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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781256  918 QPWQEIHKLEVLMEEMILYYSVSEERHIAVERDQVYAAKVENKWYRVLLKGILTNGLVSVYELDYGKHELVNIRKVQPLV 997
Cdd:cd20429      1 QPWQELHKLEVLMEEMILYYNKTEERPVAIEKNKVYAAKIENNWYRVLVKGILTNGLVSVYELDYGKHELVSIRKVQPLI 80

                           90
                   ....*....|.
gi 1241781256  998 DVFRKLPFQAV 1008
Cdd:cd20429     81 EKFRQLPFQAI 91

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 1241781256    5 DLVSKMLRAVLQSHKNGIVLPRLQGEYRSLTGDWIPFKQLGYPTLEAYLRSVPAVVRIEASRSGEIVCYAVACTETARIA 84
Cdd:cd09986      2 ELVKKMLRAVLQSSKGGVSLPRLQGEYKELTGEQIPFKQLGYHTLDALLRSMPSVVRLERSRSGEVMCFASLCNETAHIA 81

                   ....*..
gi 1241781256   85 QLVARQR 91
Cdd:cd09986     82 KLVARQR 88

The third LOTUS domain on Tudor-containing protein 7 (TDRD7); The third 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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1241781256  328 DVKEKVAELLGKYSSGLWASALPKAFEDMYKVKFPEDALKNLASLSDVCTINYISGNTQKAILYA 392
Cdd:cd09974      3 DLKEKVAQLLVKYSNGLWASALPKLFEDAYKVKFPEHILENLSLLTDICIVDYPSGNPQKAILYS 67

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781256  918 QPWQEIHKLEVLMEEMILYYSVSEERHIAVERDQVYAAKVENKWYRVLLKGILTNGLVSVYELDYGKHELVNIRKVQPLV 997
Cdd:cd20429      1 QPWQELHKLEVLMEEMILYYNKTEERPVAIEKNKVYAAKIENNWYRVLVKGILTNGLVSVYELDYGKHELVSIRKVQPLI 80

                           90
                   ....*....|.
gi 1241781256  998 DVFRKLPFQAV 1008
Cdd:cd20429     81 EKFRQLPFQAI 91

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 1241781256    5 DLVSKMLRAVLQSHKNGIVLPRLQGEYRSLTGDWIPFKQLGYPTLEAYLRSVPAVVRIEASRSGEIVCYAVACTETARIA 84
Cdd:cd09986      2 ELVKKMLRAVLQSSKGGVSLPRLQGEYKELTGEQIPFKQLGYHTLDALLRSMPSVVRLERSRSGEVMCFASLCNETAHIA 81

                   ....*..
gi 1241781256   85 QLVARQR 91
Cdd:cd09986     82 KLVARQR 88

The third LOTUS domain on Tudor-containing protein 7 (TDRD7); The third 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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1241781256  328 DVKEKVAELLGKYSSGLWASALPKAFEDMYKVKFPEDALKNLASLSDVCTINYISGNTQKAILYA 392
Cdd:cd09974      3 DLKEKVAQLLVKYSNGLWASALPKLFEDAYKVKFPEHILENLSLLTDICIVDYPSGNPQKAILYS 67

Tudor domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781256  640 MYTNVKVTNICSDGTLYCQvPCKGLNKLNDLLHKTEDYFHCKHMTSEYfiSLPFCGKICLFHCKGKWLRVEITNVHSSRA 719
Cdd:pfam00567    1 STIDVVVSHIESPSTFYIQ-PKSDSKKLEKLTEELQEYYASKPPESLP--PAVGDGCVAAFSEDGKWYRAKITESLDDGL 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1241781256  720 LDVQFLDSGNSTSVKVSELREIPPRFLQemlaIPPQAIKCCLAD 763
Cdd:pfam00567   78 VEVLFIDYGNTETVPLSDLRPLPPELES----LPPQAIKCQLAG 117

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 1241781256   10 MLRAVLQSHKNGIV-LPRLQGEYRSLTGDWIPFKQLGYPTLEAYLRSVPAVVRIEASRSGEIVC 72
Cdd:pfam12872    1 ELISLLRSDPDGWAsLSELGSEYRKLFGEDFDPRNYGFSKLSDLLKAIPDVFEIEKRGGGGLVV 64

Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished).

