Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is an RNA-binding protein directly associated with piRNA precursors. It is required for retrotransposon silencing, chromatoid body assembly, and spermiogenesis. TDRD5 participates in the repression of transposable elements and prevents their mobilization, which is essential for germline integrity. TDRD5 contains three LOTUS domains and one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495558 484 FVEYIISPSQFYIRIYSRDSSELLEDMMIEMRRCYSNQLVSDRYIMPEYFIQPGHLCCVKISEDKWWYRVIIHRILGKKE 563
Cdd:cd20419    1 FVEYIESPSQFYVRFYSKDTSEMLEDMMIEMRRCYSNEHVSERYVMPEAFIQPGQVCCVRIPEDVWWYRVIIHQVLNKQE 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 755495558 564 VEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSL 601
Cdd:cd20419   81 VEVFYPDFGDIGTVQKSRLRFLKCCYSKLPAQAIPASL 118

The third LOTUS domain on Tudor-containing protein 5 (TDRD5); The third LOTUS domain on Tudor-containing protein 5 (TDRD5): TDRD5 contains three N-terminal LOTUS domains and a C-terminal Tudor domain. It belongs to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice TDRD5 is a component of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. The exact molecular function of LOTUS domain on TDRD5 remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755495558 292 DPELKRKIQFVVSKFPQGLFISKLLGEFELTFKEQLSPKQLGFLNVTELVGALSDILRVEFSEERQDLLVFDAD 365
Cdd:cd09976    1 SRELREEIRKVVENHPNGLFIALLPTEYKVLFKEELPVKQLGFLSVTELVGSLSDILAIERREKESDWLVFDAK 74

Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is an RNA-binding protein directly associated with piRNA precursors. It is required for retrotransposon silencing, chromatoid body assembly, and spermiogenesis. TDRD5 participates in the repression of transposable elements and prevents their mobilization, which is essential for germline integrity. TDRD5 contains three LOTUS domains and one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495558 484 FVEYIISPSQFYIRIYSRDSSELLEDMMIEMRRCYSNQLVSDRYIMPEYFIQPGHLCCVKISEDKWWYRVIIHRILGKKE 563
Cdd:cd20419    1 FVEYIESPSQFYVRFYSKDTSEMLEDMMIEMRRCYSNEHVSERYVMPEAFIQPGQVCCVRIPEDVWWYRVIIHQVLNKQE 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 755495558 564 VEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSL 601
Cdd:cd20419   81 VEVFYPDFGDIGTVQKSRLRFLKCCYSKLPAQAIPASL 118

The third LOTUS domain on Tudor-containing protein 5 (TDRD5); The third LOTUS domain on Tudor-containing protein 5 (TDRD5): TDRD5 contains three N-terminal LOTUS domains and a C-terminal Tudor domain. It belongs to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice TDRD5 is a component of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. The exact molecular function of LOTUS domain on TDRD5 remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755495558 292 DPELKRKIQFVVSKFPQGLFISKLLGEFELTFKEQLSPKQLGFLNVTELVGALSDILRVEFSEERQDLLVFDAD 365
Cdd:cd09976    1 SRELREEIRKVVENHPNGLFIALLPTEYKVLFKEELPVKQLGFLSVTELVGSLSDILAIERREKESDWLVFDAK 74

Tudor domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495558  483 VFVEYIISPSQFYIRiySRDSSELLEDMMIEMRRCYSNQLvsdryiMPEYFIQPGHLCCVKISEDKWWYRVIIHRILGKK 562
Cdd:pfam00567   5 VVVSHIESPSTFYIQ--PKSDSKKLEKLTEELQEYYASKP------PESLPPAVGDGCVAAFSEDGKWYRAKITESLDDG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 755495558  563 EVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLA 602
Cdd:pfam00567  77 LVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLA 116

