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Conserved domains on  [gi|77404397|ref|NP_055205|]
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staphylococcal nuclease domain-containing protein 1 [Homo sapiens]

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, ...
 703-785 3.82e-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: 159.77  E-value: 3.82e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 703 TGTQLEKLMENMRNDIASHPPVEGSYAPRRGEFCIAKFV-DGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLS 781
Cdd:cd20433   1 TGPQLEKLMEKLRFEIASNPPLPGSYTPRKGDLCAAKFVeDGEWYRAKVEKVEGDKKVHVLYIDYGNREVLPSTRLAALP 80


                ....
gi 77404397 782 PAFS 785
Cdd:cd20433  81 PAFS 84
SNc smart00318
Staphylococcal nuclease homologues;
21-166 6.02e-41

Staphylococcal nuclease homologues;


:

Pssm-ID: 214615  Cd Length: 137  Bit Score: 147.02  E-value: 6.02e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397     21 RGIIKMVLSGCAIIVRGQPRggppPERQINLSNIRAGNLARRAAATQpdakdTPDEPWAFPAREFLRKKLIGKEVCFTIE 100
Cdd:smart00318   4 RGVVERVIDGDTIRVRLPKG----PLITIRLSGIDAPETARPNKGDG-----TPDEPFGEEAKEFLKKLLLGKKVQVEVD 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77404397    101 NKTPQGREYGMIYLGkdtNGENIAESLVAEGLATRREGMRANNPEQNRLSECEEQAKAAKKGMWSE 166
Cdd:smart00318  75 SKDRYGRFLGTVYLN---GGNNIAEELVKEGLAKVYRYADKDEYVYDELLEAEEAAKKARKGLWSD 137
SNc smart00318
Staphylococcal nuclease homologues;
525-660 5.96e-40

Staphylococcal nuclease homologues;


:

Pssm-ID: 214615  Cd Length: 137  Bit Score: 143.94  E-value: 5.96e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397    525 GRSEAVVEYVFSGSRLKLYLPKEtCLITFLLAGIECPRGARNLPGLVQEGEPFSEEATLFTKELVLQREVEVEVESMDKA 604
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPETARPNKGDGTPDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 77404397    605 GNFIGWLHIDGA-NLSVLLVEHALSKVHFTAERSSY-YKSLLSAEEAAKQKKEKVWAH 660
Cdd:smart00318  80 GRFLGTVYLNGGnNIAEELVKEGLAKVYRYADKDEYvYDELLEAEEAAKKARKGLWSD 137
SNc smart00318
Staphylococcal nuclease homologues;
193-328 4.85e-39

Staphylococcal nuclease homologues;


:

Pssm-ID: 214615  Cd Length: 137  Bit Score: 141.24  E-value: 4.85e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397    193 KPVNAIIEHVRDGSVVRALLLPDYYlVTVMLSGIKCPTFRREADGSETP-EPFAAEAKFFTESRLLQRDVQIILES-CHN 270
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKGPL-ITIRLSGIDAPETARPNKGDGTPdEPFGEEAKEFLKKLLLGKKVQVEVDSkDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 77404397    271 QNILGTILHPNG-NITELLLKEGFARCVDWSIAVYTRgAEKLRAAERFAKERRLRIWRD 328
Cdd:smart00318  80 GRFLGTVYLNGGnNIAEELVKEGLAKVYRYADKDEYV-YDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 350-496 6.22e-39

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: 140.87  E-value: 6.22e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 350 VLNADAIVVKLNSGDYKTIHLSSIRPPRLEGENTQdknkklRPLYDIPYMFEAREFLRKKLIGKKVNVTVDYirpaspat 429
Cdd:cd00175   2 VIDGDTIRVRLPPGPLITVRLSGIDAPETARPNKG------KSETDEPFGEEAKEFLKKLLLGKKVQVEVDS-------- 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 77404397 430 etvPAFSERTCATVTI-GGINIAEALVSKGLATVIRYRQDDdqrSSHYDELLAAEARAIKNGKGLHSK 496
Cdd:cd00175  68 ---KDRYGRTLGTVYLnGGENIAEELVKEGLARVYRYYPDD---SEYYDELLEAEEAAKKARKGLWSD 129
SNc super family cl00140
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 844-895 1.13e-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: 1.13e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 77404397 844 FADSKGDVGLGLVKEGLVMVeVRKEKQFQKVITEYLNAQESAKSARLNLWRY 895
Cdd:cd00175  79 YLNGGENIAEELVKEGLARV-YRYYPDDSEYYDELLEAEEAAKKARKGLWSD 129
 
Name Accession Description Interval E-value
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
 703-785 3.82e-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: 159.77  E-value: 3.82e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 703 TGTQLEKLMENMRNDIASHPPVEGSYAPRRGEFCIAKFV-DGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLS 781
Cdd:cd20433   1 TGPQLEKLMEKLRFEIASNPPLPGSYTPRKGDLCAAKFVeDGEWYRAKVEKVEGDKKVHVLYIDYGNREVLPSTRLAALP 80


                ....
gi 77404397 782 PAFS 785
Cdd:cd20433  81 PAFS 84
SNc smart00318
Staphylococcal nuclease homologues;
21-166 6.02e-41

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 147.02  E-value: 6.02e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397     21 RGIIKMVLSGCAIIVRGQPRggppPERQINLSNIRAGNLARRAAATQpdakdTPDEPWAFPAREFLRKKLIGKEVCFTIE 100
Cdd:smart00318   4 RGVVERVIDGDTIRVRLPKG----PLITIRLSGIDAPETARPNKGDG-----TPDEPFGEEAKEFLKKLLLGKKVQVEVD 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77404397    101 NKTPQGREYGMIYLGkdtNGENIAESLVAEGLATRREGMRANNPEQNRLSECEEQAKAAKKGMWSE 166
Cdd:smart00318  75 SKDRYGRFLGTVYLN---GGNNIAEELVKEGLAKVYRYADKDEYVYDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 26-166 6.92e-41

