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Conserved domains on  [gi|197927156|ref|NP_001128213|]
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tudor domain-containing protein 5 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tudor_TDRD5 cd20419
Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is ...
 484-601 9.73e-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.


:

Pssm-ID: 410490  Cd Length: 118  Bit Score: 238.89  E-value: 9.73e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  484 FVEYIISPSQFYIRIYSRDSSELLEDMMIEMRRCYSNQLVSDRYIMPEYFIQPGHLCCVKISEDKWWYRVIIHRILGKKE 563
Cdd:cd20419     1 FVEYIESPSQFYVRFYSKDTSEMLEDMMIEMRRCYSNEHVSERYVMPEAFIQPGQVCCVRIPEDVWWYRVIIHQVLNKQE 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 197927156  564 VEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSL 601
Cdd:cd20419    81 VEVFYPDFGDIGTVQKSRLRFLKCCYSKLPAQAIPASL 118
LOTUS_1_TDRD5 cd09985
The first LOTUS domain on Tudor-containing protein 5 (TDRD5); The first LOTUS domain on ...
 4-98 6.67e-52

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.


:

Pssm-ID: 193599  Cd Length: 95  Bit Score: 176.89  E-value: 6.67e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156    4 QERIQDCLRKEIRSLLISTKDGLTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSVCPGGDGTVILKAIPDES 83
Cdd:cd09985     1 QEQIMERLKKDVRSLLISSKNGLTPEQLEQDYLAMVGSPLPLRSLGFRSTMELVLDMPDVVRVHPQLDGTVILKAVGDET 80

                          90
                  ....*....|....*
gi 197927156   84 TKGIASLVAKQRRSH 98
Cdd:cd09985    81 TKGIEDLVSKQRDSK 95
LOTUS_3_TDRD5 cd09976
The third LOTUS domain on Tudor-containing protein 5 (TDRD5); The third LOTUS domain on ...
 292-365 2.28e-35

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.


:

Pssm-ID: 193590  Cd Length: 74  Bit Score: 128.69  E-value: 2.28e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 197927156  292 DPELKRKIQFVVSKFPQGLFISKLLGEFELTFKEQLSPKQLGFLNVTELVGALSDILRVEFSEERQDLLVFDAD 365
Cdd:cd09976     1 SRELREEIRKVVENHPNGLFIALLPTEYKVLFKEELPVKQLGFLSVTELVGSLSDILAIERREKESDWLVFDAK 74
LOTUS_2_TDRD5 cd09975
The second LOTUS domain on Tudor-containing protein 5 (TDRD5); The second LOTUS domain on ...
 127-196 5.48e-35

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.


:

Pssm-ID: 193589  Cd Length: 70  Bit Score: 127.69  E-value: 5.48e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  127 PAVVKSELKDLLALSPVLLSDFEKAFARRFGRSFQYMQYGFLSMFEVLNAASDVISVEQTRAGSLLTLKK 196
Cdd:cd09975     1 PAHVKSELKDLLSHSPVLLSELEKAYVARFGRSFQYTQYGFFSMLEVLSAASDFIIVKQTRTGSLLLLKK 70
 
Name Accession Description Interval E-value
Tudor_TDRD5 cd20419
Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is ...
 484-601 9.73e-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.


Pssm-ID: 410490  Cd Length: 118  Bit Score: 238.89  E-value: 9.73e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  484 FVEYIISPSQFYIRIYSRDSSELLEDMMIEMRRCYSNQLVSDRYIMPEYFIQPGHLCCVKISEDKWWYRVIIHRILGKKE 563
Cdd:cd20419     1 FVEYIESPSQFYVRFYSKDTSEMLEDMMIEMRRCYSNEHVSERYVMPEAFIQPGQVCCVRIPEDVWWYRVIIHQVLNKQE 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 197927156  564 VEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSL 601
Cdd:cd20419    81 VEVFYPDFGDIGTVQKSRLRFLKCCYSKLPAQAIPASL 118
LOTUS_1_TDRD5 cd09985
The first LOTUS domain on Tudor-containing protein 5 (TDRD5); The first LOTUS domain on ...
 4-98 6.67e-52

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.


Pssm-ID: 193599  Cd Length: 95  Bit Score: 176.89  E-value: 6.67e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156    4 QERIQDCLRKEIRSLLISTKDGLTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSVCPGGDGTVILKAIPDES 83
Cdd:cd09985     1 QEQIMERLKKDVRSLLISSKNGLTPEQLEQDYLAMVGSPLPLRSLGFRSTMELVLDMPDVVRVHPQLDGTVILKAVGDET 80

                          90
                  ....*....|....*
gi 197927156   84 TKGIASLVAKQRRSH 98
Cdd:cd09985    81 TKGIEDLVSKQRDSK 95
LOTUS_3_TDRD5 cd09976
The third LOTUS domain on Tudor-containing protein 5 (TDRD5); The third LOTUS domain on ...
 292-365 2.28e-35

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.