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1241781256   500 QTVHVGQLLAVNAEEDAWLRAQIIS-TDENKIKVCYVDYGFCENIEKSKAYRLNPRF 555
Cdd:smart00333    1 PTFKVGDKVAARWEDGEWYRARIVKvDGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781256  918 QPWQEIHKLEVLMEEMILYYSVSEERHIAVERDQVYAAKVENKWYRVLLKGILTNGLVSVYELDYGKHELVNIRKVQPLV 997
Cdd:cd20429      1 QPWQELHKLEVLMEEMILYYNKTEERPVAIEKNKVYAAKIENNWYRVLVKGILTNGLVSVYELDYGKHELVSIRKVQPLI 80

                           90
                   ....*....|.
gi 1241781256  998 DVFRKLPFQAV 1008
Cdd:cd20429     81 EKFRQLPFQAI 91

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 1241781256    5 DLVSKMLRAVLQSHKNGIVLPRLQGEYRSLTGDWIPFKQLGYPTLEAYLRSVPAVVRIEASRSGEIVCYAVACTETARIA 84
Cdd:cd09986      2 ELVKKMLRAVLQSSKGGVSLPRLQGEYKELTGEQIPFKQLGYHTLDALLRSMPSVVRLERSRSGEVMCFASLCNETAHIA 81

                   ....*..
gi 1241781256   85 QLVARQR 91
Cdd:cd09986     82 KLVARQR 88

The third LOTUS domain on Tudor-containing protein 7 (TDRD7); The third 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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1241781256  328 DVKEKVAELLGKYSSGLWASALPKAFEDMYKVKFPEDALKNLASLSDVCTINYISGNTQKAILYA 392
Cdd:cd09974      3 DLKEKVAQLLVKYSNGLWASALPKLFEDAYKVKFPEHILENLSLLTDICIVDYPSGNPQKAILYS 67

Tudor domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781256  900 EHMDVYVPVACHPGHFVIQPWQEIHKLEVLMEEMILYYS--VSEERHIAVERDQVYAAKVENKWYRVLLKGILTNGLVSV 977
Cdd:pfam00567    1 STIDVVVSHIESPSTFYIQPKSDSKKLEKLTEELQEYYAskPPESLPPAVGDGCVAAFSEDGKWYRAKITESLDDGLVEV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1241781256  978 YELDYGKHELVNIRKVQPLVDVFRKLPFQAVTAQLAG 1014
Cdd:pfam00567   81 LFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLAG 117

Tudor domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781256  451 ASPSVLVVELSNTNDVVIryVGKDYSAAQELMEDEMKEFYSKNPRVtPIQTVHVGQLLAVNAEEDAWLRAQII-STDENK 529
Cdd:pfam00567    1 STIDVVVSHIESPSTFYI--QPKSDSKKLEKLTEELQEYYASKPPE-SLPPAVGDGCVAAFSEDGKWYRAKITeSLDDGL 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1241781256  530 IKVCYVDYGFCENIEKSKAYRLNPRFCSLSFQATKCKLAG 569
Cdd:pfam00567   78 VEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLAG 117

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 1241781256    5 DLVSKMLRAVLQSHKNGIVLPRLQGEYRSLTGDWIPFKQLGYPTLEAYLRSVPAVVRIEASRSGEIVC 72
Cdd:cd08824      2 KQLAKQLRSLLQSYPGGLPLSKLPQLYKKKFGKPLDLSEYGFSKLSDLLEALPGVVIVLSQGGERIVS 69

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 1241781256  905 YVPVACHPGHFVIQPWQEIH--KLEVLMEEMILYYSVSE--ERHIAVER----DQVYAAKVENK--WYRVLLKGILTNGL 974
Cdd:cd20419      1 FVEYIESPSQFYVRFYSKDTseMLEDMMIEMRRCYSNEHvsERYVMPEAfiqpGQVCCVRIPEDvwWYRVIIHQVLNKQE 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1241781256  975 VSVYELDYGKHELVNIRKVQPLVDVFRKLPFQAVTAQL 1012
Cdd:cd20419     81 VEVFYPDFGDIGTVQKSRLRFLKCCYSKLPAQAIPASL 118

