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Conserved domains on  [gi|654822484|ref|NP_878285|]
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staphylococcal nuclease domain-containing protein 1 isoform p100L [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
 706-788 1.83e-46

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: 160.54  E-value: 1.83e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 706 TGTKLENLMESMRGEIAAQPPVEGSFAPRRGEFCIAKF-ADGEWYRARVEKVESPAKVHVFYIDYGNREVLSSTRLAALP 784
Cdd:cd20433    1 TGPQLEKLMEKLRFEIASNPPLPGSYTPRKGDLCAAKFvEDGEWYRAKVEKVEGDKKVHVLYIDYGNREVLPSTRLAALP 80


                 ....
gi 654822484 785 PAFS 788
Cdd:cd20433   81 PAFS 84
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 351-499 3.87e-38

Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.


:

Pssm-ID: 238102  Cd Length: 129  Bit Score: 138.56  E-value: 3.87e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 351 VVNADAIVVKLNSGEYKTIHLSSIRPPRLEgeeknkdKDKRFRPLYDIPYMFEAREFLRKKLIGKKVNVTVDYiraatna 430
Cdd:cd00175    2 VIDGDTIRVRLPPGPLITVRLSGIDAPETA-------RPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDS------- 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 431 memgvPAFPERTCATVTI-GGINIAEALVSKGLATVIRYRQDDdqrSSHYDELLAAEARAIKNGKGLHSK 499
Cdd:cd00175   68 -----KDRYGRTLGTVYLnGGENIAEELVKEGLARVYRYYPDD---SEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
18-167 8.34e-37

Staphylococcal nuclease homologues;


:

Pssm-ID: 214615  Cd Length: 137  Bit Score: 135.08  E-value: 8.34e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484    18 QLQRGIVKMVLSGCAIIVRGQPRggppPERQINLSNIRAGALARRAIQGQpdtkdTPDEPWAFQAREFMRKKVIGKEVCF 97
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG----PLITIRLSGIDAPETARPNKGDG-----TPDEPFGEEAKEFLKKLLLGKKVQV 71

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484    98 TVENKTPQGREYGMVYLGKdtsGENIAESLVAEGLAMVRREGIRGNNPEQvRLCDLEDQAKSSKKGLWSE 167
Cdd:smart00318  72 EVDSKDRYGRFLGTVYLNG---GNNIAEELVKEGLAKVYRYADKDEYVYD-ELLEAEEAAKKARKGLWSD 137
SNc smart00318
Staphylococcal nuclease homologues;
194-329 5.86e-36

Staphylococcal nuclease homologues;


:

Pssm-ID: 214615  Cd Length: 137  Bit Score: 132.77  E-value: 5.86e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484   194 KPVNAIIEHVRDGCMVRALLLPDYYlVTVMLSGIKSPTFKREADGSETP-EPFAAEAKFFTESRLLQRDVQIILES-CPN 271
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKGPL-ITIRLSGIDAPETARPNKGDGTPdEPFGEEAKEFLKKLLLGKKVQVEVDSkDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 654822484   272 QVILGTILHPNG-NITELLLKEGFARCVDWSMAVYTQgAEKLRAAERSAKERKVRIWKD 329
Cdd:smart00318  80 GRFLGTVYLNGGnNIAEELVKEGLAKVYRYADKDEYV-YDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 536-663 1.76e-34

Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.


:

Pssm-ID: 238102  Cd Length: 129  Bit Score: 128.16  E-value: 1.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 536 YVFSGSRLKLYMPKEtCLITFLLAGIECPRGSRNMPGGMQVAEPYSEEAMLFTKELVLQREVEVEVESMDKAGNFIGWLH 615
Cdd:cd00175    1 RVIDGDTIRVRLPPG-PLITVRLSGIDAPETARPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTVY 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 654822484 616 IEGV-NLSVALVENALSKVHFTAERSS-YYKTLVSAEESARQRKEKLWAN 663
Cdd:cd00175   80 LNGGeNIAEELVKEGLARVYRYYPDDSeYYDELLEAEEAAKKARKGLWSD 129
SNc super family cl00140
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 847-898 1.32e-04

Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.


The actual alignment was detected with superfamily member cd00175:

Pssm-ID: 469627  Cd Length: 129  Bit Score: 42.65  E-value: 1.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 654822484 847 FADTKEDVGLGLVKEGMVMVDIRKEKYLQKMvTEYLNAQESAKSARLNIWRY 898
Cdd:cd00175   79 YLNGGENIAEELVKEGLARVYRYYPDDSEYY-DELLEAEEAAKKARKGLWSD 129
 
Name Accession Description Interval E-value
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
 706-788 1.83e-46

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: 160.54  E-value: 1.83e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 706 TGTKLENLMESMRGEIAAQPPVEGSFAPRRGEFCIAKF-ADGEWYRARVEKVESPAKVHVFYIDYGNREVLSSTRLAALP 784
Cdd:cd20433    1 TGPQLEKLMEKLRFEIASNPPLPGSYTPRKGDLCAAKFvEDGEWYRAKVEKVEGDKKVHVLYIDYGNREVLPSTRLAALP 80


                 ....
gi 654822484 785 PAFS 788
Cdd:cd20433   81 PAFS 84
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 351-499 3.87e-38

Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.


Pssm-ID: 238102  Cd Length: 129  Bit Score: 138.56  E-value: 3.87e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 351 VVNADAIVVKLNSGEYKTIHLSSIRPPRLEgeeknkdKDKRFRPLYDIPYMFEAREFLRKKLIGKKVNVTVDYiraatna 430
Cdd:cd00175    2 VIDGDTIRVRLPPGPLITVRLSGIDAPETA-------RPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDS------- 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 431 memgvPAFPERTCATVTI-GGINIAEALVSKGLATVIRYRQDDdqrSSHYDELLAAEARAIKNGKGLHSK 499
Cdd:cd00175   68 -----KDRYGRTLGTVYLnGGENIAEELVKEGLARVYRYYPDD---SEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
18-167 8.34e-37

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 135.08  E-value: 8.34e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484    18 QLQRGIVKMVLSGCAIIVRGQPRggppPERQINLSNIRAGALARRAIQGQpdtkdTPDEPWAFQAREFMRKKVIGKEVCF 97
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG----PLITIRLSGIDAPETARPNKGDG-----TPDEPFGEEAKEFLKKLLLGKKVQV 71

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484    98 TVENKTPQGREYGMVYLGKdtsGENIAESLVAEGLAMVRREGIRGNNPEQvRLCDLEDQAKSSKKGLWSE 167
Cdd:smart00318  72 EVDSKDRYGRFLGTVYLNG---GNNIAEELVKEGLAKVYRYADKDEYVYD-ELLEAEEAAKKARKGLWSD 137
SNc smart00318
Staphylococcal nuclease homologues;
342-498 1.07e-36

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 134.70  E-value: 1.07e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484   342 RQFVAKVMQVVNADAIVVKLNSGEYKTIHLSSIRPPRLEGEEKNkdkdkrfRPLYDIPYMFEAREFLRKKLIGKKVNVTV 421
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKGPLITIRLSGIDAPETARPNKG-------DGTPDEPFGEEAKEFLKKLLLGKKVQVEV 73

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654822484   422 DYIraatnamemgvpAFPERTCATVTI-GGINIAEALVSKGLATVIRYRQDDDQRsshYDELLAAEARAIKNGKGLHS 498
Cdd:smart00318  74 DSK------------DRYGRFLGTVYLnGGNNIAEELVKEGLAKVYRYADKDEYV---YDELLEAEEAAKKARKGLWS 136
SNc smart00318
Staphylococcal nuclease homologues;
194-329 5.86e-36

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 132.77  E-value: 5.86e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484   194 KPVNAIIEHVRDGCMVRALLLPDYYlVTVMLSGIKSPTFKREADGSETP-EPFAAEAKFFTESRLLQRDVQIILES-CPN 271
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKGPL-ITIRLSGIDAPETARPNKGDGTPdEPFGEEAKEFLKKLLLGKKVQVEVDSkDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 654822484   272 QVILGTILHPNG-NITELLLKEGFARCVDWSMAVYTQgAEKLRAAERSAKERKVRIWKD 329
Cdd:smart00318  80 GRFLGTVYLNGGnNIAEELVKEGLAKVYRYADKDEYV-YDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 26-167 1.73e-35

Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.