Pssm-ID: 193590  Cd Length: 74  Bit Score: 128.69  E-value: 2.28e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 197927156  292 DPELKRKIQFVVSKFPQGLFISKLLGEFELTFKEQLSPKQLGFLNVTELVGALSDILRVEFSEERQDLLVFDAD 365
Cdd:cd09976     1 SRELREEIRKVVENHPNGLFIALLPTEYKVLFKEELPVKQLGFLSVTELVGSLSDILAIERREKESDWLVFDAK 74
LOTUS_2_TDRD5 cd09975
The second LOTUS domain on Tudor-containing protein 5 (TDRD5); The second LOTUS domain on ...
 127-196 5.48e-35

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.


Pssm-ID: 193589  Cd Length: 70  Bit Score: 127.69  E-value: 5.48e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  127 PAVVKSELKDLLALSPVLLSDFEKAFARRFGRSFQYMQYGFLSMFEVLNAASDVISVEQTRAGSLLTLKK 196
Cdd:cd09975     1 PAHVKSELKDLLSHSPVLLSELEKAYVARFGRSFQYTQYGFFSMLEVLSAASDFIIVKQTRTGSLLLLKK 70
TUDOR pfam00567
Tudor domain;
483-602 6.97e-22

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 91.65  E-value: 6.97e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156   483 VFVEYIISPSQFYIRiySRDSSELLEDMMIEMRRCYSNQLvsdryiMPEYFIQPGHLCCVKISEDKWWYRVIIHRILGKK 562
Cdd:pfam00567    5 VVVSHIESPSTFYIQ--PKSDSKKLEKLTEELQEYYASKP------PESLPPAVGDGCVAAFSEDGKWYRAKITESLDDG 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 197927156   563 EVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLA 602
Cdd:pfam00567   77 LVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
OST-HTH pfam12872
OST-HTH/LOTUS domain; A predicted RNA-binding domain found in insect Oskar and vertebrate ...
 14-76 8.17e-10

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.


Pssm-ID: 463735  Cd Length: 64  Bit Score: 55.64  E-value: 8.17e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 197927156    14 EIRSLLISTKDG-LTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSVCPGGDGTVIL 76
Cdd:pfam12872    1 ELISLLRSDPDGwASLSELGSEYRKLFGEDFDPRNYGFSKLSDLLKAIPDVFEIEKRGGGGLVV 64
OST-HTH pfam12872
OST-HTH/LOTUS domain; A predicted RNA-binding domain found in insect Oskar and vertebrate ...
 133-193 6.00e-08

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.


Pssm-ID: 463735  Cd Length: 64  Bit Score: 50.25  E-value: 6.00e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 197927156   133 ELKDLLALSP---VLLSDFEKAFARRFGRSFQYMQYGFLSMFEVLNAASDVISVEQTRAGSLLT 193
Cdd:pfam12872    1 ELISLLRSDPdgwASLSELGSEYRKLFGEDFDPRNYGFSKLSDLLKAIPDVFEIEKRGGGGLVV 64
OST-HTH pfam12872
OST-HTH/LOTUS domain; A predicted RNA-binding domain found in insect Oskar and vertebrate ...
 298-360 3.90e-07

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.


Pssm-ID: 463735  Cd Length: 64  Bit Score: 47.94  E-value: 3.90e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 197927156   298 KIQFVVSKFPQG-LFISKLLGEFELTFKEQLSPKQLGFLNVTELVGALSDILRVEFSEERQDLL 360
Cdd:pfam12872    1 ELISLLRSDPDGwASLSELGSEYRKLFGEDFDPRNYGFSKLSDLLKAIPDVFEIEKRGGGGLVV 64
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 534-587 6.19e-07

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).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 47.27  E-value: 6.19e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 197927156    534 IQPGHLCCVKIsEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFLKC 587
Cdd:smart00333    3 FKVGDKVAARW-EDGEWYRARIVKVDGEQLYEVFFIDYGNEEVVPPSDLRQLPE 55
 
Name Accession Description Interval E-value
Tudor_TDRD5 cd20419
Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is ...
 484-601 9.73e-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.


Pssm-ID: 410490  Cd Length: 118  Bit Score: 238.89  E-value: 9.73e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  484 FVEYIISPSQFYIRIYSRDSSELLEDMMIEMRRCYSNQLVSDRYIMPEYFIQPGHLCCVKISEDKWWYRVIIHRILGKKE 563
Cdd:cd20419     1 FVEYIESPSQFYVRFYSKDTSEMLEDMMIEMRRCYSNEHVSERYVMPEAFIQPGQVCCVRIPEDVWWYRVIIHQVLNKQE 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 197927156  564 VEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSL 601
Cdd:cd20419    81 VEVFYPDFGDIGTVQKSRLRFLKCCYSKLPAQAIPASL 118
LOTUS_1_TDRD5 cd09985
The first LOTUS domain on Tudor-containing protein 5 (TDRD5); The first LOTUS domain on ...
 4-98 6.67e-52

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.