The second LOTUS domain on Tudor-containing protein 7 (TDRD7); The second 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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1241781256  326 MPDVKEKVAELLGKYSSGLWASALPKAFEDMYKVKFPEDALKNLASLSDVCTINYI-SGNTQKAILYA 392
Cdd:cd09973      1 VQEVQNRIKELLNKYSNGVWLSKLPQLYKEMYKEDLSTEVLKQLESWPHVCTVEKPhSGDPTDLLLYP 68

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 1241781256  476 SAAQELMEDEMKEFYSKNPRVTPIQTVHVGQLLAVNAEEDA-WLRAQIISTDEN-KIKVCYVDYGFCENIEKSKAYRLNP 553
Cdd:cd20412      3 SLQLDKLVQEMTQYYESEENRHTLLTVQVGDIVAAPFRHDGsWYRARVLGFLENgNLDLYFVDYGDSGYVPLEDLRALRS 82

                           90
                   ....*....|..
gi 1241781256  554 RFCSLSFQATKC 565
Cdd:cd20412     83 DFLSLPFQAIEC 94

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 1241781256  644 VKVTNICSDGTLYCQVP--CKGLNKLNDLLHKTEDYFHCKHMTSEYFislpfcgKICL--FHCKGKWLRVEITNVHSSRA 719
Cdd:cd20440     14 VYITHVYSPAKFYCQLDrnTEILEALMEKIAEISKLFNSQILDNCKT-------RLCLakYFEDGQWYRALAHPVESSSH 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1241781256  720 LDVQFLDSGNSTSVKVSELREIPPRFLqEMLAIPPQAIKCCL 761
Cdd:cd20440     87 LSVYFVDYGNKQIVEKNEVLPIPDTAV-DLLLTPMQAIKCCL 127

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        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781256  670 LLHKTEDyFHCKHMTSEYFISLPFCGKIC--LFHcKGKWLRVEITNVHSSRALDVQFLDSGNSTSVKVSELREIPPRFlq 747
Cdd:cd20415      4 LTKKIQE-FYKEGDDGGLEILCPVQGQACvaLFE-DGAWYRARIIGLPGHREVEVKYVDFGNTATVTIKHVRKIKDDF-- 79

                           90
                   ....*....|....*.
gi 1241781256  748 emLAIPPQAIKCCLAD 763
Cdd:cd20415     80 --LSLPEKARECRLAF 93

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 1241781256  911 HPGHFVIQPW-----QEIHKLEVLMEEMilYYSVSEERHIAVERDQVYAAK--VENKWYRVLLKGI-LTNGLVSVYELDY 982
Cdd:cd20408      8 NPGEFYIQIYtlevlESLVKLTSQLKKT--YASVNNHKEYIPEVGEVCVAKysEDQNWYRALVQTVdVQQKKAGVFYIDY 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1241781256  983 GKHELVNIRKVQPLVDVFRKLPFQAVTAQLAGVKCSQ--WSEEA 1024
Cdd:cd20408     86 GNEETVPLNRIQPLKKDIELFPPCAIKCCLANVKPPSgsWSEEC 129

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
                   ....*....|....*....|....*....|....*....|....*....
gi 1241781256  950 DQVYAAKVE--NKWYRVLLKGILTNGLVSVYELDYGKHELVNIRKVQPL 996
Cdd:cd20379      2 GDLCAAKYEedGKWYRARVLEVLSNDKVEVFFVDYGNTETVPLSDLRPL 50

second 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 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 1241781256  644 VKVTNICSDGTLYCQVPC--KGLNKLNDLLhktedYFHCKHMTSEYFISLPFCGKICLFHCK-GKWLRVEITNVHSSRAL 720
Cdd:cd20437      7 VKITAAVSPSKFYCQLLSwePELSKLTTQM-----TLHYESVSKELNPSCENFGLLCAAKGKdGQWHRGFLQQLLPPSQV 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1241781256  721 DVQFLDSGNSTSVKVSELREIPPRFlqemLAIPPQAIKCCLAD 763
Cdd:cd20437     82 KVWFIDYGNSEAVSSHSVLKLPPDF----FSLPLMSFPCSLSC 120