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: 146.27  E-value: 6.92e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397  26 MVLSGCAIIVRGQPRggppPERQINLSNIRAGNLARRaaatqPDAKDTPDEPWAFPAREFLRKKLIGKEVCFTIENKTPQ 105
Cdd:cd00175   1 RVIDGDTIRVRLPPG----PLITVRLSGIDAPETARP-----NKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRY 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 77404397 106 GREYGMIYLGkdtNGENIAESLVAEGLATRREGMRANNPEQNRLSECEEQAKAAKKGMWSE 166
Cdd:cd00175  72 GRTLGTVYLN---GGENIAEELVKEGLARVYRYYPDDSEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
525-660 5.96e-40

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 143.94  E-value: 5.96e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397    525 GRSEAVVEYVFSGSRLKLYLPKEtCLITFLLAGIECPRGARNLPGLVQEGEPFSEEATLFTKELVLQREVEVEVESMDKA 604
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPETARPNKGDGTPDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 77404397    605 GNFIGWLHIDGA-NLSVLLVEHALSKVHFTAERSSY-YKSLLSAEEAAKQKKEKVWAH 660
Cdd:smart00318  80 GRFLGTVYLNGGnNIAEELVKEGLAKVYRYADKDEYvYDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 533-660 1.51e-39

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: 142.41  E-value: 1.51e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 533 YVFSGSRLKLYLPKEtCLITFLLAGIECPRGARNLPGLVQEGEPFSEEATLFTKELVLQREVEVEVESMDKAGNFIGWLH 612
Cdd:cd00175   1 RVIDGDTIRVRLPPG-PLITVRLSGIDAPETARPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTVY 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 77404397 613 IDGA-NLSVLLVEHALSKVHFTAERSS-YYKSLLSAEEAAKQKKEKVWAH 660
Cdd:cd00175  80 LNGGeNIAEELVKEGLARVYRYYPDDSeYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
193-328 4.85e-39

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 141.24  E-value: 4.85e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397    193 KPVNAIIEHVRDGSVVRALLLPDYYlVTVMLSGIKCPTFRREADGSETP-EPFAAEAKFFTESRLLQRDVQIILES-CHN 270
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKGPL-ITIRLSGIDAPETARPNKGDGTPdEPFGEEAKEFLKKLLLGKKVQVEVDSkDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 77404397    271 QNILGTILHPNG-NITELLLKEGFARCVDWSIAVYTRgAEKLRAAERFAKERRLRIWRD 328
Cdd:smart00318  80 GRFLGTVYLNGGnNIAEELVKEGLAKVYRYADKDEYV-YDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 350-496 6.22e-39

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: 140.87  E-value: 6.22e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 350 VLNADAIVVKLNSGDYKTIHLSSIRPPRLEGENTQdknkklRPLYDIPYMFEAREFLRKKLIGKKVNVTVDYirpaspat 429
Cdd:cd00175   2 VIDGDTIRVRLPPGPLITVRLSGIDAPETARPNKG------KSETDEPFGEEAKEFLKKLLLGKKVQVEVDS-------- 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 77404397 430 etvPAFSERTCATVTI-GGINIAEALVSKGLATVIRYRQDDdqrSSHYDELLAAEARAIKNGKGLHSK 496
Cdd:cd00175  68 ---KDRYGRTLGTVYLnGGENIAEELVKEGLARVYRYYPDD---SEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
341-495 6.43e-39

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 141.24  E-value: 6.43e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397    341 KQFVAKVMQVLNADAIVVKLNSGDYKTIHLSSIRPPRLEGENTQDKnkklrpLYDIPYMFEAREFLRKKLIGKKVNVTVD 420
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKGPLITIRLSGIDAPETARPNKGDG------TPDEPFGEEAKEFLKKLLLGKKVQVEVD 74

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77404397    421 YIrpaspatetvpAFSERTCATVTI-GGINIAEALVSKGLATVIRYRQDDDQRsshYDELLAAEARAIKNGKGLHS 495
Cdd:smart00318  75 SK-----------DRYGRFLGTVYLnGGNNIAEELVKEGLAKVYRYADKDEYV---YDELLEAEEAAKKARKGLWS 136
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 201-328 2.24e-37

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: 136.25  E-value: 2.24e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 201 HVRDGSVVRALLLPDYYlVTVMLSGIKCP-TFRREADGSETPEPFAAEAKFFTESRLLQRDVQIILES-CHNQNILGTIL 278
Cdd:cd00175   1 RVIDGDTIRVRLPPGPL-ITVRLSGIDAPeTARPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSkDRYGRTLGTVY 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 77404397 279 HPNG-NITELLLKEGFARCVDWSIAVyTRGAEKLRAAERFAKERRLRIWRD 328
Cdd:cd00175  80 LNGGeNIAEELVKEGLARVYRYYPDD-SEYYDELLEAEEAAKKARKGLWSD 129
TUDOR pfam00567
Tudor domain;
681-799 2.67e-30

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 115.53  E-value: 2.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397   681 SYKPVFVTEITDDLHFYVQDVETGTQLEKLMENMRNDIASHPPVegSYAPRRGEFCIAKF-VDGEWYRARVEKVESPAKI 759
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQPKSDSKKLEKLTEELQEYYASKPPE--SLPPAVGDGCVAAFsEDGKWYRAKITESLDDGLV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 77404397   760 HVFYIDYGNREVLPSTRLGTLSPAFSTrvLPAQATEYAFA 799
Cdd:pfam00567  79 EVLFIDYGNTETVPLSDLRPLPPELES--LPPQAIKCQLA 116
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 552-659 8.80e-19

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: 82.37  E-value: 8.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397   552 TFLLAGIECPRGARNLpglvQEGEPFSEEATLFTKELVLQREVEVEVESMDKAGNFIGWLHIDGANLSVLLVEHALSKVH 631
Cdd:pfam00565   1 RVRLVGIDAPETAKPN----TPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYLNGKNINEELVKEGLAWVY 76

                          90       100
                  ....*....|....*....|....*....
gi 77404397   632 FTAE-RSSYYKSLLSAEEAAKQKKEKVWA 659
Cdd:pfam00565  77 KAYPpNFKHYDELLAAEEEAKKKKKGLWS 105
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 728-784 6.32e-17

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: 75.39  E-value: 6.32e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 77404397    728 YAPRRGEFCIAKFVDGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLSPAF 784
Cdd:smart00333   1 PTFKVGDKVAARWEDGEWYRARIVKVDGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 49-166 7.79e-16

