The first LOTUS domain on Tudor-containing protein 5 (TDRD5); The first 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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354619   4 QERIQDCLRKEIRSLLISTKDGLTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSVCPGGDGTVILKAIPDES 83
Cdd:cd09985     1 QEQIMERLKKDVRSLLISSKNGLTPEQLEQDYLAMVGSPLPLRSLGFRSTMELVLDMPDVVRVHPQLDGTVILKAVGDET 80

                          90
                  ....*....|....*
gi 1720354619  84 TKGIASLVAKQRRSH 98
Cdd:cd09985    81 TKGIEDLVSKQRDSK 95

The second LOTUS domain on Tudor-containing protein 5 (TDRD5); The second 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 discovered. 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 1720354619 127 PAVVKSELKDLLALSPVLLSDFEKAFARRFGRSFQYMQYGFLSMFEVLNAASDVISVEQTRAGSLLTLKK 196
Cdd:cd09975     1 PAHVKSELKDLLSHSPVLLSELEKAYVARFGRSFQYTQYGFFSMLEVLSAASDFIIVKQTRTGSLLLLKK 70

The first LOTUS domain on Tudor-containing protein 5 (TDRD5); The first 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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354619   4 QERIQDCLRKEIRSLLISTKDGLTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSVCPGGDGTVILKAIPDES 83
Cdd:cd09985     1 QEQIMERLKKDVRSLLISSKNGLTPEQLEQDYLAMVGSPLPLRSLGFRSTMELVLDMPDVVRVHPQLDGTVILKAVGDET 80

                          90
                  ....*....|....*
gi 1720354619  84 TKGIASLVAKQRRSH 98
Cdd:cd09985    81 TKGIEDLVSKQRDSK 95

The second LOTUS domain on Tudor-containing protein 5 (TDRD5); The second 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 discovered. 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 1720354619 127 PAVVKSELKDLLALSPVLLSDFEKAFARRFGRSFQYMQYGFLSMFEVLNAASDVISVEQTRAGSLLTLKK 196
Cdd:cd09975     1 PAHVKSELKDLLSHSPVLLSELEKAYVARFGRSFQYTQYGFFSMLEVLSAASDFIIVKQTRTGSLLLLKK 70

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 1720354619  14 EIRSLLISTKDG-LTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSVCPGGDGTVIL 76
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 1720354619 298 KIQFVVSKFPQG-LFISKLLGEFELTFKEQLSPKQLGFLNVTELVGALSDILRVEFSEERQDLL 360
Cdd:pfam12872   1 ELISLLRSDPDGwASLSELGSEYRKLFGEDFDPRNYGFSKLSDLLKAIPDVFEIEKRGGGGLVV 64

The first LOTUS domain on Tudor-containing protein 5 (TDRD5); The first 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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354619   4 QERIQDCLRKEIRSLLISTKDGLTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSVCPGGDGTVILKAIPDES 83
Cdd:cd09985     1 QEQIMERLKKDVRSLLISSKNGLTPEQLEQDYLAMVGSPLPLRSLGFRSTMELVLDMPDVVRVHPQLDGTVILKAVGDET 80

                          90
                  ....*....|....*
gi 1720354619  84 TKGIASLVAKQRRSH 98
Cdd:cd09985    81 TKGIEDLVSKQRDSK 95

The second LOTUS domain on Tudor-containing protein 5 (TDRD5); The second 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 discovered. 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 1720354619 127 PAVVKSELKDLLALSPVLLSDFEKAFARRFGRSFQYMQYGFLSMFEVLNAASDVISVEQTRAGSLLTLKK 196
Cdd:cd09975     1 PAHVKSELKDLLSHSPVLLSELEKAYVARFGRSFQYTQYGFFSMLEVLSAASDFIIVKQTRTGSLLLLKK 70

Tudor domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354619 483 VFVEYIISPSQFYIRiySRDSSELLEDMMIEMRRCYSNQLvsdryiMPEYFIQPGHLCCVKISEDKWWYRVIIHRILGKK 562
Cdd:pfam00567   5 VVVSHIESPSTFYIQ--PKSDSKKLEKLTEELQEYYASKP------PESLPPAVGDGCVAAFSEDGKWYRAKITESLDDG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1720354619 563 EVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLA 602
Cdd:pfam00567  77 LVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLA 116

first 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 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 1720354619 483 VFVEYIISPSQFYIRIYSRDSSELLEDMMIEMRRCYSNQLVSDRYImPEYfiqpGHLCCVKISEDKWWYRVIIHRI-LGK 561
Cdd:cd20408     1 GTVTEFKNPGEFYIQIYTLEVLESLVKLTSQLKKTYASVNNHKEYI-PEV----GEVCVAKYSEDQNWYRALVQTVdVQQ 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1720354619 562 KEVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAWVRPAE 608
Cdd:cd20408    76 KKAGVFYIDYGNEETVPLNRIQPLKKDIELFPPCAIKCCLANVKPPS 122