Pssm-ID: 193599  Cd Length: 95  Bit Score: 176.89  E-value: 6.67e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156    4 QERIQDCLRKEIRSLLISTKDGLTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSVCPGGDGTVILKAIPDES 83
Cdd:cd09985     1 QEQIMERLKKDVRSLLISSKNGLTPEQLEQDYLAMVGSPLPLRSLGFRSTMELVLDMPDVVRVHPQLDGTVILKAVGDET 80

                          90
                  ....*....|....*
gi 197927156   84 TKGIASLVAKQRRSH 98
Cdd:cd09985    81 TKGIEDLVSKQRDSK 95
LOTUS_3_TDRD5 cd09976
The third LOTUS domain on Tudor-containing protein 5 (TDRD5); The third LOTUS domain on ...
 292-365 2.28e-35

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.


Pssm-ID: 193590  Cd Length: 74  Bit Score: 128.69  E-value: 2.28e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 197927156  292 DPELKRKIQFVVSKFPQGLFISKLLGEFELTFKEQLSPKQLGFLNVTELVGALSDILRVEFSEERQDLLVFDAD 365
Cdd:cd09976     1 SRELREEIRKVVENHPNGLFIALLPTEYKVLFKEELPVKQLGFLSVTELVGSLSDILAIERREKESDWLVFDAK 74
LOTUS_2_TDRD5 cd09975
The second LOTUS domain on Tudor-containing protein 5 (TDRD5); The second LOTUS domain on ...
 127-196 5.48e-35

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.


Pssm-ID: 193589  Cd Length: 70  Bit Score: 127.69  E-value: 5.48e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  127 PAVVKSELKDLLALSPVLLSDFEKAFARRFGRSFQYMQYGFLSMFEVLNAASDVISVEQTRAGSLLTLKK 196
Cdd:cd09975     1 PAHVKSELKDLLSHSPVLLSELEKAYVARFGRSFQYTQYGFFSMLEVLSAASDFIIVKQTRTGSLLLLKK 70
LOTUS_TDRD_OSKAR cd09972
The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7; The first LOTUS domain ...
 9-95 3.74e-31

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.


Pssm-ID: 193586  Cd Length: 87  Bit Score: 117.21  E-value: 3.74e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156    9 DCLRKEIRSLLISTKDGLTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSVCpGGDGTVILKAIPDESTKGIA 88
Cdd:cd09972     2 EEVKKVLRSLLISSKGGLTLSELERDYRELEGEPIPYRKLGYSSLEDFLRSIPDVVTVR-SSGGEVLVKAVADEKTAHIA 80


                  ....*..
gi 197927156   89 SLVAKQR 95
Cdd:cd09972    81 SLVAKQK 87
Tudor_TDRD15_rpt3 cd20438
third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 484-621 8.76e-24

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.


Pssm-ID: 410509  Cd Length: 141  Bit Score: 98.32  E-value: 8.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  484 FVEYIISPSQFYIRI--YSRDSSELLEDMMIEMRRCYSNQLVSDRyimPEyfiqPGHLCCVKISEDKWWYRVIIHRILGK 561
Cdd:cd20438    10 FVEYVLNPSNFWIRTdeYNNEFQALMKNIADIYNLCGNDEELLKK---PE----PGLLCCARYSKDRHYYRAVITEVLDL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  562 KeVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAWVRPAEEHWTARAILHFQK 621
Cdd:cd20438    83 K-VSVYFLDFGNTDTVPFYDVKTLLPEFSELPALAMCCSLAHVFPVEEVWTKNANDFFKK 141
TUDOR pfam00567
Tudor domain;
483-602 6.97e-22

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 91.65  E-value: 6.97e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156   483 VFVEYIISPSQFYIRiySRDSSELLEDMMIEMRRCYSNQLvsdryiMPEYFIQPGHLCCVKISEDKWWYRVIIHRILGKK 562
Cdd:pfam00567    5 VVVSHIESPSTFYIQ--PKSDSKKLEKLTEELQEYYASKP------PESLPPAVGDGCVAAFSEDGKWYRAKITESLDDG 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 197927156   563 EVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLA 602
Cdd:pfam00567   77 LVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 483-616 1.18e-20

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.


Pssm-ID: 410479  Cd Length: 130  Bit Score: 88.97  E-value: 1.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  483 VFVEYIISPSQFYIRIYSRDSSELLEDMMIEMRRCYSNQLVSDRYImPEYfiqpGHLCCVKISEDKWWYRVIIHRI-LGK 561
Cdd:cd20408     1 GTVTEFKNPGEFYIQIYTLEVLESLVKLTSQLKKTYASVNNHKEYI-PEV----GEVCVAKYSEDQNWYRALVQTVdVQQ 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 197927156  562 KEVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAWVRPAEEHWTARAI 616
Cdd:cd20408    76 KKAGVFYIDYGNEETVPLNRIQPLKKDIELFPPCAIKCCLANVKPPSGSWSEECI 130
Tudor_TDRD6_rpt3 cd20422
third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 483-621 4.60e-19

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.