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: 73.90  E-value: 7.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397    49 INLSNIRAGNLARRaaatqpdakDTPDEPWAFPAREFLRKKLIGKEVCFTIENKTPQGREYGMIYLgkdtNGENIAESLV 128
Cdd:pfam00565   2 VRLVGIDAPETAKP---------NTPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYL----NGKNINEELV 68

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 77404397   129 AEGLATRREGMRANNPEQNRLSECEEQAKAAKKGMWSE 166
Cdd:pfam00565  69 KEGLAWVYKAYPPNFKHYDELLAAEEEAKKKKKGLWSD 106
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 367-496 4.36e-15

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: 71.97  E-value: 4.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397   367 TIHLSSIRPPRLEGENTQDKnkklrplydiPYMFEAREFLRKKLIGKKVNVTVD----YirpaspatetvpafsERTCAT 442
Cdd:pfam00565   1 RVRLVGIDAPETAKPNTPVQ----------PFGKEAKEFLKKLVLGKKVVVLEFdkdkY---------------GRTLGY 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 77404397   443 VTIGGINIAEALVSKGLATVIRYRqddDQRSSHYDELLAAEARAIKNGKGLHSK 496
Cdd:pfam00565  56 VYLNGKNINEELVKEGLAWVYKAY---PPNFKHYDELLAAEEEAKKKKKGLWSD 106
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 220-328 6.08e-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: 68.50  E-value: 6.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397   220 TVMLSGIKCPtfrREADGSETPEPFAAEAKFFTESRLLQRDVQI-ILESCHNQNILGTILHPNGNITELLLKEGFARcVD 298
Cdd:pfam00565   1 RVRLVGIDAP---ETAKPNTPVQPFGKEAKEFLKKLVLGKKVVVlEFDKDKYGRTLGYVYLNGKNINEELVKEGLAW-VY 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 77404397   299 WSIAVYTRGAEKLRAAERFAKERRLRIWRD 328
Cdd:pfam00565  77 KAYPPNFKHYDELLAAEEEAKKKKKGLWSD 106
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
330-500 2.05e-13

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 68.94  E-value: 2.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 330 VAPTANLDQKDKQFVAKVMQVLNADAIVVKLNSGDYKtIHLSSIRPPRlegenTQDKNKKLRPLYDipymfEAREFLRKK 409
Cdd:COG1525  11 ALAALAAAAAAATLTAGVVRVIDGDTLRVRDDGKGER-VRLAGIDAPE-----LGQPCGPEQPCGE-----EARQALRAL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 410 LIGKKVNVTVD-----YirpaspatetvpafsERTCATVTIGGINIAEALVSKGLATVirYRQDDDQRssHYDELLAAEA 484
Cdd:COG1525  80 LAGKTVTLEPDegrdrY---------------GRLLAYVYVDGRDLNEELVREGLAWA--YRRYSPDK--YADRYLAAEA 140

                       170
                ....*....|....*.
gi 77404397 485 RAIKNGKGLHSKKEVP 500
Cdd:COG1525 141 EARAARRGLWSDAFPV 156
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
517-667 2.23e-13

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 68.94  E-value: 2.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 517 FLPFLQRAGRSEAVVEYVFSGSRLKLYLPKETclITFLLAGIECPRgarnLPGLVQEGEPFSEEATLFTKELVLQREVEV 596
Cdd:COG1525  14 ALAAAAAAATLTAGVVRVIDGDTLRVRDDGKG--ERVRLAGIDAPE----LGQPCGPEQPCGEEARQALRALLAGKTVTL 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 77404397 597 EV-ESMDKAGNFIGWLHIDGANLSVLLVEHALSKVHFTAERSSYYKSLLSAEEAAKQKKEKVWAHYEEQPVE 667
Cdd:COG1525  88 EPdEGRDRYGRLLAYVYVDGRDLNEELVREGLAWAYRRYSPDKYADRYLAAEAEARAARRGLWSDAFPVPPE 159
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
69-168 3.02e-11

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 62.77  E-value: 3.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397  69 DAKDTPDEPWAFPAREFLRKKLIGKEV-CFTIENKTPQGREYGMIYLgkdtNGENIAESLVAEGLAtRREGMRANNPEQN 147
Cdd:COG1525  59 GQPCGPEQPCGEEARQALRALLAGKTVtLEPDEGRDRYGRLLAYVYV----DGRDLNEELVREGLA-WAYRRYSPDKYAD 133

                        90       100
                ....*....|....*....|.
gi 77404397 148 RLSECEEQAKAAKKGMWSEGN 168
Cdd:COG1525 134 RYLAAEAEARAARRGLWSDAF 154
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
194-328 1.39e-10

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 60.85  E-value: 1.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 194 PVNAIIEHVRDGSVVRalLLPDYYLVTVMLSGIKCPtfrrEADGSETPE-PFAAEAKFFTESRLLQRDVQIILESCHNQN 272
Cdd:COG1525  23 TLTAGVVRVIDGDTLR--VRDDGKGERVRLAGIDAP----ELGQPCGPEqPCGEEARQALRALLAGKTVTLEPDEGRDRY 96

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 77404397 273 --ILGTILHPNGNITELLLKEGFARcvDWSIAVYTRGAEKLRAAERFAKERRLRIWRD 328
Cdd:COG1525  97 grLLAYVYVDGRDLNEELVREGLAW--AYRRYSPDKYADRYLAAEAEARAARRGLWSD 152
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 844-895 1.13e-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: 1.13e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 77404397 844 FADSKGDVGLGLVKEGLVMVeVRKEKQFQKVITEYLNAQESAKSARLNLWRY 895
Cdd:cd00175  79 YLNGGENIAEELVKEGLARV-YRYYPDDSEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
844-895 6.70e-04

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 40.71  E-value: 6.70e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 77404397    844 FADSKGDVGLGLVKEGLVmvEVRKEKQFQKV-ITEYLNAQESAKSARLNLWRY 895
Cdd:smart00318  87 YLNGGNNIAEELVKEGLA--KVYRYADKDEYvYDELLEAEEAAKKARKGLWSD 137
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 850-893 1.20e-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: 39.23  E-value: 1.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 77404397   850 DVGLGLVKEGLVMVEVRKEKQFQKvITEYLNAQESAKSARLNLW 893
Cdd:pfam00565  62 NINEELVKEGLAWVYKAYPPNFKH-YDELLAAEEEAKKKKKGLW 104
 