OST-HTH/LOTUS domain; A predicted RNA-binding domain found in insect Oskar and vertebrate TDRD5/TDRD7 proteins that nucleate or organize structurally related ribonucleoprotein (RNP) complexes, the polar granule and nuage, is poorly understood. The domain adopts the winged helix-turn- helix fold and bind RNA with a potential specificity for dsRNA.In eukaryotes this domain is often combined in the same polypeptide with protein-protein- or lipid- interaction domains that might play a role in anchoring these proteins to specific cytoskeletal structures. Thus, proteins with this domain might have a key role in the recognition and localization of dsRNA, including miRNAs, rasiRNAs and piRNAs hybridized to their targets. In other cases, this domain is fused to ubiquitin-binding, E3 ligase and ubiquitin-like domains indicating a previously under-appreciated role for ubiquitination in regulating the assembly and stability of nuage-like RNP complexes. Both bacteria and eukaryotes encode a conserved family of proteins that combines this predicted RNA-binding domain with a previously uncharacterized RNase domain belonging to the superfamily that includes the 5'->3' nucleases, PIN and NYN domains.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755495558  133 ELKDLLALSP---VLLSDFEKAFARRFGRSFQYMQYGFLSMFEVLNAASDVISVEQTRAGSLLT 193
Cdd:pfam12872   1 ELISLLRSDPdgwASLSELGSEYRKLFGEDFDPRNYGFSKLSDLLKAIPDVFEIEKRGGGGLVV 64

OST-HTH/LOTUS domain; A predicted RNA-binding domain found in insect Oskar and vertebrate TDRD5/TDRD7 proteins that nucleate or organize structurally related ribonucleoprotein (RNP) complexes, the polar granule and nuage, is poorly understood. The domain adopts the winged helix-turn- helix fold and bind RNA with a potential specificity for dsRNA.In eukaryotes this domain is often combined in the same polypeptide with protein-protein- or lipid- interaction domains that might play a role in anchoring these proteins to specific cytoskeletal structures. Thus, proteins with this domain might have a key role in the recognition and localization of dsRNA, including miRNAs, rasiRNAs and piRNAs hybridized to their targets. In other cases, this domain is fused to ubiquitin-binding, E3 ligase and ubiquitin-like domains indicating a previously under-appreciated role for ubiquitination in regulating the assembly and stability of nuage-like RNP complexes. Both bacteria and eukaryotes encode a conserved family of proteins that combines this predicted RNA-binding domain with a previously uncharacterized RNase domain belonging to the superfamily that includes the 5'->3' nucleases, PIN and NYN domains.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755495558  298 KIQFVVSKFPQG-LFISKLLGEFELTFKEQLSPKQLGFLNVTELVGALSDILRVEFSEERQDLL 360
Cdd:pfam12872   1 ELISLLRSDPDGwASLSELGSEYRKLFGEDFDPRNYGFSKLSDLLKAIPDVFEIEKRGGGGLVV 64

Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is an RNA-binding protein directly associated with piRNA precursors. It is required for retrotransposon silencing, chromatoid body assembly, and spermiogenesis. TDRD5 participates in the repression of transposable elements and prevents their mobilization, which is essential for germline integrity. TDRD5 contains three LOTUS domains and one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495558 484 FVEYIISPSQFYIRIYSRDSSELLEDMMIEMRRCYSNQLVSDRYIMPEYFIQPGHLCCVKISEDKWWYRVIIHRILGKKE 563
Cdd:cd20419    1 FVEYIESPSQFYVRFYSKDTSEMLEDMMIEMRRCYSNEHVSERYVMPEAFIQPGQVCCVRIPEDVWWYRVIIHQVLNKQE 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 755495558 564 VEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSL 601
Cdd:cd20419   81 VEVFYPDFGDIGTVQKSRLRFLKCCYSKLPAQAIPASL 118