Pssm-ID: 238102  Cd Length: 129  Bit Score: 130.86  E-value: 1.73e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484  26 MVLSGCAIIVRGQPRggppPERQINLSNIRAGALARRAIQgqpdtKDTPDEPWAFQAREFMRKKVIGKEVCFTVENKTPQ 105
Cdd:cd00175    1 RVIDGDTIRVRLPPG----PLITVRLSGIDAPETARPNKG-----KSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRY 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654822484 106 GREYGMVYLGKdtsGENIAESLVAEGLAMVRReGIRGNNPEQVRLCDLEDQAKSSKKGLWSE 167
Cdd:cd00175   72 GRTLGTVYLNG---GENIAEELVKEGLARVYR-YYPDDSEYYDELLEAEEAAKKARKGLWSD 129
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 536-663 1.76e-34

Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.


Pssm-ID: 238102  Cd Length: 129  Bit Score: 128.16  E-value: 1.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 536 YVFSGSRLKLYMPKEtCLITFLLAGIECPRGSRNMPGGMQVAEPYSEEAMLFTKELVLQREVEVEVESMDKAGNFIGWLH 615
Cdd:cd00175    1 RVIDGDTIRVRLPPG-PLITVRLSGIDAPETARPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTVY 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 654822484 616 IEGV-NLSVALVENALSKVHFTAERSS-YYKTLVSAEESARQRKEKLWAN 663
Cdd:cd00175   80 LNGGeNIAEELVKEGLARVYRYYPDDSeYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
528-663 2.45e-34

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 128.15  E-value: 2.45e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484   528 GRSEAVVEYVFSGSRLKLYMPKEtCLITFLLAGIECPRGSRNMPGGMQVAEPYSEEAMLFTKELVLQREVEVEVESMDKA 607
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPETARPNKGDGTPDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 654822484   608 GNFIGWLHI-EGVNLSVALVENALSKVHFTAERSSY-YKTLVSAEESARQRKEKLWAN 663
Cdd:smart00318  80 GRFLGTVYLnGGNNIAEELVKEGLAKVYRYADKDEYvYDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 202-329 4.92e-34

Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.


Pssm-ID: 238102  Cd Length: 129  Bit Score: 126.62  E-value: 4.92e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 202 HVRDGCMVRALLLPDYYlVTVMLSGIKSPTFKREA-DGSETPEPFAAEAKFFTESRLLQRDVQIILES-CPNQVILGTIL 279
Cdd:cd00175    1 RVIDGDTIRVRLPPGPL-ITVRLSGIDAPETARPNkGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSkDRYGRTLGTVY 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 654822484 280 HPNG-NITELLLKEGFARCVDWSMAVyTQGAEKLRAAERSAKERKVRIWKD 329
Cdd:cd00175   80 LNGGeNIAEELVKEGLARVYRYYPDD-SEYYDELLEAEEAAKKARKGLWSD 129
TUDOR pfam00567
Tudor domain;
684-802 1.96e-30

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 115.91  E-value: 1.96e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484  684 KYRSVYVTEITDGLHFYAQDVETGTKLENLMESMRGEIAAQPPVegSFAPRRGEFCIAKFA-DGEWYRARVEKVESPAKV 762
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQPKSDSKKLEKLTEELQEYYASKPPE--SLPPAVGDGCVAAFSeDGKWYRAKITESLDDGLV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 654822484  763 HVFYIDYGNREVLSSTRLAALPPAFstRTLPPQATEYAFA 802
Cdd:pfam00567  79 EVLFIDYGNTETVPLSDLRPLPPEL--ESLPPQAIKCQLA 116
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 555-663 4.27e-18

Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in the transcriptional coactivator p100: these, however, appear to lack the active site residues of Staphylococcal nuclease. Positions 14 (Asp-21), 34 (Arg-35), 39 (Asp-40), 42 (Glu-43) and 110 (Arg-87) [SNase numbering in parentheses] are thought to be involved in substrate-binding and catalysis.


Pssm-ID: 395448  Cd Length: 106  Bit Score: 80.44  E-value: 4.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484  555 TFLLAGIECPRGSRNMpggmQVAEPYSEEAMLFTKELVLQREVEVEVESMDKAGNFIGWLHIEGVNLSVALVENALSKVH 634
Cdd:pfam00565   1 RVRLVGIDAPETAKPN----TPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYLNGKNINEELVKEGLAWVY 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 654822484  635 FTAE-RSSYYKTLVSAEESARQRKEKLWAN 663
Cdd:pfam00565  77 KAYPpNFKHYDELLAAEEEAKKKKKGLWSD 106
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 732-787 2.56e-16

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: 73.85  E-value: 2.56e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 654822484   732 APRRGEFCIAKFADGEWYRARVEKVESPAKVHVFYIDYGNREVLSSTRLAALPPAF 787
Cdd:smart00333   2 TFKVGDKVAARWEDGEWYRARIVKVDGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 49-167 1.94e-14

Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in the transcriptional coactivator p100: these, however, appear to lack the active site residues of Staphylococcal nuclease. Positions 14 (Asp-21), 34 (Arg-35), 39 (Asp-40), 42 (Glu-43) and 110 (Arg-87) [SNase numbering in parentheses] are thought to be involved in substrate-binding and catalysis.


Pssm-ID: 395448  Cd Length: 106  Bit Score: 70.04  E-value: 1.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484   49 INLSNIRAgalarraiqgqPDTKD--TPDEPWAFQAREFMRKKVIGKEVCFTVENKTPQGREYGMVYLGkdtsGENIAES 126
Cdd:pfam00565   2 VRLVGIDA-----------PETAKpnTPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYLN----GKNINEE 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 654822484  127 LVAEGLAMVRREgIRGNNPEQVRLCDLEDQAKSSKKGLWSE 167
Cdd:pfam00565  67 LVKEGLAWVYKA-YPPNFKHYDELLAAEEEAKKKKKGLWSD 106
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 368-499 2.01e-14

Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in the transcriptional coactivator p100: these, however, appear to lack the active site residues of Staphylococcal nuclease. Positions 14 (Asp-21), 34 (Arg-35), 39 (Asp-40), 42 (Glu-43) and 110 (Arg-87) [SNase numbering in parentheses] are thought to be involved in substrate-binding and catalysis.


Pssm-ID: 395448  Cd Length: 106  Bit Score: 70.04  E-value: 2.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484  368 TIHLSSIRPPrlegeEKNKdkdkrfRPLYDIPYMFEAREFLRKKLIGKKVNVTVD----YiraatnamemgvpafpERTC 443
Cdd:pfam00565   1 RVRLVGIDAP-----ETAK------PNTPVQPFGKEAKEFLKKLVLGKKVVVLEFdkdkY----------------GRTL 53

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 654822484  444 ATVTIGGINIAEALVSKGLATVIRYRqddDQRSSHYDELLAAEARAIKNGKGLHSK 499
Cdd:pfam00565  54 GYVYLNGKNINEELVKEGLAWVYKAY---PPNFKHYDELLAAEEEAKKKKKGLWSD 106
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
331-503 8.72e-14

Endonuclease YncB, thermonuclease family [Replication, recombination and repair];