Name Accession Description Interval E-value
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
 703-785 3.82e-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: 159.77  E-value: 3.82e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 703 TGTQLEKLMENMRNDIASHPPVEGSYAPRRGEFCIAKFV-DGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLS 781
Cdd:cd20433   1 TGPQLEKLMEKLRFEIASNPPLPGSYTPRKGDLCAAKFVeDGEWYRAKVEKVEGDKKVHVLYIDYGNREVLPSTRLAALP 80


                ....
gi 77404397 782 PAFS 785
Cdd:cd20433  81 PAFS 84
SNc smart00318
Staphylococcal nuclease homologues;
21-166 6.02e-41

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 147.02  E-value: 6.02e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397     21 RGIIKMVLSGCAIIVRGQPRggppPERQINLSNIRAGNLARRAAATQpdakdTPDEPWAFPAREFLRKKLIGKEVCFTIE 100
Cdd:smart00318   4 RGVVERVIDGDTIRVRLPKG----PLITIRLSGIDAPETARPNKGDG-----TPDEPFGEEAKEFLKKLLLGKKVQVEVD 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77404397    101 NKTPQGREYGMIYLGkdtNGENIAESLVAEGLATRREGMRANNPEQNRLSECEEQAKAAKKGMWSE 166
Cdd:smart00318  75 SKDRYGRFLGTVYLN---GGNNIAEELVKEGLAKVYRYADKDEYVYDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 26-166 6.92e-41

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: 146.27  E-value: 6.92e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397  26 MVLSGCAIIVRGQPRggppPERQINLSNIRAGNLARRaaatqPDAKDTPDEPWAFPAREFLRKKLIGKEVCFTIENKTPQ 105
Cdd:cd00175   1 RVIDGDTIRVRLPPG----PLITVRLSGIDAPETARP-----NKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRY 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 77404397 106 GREYGMIYLGkdtNGENIAESLVAEGLATRREGMRANNPEQNRLSECEEQAKAAKKGMWSE 166
Cdd:cd00175  72 GRTLGTVYLN---GGENIAEELVKEGLARVYRYYPDDSEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
525-660 5.96e-40

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 143.94  E-value: 5.96e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397    525 GRSEAVVEYVFSGSRLKLYLPKEtCLITFLLAGIECPRGARNLPGLVQEGEPFSEEATLFTKELVLQREVEVEVESMDKA 604
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPETARPNKGDGTPDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 77404397    605 GNFIGWLHIDGA-NLSVLLVEHALSKVHFTAERSSY-YKSLLSAEEAAKQKKEKVWAH 660
Cdd:smart00318  80 GRFLGTVYLNGGnNIAEELVKEGLAKVYRYADKDEYvYDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 533-660 1.51e-39

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: 142.41  E-value: 1.51e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 533 YVFSGSRLKLYLPKEtCLITFLLAGIECPRGARNLPGLVQEGEPFSEEATLFTKELVLQREVEVEVESMDKAGNFIGWLH 612
Cdd:cd00175   1 RVIDGDTIRVRLPPG-PLITVRLSGIDAPETARPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTVY 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 77404397 613 IDGA-NLSVLLVEHALSKVHFTAERSS-YYKSLLSAEEAAKQKKEKVWAH 660
Cdd:cd00175  80 LNGGeNIAEELVKEGLARVYRYYPDDSeYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
193-328 4.85e-39

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 141.24  E-value: 4.85e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397    193 KPVNAIIEHVRDGSVVRALLLPDYYlVTVMLSGIKCPTFRREADGSETP-EPFAAEAKFFTESRLLQRDVQIILES-CHN 270
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKGPL-ITIRLSGIDAPETARPNKGDGTPdEPFGEEAKEFLKKLLLGKKVQVEVDSkDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 77404397    271 QNILGTILHPNG-NITELLLKEGFARCVDWSIAVYTRgAEKLRAAERFAKERRLRIWRD 328
Cdd:smart00318  80 GRFLGTVYLNGGnNIAEELVKEGLAKVYRYADKDEYV-YDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 350-496 6.22e-39

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: 140.87  E-value: 6.22e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 350 VLNADAIVVKLNSGDYKTIHLSSIRPPRLEGENTQdknkklRPLYDIPYMFEAREFLRKKLIGKKVNVTVDYirpaspat 429
Cdd:cd00175   2 VIDGDTIRVRLPPGPLITVRLSGIDAPETARPNKG------KSETDEPFGEEAKEFLKKLLLGKKVQVEVDS-------- 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 77404397 430 etvPAFSERTCATVTI-GGINIAEALVSKGLATVIRYRQDDdqrSSHYDELLAAEARAIKNGKGLHSK 496
Cdd:cd00175  68 ---KDRYGRTLGTVYLnGGENIAEELVKEGLARVYRYYPDD---SEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
341-495 6.43e-39

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 141.24  E-value: 6.43e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397    341 KQFVAKVMQVLNADAIVVKLNSGDYKTIHLSSIRPPRLEGENTQDKnkklrpLYDIPYMFEAREFLRKKLIGKKVNVTVD 420
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKGPLITIRLSGIDAPETARPNKGDG------TPDEPFGEEAKEFLKKLLLGKKVQVEVD 74

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77404397    421 YIrpaspatetvpAFSERTCATVTI-GGINIAEALVSKGLATVIRYRQDDDQRsshYDELLAAEARAIKNGKGLHS 495
Cdd:smart00318  75 SK-----------DRYGRFLGTVYLnGGNNIAEELVKEGLAKVYRYADKDEYV---YDELLEAEEAAKKARKGLWS 136
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 201-328 2.24e-37

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: 136.25  E-value: 2.24e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 201 HVRDGSVVRALLLPDYYlVTVMLSGIKCP-TFRREADGSETPEPFAAEAKFFTESRLLQRDVQIILES-CHNQNILGTIL 278
Cdd:cd00175   1 RVIDGDTIRVRLPPGPL-ITVRLSGIDAPeTARPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSkDRYGRTLGTVY 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 77404397 279 HPNG-NITELLLKEGFARCVDWSIAVyTRGAEKLRAAERFAKERRLRIWRD 328
Cdd:cd00175  80 LNGGeNIAEELVKEGLARVYRYYPDD-SEYYDELLEAEEAAKKARKGLWSD 129
TUDOR pfam00567
Tudor domain;
681-799 2.67e-30