The third LOTUS domain on Tudor-containing protein 5 (TDRD5); The third LOTUS domain on Tudor-containing protein 5 (TDRD5): TDRD5 contains three N-terminal LOTUS domains and a C-terminal Tudor domain. It belongs to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice TDRD5 is a component of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. The exact molecular function of LOTUS domain on TDRD5 remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755495558 292 DPELKRKIQFVVSKFPQGLFISKLLGEFELTFKEQLSPKQLGFLNVTELVGALSDILRVEFSEERQDLLVFDAD 365
Cdd:cd09976    1 SRELREEIRKVVENHPNGLFIALLPTEYKVLFKEELPVKQLGFLSVTELVGSLSDILAIERREKESDWLVFDAK 74

The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7; The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7: The LOTUS containing proteins are germline-specific and are found in the nuage/polar granules of germ cells. Tudor-containing protein 5 and 7 belong to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD5 and TDRD7 are components of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. Oskar protein is a critical component of the pole plasm in the Drosophila oocyte, which is required for germ cell formation.The exact molecular function of LOTUS domain remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495558   9 DCLRKEIRSLLISTKDGLTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSVCpGGDGTVILKAIPDESTKGIA 88
Cdd:cd09972    2 EEVKKVLRSLLISSKGGLTLSELERDYRELEGEPIPYRKLGYSSLEDFLRSIPDVVTVR-SSGGEVLVKAVADEKTAHIA 80

                 ....*..
gi 755495558  89 SLVAKQR 95
Cdd:cd09972   81 SLVAKQK 87

third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495558 484 FVEYIISPSQFYIRI--YSRDSSELLEDMMIEMRRCYSNQLVSDRyimPEyfiqPGHLCCVKISEDKWWYRVIIHRILGK 561
Cdd:cd20438   10 FVEYVLNPSNFWIRTdeYNNEFQALMKNIADIYNLCGNDEELLKK---PE----PGLLCCARYSKDRHYYRAVITEVLDL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 755495558 562 KeVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAWVRPAE 608
Cdd:cd20438   83 K-VSVYFLDFGNTDTVPFYDVKTLLPEFSELPALAMCCSLAHVFPVE 128

Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar proteins; dTUD is required during oogenesis for the formation of primordial germ cells and for normal abdominal segmentation. It contains 11 Tudor domains. The family also includes mitochondrial A-kinase anchor protein 1 (AKAP1) and Tudor domain-containing proteins (TDRDs). AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), or dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), or protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. TDRDs have diverse biological functions and may contain one or more copies of the Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 755495558 536 PGHLCCVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFL 585
Cdd:cd20379    1 VGDLCAAKYEEDGKWYRARVLEVLSNDKVEVFFVDYGNTETVPLSDLRPL 50

fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495558 488 IISPSQFYI-RIYSRDSSELLEDMMIEMRRCYSNQLVSDRYImPeyfiQPGHLCCVKISEDKWWYRVIIHRIlGKKEVEV 566
Cdd:cd20411    6 VISPDLFYAlPKTGQVNVEKLKALMTELAEYCSKQSVPQQFR-P----RIGDACCARFTGDKNWYRAVVLET-SDSEVKV 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755495558 567 FYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLA 602
Cdd:cd20411   80 LYADYGNTETLPLSRILPITKSHLELPFQIIRCSLA 115

seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the seventh one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495558 484 FVEYIISPSQFYIRiYSRDSSELLEDMMIEMRRcysnQLVSDRYIMPEyfIQPGHLCCVKISEDKWWYRVIIHRILGKKe 563
Cdd:cd20426    4 YATAVDSPEYFWCQ-FATEKIQCLAVKVQEAGE----QVADRGNFIPS--IYVGDPCIVKYSEDNHWYRALVTKINDNL- 75

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 755495558 564 VEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLA 602
Cdd:cd20426   76 VSVRFVDYGNEEDVVREQVRALPSELLKIPVQAFPCCLS 114

sixth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the sixth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495558 483 VFVEYIISPSQFYIRIySRDSSELLedMMIEmrrCYSNQLVSDRYIMPEYFiQPGHLCCVKISEDKWWYRVIIHRILGKK 562
Cdd:cd20425    4 VYVSHVNSPSDFYVQL-AQDEDELS--MISE---KLNASKANDEEVECESL-QLGDLICAEYPEDGLWYRAVVKEKIPNN 76