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 70.09  E-value: 8.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 331 VAPTANLDQKDRQFVAKVMQVVNADAIVVKLNSGEYKtIHLSSIRPPRLegeeknKDKDKRFRPLYDipymfEAREFLRK 410
Cdd:COG1525   11 ALAALAAAAAAATLTAGVVRVIDGDTLRVRDDGKGER-VRLAGIDAPEL------GQPCGPEQPCGE-----EARQALRA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 411 KLIGKKVNVTVDYIRAATNamemgvpafpeRTCATVTIGGINIAEALVSKGLATVirYRQDDDQRssHYDELLAAEARAI 490
Cdd:COG1525   79 LLAGKTVTLEPDEGRDRYG-----------RLLAYVYVDGRDLNEELVREGLAWA--YRRYSPDK--YADRYLAAEAEAR 143

                        170
                 ....*....|...
gi 654822484 491 KNGKGLHSKKEVP 503
Cdd:COG1525  144 AARRGLWSDAFPV 156
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
520-670 6.26e-13

Endonuclease YncB, thermonuclease family [Replication, recombination and repair];


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 67.40  E-value: 6.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 520 FFPFLQRAGRSEAVVEYVFSGSRLKLYMPKETclITFLLAGIECPRgsrnMPGGMQVAEPYSEEAMLFTKELVLQREVEV 599
Cdd:COG1525   14 ALAAAAAAATLTAGVVRVIDGDTLRVRDDGKG--ERVRLAGIDAPE----LGQPCGPEQPCGEEARQALRALLAGKTVTL 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654822484 600 EV-ESMDKAGNFIGWLHIEGVNLSVALVENALSKVHFTAERSSYYKTLVSAEESARQRKEKLWANYEEKPKE 670
Cdd:COG1525   88 EPdEGRDRYGRLLAYVYVDGRDLNEELVREGLAWAYRRYSPDKYADRYLAAEAEARAARRGLWSDAFPVPPE 159
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 221-329 1.68e-12

Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in the transcriptional coactivator p100: these, however, appear to lack the active site residues of Staphylococcal nuclease. Positions 14 (Asp-21), 34 (Arg-35), 39 (Asp-40), 42 (Glu-43) and 110 (Arg-87) [SNase numbering in parentheses] are thought to be involved in substrate-binding and catalysis.


Pssm-ID: 395448  Cd Length: 106  Bit Score: 64.65  E-value: 1.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484  221 TVMLSGIKSPtfkREADGSETPEPFAAEAKFFTESRLLQRDVQI-ILESCPNQVILGTILHPNGNITELLLKEGFARcvd 299
Cdd:pfam00565   1 RVRLVGIDAP---ETAKPNTPVQPFGKEAKEFLKKLVLGKKVVVlEFDKDKYGRTLGYVYLNGKNINEELVKEGLAW--- 74

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 654822484  300 wsmaVYTQ------GAEKLRAAERSAKERKVRIWKD 329
Cdd:pfam00565  75 ----VYKAyppnfkHYDELLAAEEEAKKKKKGLWSD 106
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
69-167 1.72e-12

Endonuclease YncB, thermonuclease family [Replication, recombination and repair];


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 66.24  E-value: 1.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484  69 DTKDTPDEPWAFQAREFMRKKVIGKEV-CFTVENKTPQGREYGMVYLGkdtsGENIAESLVAEGLAMVRREGIRGNNPEq 147
Cdd:COG1525   59 GQPCGPEQPCGEEARQALRALLAGKTVtLEPDEGRDRYGRLLAYVYVD----GRDLNEELVREGLAWAYRRYSPDKYAD- 133

                         90       100
                 ....*....|....*....|
gi 654822484 148 vRLCDLEDQAKSSKKGLWSE 167
Cdd:COG1525  134 -RYLAAEAEARAARRGLWSD 152
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
195-329 1.31e-08

Endonuclease YncB, thermonuclease family [Replication, recombination and repair];


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 55.07  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 195 PVNAIIEHVRDGCMVRalLLPDYYLVTVMLSGIKSPtfkrEADGSETPE-PFAAEAKFFTESRLLQRDVQIILESCP--N 271
Cdd:COG1525   23 TLTAGVVRVIDGDTLR--VRDDGKGERVRLAGIDAP----ELGQPCGPEqPCGEEARQALRALLAGKTVTLEPDEGRdrY 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 272 QVILGTILHPNGNITELLLKEGFArcvdWSMAVY--TQGAEKLRAAERSAKERKVRIWKD 329
Cdd:COG1525   97 GRLLAYVYVDGRDLNEELVREGLA----WAYRRYspDKYADRYLAAEAEARAARRGLWSD 152
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 847-898 1.32e-04

Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.


Pssm-ID: 238102  Cd Length: 129  Bit Score: 42.65  E-value: 1.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 654822484 847 FADTKEDVGLGLVKEGMVMVDIRKEKYLQKMvTEYLNAQESAKSARLNIWRY 898
Cdd:cd00175   79 YLNGGENIAEELVKEGLARVYRYYPDDSEYY-DELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
749-898 1.68e-04

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 42.63  E-value: 1.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484   749 YRARVEKVESPAKVHVfyidYGNREVLSSTRLAAL-PPAFSTRTLPPQATEYAFAyiqvpqdEDARADAVDSVVRdiHNT 827
Cdd:smart00318   3 IRGVVERVIDGDTIRV----RLPKGPLITIRLSGIdAPETARPNKGDGTPDEPFG-------EEAKEFLKKLLLG--KKV 69

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654822484   828 QC-LLNVEYSGSVCPQVtlqFADTKEDVGLGLVKEGMVMVDIRKEKYLQKMvTEYLNAQESAKSARLNIWRY 898
Cdd:smart00318  70 QVeVDSKDRYGRFLGTV---YLNGGNNIAEELVKEGLAKVYRYADKDEYVY-DELLEAEEAAKKARKGLWSD 137
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
852-897 6.57e-03

Endonuclease YncB, thermonuclease family [Replication, recombination and repair];


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 38.51  E-value: 6.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 654822484 852 EDVGLGLVKEGMVMVDIRKEKYlqKMVTEYLNAQESAKSARLNIWR 897
Cdd:COG1525  108 RDLNEELVREGLAWAYRRYSPD--KYADRYLAAEAEARAARRGLWS 151
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 851-896 8.42e-03

Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in the transcriptional coactivator p100: these, however, appear to lack the active site residues of Staphylococcal nuclease. Positions 14 (Asp-21), 34 (Arg-35), 39 (Asp-40), 42 (Glu-43) and 110 (Arg-87) [SNase numbering in parentheses] are thought to be involved in substrate-binding and catalysis.


Pssm-ID: 395448  Cd Length: 106  Bit Score: 36.92  E-value: 8.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 654822484  851 KEDVGLGLVKEGMVMV---DIRKEKYLQkmvtEYLNAQESAKSARLNIW 896
Cdd:pfam00565  60 GKNINEELVKEGLAWVykaYPPNFKHYD----ELLAAEEEAKKKKKGLW 104
 
Name Accession Description Interval E-value
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
 706-788 1.83e-46

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: 160.54  E-value: 1.83e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 706 TGTKLENLMESMRGEIAAQPPVEGSFAPRRGEFCIAKF-ADGEWYRARVEKVESPAKVHVFYIDYGNREVLSSTRLAALP 784
Cdd:cd20433    1 TGPQLEKLMEKLRFEIASNPPLPGSYTPRKGDLCAAKFvEDGEWYRAKVEKVEGDKKVHVLYIDYGNREVLPSTRLAALP 80


                 ....
gi 654822484 785 PAFS 788
Cdd:cd20433   81 PAFS 84
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 351-499 3.87e-38

Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.