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 115.53  E-value: 2.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397   681 SYKPVFVTEITDDLHFYVQDVETGTQLEKLMENMRNDIASHPPVegSYAPRRGEFCIAKF-VDGEWYRARVEKVESPAKI 759
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQPKSDSKKLEKLTEELQEYYASKPPE--SLPPAVGDGCVAAFsEDGKWYRAKITESLDDGLV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 77404397   760 HVFYIDYGNREVLPSTRLGTLSPAFSTrvLPAQATEYAFA 799
Cdd:pfam00567  79 EVLFIDYGNTETVPLSDLRPLPPELES--LPPQAIKCQLA 116
Tudor_AtTudor1-like cd20443
Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor ...
 696-804 2.75e-21

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: 89.83  E-value: 2.75e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 696 FYVQDVETG------TQLEKLmenmrnDIASHPPVEGSYAPRRGEFCIAKF-VDGEWYRARVekVESPA--------KIH 760
Cdd:cd20443   4 FYVQVVSDQrlssiqQQLEGL------SLKDKANPPGGFNPKKGELVLAQFsADNSWNRAMV--VNAPRqgtqspkdEYE 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 77404397 761 VFYIDYGNREVLPSTRLGTLSPAFSTrvLPAQATEYAFAFIQVP 804
Cdd:cd20443  76 VFYIDYGNQETVPLSALRPLDPSVSS--APGLAQLCSLAHIKVP 117
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 685-806 1.13e-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: 85.88  E-value: 1.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 685 VFVTEITDDLHFYVQdVETGTQLEKLME---NMRNDIAShPPVEGSYAPRRGEFCIAKF-VDGEWYRARVEKVESPAKI- 759
Cdd:cd20408   1 GTVTEFKNPGEFYIQ-IYTLEVLESLVKltsQLKKTYAS-VNNHKEYIPEVGEVCVAKYsEDQNWYRALVQTVDVQQKKa 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 77404397 760 HVFYIDYGNREVLPSTRLGTLSPAFStrVLPAQATEYAFAFIQVPQD 806
Cdd:cd20408  79 GVFYIDYGNEETVPLNRIQPLKKDIE--LFPPCAIKCCLANVKPPSG 123
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 552-659 8.80e-19

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: 82.37  E-value: 8.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397   552 TFLLAGIECPRGARNLpglvQEGEPFSEEATLFTKELVLQREVEVEVESMDKAGNFIGWLHIDGANLSVLLVEHALSKVH 631
Cdd:pfam00565   1 RVRLVGIDAPETAKPN----TPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYLNGKNINEELVKEGLAWVY 76

                          90       100
                  ....*....|....*....|....*....
gi 77404397   632 FTAE-RSSYYKSLLSAEEAAKQKKEKVWA 659
Cdd:pfam00565  77 KAYPpNFKHYDELLAAEEEAKKKKKGLWS 105
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 728-784 6.32e-17

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: 75.39  E-value: 6.32e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 77404397    728 YAPRRGEFCIAKFVDGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLSPAF 784
Cdd:smart00333   1 PTFKVGDKVAARWEDGEWYRARIVKVDGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 49-166 7.79e-16

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: 73.90  E-value: 7.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397    49 INLSNIRAGNLARRaaatqpdakDTPDEPWAFPAREFLRKKLIGKEVCFTIENKTPQGREYGMIYLgkdtNGENIAESLV 128
Cdd:pfam00565   2 VRLVGIDAPETAKP---------NTPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYL----NGKNINEELV 68

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 77404397   129 AEGLATRREGMRANNPEQNRLSECEEQAKAAKKGMWSE 166
Cdd:pfam00565  69 KEGLAWVYKAYPPNFKHYDELLAAEEEAKKKKKGLWSD 106
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 367-496 4.36e-15

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: 71.97  E-value: 4.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397   367 TIHLSSIRPPRLEGENTQDKnkklrplydiPYMFEAREFLRKKLIGKKVNVTVD----YirpaspatetvpafsERTCAT 442
Cdd:pfam00565   1 RVRLVGIDAPETAKPNTPVQ----------PFGKEAKEFLKKLVLGKKVVVLEFdkdkY---------------GRTLGY 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 77404397   443 VTIGGINIAEALVSKGLATVIRYRqddDQRSSHYDELLAAEARAIKNGKGLHSK 496
Cdd:pfam00565  56 VYLNGKNINEELVKEGLAWVYKAY---PPNFKHYDELLAAEEEAKKKKKGLWSD 106
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 220-328 6.08e-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: 68.50  E-value: 6.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397   220 TVMLSGIKCPtfrREADGSETPEPFAAEAKFFTESRLLQRDVQI-ILESCHNQNILGTILHPNGNITELLLKEGFARcVD 298
Cdd:pfam00565   1 RVRLVGIDAP---ETAKPNTPVQPFGKEAKEFLKKLVLGKKVVVlEFDKDKYGRTLGYVYLNGKNINEELVKEGLAW-VY 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 77404397   299 WSIAVYTRGAEKLRAAERFAKERRLRIWRD 328
Cdd:pfam00565  77 KAYPPNFKHYDELLAAEEEAKKKKKGLWSD 106
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 733-777 1.80e-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: 65.23  E-value: 1.80e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 77404397 733 GEFCIAKF-VDGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRL 777
Cdd:cd20379   2 GDLCAAKYeEDGKWYRARVLEVLSNDKVEVFFVDYGNTETVPLSDL 47
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
330-500 2.05e-13

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 68.94  E-value: 2.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 330 VAPTANLDQKDKQFVAKVMQVLNADAIVVKLNSGDYKtIHLSSIRPPRlegenTQDKNKKLRPLYDipymfEAREFLRKK 409
Cdd:COG1525  11 ALAALAAAAAAATLTAGVVRVIDGDTLRVRDDGKGER-VRLAGIDAPE-----LGQPCGPEQPCGE-----EARQALRAL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 410 LIGKKVNVTVD-----YirpaspatetvpafsERTCATVTIGGINIAEALVSKGLATVirYRQDDDQRssHYDELLAAEA 484
Cdd:COG1525  80 LAGKTVTLEPDegrdrY---------------GRLLAYVYVDGRDLNEELVREGLAWA--YRRYSPDK--YADRYLAAEA 140

