        1077 AA.
AC   Q5M7P8;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Tudor domain-containing protein 7;
GN   Name=tdrd7;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of specific cytoplasmic RNA granules involved in
CC       post-transcriptional regulation of specific genes: probably acts by
CC       binding to specific mRNAs and regulating their translation. Probably
CC       required during spermatogenesis (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localizes to cytoplasmic RNA
CC       granules. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TDRD7 family. {ECO:0000305}.
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DR   EMBL; BC088519; AAH88519.1; -; mRNA.
DR   RefSeq; NP_001011355.2; NM_001011355.2.
DR   AlphaFoldDB; Q5M7P8; -.
DR   SMR; Q5M7P8; -.
DR   STRING; 8364.ENSXETP00000005565; -.
DR   GeneID; 496822; -.
DR   KEGG; xtr:496822; -.
DR   CTD; 23424; -.
DR   Xenbase; XB-GENE-944683; tdrd7.
DR   eggNOG; KOG2039; Eukaryota.
DR   InParanoid; Q5M7P8; -.
DR   OrthoDB; 1276848at2759; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0043186; C:P granule; IBA:GO_Central.
DR   GO; GO:0035770; C:ribonucleoprotein granule; ISS:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR   GO; GO:0070306; P:lens fiber cell differentiation; ISS:UniProtKB.
DR   GO; GO:0002089; P:lens morphogenesis in camera-type eye; ISS:UniProtKB.
DR   GO; GO:0030719; P:P granule organization; IBA:GO_Central.
DR   GO; GO:0034587; P:piRNA metabolic process; IBA:GO_Central.
DR   GO; GO:0010608; P:post-transcriptional regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   CDD; cd09974; LOTUS_3_TDRD7; 1.
DR   CDD; cd04508; TUDOR; 3.
DR   Gene3D; 2.40.50.90; -; 3.
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; IPR037978; TDRD7_LOTUS_3.
DR   InterPro; IPR002999; Tudor.
DR   Pfam; PF12872; OST-HTH; 2.
DR   Pfam; PF00567; TUDOR; 3.
DR   SMART; SM00333; TUDOR; 3.
DR   PROSITE; PS51644; HTH_OST; 3.
DR   PROSITE; PS50304; TUDOR; 2.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Differentiation; Reference proteome; Repeat; RNA-binding;
KW   Spermatogenesis.
FT   CHAIN           1..1077
FT                   /note="Tudor domain-containing protein 7"
FT                   /id="PRO_0000409521"
FT   DOMAIN          1..67
FT                   /note="HTH OST-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT   DOMAIN          220..289
FT                   /note="HTH OST-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT   DOMAIN          330..398
FT                   /note="HTH OST-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT   DOMAIN          494..551
FT                   /note="Tudor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT   DOMAIN          684..741
FT                   /note="Tudor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT   REGION          300..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1077 AA;  120613 MW;  C9E1D056023AC478 CRC64;
     MLRAVLQANK NGVPLSKLQA EYKSFTGEPI PFKDMGFHAL DAYLKSIPSV VRIEVSRVGE
     VICYAVVCKE TARIAALVAH QRSSKKKSGG QVNCQMRLKY TAPVSHFGKP KATLRQPGFT
     PPQEKIIRKP VPTSAWGKGN TFGSRTFEYS PPPIPQLFGI APIQMHLPNI NRPERKVTLP
     PRFQREVNSF LNPTPMTDSN ANHTQSLKSV VPGSGQPRCD LSVIQNNLKE LLNKHSNGLW
     LSKLPQLYKE TYKQDLGGEM LKQVPSWTHI CMVQKLVTMG HTEMVLYSTA IKQPSFTKNV
     QNHSNNQAKP NVPVDSTPSS PPLQSSGNIP KDELKQKISK VLTKYSNGLW YHALPKVFED
     MFKQKLPTEV LNLDSLTDIC TVDLISEEPF KAILYAKSAE RANQNSNPSV NNNIPQKLQD
     RESPLLPEEP EMNMTPPPLV IPSEASPSVL VVELSSTNDV VIRYIGRDYS AAQEHMEDEM
     KDFCSKSSTA KIGFLRVGQL VAAKAEEDVW LRAQISAIEG KKVKVCYVDY GFSEIVDITK
     VCKLGKQFYT LPFQATKCRL AGLEAFCDDS IIIKALELKA CGKILAVEIL EKSEKPLVVL
     YDTSGDDDIN INAACLKELC DRSLSLQLKA NSSFSNVIVT NVCSDGTLFC QLPSKGLAKL
     YETLQKVDSE FQSKQVTSHL YVSLPFCGKI CLYHYKGKWA RVEITSVHSS RALDVQFLDS
     GTIASVKVSE LKEIPPPLLR DLISIPPQAL RCCLADLPLR IGMWTPDAVL WLRNTVLNCL
     ECSIRVVKVD EATNMVHIYL FTSNNFPDLE RSINRQITNE ELWKHQKDVF LNLSASTLES
     SRGGGAQASE LSPPGLCKDH TSAVKKPDMQ QSSSVPSFNM PPPLPLPRPG EHMDVFVSVA
     CHPGHFVCQP WQELHKLEVV MEEMLLHYST TEEKPVALEK NKLYAAKVEN KWYRVLVKGI
     LTNGLVSVYE LDYGRHELVS CRKVQPLIEK FMQLPFQAIT SQLAGVSCEH WSEEASIVFR
     NHVEKKPLVA LVQTIHESTH PWDRRAVAYI VDTSLPDTDI WIHELMTEYH IQLSKPE