Pssm-ID: 238102  Cd Length: 129  Bit Score: 138.56  E-value: 3.87e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 351 VVNADAIVVKLNSGEYKTIHLSSIRPPRLEgeeknkdKDKRFRPLYDIPYMFEAREFLRKKLIGKKVNVTVDYiraatna 430
Cdd:cd00175    2 VIDGDTIRVRLPPGPLITVRLSGIDAPETA-------RPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDS------- 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 431 memgvPAFPERTCATVTI-GGINIAEALVSKGLATVIRYRQDDdqrSSHYDELLAAEARAIKNGKGLHSK 499
Cdd:cd00175   68 -----KDRYGRTLGTVYLnGGENIAEELVKEGLARVYRYYPDD---SEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
18-167 8.34e-37

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 135.08  E-value: 8.34e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484    18 QLQRGIVKMVLSGCAIIVRGQPRggppPERQINLSNIRAGALARRAIQGQpdtkdTPDEPWAFQAREFMRKKVIGKEVCF 97
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG----PLITIRLSGIDAPETARPNKGDG-----TPDEPFGEEAKEFLKKLLLGKKVQV 71

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484    98 TVENKTPQGREYGMVYLGKdtsGENIAESLVAEGLAMVRREGIRGNNPEQvRLCDLEDQAKSSKKGLWSE 167
Cdd:smart00318  72 EVDSKDRYGRFLGTVYLNG---GNNIAEELVKEGLAKVYRYADKDEYVYD-ELLEAEEAAKKARKGLWSD 137
SNc smart00318
Staphylococcal nuclease homologues;
342-498 1.07e-36

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 134.70  E-value: 1.07e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484   342 RQFVAKVMQVVNADAIVVKLNSGEYKTIHLSSIRPPRLEGEEKNkdkdkrfRPLYDIPYMFEAREFLRKKLIGKKVNVTV 421
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKGPLITIRLSGIDAPETARPNKG-------DGTPDEPFGEEAKEFLKKLLLGKKVQVEV 73

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654822484   422 DYIraatnamemgvpAFPERTCATVTI-GGINIAEALVSKGLATVIRYRQDDDQRsshYDELLAAEARAIKNGKGLHS 498
Cdd:smart00318  74 DSK------------DRYGRFLGTVYLnGGNNIAEELVKEGLAKVYRYADKDEYV---YDELLEAEEAAKKARKGLWS 136
SNc smart00318
Staphylococcal nuclease homologues;
194-329 5.86e-36

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 132.77  E-value: 5.86e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484   194 KPVNAIIEHVRDGCMVRALLLPDYYlVTVMLSGIKSPTFKREADGSETP-EPFAAEAKFFTESRLLQRDVQIILES-CPN 271
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKGPL-ITIRLSGIDAPETARPNKGDGTPdEPFGEEAKEFLKKLLLGKKVQVEVDSkDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 654822484   272 QVILGTILHPNG-NITELLLKEGFARCVDWSMAVYTQgAEKLRAAERSAKERKVRIWKD 329
Cdd:smart00318  80 GRFLGTVYLNGGnNIAEELVKEGLAKVYRYADKDEYV-YDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 26-167 1.73e-35

Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.


Pssm-ID: 238102  Cd Length: 129  Bit Score: 130.86  E-value: 1.73e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484  26 MVLSGCAIIVRGQPRggppPERQINLSNIRAGALARRAIQgqpdtKDTPDEPWAFQAREFMRKKVIGKEVCFTVENKTPQ 105
Cdd:cd00175    1 RVIDGDTIRVRLPPG----PLITVRLSGIDAPETARPNKG-----KSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRY 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654822484 106 GREYGMVYLGKdtsGENIAESLVAEGLAMVRReGIRGNNPEQVRLCDLEDQAKSSKKGLWSE 167
Cdd:cd00175   72 GRTLGTVYLNG---GENIAEELVKEGLARVYR-YYPDDSEYYDELLEAEEAAKKARKGLWSD 129
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 536-663 1.76e-34

Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.


Pssm-ID: 238102  Cd Length: 129  Bit Score: 128.16  E-value: 1.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 536 YVFSGSRLKLYMPKEtCLITFLLAGIECPRGSRNMPGGMQVAEPYSEEAMLFTKELVLQREVEVEVESMDKAGNFIGWLH 615
Cdd:cd00175    1 RVIDGDTIRVRLPPG-PLITVRLSGIDAPETARPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTVY 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 654822484 616 IEGV-NLSVALVENALSKVHFTAERSS-YYKTLVSAEESARQRKEKLWAN 663
Cdd:cd00175   80 LNGGeNIAEELVKEGLARVYRYYPDDSeYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
528-663 2.45e-34

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 128.15  E-value: 2.45e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484   528 GRSEAVVEYVFSGSRLKLYMPKEtCLITFLLAGIECPRGSRNMPGGMQVAEPYSEEAMLFTKELVLQREVEVEVESMDKA 607
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPETARPNKGDGTPDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 654822484   608 GNFIGWLHI-EGVNLSVALVENALSKVHFTAERSSY-YKTLVSAEESARQRKEKLWAN 663
Cdd:smart00318  80 GRFLGTVYLnGGNNIAEELVKEGLAKVYRYADKDEYvYDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 202-329 4.92e-34

Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.


Pssm-ID: 238102  Cd Length: 129  Bit Score: 126.62  E-value: 4.92e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 202 HVRDGCMVRALLLPDYYlVTVMLSGIKSPTFKREA-DGSETPEPFAAEAKFFTESRLLQRDVQIILES-CPNQVILGTIL 279
Cdd:cd00175    1 RVIDGDTIRVRLPPGPL-ITVRLSGIDAPETARPNkGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSkDRYGRTLGTVY 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 654822484 280 HPNG-NITELLLKEGFARCVDWSMAVyTQGAEKLRAAERSAKERKVRIWKD 329
Cdd:cd00175   80 LNGGeNIAEELVKEGLARVYRYYPDD-SEYYDELLEAEEAAKKARKGLWSD 129
TUDOR pfam00567
Tudor domain;
684-802 1.96e-30

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 115.91  E-value: 1.96e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484  684 KYRSVYVTEITDGLHFYAQDVETGTKLENLMESMRGEIAAQPPVegSFAPRRGEFCIAKFA-DGEWYRARVEKVESPAKV 762
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQPKSDSKKLEKLTEELQEYYASKPPE--SLPPAVGDGCVAAFSeDGKWYRAKITESLDDGLV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 654822484  763 HVFYIDYGNREVLSSTRLAALPPAFstRTLPPQATEYAFA 802
Cdd:pfam00567  79 EVLFIDYGNTETVPLSDLRPLPPEL--ESLPPQAIKCQLA 116
Tudor_AtTudor1-like cd20443
Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor ...
 699-807 4.16e-23

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: 95.23  E-value: 4.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 699 FYAQDVETGtKLENLMESMRG-EIAAQPPVEGSFAPRRGEFCIAKF-ADGEWYRARVekVESPA--------KVHVFYID 768
Cdd:cd20443    4 FYVQVVSDQ-RLSSIQQQLEGlSLKDKANPPGGFNPKKGELVLAQFsADNSWNRAMV--VNAPRqgtqspkdEYEVFYID 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 654822484 769 YGNREVLSSTRLAALPPAFStrTLPPQATEYAFAYIQVP 807
Cdd:cd20443   81 YGNQETVPLSALRPLDPSVS--SAPGLAQLCSLAHIKVP 117
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 688-809 9.01e-19

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: 83.19  E-value: 9.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 688 VYVTEITDGLHFYAQdVETGTKLENLME--SMRGEIAAQPPVEGSFAPRRGEFCIAKFA-DGEWYRARVEKVESPAK-VH 763
Cdd:cd20408    1 GTVTEFKNPGEFYIQ-IYTLEVLESLVKltSQLKKTYASVNNHKEYIPEVGEVCVAKYSeDQNWYRALVQTVDVQQKkAG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 654822484 764 VFYIDYGNREVLSSTRLAALPPAFStrTLPPQATEYAFAYIQVPQD 809
Cdd:cd20408   80 VFYIDYGNEETVPLNRIQPLKKDIE--LFPPCAIKCCLANVKPPSG 123
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 555-663 4.27e-18

Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in the transcriptional coactivator p100: these, however, appear to lack the active site residues of Staphylococcal nuclease. Positions 14 (Asp-21), 34 (Arg-35), 39 (Asp-40), 42 (Glu-43) and 110 (Arg-87) [SNase numbering in parentheses] are thought to be involved in substrate-binding and catalysis.