third 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 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 1720354619 483 VFVEYIISPSQFYIRIysRDSSELLEDMMIEMRRCYSNQLVSDRYIMPEyfiQPGHLCCVKISEDKWwYRVIIHRILGKK 562
Cdd:cd20422     4 AQVEFVKDPSEFWIRL--GEHAVPFSKLMRSMTAFYSQASKLDGVVLKP---QPGQLCCAKWKEDRY-YRAIVTAVKGKM 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1720354619 563 eVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAWVRP 606
Cdd:cd20422    78 -VEVFLVDRGNTEMVDWYDVKKLLPQFRELPALALKCCLADICP 120

second 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 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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354619 473 PPLDTSTLVGVFVEYIISPSQFYIRIysRDSSELLEDMMIEMRRCYSNQLVSDRYIMPEyfiQPGHLCCVKiSEDKWWYR 552
Cdd:cd20421     5 PQLQVGVTETVVVTEVTDPHRIFCQL--RSLSQELKRLSESMHQYYEGRVGSGYETRPE---KLGSPCAAR-GSDGRWYR 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720354619 553 VIIHRIL-GKKEVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSL 601
Cdd:cd20421    79 AVLQQVFsANRVVEVLHVDYGRKEVVSVSNLRYLAPEYFRMPVVTYPCAL 128

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720354619   9 DCLRKEIRSLLISTKDGLTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSVCPGGDGTVI 75
Cdd:cd08824     2 KQLAKQLRSLLQSYPGGLPLSKLPQLYKKKFGKPLDLSEYGFSKLSDLLEALPGVVIVLSQGGERIV 68

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 1720354619 541 CVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAWVRP 606
Cdd:cd20415    31 CVALFEDGAWYRARIIGLPGHREVEVKYVDFGNTATVTIKHVRKIKDDFLSLPEKARECRLAFIEP 96

fourth 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 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 1720354619 479 TLVGVFVEYIISPSQFYIRIYSRdsSELLEDMMIEMRRCYSNQlvSDRYimpeyfiQPGHLCCV-KISEDKWWYRVIIHR 557
Cdd:cd20439    10 SVVDVKCSYVNSPGDFWCQLQTK--SSELKSLMKQIQSYYLIH--NDPY-------KHGQIACVaKYSKDGKWYRAAVLK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1720354619 558 ILGKKEVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSL 601
Cdd:cd20439    79 QVSAKEVDVIFVDYGNQERVLISDLRAIKPQFLLLEGQAFRCSL 122

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 1720354619 483 VFVEYIISPSQFYIRIySRDSSelledmMIEMRRCYSNQLVSDryIMP-EYFIQPGHLCCVKISeDKWWYRVIIhrILGK 561
Cdd:cd20424    16 VYITYVNDPWTFYCQL-ARNAG------VLDQLASAISRLSSE--IRKlELSVNPGTLCLAKYS-DQHWYRGII--ITNK 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720354619 562 KEVEVFYPDFGNIGTVQKSSLRFL---KCCYTKLPAQAIPCSL 601
Cdd:cd20424    84 NSTEVFFVDYGNTEKVEKEDMLPIpsdAYELLLLPMQAIKCSL 126

fifth 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 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 1720354619 483 VFVEYIISPSQFYIRIySRDSsELLEDMMIEMRRcYSNQLVSDRYIMPEyfiqpGHLCCVKISEDKWWYRVIIHRILGKK 562
Cdd:cd20440    14 VYITHVYSPAKFYCQL-DRNT-EILEALMEKIAE-ISKLFNSQILDNCK-----TRLCLAKYFEDGQWYRALAHPVESSS 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720354619 563 EVEVFYPDFGNIGTVQKSSLRFLKCCYTKL---PAQAIPCSL 601
Cdd:cd20440    86 HLSVYFVDYGNKQIVEKNEVLPIPDTAVDLlltPMQAIKCCL 127

Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, also called Tudor and KH domain-containing protein (TDRKH), participates in the primary piwi-interacting RNA (piRNA) biogenesis pathway and is required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for germline integrity. The family also includes the TDRD2 homolog found in Drosophila melanogaster (dTDRKH), which is also called partner of PIWIs protein, or PAPI, and is involved in Zucchini-mediated piRNA 3'-end maturation. TDRD2 contains two KH 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 1720354619 507 LEDMMIEMRRCYSnqlvSDRYIMPEYFIQPGHLCCVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFLK 586
Cdd:cd20412     6 LDKLVQEMTQYYE----SEENRHTLLTVQVGDIVAAPFRHDGSWYRARVLGFLENGNLDLYFVDYGDSGYVPLEDLRALR 81