Pssm-ID: 410493  Cd Length: 135  Bit Score: 84.48  E-value: 4.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  483 VFVEYIISPSQFYIRIysRDSSELLEDMMIEMRRCYSNQLVSDRYIMPEyfiQPGHLCCVKISEDKWwYRVIIHRILGKK 562
Cdd:cd20422     4 AQVEFVKDPSEFWIRL--GEHAVPFSKLMRSMTAFYSQASKLDGVVLKP---QPGQLCCAKWKEDRY-YRAIVTAVKGKM 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 197927156  563 eVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAWVRPAEEHWTARAILHFQK 621
Cdd:cd20422    78 -VEVFLVDRGNTEMVDWYDVKKLLPQFRELPALALKCCLADICPLGERWSPEAISAFKR 135
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 536-585 2.59e-15

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.


Pssm-ID: 410450  Cd Length: 50  Bit Score: 70.62  E-value: 2.59e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 197927156  536 PGHLCCVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFL 585
Cdd:cd20379     1 VGDLCAAKYEEDGKWYRARVLEVLSNDKVEVFFVDYGNTETVPLSDLRPL 50
Tudor_TDRD1_rpt4 cd20411
fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 488-602 4.18e-14

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.


Pssm-ID: 410482  Cd Length: 116  Bit Score: 69.78  E-value: 4.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  488 IISPSQFYI-RIYSRDSSELLEDMMIEMRRCYSNQLVSDRYImPeyfiQPGHLCCVKISEDKWWYRVIIHRIlGKKEVEV 566
Cdd:cd20411     6 VISPDLFYAlPKTGQVNVEKLKALMTELAEYCSKQSVPQQFR-P----RIGDACCARFTGDKNWYRAVVLET-SDSEVKV 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 197927156  567 FYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLA 602
Cdd:cd20411    80 LYADYGNTETLPLSRILPITKSHLELPFQIIRCSLA 115
Tudor_TDRD6_rpt2 cd20421
second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 473-601 9.65e-13

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.


Pssm-ID: 410492  Cd Length: 130  Bit Score: 66.29  E-value: 9.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  473 PPLDTSTLVGVFVEYIISPSQFYIRIysRDSSELLEDMMIEMRRCYSNQLVSDRYIMPEyfiQPGHLCCVKiSEDKWWYR 552
Cdd:cd20421     5 PQLQVGVTETVVVTEVTDPHRIFCQL--RSLSQELKRLSESMHQYYEGRVGSGYETRPE---KLGSPCAAR-GSDGRWYR 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 197927156  553 VIIHRIL-GKKEVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSL 601
Cdd:cd20421    79 AVLQQVFsANRVVEVLHVDYGRKEVVSVSNLRYLAPEYFRMPVVTYPCAL 128
Tudor_TDRD6_rpt7 cd20426
seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 484-619 1.06e-12

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.


Pssm-ID: 410497  Cd Length: 140  Bit Score: 66.37  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  484 FVEYIISPSQFYIRiYSRDSSELLEDMMIEMRRcysnQLVSDRYIMPEyfIQPGHLCCVKISEDKWWYRVIIHRILGKKe 563
Cdd:cd20426     4 YATAVDSPEYFWCQ-FATEKIQCLAVKVQEAGE----QVADRGNFIPS--IYVGDPCIVKYSEDNHWYRALVTKINDNL- 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 197927156  564 VEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAWVRPAEEHWTARAILHF 619
Cdd:cd20426    76 VSVRFVDYGNEEDVVREQVRALPSELLKIPVQAFPCCLSGFNLSEGLWSDEANDYF 131
LOTUS cd08824
LOTUS is an uncharacterized small globular domain found in Limkain b1, Oskar and ...
 9-75 2.69e-12

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.


Pssm-ID: 193585 [Multi-domain]  Cd Length: 70  Bit Score: 63.02  E-value: 2.69e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 197927156    9 DCLRKEIRSLLISTKDGLTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSVCPGGDGTVI 75
Cdd:cd08824     2 KQLAKQLRSLLQSYPGGLPLSKLPQLYKKKFGKPLDLSEYGFSKLSDLLEALPGVVIVLSQGGERIV 68
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 541-606 3.07e-11

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.


Pssm-ID: 410486  Cd Length: 96  Bit Score: 60.91  E-value: 3.07e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 197927156  541 CVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAWVRP 606
Cdd:cd20415    31 CVALFEDGAWYRARIIGLPGHREVEVKYVDFGNTATVTIKHVRKIKDDFLSLPEKARECRLAFIEP 96
Tudor_TDRD15_rpt2 cd20437
second Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 489-602 3.39e-11

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.