Pssm-ID: 395448  Cd Length: 106  Bit Score: 80.44  E-value: 4.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484  555 TFLLAGIECPRGSRNMpggmQVAEPYSEEAMLFTKELVLQREVEVEVESMDKAGNFIGWLHIEGVNLSVALVENALSKVH 634
Cdd:pfam00565   1 RVRLVGIDAPETAKPN----TPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYLNGKNINEELVKEGLAWVY 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 654822484  635 FTAE-RSSYYKTLVSAEESARQRKEKLWAN 663
Cdd:pfam00565  77 KAYPpNFKHYDELLAAEEEAKKKKKGLWSD 106
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 732-787 2.56e-16

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: 73.85  E-value: 2.56e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 654822484   732 APRRGEFCIAKFADGEWYRARVEKVESPAKVHVFYIDYGNREVLSSTRLAALPPAF 787
Cdd:smart00333   2 TFKVGDKVAARWEDGEWYRARIVKVDGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
Tudor_TDRD1_rpt2 cd20409
second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 707-785 1.46e-14

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: 69.41  E-value: 1.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 707 GTKLENLMESMRGEiAAQPPVEGSFAPRRGEFCIAKF-ADGEWYRARVEKVESPAKVHVFYIDYGNREVLSSTRLAALPP 785
Cdd:cd20409    1 GRQLAELQESLSAY-CKVAPASSDFSPAVGEVCCAQFtEDNQWYRASVLAYSSEDSVLVGYIDFGNSEEVALSRLRPIPP 79
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 49-167 1.94e-14

Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in the transcriptional coactivator p100: these, however, appear to lack the active site residues of Staphylococcal nuclease. Positions 14 (Asp-21), 34 (Arg-35), 39 (Asp-40), 42 (Glu-43) and 110 (Arg-87) [SNase numbering in parentheses] are thought to be involved in substrate-binding and catalysis.


Pssm-ID: 395448  Cd Length: 106  Bit Score: 70.04  E-value: 1.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484   49 INLSNIRAgalarraiqgqPDTKD--TPDEPWAFQAREFMRKKVIGKEVCFTVENKTPQGREYGMVYLGkdtsGENIAES 126
Cdd:pfam00565   2 VRLVGIDA-----------PETAKpnTPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYLN----GKNINEE 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 654822484  127 LVAEGLAMVRREgIRGNNPEQVRLCDLEDQAKSSKKGLWSE 167
Cdd:pfam00565  67 LVKEGLAWVYKA-YPPNFKHYDELLAAEEEAKKKKKGLWSD 106
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 368-499 2.01e-14

Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in the transcriptional coactivator p100: these, however, appear to lack the active site residues of Staphylococcal nuclease. Positions 14 (Asp-21), 34 (Arg-35), 39 (Asp-40), 42 (Glu-43) and 110 (Arg-87) [SNase numbering in parentheses] are thought to be involved in substrate-binding and catalysis.


Pssm-ID: 395448  Cd Length: 106  Bit Score: 70.04  E-value: 2.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484  368 TIHLSSIRPPrlegeEKNKdkdkrfRPLYDIPYMFEAREFLRKKLIGKKVNVTVD----YiraatnamemgvpafpERTC 443
Cdd:pfam00565   1 RVRLVGIDAP-----ETAK------PNTPVQPFGKEAKEFLKKLVLGKKVVVLEFdkdkY----------------GRTL 53

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 654822484  444 ATVTIGGINIAEALVSKGLATVIRYRqddDQRSSHYDELLAAEARAIKNGKGLHSK 499
Cdd:pfam00565  54 GYVYLNGKNINEELVKEGLAWVYKAY---PPNFKHYDELLAAEEEAKKKKKGLWSD 106
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
331-503 8.72e-14

Endonuclease YncB, thermonuclease family [Replication, recombination and repair];


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 70.09  E-value: 8.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 331 VAPTANLDQKDRQFVAKVMQVVNADAIVVKLNSGEYKtIHLSSIRPPRLegeeknKDKDKRFRPLYDipymfEAREFLRK 410
Cdd:COG1525   11 ALAALAAAAAAATLTAGVVRVIDGDTLRVRDDGKGER-VRLAGIDAPEL------GQPCGPEQPCGE-----EARQALRA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 411 KLIGKKVNVTVDYIRAATNamemgvpafpeRTCATVTIGGINIAEALVSKGLATVirYRQDDDQRssHYDELLAAEARAI 490
Cdd:COG1525   79 LLAGKTVTLEPDEGRDRYG-----------RLLAYVYVDGRDLNEELVREGLAWA--YRRYSPDK--YADRYLAAEAEAR 143

                        170
                 ....*....|...
gi 654822484 491 KNGKGLHSKKEVP 503
Cdd:COG1525  144 AARRGLWSDAFPV 156
Tudor_TDRD15_rpt5 cd20440
fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 688-796 9.18e-14

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: 68.64  E-value: 9.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 688 VYVTEITDGLHFYAQDVETGTKLENLMESMrGEIAAQPPVEgSFAPRRGEFCIAK-FADGEWYRARVEKVESPAKVHVFY 766
Cdd:cd20440   14 VYITHVYSPAKFYCQLDRNTEILEALMEKI-AEISKLFNSQ-ILDNCKTRLCLAKyFEDGQWYRALAHPVESSSHLSVYF 91

                         90       100       110
                 ....*....|....*....|....*....|.
gi 654822484 767 IDYGNREVLSSTRLAALPPAFSTRTLPP-QA 796
Cdd:cd20440   92 VDYGNKQIVEKNEVLPIPDTAVDLLLTPmQA 122
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 736-783 1.23e-13

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: 66.00  E-value: 1.23e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 654822484 736 GEFCIAKF-ADGEWYRARVEKVESPAKVHVFYIDYGNREVLSSTRLAAL 783
Cdd:cd20379    2 GDLCAAKYeEDGKWYRARVLEVLSNDKVEVFFVDYGNTETVPLSDLRPL 50
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
520-670 6.26e-13

Endonuclease YncB, thermonuclease family [Replication, recombination and repair];


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 67.40  E-value: 6.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 520 FFPFLQRAGRSEAVVEYVFSGSRLKLYMPKETclITFLLAGIECPRgsrnMPGGMQVAEPYSEEAMLFTKELVLQREVEV 599
Cdd:COG1525   14 ALAAAAAAATLTAGVVRVIDGDTLRVRDDGKG--ERVRLAGIDAPE----LGQPCGPEQPCGEEARQALRALLAGKTVTL 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654822484 600 EV-ESMDKAGNFIGWLHIEGVNLSVALVENALSKVHFTAERSSYYKTLVSAEESARQRKEKLWANYEEKPKE 670
Cdd:COG1525   88 EPdEGRDRYGRLLAYVYVDGRDLNEELVREGLAWAYRRYSPDKYADRYLAAEAEARAARRGLWSDAFPVPPE 159
Tudor_TDRD15_rpt2 cd20437
second Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 699-792 9.78e-13

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: 65.52  E-value: 9.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 699 FYAQDVETGTKLENLMESM-----RGEIAAQPPVEgSFaprrGEFCIAKFADGEWYRARVEKVESPAKVHVFYIDYGNRE 773
Cdd:cd20437   18 FYCQLLSWEPELSKLTTQMtlhyeSVSKELNPSCE-NF----GLLCAAKGKDGQWHRGFLQQLLPPSQVKVWFIDYGNSE 92

                         90
                 ....*....|....*....
gi 654822484 774 VLSSTRLAALPPAFSTRTL 792
Cdd:cd20437   93 AVSSHSVLKLPPDFFSLPL 111
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 221-329 1.68e-12

Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in the transcriptional coactivator p100: these, however, appear to lack the active site residues of Staphylococcal nuclease. Positions 14 (Asp-21), 34 (Arg-35), 39 (Asp-40), 42 (Glu-43) and 110 (Arg-87) [SNase numbering in parentheses] are thought to be involved in substrate-binding and catalysis.