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 755495558 563 EVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSL 601
Cdd:cd20425   77 LVSVQFIDYGNTSVVQPSKIHRLPKELLSIPALSIHCFL 115

second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755495558 541 CVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAWVRP 606
Cdd:cd20415   31 CVALFEDGAWYRARIIGLPGHREVEVKYVDFGNTATVTIKHVRKIKDDFLSLPEKARECRLAFIEP 96

fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495558 483 VFVEYIISPSQFYIRIySRDSSelledmMIEMRRCYSNQLVSDryIMP-EYFIQPGHLCCVKISeDKWWYRVIIhrILGK 561
Cdd:cd20424   16 VYITYVNDPWTFYCQL-ARNAG------VLDQLASAISRLSSE--IRKlELSVNPGTLCLAKYS-DQHWYRGII--ITNK 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 755495558 562 KEVEVFYPDFGNIGTVQKSSLRFL---KCCYTKLPAQAIPCSL 601
Cdd:cd20424   84 NSTEVFFVDYGNTEKVEKEDMLPIpsdAYELLLLPMQAIKCSL 126

sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the sixth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495558 490 SPSQFYIRIySRDSSELLeDMMIEM-------RRCYSNQLVSDRYIMPEYfiqpghlccvkiSEDKWWYRVIIHRILGKK 562
Cdd:cd20441    1 SPSRFFIQL-SEDEKVIL-QLAEELnetseksRENAAVKLKVGDLVAAEY------------DEDLALYRAVITAVLPGK 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 755495558 563 EVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLA 602
Cdd:cd20441   67 SFKVEFIDYGNTAVVDKSNIYTLQEKFLSLPRLSIPCSLS 106

OST-HTH/LOTUS domain; A predicted RNA-binding domain found in insect Oskar and vertebrate TDRD5/TDRD7 proteins that nucleate or organize structurally related ribonucleoprotein (RNP) complexes, the polar granule and nuage, is poorly understood. The domain adopts the winged helix-turn- helix fold and bind RNA with a potential specificity for dsRNA.In eukaryotes this domain is often combined in the same polypeptide with protein-protein- or lipid- interaction domains that might play a role in anchoring these proteins to specific cytoskeletal structures. Thus, proteins with this domain might have a key role in the recognition and localization of dsRNA, including miRNAs, rasiRNAs and piRNAs hybridized to their targets. In other cases, this domain is fused to ubiquitin-binding, E3 ligase and ubiquitin-like domains indicating a previously under-appreciated role for ubiquitination in regulating the assembly and stability of nuage-like RNP complexes. Both bacteria and eukaryotes encode a conserved family of proteins that combines this predicted RNA-binding domain with a previously uncharacterized RNase domain belonging to the superfamily that includes the 5'->3' nucleases, PIN and NYN domains.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755495558   14 EIRSLLISTKDG-LTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSVCPGGDGTVIL 76
Cdd:pfam12872   1 ELISLLRSDPDGwASLSELGSEYRKLFGEDFDPRNYGFSKLSDLLKAIPDVFEIEKRGGGGLVV 64

first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; TDRD7, also called PCTAIRE2-binding protein, or Tudor repeat associator with PCTAIRE-2 (Trap), is a component of specific cytoplasmic RNA granules involved in post-transcriptional regulation of specific genes: probably acts by binding to specific mRNAs and regulating their translation. It is required for lens transparency during lens development, by regulating translation of genes such as CRYBB3 and HSPB1 in the developing lens. It is also essential for dynamic ribonucleoprotein (RNP) remodeling of chromatoid bodies during spermatogenesis. TDRD7 contains three Tudor domains. The model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495558 505 ELLEDmmiEMRRCYSNqlvsDRYIMPEYFIQPGHLCCVKISEDKWwYRVIIHRILGKKeVEVFYPDFGNIGTVQKSSLRF 584
Cdd:cd20427    1 EQMED---EMKEFYSK----SSTAMCLRSPSVGQLVAVKAEEDAW-LRAQVIEVEEDK-VKVYYVDHGFSEVVERSKLFK 71

