TDRD5_AILME
ID TDRD5_AILME Reviewed; 982 AA.
AC D2H3M0;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Tudor domain-containing protein 5;
GN Name=TDRD5; ORFNames=PANDA_004307;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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. Required for chromatoid body (CB) assembly (By
CC 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; GL192465; EFB26879.1; -; Genomic_DNA.
DR AlphaFoldDB; D2H3M0; -.
DR SMR; D2H3M0; -.
DR STRING; 9646.ENSAMEP00000015531; -.
DR PRIDE; D2H3M0; -.
DR eggNOG; KOG2039; Eukaryota.
DR InParanoid; D2H3M0; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
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 SMART; SM00333; TUDOR; 1.
DR PROSITE; PS51644; HTH_OST; 3.
DR PROSITE; PS50304; TUDOR; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Developmental protein; Differentiation; Phosphoprotein;
KW Reference proteome; Repeat; Spermatogenesis.
FT CHAIN 1..982
FT /note="Tudor domain-containing protein 5"
FT /id="PRO_0000408345"
FT DOMAIN 7..80
FT /note="HTH OST-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 127..202
FT /note="HTH OST-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 297..371
FT /note="HTH OST-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 527..586
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 816..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VCS6"
SQ SEQUENCE 982 AA; 109911 MW; 8C35DCD9B0B4D389 CRC64;
MSEQERVQEC LRKEIRSLLI STKDGLTPQQ LEKEYLLMVG SHLPLRILGY RSTMELVLDM
PDVVTVCPYG DGTVILRAIP DESTKGIASL VAKQRSSHKV RNSAQKGRAS VCSGPSSRRQ
VPYRGRLPPI LPAVVKSELK DLLALSPILL SDFEKAFVRR FGRSFQYVQY GFFSMFEVLN
AASDVISVEQ TRAGSLLMLK KSVSEEKQRG WPAGGKMFTQ PFRMKQQGSY STGSPVAKAR
FSQPTSNMEP PKQILNVEKT FKSNVVETSR LNHTEKLNQL ENTFKSVIAQ IGPGGTISPE
LKHKIRFVVS KFPEGLLISK LLREFEIIFK EQLSPKKLGF LNVIELVGAL SDILRVEFRE
GEQDLLVFDA DMKPLPPAQS DKKIEVKAYV SSPPRNSLST AAVKETTWDC PPKNRKEPEQ
KICKKPNLVV KPLQLQVEVN KSQRNLAMAN HDIPPDAVRD KKLCRLPLLD TSTLVGVFVE
YIISPSQFYI RIYSRDSSEL LEDMMIEMRR CYSNQLVSDR YTLPEYFIQP GHLCCVRISE
DKWWYRVIIH RVLGKQEVEV FYPDFGNIGT VQKSSLRFLK CCYTKLPAQA IPCSLAWVRP
VEEHWTSKAI LQFQKLCGLK PLVGVVDEYV DGILNIFLCD TSSNEDVYFH HVLRTEGHAI
VCRENVPSKG FRELNPLALY TKSSSGPEDV VLTELGYPSQ QHYFNEDREI SPQSKESELS
TLDEIPTGMP CLESVTIGDD VWDENWLPLQ AKMGKGGDAA SHLFTSSLGG KKPYPSCKEM
PQKDWCFSGP KDVWDDSWQP SGLMNGVKVE VQKQEGLGAQ EKNTGTTRIQ KPPPVESSLD
LSTLPKLEEF YSSLIQSQQS AEGSQPEPSC IQTPAKPVQL STAALSASPM ALDSAEKHSG
SVESSPESLK NDFSSSHAIT VFKDKSHGAM DQLSLILSPE HQISQKLYIP RSTATAALGA
AARLATSRSL LHWYPSVKRM EA