Pssm-ID: 395448  Cd Length: 106  Bit Score: 64.65  E-value: 1.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484  221 TVMLSGIKSPtfkREADGSETPEPFAAEAKFFTESRLLQRDVQI-ILESCPNQVILGTILHPNGNITELLLKEGFARcvd 299
Cdd:pfam00565   1 RVRLVGIDAP---ETAKPNTPVQPFGKEAKEFLKKLVLGKKVVVlEFDKDKYGRTLGYVYLNGKNINEELVKEGLAW--- 74

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 654822484  300 wsmaVYTQ------GAEKLRAAERSAKERKVRIWKD 329
Cdd:pfam00565  75 ----VYKAyppnfkHYDELLAAEEEAKKKKKGLWSD 106
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
69-167 1.72e-12

Endonuclease YncB, thermonuclease family [Replication, recombination and repair];


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 66.24  E-value: 1.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484  69 DTKDTPDEPWAFQAREFMRKKVIGKEV-CFTVENKTPQGREYGMVYLGkdtsGENIAESLVAEGLAMVRREGIRGNNPEq 147
Cdd:COG1525   59 GQPCGPEQPCGEEARQALRALLAGKTVtLEPDEGRDRYGRLLAYVYVD----GRDLNEELVREGLAWAYRRYSPDKYAD- 133

                         90       100
                 ....*....|....*....|
gi 654822484 148 vRLCDLEDQAKSSKKGLWSE 167
Cdd:COG1525  134 -RYLAAEAEARAARRGLWSD 152
Tudor_TDRD6_rpt5 cd20424
fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 688-796 4.65e-12

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: 64.06  E-value: 4.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 688 VYVTEITDGLHFYAQDVETGTKLENLMESMRGEIAAQPPVEGSFAPrrGEFCIAKFADGEWYRARVEKVESPAKvhVFYI 767
Cdd:cd20424   16 VYITYVNDPWTFYCQLARNAGVLDQLASAISRLSSEIRKLELSVNP--GTLCLAKYSDQHWYRGIIITNKNSTE--VFFV 91

                         90       100       110
                 ....*....|....*....|....*....|
gi 654822484 768 DYGNREVLSSTRLAALPP-AFSTRTLPPQA 796
Cdd:cd20424   92 DYGNTEKVEKEDMLPIPSdAYELLLLPMQA 121
Tudor_TDRD6_rpt2 cd20421
second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 687-787 1.09e-11

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: 62.83  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 687 SVYVTEITDGLHFYAQDVETGTKLENLMESMRGEIAAQPPVEGSFAPRR-GEFCIAKFADGEWYRARVEKVESPAK-VHV 764
Cdd:cd20421   14 TVVVTEVTDPHRIFCQLRSLSQELKRLSESMHQYYEGRVGSGYETRPEKlGSPCAARGSDGRWYRAVLQQVFSANRvVEV 93

                         90       100
                 ....*....|....*....|...
gi 654822484 765 FYIDYGNREVLSSTRLAALPPAF 787
Cdd:cd20421   94 LHVDYGRKEVVSVSNLRYLAPEY 116
Tudor_TDRD1_rpt4 cd20411
fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 690-787 1.13e-11

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: 62.46  E-value: 1.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 690 VTEITDGLHFYA------QDVEtgtKLENLMESMrGEIAAQPPVEGSFAPRRGEFCIAKFA-DGEWYRARVEKVeSPAKV 762
Cdd:cd20411    3 VLEVISPDLFYAlpktgqVNVE---KLKALMTEL-AEYCSKQSVPQQFRPRIGDACCARFTgDKNWYRAVVLET-SDSEV 77

                         90       100
                 ....*....|....*....|....*
gi 654822484 763 HVFYIDYGNREVLSSTRLAALPPAF 787
Cdd:cd20411   78 KVLYADYGNTETLPLSRILPITKSH 102
Tudor_TDRD1_rpt3 cd20410
third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 731-787 2.91e-11

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: 59.28  E-value: 2.91e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 654822484 731 FAPRRGEFCIAKFA-DGEWYRARVEKVESPAKVHVFYIDYGNREVLSSTRLAALPPAF 787
Cdd:cd20410    1 FKPIVGEPCCAFFSgDGNWYRAMVKEILPGGAVKVHFVDYGNVEEVTLDKLRKITSTF 58
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
 691-793 8.21e-11

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: 59.71  E-value: 8.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 691 TEITDGLHFYAQ--DVETGTKLENLMESMRGEIAAQPPVEgsfaPRRGEFCIAKFADGE---WYRARVEKVeSPAKVHVF 765
Cdd:cd20431    1 TEVVEVGHFWGYriDENSSEILQQLTAEINQRQLVPLTTK----PVPNLLCLAPFTDADmkkYYRAKILYV-SGSSAEVF 75

                         90       100
                 ....*....|....*....|....*...
gi 654822484 766 YIDYGNREVLSSTRLAALPPAFstRTLP 793
Cdd:cd20431   76 FVDYGNTSQVPSSLLREIPETL--LTLP 101
Tudor_TDRD8 cd20430
Tudor domain found in Tudor domain-containing protein 8 (TDRD8) and similar proteins; TDRD8, ...
 725-788 1.65e-10

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: 57.69  E-value: 1.65e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654822484 725 PPVEGSFAPRR--GefciAKFA-DGEWYRARVEKVESPAKVHVFYIDYGNREVLSSTRLAALPPAFS 788
Cdd:cd20430   13 PPLFGTPDPNKiyG----GKFSeDNCWYRCKVKSILSDEKCTVQYIDYGNTETVSRSSIVELPPDLQ 75
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 728-805 1.99e-10

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: 58.21  E-value: 1.99e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654822484 728 EGSFAPRRGEFCIAKFADGEWYRARVEKVESPAKVHVFYIDYGNREVLSSTRLAALPPAFStrTLPPQATEYAFAYIQ 805
Cdd:cd20415   20 LEILCPVQGQACVALFEDGAWYRARIIGLPGHREVEVKYVDFGNTATVTIKHVRKIKDDFL--SLPEKARECRLAFIE 95
Tudor_TDRD6_rpt6 cd20425
sixth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 687-787 2.78e-10

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: 58.62  E-value: 2.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 687 SVYVTEITDGLHFYAQDVETGTKLENLMESMRGEIAAQPPVEGSfAPRRGEFCIAKFA-DGEWYRARVEKVESPAKVHVF 765
Cdd:cd20425    3 EVYVSHVNSPSDFYVQLAQDEDELSMISEKLNASKANDEEVECE-SLQLGDLICAEYPeDGLWYRAVVKEKIPNNLVSVQ 81

                         90       100
                 ....*....|....*....|..
gi 654822484 766 YIDYGNREVLSSTRLAALPPAF 787
Cdd:cd20425   82 FIDYGNTSVVQPSKIHRLPKEL 103
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 733-811 6.01e-10

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: 58.03  E-value: 6.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 733 PRRGEFCIAKFADGEWYRARVEKVE------SPAKVHVFYIDYGNREVLSSTRLAALPPAFstRTLPPQATEYAFAYIQv 806
Cdd:cd20435   50 VKVGDLCAVEDENNLYHRVKVLEITekddktKPREVLVKFIDEGRVETVVVSQLLELPEEL--KSLPPQAVEVFLCNVK- 126


                 ....*
gi 654822484 807 PQDED 811
Cdd:cd20435  127 PVDND 131
Tudor_TDRD15_rpt4 cd20439
fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 698-787 1.95e-09

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: 56.34  E-value: 1.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 698 HFYAQDVETGTKLENLMESMRG--EIAAQPPVEGSFAprrgefCIAKFA-DGEWYRARVEKVESPAKVHVFYIDYGNREV 774
Cdd:cd20439   24 DFWCQLQTKSSELKSLMKQIQSyyLIHNDPYKHGQIA------CVAKYSkDGKWYRAAVLKQVSAKEVDVIFVDYGNQER 97