                       170
                ....*....|....*.
gi 77404397 485 RAIKNGKGLHSKKEVP 500
Cdd:COG1525 141 EARAARRGLWSDAFPV 156
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
517-667 2.23e-13

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 68.94  E-value: 2.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 517 FLPFLQRAGRSEAVVEYVFSGSRLKLYLPKETclITFLLAGIECPRgarnLPGLVQEGEPFSEEATLFTKELVLQREVEV 596
Cdd:COG1525  14 ALAAAAAAATLTAGVVRVIDGDTLRVRDDGKG--ERVRLAGIDAPE----LGQPCGPEQPCGEEARQALRALLAGKTVTL 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 77404397 597 EV-ESMDKAGNFIGWLHIDGANLSVLLVEHALSKVHFTAERSSYYKSLLSAEEAAKQKKEKVWAHYEEQPVE 667
Cdd:COG1525  88 EPdEGRDRYGRLLAYVYVDGRDLNEELVREGLAWAYRRYSPDKYADRYLAAEAEARAARRGLWSDAFPVPPE 159
Tudor_TDRD15_rpt5 cd20440
fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 685-802 9.45e-13

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: 65.94  E-value: 9.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 685 VFVTEITDDLHFYVQDVETGTQLEKLMENMRNdiASHPPVEGSYAPRRGEFCIAKFV-DGEWYRARVEKVESPAKIHVFY 763
Cdd:cd20440  14 VYITHVYSPAKFYCQLDRNTEILEALMEKIAE--ISKLFNSQILDNCKTRLCLAKYFeDGQWYRALAHPVESSSHLSVYF 91

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 77404397 764 IDYGNREVLPSTRLgtlspafstRVLPAQATEYAFAFIQ 802
Cdd:cd20440  92 VDYGNKQIVEKNEV---------LPIPDTAVDLLLTPMQ 121
Tudor_TDRD1_rpt2 cd20409
second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 704-782 9.94e-13

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: 64.40  E-value: 9.94e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 704 GTQLEKLMENMRNDiASHPPVEGSYAPRRGEFCIAKFV-DGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLSP 782
Cdd:cd20409   1 GRQLAELQESLSAY-CKVAPASSDFSPAVGEVCCAQFTeDNQWYRASVLAYSSEDSVLVGYIDFGNSEEVALSRLRPIPP 79
Tudor_TDRD6_rpt2 cd20421
second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 684-784 3.09e-12

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: 64.37  E-value: 3.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 684 PVFVTEITDDLHFYVQDVETGTQLEKLMENM-RNDIASHPPVEGSYAPRRGEFCIAKFVDGEWYRARVEKVESPAK-IHV 761
Cdd:cd20421  14 TVVVTEVTDPHRIFCQLRSLSQELKRLSESMhQYYEGRVGSGYETRPEKLGSPCAARGSDGRWYRAVLQQVFSANRvVEV 93

                        90       100
                ....*....|....*....|...
gi 77404397 762 FYIDYGNREVLPSTRLGTLSPAF 784
Cdd:cd20421  94 LHVDYGRKEVVSVSNLRYLAPEY 116
Tudor_TDRD1_rpt4 cd20411
fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 687-784 3.42e-12

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: 64.00  E-value: 3.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 687 VTEITDDLHFYVQDVETGTQLEKLMENMRnDIA---SHPPVEGSYAPRRGEFCIAKFV-DGEWYRARVEKVeSPAKIHVF 762
Cdd:cd20411   3 VLEVISPDLFYALPKTGQVNVEKLKALMT-ELAeycSKQSVPQQFRPRIGDACCARFTgDKNWYRAVVLET-SDSEVKVL 80

                        90       100
                ....*....|....*....|..
gi 77404397 763 YIDYGNREVLPSTRLGTLSPAF 784
Cdd:cd20411  81 YADYGNTETLPLSRILPITKSH 102
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
69-168 3.02e-11

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 62.77  E-value: 3.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397  69 DAKDTPDEPWAFPAREFLRKKLIGKEV-CFTIENKTPQGREYGMIYLgkdtNGENIAESLVAEGLAtRREGMRANNPEQN 147
Cdd:COG1525  59 GQPCGPEQPCGEEARQALRALLAGKTVtLEPDEGRDRYGRLLAYVYV----DGRDLNEELVREGLA-WAYRRYSPDKYAD 133

                        90       100
                ....*....|....*....|.
gi 77404397 148 RLSECEEQAKAAKKGMWSEGN 168
Cdd:COG1525 134 RYLAAEAEARAARRGLWSDAF 154
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 725-802 1.07e-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: 58.99  E-value: 1.07e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 77404397 725 EGSYAPRRGEFCIAKFVDGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLSPAFSTrvLPAQATEYAFAFIQ 802
Cdd:cd20415  20 LEILCPVQGQACVALFEDGAWYRARIIGLPGHREVEVKYVDFGNTATVTIKHVRKIKDDFLS--LPEKARECRLAFIE 95
Tudor_TDRD6_rpt5 cd20424
fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 685-793 1.25e-10

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


Pssm-ID: 410495  Cd Length: 126  Bit Score: 59.83  E-value: 1.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 685 VFVTEITDDLHFYVQDVETGTQLEKLMENMRNDIASHPPVEGSYAPrrGEFCIAKFVDGEWYRARVEKVESPAKihVFYI 764
Cdd:cd20424  16 VYITYVNDPWTFYCQLARNAGVLDQLASAISRLSSEIRKLELSVNP--GTLCLAKYSDQHWYRGIIITNKNSTE--VFFV 91

                        90       100       110
                ....*....|....*....|....*....|
gi 77404397 765 DYGNREVLPSTRLGTL-SPAFSTRVLPAQA 793
Cdd:cd20424  92 DYGNTEKVEKEDMLPIpSDAYELLLLPMQA 121
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
194-328 1.39e-10

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 60.85  E-value: 1.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 194 PVNAIIEHVRDGSVVRalLLPDYYLVTVMLSGIKCPtfrrEADGSETPE-PFAAEAKFFTESRLLQRDVQIILESCHNQN 272
Cdd:COG1525  23 TLTAGVVRVIDGDTLR--VRDDGKGERVRLAGIDAP----ELGQPCGPEqPCGEEARQALRALLAGKTVTLEPDEGRDRY 96