Pssm-ID: 410508  Cd Length: 120  Bit Score: 61.28  E-value: 3.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  489 ISPSQFYIRIYSrdSSELLEDMMIEMRRCY---SNQLVSdryiMPEYFiqpGHLCCVKiSEDKWWYRVIIHRILGKKEVE 565
Cdd:cd20437    13 VSPSKFYCQLLS--WEPELSKLTTQMTLHYesvSKELNP----SCENF---GLLCAAK-GKDGQWHRGFLQQLLPPSQVK 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 197927156  566 VFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLA 602
Cdd:cd20437    83 VWFIDYGNSEAVSSHSVLKLPPDFFSLPLMSFPCSLS 119
Tudor_TDRD15_rpt4 cd20439
fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 479-601 4.03e-11

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.


Pssm-ID: 410510  Cd Length: 125  Bit Score: 61.35  E-value: 4.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  479 TLVGVFVEYIISPSQFYIRIYSRdsSELLEDMMIEMRRCYSNQlvSDRYimpeyfiQPGHLCCV-KISEDKWWYRVIIHR 557
Cdd:cd20439    10 SVVDVKCSYVNSPGDFWCQLQTK--SSELKSLMKQIQSYYLIH--NDPY-------KHGQIACVaKYSKDGKWYRAAVLK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 197927156  558 ILGKKEVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSL 601
Cdd:cd20439    79 QVSAKEVDVIFVDYGNQERVLISDLRAIKPQFLLLEGQAFRCSL 122
Tudor_TDRD6_rpt6 cd20425
sixth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 483-601 4.49e-11

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.


Pssm-ID: 410496  Cd Length: 115  Bit Score: 60.93  E-value: 4.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  483 VFVEYIISPSQFYIRIySRDSSELLedMMIEmrrCYSNQLVSDRYIMPEYFiQPGHLCCVKISEDKWWYRVIIHRILGKK 562
Cdd:cd20425     4 VYVSHVNSPSDFYVQL-AQDEDELS--MISE---KLNASKANDEEVECESL-QLGDLICAEYPEDGLWYRAVVKEKIPNN 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 197927156  563 EVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSL 601
Cdd:cd20425    77 LVSVQFIDYGNTSVVQPSKIHRLPKELLSIPALSIHCFL 115
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 534-601 3.43e-10

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.


Pssm-ID: 410494  Cd Length: 80  Bit Score: 57.11  E-value: 3.43e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 197927156  534 IQPGHLCCVKISEDKWWYRVIIHRI-LGKKEVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSL 601
Cdd:cd20423     3 SLPNPVCLAKYSEDGKWCRALIDNVyEPVEMVEVTYVDYGNKELVSLKNLRSISEEFLKLKAQAFRCSL 71
Tudor_TDRD6_rpt5 cd20424
fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 483-601 4.98e-10

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.


Pssm-ID: 410495  Cd Length: 126  Bit Score: 58.28  E-value: 4.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  483 VFVEYIISPSQFYIRIySRDSSelledmMIEMRRCYSNQLVSDryIMP-EYFIQPGHLCCVKISeDKWWYRVIIhrILGK 561
Cdd:cd20424    16 VYITYVNDPWTFYCQL-ARNAG------VLDQLASAISRLSSE--IRKlELSVNPGTLCLAKYS-DQHWYRGII--ITNK 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 197927156  562 KEVEVFYPDFGNIGTVQKSSLRFL---KCCYTKLPAQAIPCSL 601
Cdd:cd20424    84 NSTEVFFVDYGNTEKVEKEDMLPIpsdAYELLLLPMQAIKCSL 126
Tudor_TDRD15_rpt6 cd20441
sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 490-602 5.96e-10

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.


Pssm-ID: 410512  Cd Length: 108  Bit Score: 57.44  E-value: 5.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  490 SPSQFYIRIySRDSSELLeDMMIEM-------RRCYSNQLVSDRYIMPEYfiqpghlccvkiSEDKWWYRVIIHRILGKK 562
Cdd:cd20441     1 SPSRFFIQL-SEDEKVIL-QLAEELnetseksRENAAVKLKVGDLVAAEY------------DEDLALYRAVITAVLPGK 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 197927156  563 EVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLA 602
Cdd:cd20441    67 SFKVEFIDYGNTAVVDKSNIYTLQEKFLSLPRLSIPCSLS 106
Tudor_TDRD15_rpt5 cd20440
fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 483-601 6.22e-10

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.