                         90
                 ....*....|...
gi 654822484 775 LSSTRLAALPPAF 787
Cdd:cd20439   98 VLISDLRAIKPQF 110
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
195-329 1.31e-08

Endonuclease YncB, thermonuclease family [Replication, recombination and repair];


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 55.07  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 195 PVNAIIEHVRDGCMVRalLLPDYYLVTVMLSGIKSPtfkrEADGSETPE-PFAAEAKFFTESRLLQRDVQIILESCP--N 271
Cdd:COG1525   23 TLTAGVVRVIDGDTLR--VRDDGKGERVRLAGIDAP----ELGQPCGPEqPCGEEARQALRALLAGKTVTLEPDEGRdrY 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 272 QVILGTILHPNGNITELLLKEGFArcvdWSMAVY--TQGAEKLRAAERSAKERKVRIWKD 329
Cdd:COG1525   97 GRLLAYVYVDGRDLNEELVREGLA----WAYRRYspDKYADRYLAAEAEARAARRGLWSD 152
Tudor_TDRD6_rpt3 cd20422
third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 688-804 1.57e-08

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: 54.05  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 688 VYVTEITDGLHFYAQDVETGTKLENLMESMRGEIAAQPPVEGSF-APRRGEFCIAKFADGEWYRARVEKVESPAkVHVFY 766
Cdd:cd20422    4 AQVEFVKDPSEFWIRLGEHAVPFSKLMRSMTAFYSQASKLDGVVlKPQPGQLCCAKWKEDRYYRAIVTAVKGKM-VEVFL 82

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 654822484 767 IDYGNREVLSSTRLAALPPAFstRTLPPQATEYAFAYI 804
Cdd:cd20422   83 VDRGNTEMVDWYDVKKLLPQF--RELPALALKCCLADI 118
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 739-798 1.60e-08

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: 52.48  E-value: 1.60e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654822484 739 CIAKFA-DGEWYRARVEKVESPAK-VHVFYIDYGNREVLSSTRLAALPPAFStrTLPPQATE 798
Cdd:cd20423    9 CLAKYSeDGKWCRALIDNVYEPVEmVEVTYVDYGNKELVSLKNLRSISEEFL--KLKAQAFR 68
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 739-806 9.35e-08

fifth 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 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: 410489  Cd Length: 105  Bit Score: 50.87  E-value: 9.35e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 739 CIAKFADGEWYRARVEKVES--PAKVHVFYIDYGNREVLSSTRLaalppafstRTLPPQATEYAFAYIQV 806
Cdd:cd20418   10 CLAEYSDGKWYRAKLLSILEfnPVKILVRHVDYGSTAALPTSRL---------RQIPAELMQYPCQAIKV 70
Tudor_TDRD15_rpt1 cd20436
first Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 715-804 1.86e-07

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: 51.27  E-value: 1.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 715 ESMRGEIAAQPPVEGSFAprRGEFCIAK-FADGEWYRARVEKVESpAKVHVFYIDYGNREVLSSTRLAALPPAFStrTLP 793
Cdd:cd20436   31 HILQNEIQNATKSKSSWG--VGEFCLVEdTTSGEWYRGRVLEKID-EKYEVFLIDRGEVLNVHATNMASASGELF--QLP 105

                         90
                 ....*....|.
gi 654822484 794 PQATEYAFAYI 804
Cdd:cd20436  106 PKAVCGIFANI 116
Tudor_TDRD7_rpt1 cd20427
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 709-810 2.49e-07

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: 49.73  E-value: 2.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 709 KLENLMESMRGEIAAQPPVEgsfAPRRGEFCIAKFADGEWYRARVEKVESpAKVHVFYIDYGNREVLSSTRLAALPPAFS 788
Cdd:cd20427    2 QMEDEMKEFYSKSSTAMCLR---SPSVGQLVAVKAEEDAWLRAQVIEVEE-DKVKVYYVDHGFSEVVERSKLFKLNKQFY 77

                         90       100
                 ....*....|....*....|..
gi 654822484 789 trTLPPQATEYAFAYIQVPQDE 810
Cdd:cd20427   78 --SLPFQATKCKLAGLEPFSDD 97
Tudor_TDRD6_rpt7 cd20426
seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 689-784 3.59e-07

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: 50.19  E-value: 3.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 689 YVTEITDGLHFYAQdvETGTKLENLMESMRgEIAAQPPVEGSFAP--RRGEFCIAKFA-DGEWYRARVEKVESpAKVHVF 765
Cdd:cd20426    4 YATAVDSPEYFWCQ--FATEKIQCLAVKVQ-EAGEQVADRGNFIPsiYVGDPCIVKYSeDNHWYRALVTKIND-NLVSVR 79

                         90
                 ....*....|....*....
gi 654822484 766 YIDYGNREVLSSTRLAALP 784
Cdd:cd20426   80 FVDYGNEEDVVREQVRALP 98
Tudor_vreteno-like_rpt1 cd20444
first Tudor domain found in Drosophila melanogaster protein vreteno and similar proteins; ...
 733-784 5.57e-07

first Tudor domain found in Drosophila melanogaster protein vreteno and similar proteins; Vreteno is a gonad-specific protein essential for germline development to repress transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process in both germline and somatic gonadal tissues by mediating the repression of transposable elements during meiosis. Vreteno contains two 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: 410515  Cd Length: 55  Bit Score: 47.30  E-value: 5.57e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 654822484 733 PRRGEFCIAKFaDGEWYRARVEKVESP-AKVHVFYIDYGNREVLSSTRLAALP 784
Cdd:cd20444    1 PTPGQMVIAKF-DGNHYRAIVLRVLNPdLKILVRFVDFGNVEVMKLENLYECP 52
Tudor_TDRD5 cd20419
Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is ...
 689-796 6.28e-07

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: 48.98  E-value: 6.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 689 YVTEITDGLHFYAQDV--ETGTKLENLMESMRGEIAAQPPVEGSFAP----RRGEFCIAKF-ADGEWYRARVEKVESPAK 761
Cdd:cd20419    1 FVEYIESPSQFYVRFYskDTSEMLEDMMIEMRRCYSNEHVSERYVMPeafiQPGQVCCVRIpEDVWWYRVIIHQVLNKQE 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 654822484 762 VHVFYIDYGNREVLSSTRLAALPPAFStrTLPPQA 796
Cdd:cd20419   81 VEVFYPDFGDIGTVQKSRLRFLKCCYS--KLPAQA 113
Tudor_TDRD2 cd20412
Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, ...
 708-798 1.15e-06

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: 47.68  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 708 TKLENLMESMRGEIAAQPPVEGSFAPRRGEFCIAKFA-DGEWYRARVEKVESPAKVHVFYIDYGNREVLSSTRLAALPPA 786
Cdd:cd20412    4 LQLDKLVQEMTQYYESEENRHTLLTVQVGDIVAAPFRhDGSWYRARVLGFLENGNLDLYFVDYGDSGYVPLEDLRALRSD 83

                         90
                 ....*....|..
gi 654822484 787 FstRTLPPQATE 798
Cdd:cd20412   84 F--LSLPFQAIE 93
Tudor_TDRD7_rpt3 cd20429
third Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 709-796 1.95e-05

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: 44.02  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 709 KLENLMESMRGEIAAQPpvEGSFAPRRGEFCIAKFaDGEWYRARVEKVESPAKVHVFYIDYGNREVLSSTRLAALPPAFs 788
Cdd:cd20429    8 KLEVLMEEMILYYNKTE--ERPVAIEKNKVYAAKI-ENNWYRVLVKGILTNGLVSVYELDYGKHELVSIRKVQPLIEKF- 83