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 77404397 273 --ILGTILHPNGNITELLLKEGFARcvDWSIAVYTRGAEKLRAAERFAKERRLRIWRD 328
Cdd:COG1525  97 grLLAYVYVDGRDLNEELVREGLAW--AYRRYSPDKYADRYLAAEAEARAARRGLWSD 152
Tudor_TDRD6_rpt6 cd20425
sixth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 685-784 2.28e-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: 2.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 685 VFVTEITDDLHFYVQDVETGTQLEKLMENMRNDIASHPPVEGSYApRRGEFCIAKFV-DGEWYRARVEKVESPAKIHVFY 763
Cdd:cd20425   4 VYVSHVNSPSDFYVQLAQDEDELSMISEKLNASKANDEEVECESL-QLGDLICAEYPeDGLWYRAVVKEKIPNNLVSVQF 82

                        90       100
                ....*....|....*....|.
gi 77404397 764 IDYGNREVLPSTRLGTLSPAF 784
Cdd:cd20425  83 IDYGNTSVVQPSKIHRLPKEL 103
Tudor_TDRD1_rpt3 cd20410
third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 728-784 2.59e-10

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: 56.58  E-value: 2.59e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 77404397 728 YAPRRGEFCIAKFV-DGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLSPAF 784
Cdd:cd20410   1 FKPIVGEPCCAFFSgDGNWYRAMVKEILPGGAVKVHFVDYGNVEEVTLDKLRKITSTF 58
Tudor_TDRD15_rpt3 cd20438
third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 686-807 1.78e-09

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: 57.10  E-value: 1.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 686 FVTEITDDLHFYVQDVETGTQLEKLMENMrNDIASHPPVEGSY--APRRGEFCIAKFV-DGEWYRARVEKVESpAKIHVF 762
Cdd:cd20438  10 FVEYVLNPSNFWIRTDEYNNEFQALMKNI-ADIYNLCGNDEELlkKPEPGLLCCARYSkDRHYYRAVITEVLD-LKVSVY 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 77404397 763 YIDYGNREVLPSTRLGTLSPAFStrVLPAQATEYAFAFIqVPQDD 807
Cdd:cd20438  88 FLDFGNTDTVPFYDVKTLLPEFS--ELPALAMCCSLAHV-FPVEE 129
Tudor_TDRD15_rpt2 cd20437
second Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 696-787 2.54e-09

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: 55.89  E-value: 2.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 696 FYVQDVETGTQLEKLMENM-----RNDIASHPPVEGSyaprrGEFCIAKFVDGEWYRARVEKVESPAKIHVFYIDYGNRE 770
Cdd:cd20437  18 FYCQLLSWEPELSKLTTQMtlhyeSVSKELNPSCENF-----GLLCAAKGKDGQWHRGFLQQLLPPSQVKVWFIDYGNSE 92

                        90
                ....*....|....*..
gi 77404397 771 VLPSTRLGTLSPAFSTR 787
Cdd:cd20437  93 AVSSHSVLKLPPDFFSL 109
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
 688-786 3.21e-09

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: 55.09  E-value: 3.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 688 TEITDDLHFYVQ--DVETGTQLEKLMENMRNDIASHPPVEgsyaPRRGEFCIAKFVDGE---WYRARVEKVeSPAKIHVF 762
Cdd:cd20431   1 TEVVEVGHFWGYriDENSSEILQQLTAEINQRQLVPLTTK----PVPNLLCLAPFTDADmkkYYRAKILYV-SGSSAEVF 75

                        90       100
                ....*....|....*....|....
gi 77404397 763 YIDYGNREVLPSTRLGTLSPAFST 786
Cdd:cd20431  76 FVDYGNTSQVPSSLLREIPETLLT 99
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 736-795 9.59e-09

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: 52.87  E-value: 9.59e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 77404397 736 CIAKF-VDGEWYRARVEKVESPAK-IHVFYIDYGNREVLPSTRLGTLSPAFSTrvLPAQATE 795
Cdd:cd20423   9 CLAKYsEDGKWCRALIDNVYEPVEmVEVTYVDYGNKELVSLKNLRSISEEFLK--LKAQAFR 68
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 736-803 1.14e-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: 53.57  E-value: 1.14e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 736 CIAKFVDGEWYRARVEKVES--PAKIHVFYIDYGNREVLPSTRLgtlspafstRVLPAQATEYAFAFIQV 803
Cdd:cd20418  10 CLAEYSDGKWYRAKLLSILEfnPVKILVRHVDYGSTAALPTSRL---------RQIPAELMQYPCQAIKV 70
Tudor_TDRD8 cd20430
Tudor domain found in Tudor domain-containing protein 8 (TDRD8) and similar proteins; TDRD8, ...
 722-785 4.71e-08

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: 50.75  E-value: 4.71e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 77404397 722 PPVEGSYAPRR--GefciAKF-VDGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLSPAFS 785
Cdd:cd20430  13 PPLFGTPDPNKiyG----GKFsEDNCWYRCKVKSILSDEKCTVQYIDYGNTETVSRSSIVELPPDLQ 75
Tudor_TDRD2 cd20412
Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, ...
 705-795 5.11e-08

Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, also called Tudor and KH domain-containing protein (TDRKH), participates in the primary piwi-interacting RNA (piRNA) biogenesis pathway and is required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for germline integrity. The family also includes the TDRD2 homolog found in Drosophila melanogaster (dTDRKH), which is also called partner of PIWIs protein, or PAPI, and is involved in Zucchini-mediated piRNA 3'-end maturation. TDRD2 contains two KH domains and one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410483  Cd Length: 95  Bit Score: 51.53  E-value: 5.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 705 TQLEKLMENMRNDIASHPPVEGSYAPRRGEFCIAKFV-DGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLSPA 783
Cdd:cd20412   4 LQLDKLVQEMTQYYESEENRHTLLTVQVGDIVAAPFRhDGSWYRARVLGFLENGNLDLYFVDYGDSGYVPLEDLRALRSD 83

                        90
                ....*....|..
gi 77404397 784 FSTrvLPAQATE 795
Cdd:cd20412  84 FLS--LPFQAIE 93
Tudor_TDRD15_rpt4 cd20439
fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 695-793 8.08e-08