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
                   ....*....|....*....|....*....|....*....|....*....
gi 1241781256  695 GKICL--FHCKGKWLRVEITNVHSSRALDVQFLDSGNSTSVKVSELREI 741
Cdd:cd20379      2 GDLCAakYEEDGKWYRARVLEVLSNDKVEVFFVDYGNTETVPLSDLRPL 50

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 1241781256  646 VTNICSDGTLYCQVPC-KGLNKLNDLLHKTEDYFHCKHMTSEYfisLPFCGKICL--FHCKGKWLRVEITNVHSS-RALD 721
Cdd:cd20408      3 VTEFKNPGEFYIQIYTlEVLESLVKLTSQLKKTYASVNNHKEY---IPEVGEVCVakYSEDQNWYRALVQTVDVQqKKAG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1241781256  722 VQFLDSGNSTSVKVSELREIPPrflqEMLAIPPQAIKCCLADLPQSIGMWTPDAV 776
Cdd:cd20408     80 VFYIDYGNEETVPLNRIQPLKK----DIELFPPCAIKCCLANVKPPSGSWSEECI 130

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 1241781256  223 MDEVQNRIKEILDKHNNGIWISKLPHFYKEFYKEDLNQGVL--QQFEHWPH-ICTVEKPCGGGQDSLLY 288
Cdd:cd08824      1 LKQLAKQLRSLLQSYPGGLPLSKLPQLYKKKFGKPLDLSEYgfSKLSDLLEaLPGVVIVLSQGGERIVS 69

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
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1241781256  514 EDAWLRAQIISTDENKIKVCYVDYGFCENIEKSKAYRLNPRFCSLSFQATKCKLAG 569
Cdd:cd20411     61 DKNWYRAVVLETSDSEVKVLYADYGNTETLPLSRILPITKSHLELPFQIIRCSLAG 116

fourth 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 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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1241781256  508 LAVNAEEDAWLRAQIISTDENK--IKVCYVDYGFCENIEKSKAYRLNPRFCSLSFQATKCKLAGL 570
Cdd:cd20423     10 LAKYSEDGKWCRALIDNVYEPVemVEVTYVDYGNKELVSLKNLRSISEEFLKLKAQAFRCSLYNL 74

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1241781256  497 TPIQtvhVGQLLAVNAEeDAWLRAQIIST--DENKIKVCYVDYGFCENIEKSKAYRLNPRFCSLSFQATKCKLAGLE 571
Cdd:cd20407      3 EPIE---VGVICAAPVM-NAWYRAQVVGVfeETDEVEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATECYLANIE 75

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        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781256  485 EMKEFYSKNPR-----VTPIQtvhvGQLLAVNAEEDAWLRAQIIS-TDENKIKVCYVDYGFCENIEKSKAYRLNPRFCSL 558
Cdd:cd20415      7 KIQEFYKEGDDggleiLCPVQ----GQACVALFEDGAWYRARIIGlPGHREVEVKYVDFGNTATVTIKHVRKIKDDFLSL 82

                           90
                   ....*....|...
gi 1241781256  559 SFQATKCKLAGLE 571
Cdd:cd20415     83 PEKARECRLAFIE 95

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 1241781256  904 VYVPVACHPGHFVIQPWQEIHKLEVLMEEMILYYsvsEERHiaVERDQVYAAKV---------ENKWYR-VLLKGILTNG 973
Cdd:cd20421     15 VVVTEVTDPHRIFCQLRSLSQELKRLSESMHQYY---EGRV--GSGYETRPEKLgspcaargsDGRWYRaVLQQVFSANR 89

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1241781256  974 LVSVYELDYGKHELVNIRKVQPLVDVFRKLP 1004
Cdd:cd20421     90 VVEVLHVDYGRKEVVSVSNLRYLAPEYFRMP 120

fourth 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 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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1241781256  957 VENKWYRVLLKGILTN-GLVSVYELDYGKHELVNIRKVQPLVDVFRKLPFQAVTAQLAGVKcsQWS 1021
Cdd:cd20423     15 EDGKWCRALIDNVYEPvEMVEVTYVDYGNKELVSLKNLRSISEEFLKLKAQAFRCSLYNLI--QPS 78