                         90       100
                 ....*....|....*....|..
gi 755495558 585 LKCCYTKLPAQAIPCSLAWVRP 606
Cdd:cd20427   72 LNKQFYSLPFQATKCKLAGLEP 93

OST-HTH/LOTUS domain; A predicted RNA-binding domain found in insect Oskar and vertebrate TDRD5/TDRD7 proteins that nucleate or organize structurally related ribonucleoprotein (RNP) complexes, the polar granule and nuage, is poorly understood. The domain adopts the winged helix-turn- helix fold and bind RNA with a potential specificity for dsRNA.In eukaryotes this domain is often combined in the same polypeptide with protein-protein- or lipid- interaction domains that might play a role in anchoring these proteins to specific cytoskeletal structures. Thus, proteins with this domain might have a key role in the recognition and localization of dsRNA, including miRNAs, rasiRNAs and piRNAs hybridized to their targets. In other cases, this domain is fused to ubiquitin-binding, E3 ligase and ubiquitin-like domains indicating a previously under-appreciated role for ubiquitination in regulating the assembly and stability of nuage-like RNP complexes. Both bacteria and eukaryotes encode a conserved family of proteins that combines this predicted RNA-binding domain with a previously uncharacterized RNase domain belonging to the superfamily that includes the 5'->3' nucleases, PIN and NYN domains.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755495558  133 ELKDLLALSP---VLLSDFEKAFARRFGRSFQYMQYGFLSMFEVLNAASDVISVEQTRAGSLLT 193
Cdd:pfam12872   1 ELISLLRSDPdgwASLSELGSEYRKLFGEDFDPRNYGFSKLSDLLKAIPDVFEIEKRGGGGLVV 64

LOTUS is an uncharacterized small globular domain found in Limkain b1, Oskar and Tudor-containing proteins 5 and 7; LOTUS is an uncharacterized small globular domain found in Limkain b1, Oskar and Tudor-containing proteins 5 and 7. The LOTUS containing proteins are germline-specific and are found in the nuage/polar granules of germ cells. Tudor-containing protein 5 and 7 belong to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD5 and TDRD7 are components of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. Oskar protein is a critical component of the pole plasm in the Drosophila oocyte, which is required for germ cell formation. Limkain b1 is a novel human autoantigen, localized to a subset of ABCD3 and PXF marked peroxisomes. Limkain b1 may be a relatively common target of human autoantibodies reactive to cytoplasmic vesicle-like structures. Limkain b1 contains multiple copies of LOTUS domains and a conserved RNA recognition motif. The exact molecular function of LOTUS domain remains to be characterized. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755495558 294 ELKRKIQFVVSKFPQGLFISKLLGEFELTFKEQLSPKQLGFLNVTELVGALSDILRVEFSEER 356
Cdd:cd08824    3 QLAKQLRSLLQSYPGGLPLSKLPQLYKKKFGKPLDLSEYGFSKLSDLLEALPGVVIVLSQGGE 65

Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor 2 (AtTudor2), and similar proteins; The family includes AtTudor1 (also called Tudor-SN protein 1) and AtTudor2 (also called Tudor-SN protein 2 or 100 kDa coactivator-like protein). They are cytoprotective ribonucleases (RNases) required for resistance to abiotic stresses, acting as positive regulators of mRNA decapping during stress. Members of this family contain one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755495558 535 QPGHLCCVKISEDKWWYRVII------HRILGKKEVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAWVRP 606
Cdd:cd20443   39 KKGELVLAQFSADNSWNRAMVvnaprqGTQSPKDEYEVFYIDYGNQETVPLSALRPLDPSVSSAPGLAQLCSLAHIKV 116