                 ....*...
gi 654822484 789 tRTLPPQA 796
Cdd:cd20429   84 -RQLPFQA 90
Tudor_TDRD15_rpt3 cd20438
third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 732-810 2.86e-05

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: 44.77  E-value: 2.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 732 APRRGEFCIAKFA-DGEWYRARVEKVESpAKVHVFYIDYGNREVLSSTRLAALPPAFStrTLPPQATEYAFAYIqVPQDE 810
Cdd:cd20438   54 KPEPGLLCCARYSkDRHYYRAVITEVLD-LKVSVYFLDFGNTDTVPFYDVKTLLPEFS--ELPALAMCCSLAHV-FPVEE 129
Tudor_vreteno-like_rpt2 cd20445
second Tudor domain found in Drosophila melanogaster protein vreteno and similar proteins; ...
 737-789 9.39e-05

second Tudor domain found in Drosophila melanogaster protein vreteno and similar proteins; Vreteno is a gonad-specific protein essential for germline development to repress transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process in both germline and somatic gonadal tissues by mediating the repression of transposable elements during meiosis. Vreteno contains two 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: 410516  Cd Length: 56  Bit Score: 40.87  E-value: 9.39e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 654822484 737 EFCIAKFADgEWYRARVEKVESPAKVHVFYIDYGNREVLSSTRLAALPPAFST 789
Cdd:cd20445    3 ELCIAKYMD-KWYRAVCLESVGDGRPTVLFCDYGNILMARLTDIRPFPPTFAT 54
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 847-898 1.32e-04

Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.


Pssm-ID: 238102  Cd Length: 129  Bit Score: 42.65  E-value: 1.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 654822484 847 FADTKEDVGLGLVKEGMVMVDIRKEKYLQKMvTEYLNAQESAKSARLNIWRY 898
Cdd:cd00175   79 YLNGGENIAEELVKEGLARVYRYYPDDSEYY-DELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
749-898 1.68e-04

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 42.63  E-value: 1.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484   749 YRARVEKVESPAKVHVfyidYGNREVLSSTRLAAL-PPAFSTRTLPPQATEYAFAyiqvpqdEDARADAVDSVVRdiHNT 827
Cdd:smart00318   3 IRGVVERVIDGDTIRV----RLPKGPLITIRLSGIdAPETARPNKGDGTPDEPFG-------EEAKEFLKKLLLG--KKV 69

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654822484   828 QC-LLNVEYSGSVCPQVtlqFADTKEDVGLGLVKEGMVMVDIRKEKYLQKMvTEYLNAQESAKSARLNIWRY 898
Cdd:smart00318  70 QVeVDSKDRYGRFLGTV---YLNGGNNIAEELVKEGLAKVYRYADKDEYVY-DELLEAEEAAKKARKGLWSD 137
Tudor_SF cd04508
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
 736-780 3.65e-04

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


Pssm-ID: 410449 [Multi-domain]  Cd Length: 47  Bit Score: 39.11  E-value: 3.65e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 654822484 736 GEFCIAKF-ADGEWYRARVEKVESPAKVHVFYiDYGNREVLSSTRL 780
Cdd:cd04508    1 GDRVEAKWsDDGQWYPATVVAVNDDGKYTVLF-DDGNEEEVSEDDI 45
Tudor_TDRD3 cd20413
Tudor domain found in Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is ...
 734-775 4.91e-04

Tudor domain found in Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is a scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. In the nucleus, it acts as a coactivator; it recognizes and binds asymmetric dimethylation on the core histone tails associated with transcriptional activation (H3R17me2a and H4R3me2a) and recruits proteins at these arginine-methylated loci. In the cytoplasm, it may play a role in the assembly and/or disassembly of mRNA stress granules and in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins. TDRD3 contains 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: 410484  Cd Length: 53  Bit Score: 38.86  E-value: 4.91e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 654822484 734 RRGEFCIAKF-ADGEWYRARVEKVESPAKVH-VFYIDYGN-REVL 775
Cdd:cd20413    2 KPGDECLAKYwEDNKFYRAEVTAVHPSGKTAvVKFMEYGNyEEVL 46
Tudor_TDRD15_rpt6 cd20441
sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 711-790 6.04e-04

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: 40.11  E-value: 6.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 711 ENLMESMRGEIAAQPPVEGSFA---PRRGEFCIAKFA-DGEWYRARVEKVESPAKVHVFYIDYGNREVLSSTRLAALP-- 784
Cdd:cd20441   13 EKVILQLAEELNETSEKSRENAavkLKVGDLVAAEYDeDLALYRAVITAVLPGKSFKVEFIDYGNTAVVDKSNIYTLQek 92

                         90
                 ....*....|
gi 654822484 785 ----PAFSTR 790
Cdd:cd20441   93 flslPRLSIP 102
Tudor_SMN_SPF30-like cd21182
Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing ...
 736-776 1.38e-03

Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing factor 30 (SPF30), and similar proteins; This group contains SMN, SPF30, Tudor domain-containing protein 3 (TDRD3), DNA excision repair protein ERCC-6-like 2 (ERCC6L2), and similar proteins. SMN, also called component of gems 1, or Gemin-1, is part of a multimeric SMN complex that includes spliceosomal Sm core proteins and plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. SPF30, also called 30 kDa splicing factor SMNrp, SMN-related protein, or survival motor neuron domain-containing protein 1 (SMNDC1), is an essential pre-mRNA splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. TDRD3 is a scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. ERCC6L2, also called DNA repair and recombination protein RAD26-like (RAD26L), may be involved in early DNA damage response. It regulates RNA Pol II-mediated transcription via its interaction with DNA-dependent protein kinase (DNA-PK) to resolve R loops and minimize transcription-associated genome instability. Members of this group contain a single 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: 410549  Cd Length: 50  Bit Score: 37.62  E-value: 1.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 654822484 736 GEFCIAKFA-DGEWYRARVEKV-ESPAKVHVFYIDYGNREVLS 776
Cdd:cd21182    1 GDKCLAPYSdDGKYYEATIEEItEESDTATVVFDGYGNSEEVP 43
Tudor_TDRD7_rpt2 cd20428
second Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 685-796 2.16e-03

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: 39.35  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654822484 685 YRSVYVTEI-TDGLhFYAQDVETG-TKLENLMESMRGEIAAQPPVEGSFA--PRRGEFCIAKFAdGEWYRARVEKVESPA 760
Cdd:cd20428    1 YTNVRVTNVcSDGT-LYCQVPSKGlSKLNEILDKIEYYFHSRQMTSEYFVslPFCGKICLARYK-GKWARVEITNVHSSR 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 654822484 761 KVHVFYIDYGNREVLSSTRLAALPPAF--STRTLPPQA 796
Cdd:cd20428   79 ALDVHFLDTGTVASVKVSELREIPPPFlrELISIPPQA 116
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
852-897 6.57e-03

Endonuclease YncB, thermonuclease family [Replication, recombination and repair];


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 38.51  E-value: 6.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 654822484 852 EDVGLGLVKEGMVMVDIRKEKYlqKMVTEYLNAQESAKSARLNIWR 897
Cdd:COG1525  108 RDLNEELVREGLAWAYRRYSPD--KYADRYLAAEAEARAARRGLWS 151
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 851-896 8.42e-03

Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in the transcriptional coactivator p100: these, however, appear to lack the active site residues of Staphylococcal nuclease. Positions 14 (Asp-21), 34 (Arg-35), 39 (Asp-40), 42 (Glu-43) and 110 (Arg-87) [SNase numbering in parentheses] are thought to be involved in substrate-binding and catalysis.


Pssm-ID: 395448  Cd Length: 106  Bit Score: 36.92  E-value: 8.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 654822484  851 KEDVGLGLVKEGMVMV---DIRKEKYLQkmvtEYLNAQESAKSARLNIW 896
Cdd:pfam00565  60 GKNINEELVKEGLAWVykaYPPNFKHYD----ELLAAEEEAKKKKKGLW 104
 
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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