Pssm-ID: 410511  Cd Length: 127  Bit Score: 57.85  E-value: 6.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  483 VFVEYIISPSQFYIRIySRDSsELLEDMMIEMRRcYSNQLVSdryimPEYFIQPGHLCCVKISEDKWWYRVIIHRILGKK 562
Cdd:cd20440    14 VYITHVYSPAKFYCQL-DRNT-EILEALMEKIAE-ISKLFNS-----QILDNCKTRLCLAKYFEDGQWYRALAHPVESSS 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 197927156  563 EVEVFYPDFGNIGTVQKSSLRFLKCCYTKL---PAQAIPCSL 601
Cdd:cd20440    86 HLSVYFVDYGNKQIVEKNEVLPIPDTAVDLlltPMQAIKCCL 127
OST-HTH pfam12872
OST-HTH/LOTUS domain; A predicted RNA-binding domain found in insect Oskar and vertebrate ...
 14-76 8.17e-10

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.


Pssm-ID: 463735  Cd Length: 64  Bit Score: 55.64  E-value: 8.17e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 197927156    14 EIRSLLISTKDG-LTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSVCPGGDGTVIL 76
Cdd:pfam12872    1 ELISLLRSDPDGwASLSELGSEYRKLFGEDFDPRNYGFSKLSDLLKAIPDVFEIEKRGGGGLVV 64
Tudor_TDRD2 cd20412
Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, ...
 507-600 1.72e-08

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.


Pssm-ID: 410483  Cd Length: 95  Bit Score: 53.07  E-value: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  507 LEDMMIEMRRCYSnqlvSDRYIMPEYFIQPGHLCCVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFLK 586
Cdd:cd20412     6 LDKLVQEMTQYYE----SEENRHTLLTVQVGDIVAAPFRHDGSWYRARVLGFLENGNLDLYFVDYGDSGYVPLEDLRALR 81

                          90
                  ....*....|....
gi 197927156  587 CCYTKLPAQAIPCS 600
Cdd:cd20412    82 SDFLSLPFQAIECS 95
Tudor_TDRD7_rpt1 cd20427
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 505-606 5.25e-08

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.


Pssm-ID: 410498  Cd Length: 98  Bit Score: 51.66  E-value: 5.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  505 ELLEDmmiEMRRCYSNqlvsDRYIMPEYFIQPGHLCCVKISEDKWwYRVIIHRILGKKeVEVFYPDFGNIGTVQKSSLRF 584
Cdd:cd20427     1 EQMED---EMKEFYSK----SSTAMCLRSPSVGQLVAVKAEEDAW-LRAQVIEVEEDK-VKVYYVDHGFSEVVERSKLFK 71

                          90       100
                  ....*....|....*....|..
gi 197927156  585 LKCCYTKLPAQAIPCSLAWVRP 606
Cdd:cd20427    72 LNKQFYSLPFQATKCKLAGLEP 93
LOTUS cd08824
LOTUS is an uncharacterized small globular domain found in Limkain b1, Oskar and ...
 294-356 5.65e-08

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.


Pssm-ID: 193585 [Multi-domain]  Cd Length: 70  Bit Score: 50.70  E-value: 5.65e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 197927156  294 ELKRKIQFVVSKFPQGLFISKLLGEFELTFKEQLSPKQLGFLNVTELVGALSDILRVEFSEER 356
Cdd:cd08824     3 QLAKQLRSLLQSYPGGLPLSKLPQLYKKKFGKPLDLSEYGFSKLSDLLEALPGVVIVLSQGGE 65
OST-HTH pfam12872
OST-HTH/LOTUS domain; A predicted RNA-binding domain found in insect Oskar and vertebrate ...
 133-193 6.00e-08

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.


Pssm-ID: 463735  Cd Length: 64  Bit Score: 50.25  E-value: 6.00e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 197927156   133 ELKDLLALSP---VLLSDFEKAFARRFGRSFQYMQYGFLSMFEVLNAASDVISVEQTRAGSLLT 193
Cdd:pfam12872    1 ELISLLRSDPdgwASLSELGSEYRKLFGEDFDPRNYGFSKLSDLLKAIPDVFEIEKRGGGGLVV 64
Tudor_TDRD15_rpt7 cd20442
seventh Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 487-610 7.17e-08

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.


Pssm-ID: 410513  Cd Length: 160  Bit Score: 53.12  E-value: 7.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  487 YIISPSQFYIRIYSRDSSELLEDMMI--EMRRCYsnqlvsdryIMPEYFIQPGHLCCVKISEDKWWYR-VIIHRILGKKE 563
Cdd:cd20442    10 SVSKNGTFYVRLLRNSEQLTDLESLIakEAKKCK---------FVPVEDIKEGLECLAKSKKNLKWYRaVVEHLYPETEK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 197927156  564 VEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAWVRPAEEH 610
Cdd:cd20442    81 MLVFFVDHGITEVVSMGNIKQLSNDLLQIPRQAVLCRWNWPESSKEL 127
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
 507-586 7.82e-08

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.