OST-HTH/LOTUS domain; A predicted RNA-binding domain found in insect Oskar and vertebrate TDRD5/TDRD7 proteins that nucleate or organize structurally related ribonucleoprotein (RNP) complexes, the polar granule and nuage, is poorly understood. The domain adopts the winged helix-turn- helix fold and bind RNA with a potential specificity for dsRNA.In eukaryotes this domain is often combined in the same polypeptide with protein-protein- or lipid- interaction domains that might play a role in anchoring these proteins to specific cytoskeletal structures. Thus, proteins with this domain might have a key role in the recognition and localization of dsRNA, including miRNAs, rasiRNAs and piRNAs hybridized to their targets. In other cases, this domain is fused to ubiquitin-binding, E3 ligase and ubiquitin-like domains indicating a previously under-appreciated role for ubiquitination in regulating the assembly and stability of nuage-like RNP complexes. Both bacteria and eukaryotes encode a conserved family of proteins that combines this predicted RNA-binding domain with a previously uncharacterized RNase domain belonging to the superfamily that includes the 5'->3' nucleases, PIN and NYN domains.

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gi 755495558  298 KIQFVVSKFPQG-LFISKLLGEFELTFKEQLSPKQLGFLNVTELVGALSDILRVEFSEERQDLL 360
Cdd:pfam12872   1 ELISLLRSDPDGwASLSELGSEYRKLFGEDFDPRNYGFSKLSDLLKAIPDVFEIEKRGGGGLVV 64

Tudor domain found in Tudor domain-containing protein 8 (TDRD8) and similar proteins; TDRD8, also called serine/threonine-protein kinase (EC 2.7.11.1) 31 (STK31), serine/threonine-protein kinase NYD-SPK, or Sugen kinase 396 (SgK396), is a germ cell-specific factor expressed in embryonic gonocytes of both sexes, and in postnatal spermatocytes and round spermatids in males. It acts as a cell-cycle regulated protein that contributes to the tumorigenicity of epithelial cancer cells. TDRD8 contains a Tudor domain and a serine/threonine kinase domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

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                 ....*....|....*....|....*....|....*....|....*....|..
gi 755495558 534 IQPGHLCCVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFL 585
Cdd:cd20430   19 PDPNKIYGGKFSEDNCWYRCKVKSILSDEKCTVQYIDYGNTETVSRSSIVEL 70

third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

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                 ....*....|....*....|....*....|....*....|....*....
gi 755495558 535 QPGHLCCVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLR 583
Cdd:cd20410    4 IVGEPCCAFFSGDGNWYRAMVKEILPGGAVKVHFVDYGNVEEVTLDKLR 52

third Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

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                 ....*....|....*....|....*....|....*....|....*..
gi 755495558 540 CCVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFLK 586
Cdd:cd20416   25 CAVQIQDKKQWRRGQIIRVVSDTLVEVFLYDFGNKEVVNIDCLRKLE 71

second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

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                 ....*....|....*....|....*....|....*....|....*...
gi 755495558 536 PGHLCCVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLR 583
Cdd:cd20409   28 VGEVCCAQFTEDNQWYRASVLAYSSEDSVLVGYIDFGNSEEVALSRLR 75

Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is an ATP-dependent DEAD-like RNA helicase required during spermatogenesis. It is involved in the biosynthesis of PIWI-interacting RNAs (piRNAs). A recessive deleterious mutation mutation in TDRD9 causes non-obstructive azoospermia in infertile men. TDRD9 contains an N-terminal HrpA-like RNA helicase module and a Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495558 488 IISPSQFYIRIYSRDSSELLEDMMIEMRRcysNQLVSDRYIMPeyfiqPGHLCCV--KISEDKWWYRVIIHRILGKkEVE 565
Cdd:cd20431    3 VVEVGHFWGYRIDENSSEILQQLTAEINQ---RQLVPLTTKPV-----PNLLCLApfTDADMKKYYRAKILYVSGS-SAE 73

                         90       100
                 ....*....|....*....|....*...
gi 755495558 566 VFYPDFGNIGTVQKSSLRFLKCCYTKLP 593
Cdd:cd20431   74 VFFVDYGNTSQVPSSLLREIPETLLTLP 101