                          90
                  ....*....|....
gi 1720354619 587 CCYTKLPAQAIPCS 600
Cdd:cd20412    82 SDFLSLPFQAIECS 95

Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, also called Staphylococcal nuclease domain-containing protein 1 (SND1), 100 kDa coactivator, EBNA2 coactivator p100, or p100 co-activator, is a multifunctional protein that is reportedly associated with different types of RNA molecules, including mRNA, miRNA, pre-miRNA, and dsRNA. It has been implicated in a number of biological processes in eukaryotic cells, including the cell cycle, DNA damage repair, proliferation, and apoptosis. TDRD11 is overexpressed in multiple cancers and functions as an oncogene. It contains multiple Staphylococcal nuclease (SN) domains and a C-terminal 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 1720354619 507 LEDMMIEMRRCYSNQLVsdryIMPEYFIQPGHLCCVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFLK 586
Cdd:cd20433     5 LEKLMEKLRFEIASNPP----LPGSYTPRKGDLCAAKFVEDGEWYRAKVEKVEGDKKVHVLYIDYGNREVLPSTRLAALP 80

The first LOTUS domain on Tudor-containing protein 7 (TDRD7); The first LOTUS domain on Tudor-containing protein 7 (TDRD7): TDRD7 contains three N-terminal LOTUS domains and three Tudor domain repeats at the C-terminus. It belongs to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD7 together with TDRD1/MTR-1, TDRD5 and TDRD6 forms a ribonucleoprotein complex in the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs) involving in RNA processing for spermatogenesis. TDRD7 is functionally essential for the differentiation of germ cells. The exact molecular function of LOTUS domain on TDRD7 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354619   9 DCLRKEIRSLLISTKDGLTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSVCPGGDGTVILKAIPDESTKGIA 88
Cdd:cd09986     2 ELVKKMLRAVLQSSKGGVSLPRLQGEYKELTGEQIPFKQLGYHTLDALLRSMPSVVRLERSRSGEVMCFASLCNETAHIA 81

                  ....*..
gi 1720354619  89 SLVAKQR 95
Cdd:cd09986    82 KLVARQR 88

seventh 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 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 1720354619 487 YIISPSQFYIRIYSRDSSELLEDMMI--EMRRCYsnqlvsdryIMPEYFIQPGHLCCVKISEDKWWYR-VIIHRILGKKE 563
Cdd:cd20442    10 SVSKNGTFYVRLLRNSEQLTDLESLIakEAKKCK---------FVPVEDIKEGLECLAKSKKNLKWYRaVVEHLYPETEK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1720354619 564 VEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAW 603
Cdd:cd20442    81 MLVFFVDHGITEVVSMGNIKQLSNDLLQIPRQAVLCRWNW 120

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 1720354619 298 KIQFVVSKFPQG-LFISKLLGEFELTFKEQLSPKQLGFLNVTELVGALSDILRVEFSEERQDLL 360
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 1720354619 127 PAVVKSELKDLLALSP--VLLSDFEKAFARRFGRSFQYMQYGFLSMFEVLNAASDVISVEQTRAGSLLTL 194
Cdd:cd08824     1 LKQLAKQLRSLLQSYPggLPLSKLPQLYKKKFGKPLDLSEYGFSKLSDLLEALPGVVIVLSQGGERIVSL 70

second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; TDRD12, also called ES cell-associated transcript 8 protein (ECAT8), is a putative ATP-dependent DEAD-like RNA helicase that is essential for germ cell development and maintenance. It acts as a unique piRNA biogenesis factor essential for secondary PIWI interacting RNA (piRNA) biogenesis. TDRD12 contains two Tudor domains, one at the N-terminus and the other at the C-terminal end. The model corresponds to the second/C-terminal 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 1720354619 490 SPSQFYIRIYS---------RDSSELLEDMMIEMRRCYSNQlvSDRyiMPEYFIQPGHLCCVKISEDKWwYRVIIHRIL- 559
Cdd:cd20435     1 DATHYSARILEhrssdgevtKSMSSTYLKLSMKLNMYYSDP--SNR--ILHGKVKVGDLCAVEDENNLY-HRVKVLEITe 75

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gi 1720354619 560 -----GKKEVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAI 597
Cdd:cd20435    76 kddktKPREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAV 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.

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gi 1720354619  11 LRKEIRSLLISTKDGLTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSV 66
Cdd:cd09976     4 LREEIRKVVENHPNGLFIALLPTEYKVLFKEELPVKQLGFLSVTELVGSLSDILAI 59

third 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 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 1720354619 507 LEDMMIEMRRCYSNQlvSDRYIMpeyfIQPGHLCCVKIseDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFLK 586
Cdd:cd20429     9 LEVLMEEMILYYNKT--EERPVA----IEKNKVYAAKI--ENNWYRVLVKGILTNGLVSVYELDYGKHELVSIRKVQPLI 80

                          90
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gi 1720354619 587 CCYTKLPAQAI 597
Cdd:cd20429    81 EKFRQLPFQAI 91

Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), 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. It contains a C-terminal 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 1720354619 534 IQPGhLCCVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAWVRP 606
Cdd:cd20407     5 IEVG-VICAAPVMNAWYRAQVVGVFEETDEVEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATECYLANIEP 76

Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain.

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gi 1720354619 545 SEDKWWYRVIIHRILGKKEVEVFYpDFGNIGTVQKSSLR 583
Cdd:cd04508     9 SDDGQWYPATVVAVNDDGKYTVLF-DDGNEEEVSEDDIR 46