Pssm-ID: 410504 [Multi-domain]  Cd Length: 84  Bit Score: 50.76  E-value: 7.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  507 LEDMMIEMRRCYSNQLVsdryIMPEYFIQPGHLCCVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFLK 586
Cdd:cd20433     5 LEKLMEKLRFEIASNPP----LPGSYTPRKGDLCAAKFVEDGEWYRAKVEKVEGDKKVHVLYIDYGNREVLPSTRLAALP 80
LOTUS_1_TDRD7 cd09986
The first LOTUS domain on Tudor-containing protein 7 (TDRD7); The first LOTUS domain on ...
 9-95 8.27e-08

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.


Pssm-ID: 193600  Cd Length: 88  Bit Score: 50.96  E-value: 8.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156    9 DCLRKEIRSLLISTKDGLTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSVCPGGDGTVILKAIPDESTKGIA 88
Cdd:cd09986     2 ELVKKMLRAVLQSSKGGVSLPRLQGEYKELTGEQIPFKQLGYHTLDALLRSMPSVVRLERSRSGEVMCFASLCNETAHIA 81


                  ....*..
gi 197927156   89 SLVAKQR 95
Cdd:cd09986    82 KLVARQR 88
OST-HTH pfam12872
OST-HTH/LOTUS domain; A predicted RNA-binding domain found in insect Oskar and vertebrate ...
 298-360 3.90e-07

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.


Pssm-ID: 463735  Cd Length: 64  Bit Score: 47.94  E-value: 3.90e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 197927156   298 KIQFVVSKFPQG-LFISKLLGEFELTFKEQLSPKQLGFLNVTELVGALSDILRVEFSEERQDLL 360
Cdd:pfam12872    1 ELISLLRSDPDGwASLSELGSEYRKLFGEDFDPRNYGFSKLSDLLKAIPDVFEIEKRGGGGLVV 64
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 490-611 4.16e-07

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.


Pssm-ID: 410506  Cd Length: 134  Bit Score: 49.94  E-value: 4.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  490 SPSQFYIRIYS---------RDSSELLEDMMIEMRRCYSNQlvSDRyiMPEYFIQPGHLCCVKISEDKWwYRVIIHRIL- 559
Cdd:cd20435     1 DATHYSARILEhrssdgevtKSMSSTYLKLSMKLNMYYSDP--SNR--ILHGKVKVGDLCAVEDENNLY-HRVKVLEITe 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 197927156  560 -----GKKEVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAWVRPA--EEHW 611
Cdd:cd20435    76 kddktKPREVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPVdnDTEW 134
Tudor_AtTudor1-like cd20443
Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor ...
 535-606 4.42e-07

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.


Pssm-ID: 410514 [Multi-domain]  Cd Length: 117  Bit Score: 49.77  E-value: 4.42e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 197927156  535 QPGHLCCVKISEDKWWYRVII------HRILGKKEVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAWVRP 606
Cdd:cd20443    39 KKGELVLAQFSADNSWNRAMVvnaprqGTQSPKDEYEVFYIDYGNQETVPLSALRPLDPSVSSAPGLAQLCSLAHIKV 116
LOTUS cd08824
LOTUS is an uncharacterized small globular domain found in Limkain b1, Oskar and ...
 127-194 5.12e-07

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.


Pssm-ID: 193585 [Multi-domain]  Cd Length: 70  Bit Score: 48.00  E-value: 5.12e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  127 PAVVKSELKDLLALSP--VLLSDFEKAFARRFGRSFQYMQYGFLSMFEVLNAASDVISVEQTRAGSLLTL 194
Cdd:cd08824     1 LKQLAKQLRSLLQSYPggLPLSKLPQLYKKKFGKPLDLSEYGFSKLSDLLEALPGVVIVLSQGGERIVSL 70
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 534-587 6.19e-07

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).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 47.27  E-value: 6.19e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 197927156    534 IQPGHLCCVKIsEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFLKC 587
Cdd:smart00333    3 FKVGDKVAARW-EDGEWYRARIVKVDGEQLYEVFFIDYGNEEVVPPSDLRQLPE 55
Tudor_TDRD8 cd20430
Tudor domain found in Tudor domain-containing protein 8 (TDRD8) and similar proteins; TDRD8, ...
 534-585 1.20e-06

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.


Pssm-ID: 410501 [Multi-domain]  Cd Length: 75  Bit Score: 46.90  E-value: 1.20e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 197927156  534 IQPGHLCCVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFL 585
Cdd:cd20430    19 PDPNKIYGGKFSEDNCWYRCKVKSILSDEKCTVQYIDYGNTETVSRSSIVEL 70
Tudor_TDRD1_rpt3 cd20410
third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 535-583 7.09e-06

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.


Pssm-ID: 410481 [Multi-domain]  Cd Length: 59  Bit Score: 44.25  E-value: 7.09e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 197927156  535 QPGHLCCVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLR 583
Cdd:cd20410     4 IVGEPCCAFFSGDGNWYRAMVKEILPGGAVKVHFVDYGNVEEVTLDKLR 52
LOTUS_3_TDRD5 cd09976
The third LOTUS domain on Tudor-containing protein 5 (TDRD5); The third LOTUS domain on ...
 11-66 8.31e-06

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.


Pssm-ID: 193590  Cd Length: 74  Bit Score: 44.72  E-value: 8.31e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 197927156   11 LRKEIRSLLISTKDGLTPQQLEKEYLLMVGNHLPLRILGYRSTMELVLDMPDVVSV 66
Cdd:cd09976     4 LREEIRKVVENHPNGLFIALLPTEYKVLFKEELPVKQLGFLSVTELVGSLSDILAI 59
Tudor_TDRD4_rpt3 cd20416
third Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 540-586 1.86e-05

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.


Pssm-ID: 410487  Cd Length: 82  Bit Score: 44.01  E-value: 1.86e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 197927156  540 CCVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFLK 586
Cdd:cd20416    25 CAVQIQDKKQWRRGQIIRVVSDTLVEVFLYDFGNKEVVNIDCLRKLE 71
Tudor_TDRD7_rpt3 cd20429
third Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 507-597 1.24e-04

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.


Pssm-ID: 410500  Cd Length: 91  Bit Score: 41.70  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  507 LEDMMIEMRRCYSNQlvSDRYIMpeyfIQPGHLCCVKIseDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFLK 586
Cdd:cd20429     9 LEVLMEEMILYYNKT--EERPVA----IEKNKVYAAKI--ENNWYRVLVKGILTNGLVSVYELDYGKHELVSIRKVQPLI 80

                          90
                  ....*....|.
gi 197927156  587 CCYTKLPAQAI 597
Cdd:cd20429    81 EKFRQLPFQAI 91
Tudor_AKAP1 cd20407
Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; ...
 534-606 1.56e-04

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.


Pssm-ID: 410478  Cd Length: 76  Bit Score: 41.04  E-value: 1.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 197927156  534 IQPGhLCCVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAWVRP 606
Cdd:cd20407     5 IEVG-VICAAPVMNAWYRAQVVGVFEETDEVEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATECYLANIEP 76
Tudor_TDRD1_rpt2 cd20409
second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 536-583 1.88e-04

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.


Pssm-ID: 410480  Cd Length: 82  Bit Score: 40.90  E-value: 1.88e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 197927156  536 PGHLCCVKISEDKWWYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLR 583
Cdd:cd20409    28 VGEVCCAQFTEDNQWYRASVLAYSSEDSVLVGYIDFGNSEEVALSRLR 75
Tudor_TDRD7_rpt2 cd20428
second Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 525-617 3.75e-04

second 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 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.


Pssm-ID: 410499  Cd Length: 140  Bit Score: 41.66  E-value: 3.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  525 DRYIMPEYFI-QPghLC---CVKISEDKWwYRVIIHRILGKKEVEVFYPDFGNIGTVQKSSLR-----FLKcCYTKLPAQ 595
Cdd:cd20428    40 SRQMTSEYFVsLP--FCgkiCLARYKGKW-ARVEITNVHSSRALDVHFLDTGTVASVKVSELReipppFLR-ELISIPPQ 115

                          90       100
                  ....*....|....*....|..
gi 197927156  596 AIPCSLAWVRPAEEHWTARAIL 617
Cdd:cd20428   116 ALKCCLADLPLNIGMWTPDAVL 137
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
 488-593 5.72e-04

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.


Pssm-ID: 410502  Cd Length: 101  Bit Score: 40.06  E-value: 5.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  488 IISPSQFYIRIYSRDSSELLEDMMIEMRRcysNQLVSDRYIMPeyfiqPGHLCCV--KISEDKWWYRVIIHRILGKkEVE 565
Cdd:cd20431     3 VVEVGHFWGYRIDENSSEILQQLTAEINQ---RQLVPLTTKPV-----PNLLCLApfTDADMKKYYRAKILYVSGS-SAE 73

                          90       100
                  ....*....|....*....|....*...
gi 197927156  566 VFYPDFGNIGTVQKSSLRFLKCCYTKLP 593
Cdd:cd20431    74 VFFVDYGNTSQVPSSLLREIPETLLTLP 101
Tudor_TDRD15_rpt1 cd20436
first Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 534-625 5.10e-03

first 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 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.


Pssm-ID: 410507  Cd Length: 147  Bit Score: 38.56  E-value: 5.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927156  534 IQPGHLCCVKISEDKWWYRviiHRILGKKE--VEVFYPDFGNIGTVQKSSLRFLKCCYTKLPAQAIPCSLAWVRPAEEHW 611
Cdd:cd20436    47 WGVGEFCLVEDTTSGEWYR---GRVLEKIDekYEVFLIDRGEVLNVHATNMASASGELFQLPPKAVCGIFANILPIGEKW 123

                          90
                  ....*....|....
gi 197927156  612 TARAILHFQKLCGL 625
Cdd:cd20436   124 SSTAVNYFSSLIGS 137
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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