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: 51.72  E-value: 8.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 695 HFYVQDVETGTQLEKLMENMRN--DIASHPPVEGSYAprrgefCIAKFV-DGEWYRARVEKVESPAKIHVFYIDYGNREV 771
Cdd:cd20439  24 DFWCQLQTKSSELKSLMKQIQSyyLIHNDPYKHGQIA------CVAKYSkDGKWYRAAVLKQVSAKEVDVIFVDYGNQER 97

                        90       100
                ....*....|....*....|..
gi 77404397 772 LPSTRLGTLSPAFSTrvLPAQA 793
Cdd:cd20439  98 VLISDLRAIKPQFLL--LEGQA 117
Tudor_TDRD7_rpt1 cd20427
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 706-807 9.75e-08

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


Pssm-ID: 410498  Cd Length: 98  Bit Score: 50.89  E-value: 9.75e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 706 QLEKLMENMRNDIASHPPVEgsyAPRRGEFCIAKFVDGEWYRARVEKVESpAKIHVFYIDYGNREVLPSTRLGTLSPAFS 785
Cdd:cd20427   2 QMEDEMKEFYSKSSTAMCLR---SPSVGQLVAVKAEEDAWLRAQVIEVEE-DKVKVYYVDHGFSEVVERSKLFKLNKQFY 77

                        90       100
                ....*....|....*....|..
gi 77404397 786 TrvLPAQATEYAFAFIQVPQDD 807
Cdd:cd20427  78 S--LPFQATKCKLAGLEPFSDD 97
Tudor_vreteno-like_rpt1 cd20444
first Tudor domain found in Drosophila melanogaster protein vreteno and similar proteins; ...
 730-771 4.43e-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: 4.43e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 77404397 730 PRRGEFCIAKFvDGEWYRARVEKVESP-AKIHVFYIDYGNREV 771
Cdd:cd20444   1 PTPGQMVIAKF-DGNHYRAIVLRVLNPdLKILVRFVDFGNVEV 42
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 730-808 4.91e-07

second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; TDRD12, also called ES cell-associated transcript 8 protein (ECAT8), is a putative ATP-dependent DEAD-like RNA helicase that is essential for germ cell development and maintenance. It acts as a unique piRNA biogenesis factor essential for secondary PIWI interacting RNA (piRNA) biogenesis. TDRD12 contains two Tudor domains, one at the N-terminus and the other at the C-terminal end. The model corresponds to the second/C-terminal one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410506  Cd Length: 134  Bit Score: 49.56  E-value: 4.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 730 PRRGEFCIAKFVDGEWYRARVEKVE------SPAKIHVFYIDYGNREVLPSTRLGTLSPAFstRVLPAQATEYAFAFIQv 803
Cdd:cd20435  50 VKVGDLCAVEDENNLYHRVKVLEITekddktKPREVLVKFIDEGRVETVVVSQLLELPEEL--KSLPPQAVEVFLCNVK- 126


                ....*
gi 77404397 804 PQDDD 808
Cdd:cd20435 127 PVDND 131
Tudor_TDRD5 cd20419
Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is ...
 686-793 6.89e-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: 6.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 686 FVTEITDDLHFYVQDV--ETGTQLEKLMENMRNdIASHPPVEGSY-AP----RRGEFCIAKF-VDGEWYRARVEKVESPA 757
Cdd:cd20419   1 FVEYIESPSQFYVRFYskDTSEMLEDMMIEMRR-CYSNEHVSERYvMPeafiQPGQVCCVRIpEDVWWYRVIIHQVLNKQ 79

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 77404397 758 KIHVFYIDYGNREVLPSTRLGTLSPAFSTrvLPAQA 793
Cdd:cd20419  80 EVEVFYPDFGDIGTVQKSRLRFLKCCYSK--LPAQA 113
Tudor_TDRD6_rpt3 cd20422
third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 685-793 7.91e-07

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: 49.05  E-value: 7.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 685 VFVTEITDDLHFYVQDVETGTQLEKLMENMRNDIASHPPVEGSY-APRRGEFCIAKFVDGEWYRARVEKVESPAkIHVFY 763
Cdd:cd20422   4 AQVEFVKDPSEFWIRLGEHAVPFSKLMRSMTAFYSQASKLDGVVlKPQPGQLCCAKWKEDRYYRAIVTAVKGKM-VEVFL 82

                        90       100       110
                ....*....|....*....|....*....|
gi 77404397 764 IDYGNREVLPSTRLGTLSPAFstRVLPAQA 793
Cdd:cd20422  83 VDRGNTEMVDWYDVKKLLPQF--RELPALA 110
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 844-895 1.13e-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: 1.13e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 77404397 844 FADSKGDVGLGLVKEGLVMVeVRKEKQFQKVITEYLNAQESAKSARLNLWRY 895
Cdd:cd00175  79 YLNGGENIAEELVKEGLARV-YRYYPDDSEYYDELLEAEEAAKKARKGLWSD 129
Tudor_vreteno-like_rpt2 cd20445
second Tudor domain found in Drosophila melanogaster protein vreteno and similar proteins; ...
 734-786 1.24e-04

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: 40.48  E-value: 1.24e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 77404397 734 EFCIAKFVDgEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLSPAFST 786
Cdd:cd20445   3 ELCIAKYMD-KWYRAVCLESVGDGRPTVLFCDYGNILMARLTDIRPFPPTFAT 54
Tudor_TDRD7_rpt3 cd20429
third Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 706-793 2.75e-04

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


Pssm-ID: 410500  Cd Length: 91  Bit Score: 40.55  E-value: 2.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 706 QLEKLMENMRndIASHPPVEGSYAPRRGEFCIAKfVDGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLSPAFs 785
Cdd:cd20429   8 KLEVLMEEMI--LYYNKTEERPVAIEKNKVYAAK-IENNWYRVLVKGILTNGLVSVYELDYGKHELVSIRKVQPLIEKF- 83


                ....*...
gi 77404397 786 tRVLPAQA 793
Cdd:cd20429  84 -RQLPFQA 90
Tudor_TDRD15_rpt1 cd20436
first Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 714-768 3.32e-04

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: 42.02  E-value: 3.32e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 77404397 714 MRNDIASHPPVEGSYAprRGEFCIAK-FVDGEWYRARVEKVESpAKIHVFYIDYGN 768
Cdd:cd20436  33 LQNEIQNATKSKSSWG--VGEFCLVEdTTSGEWYRGRVLEKID-EKYEVFLIDRGE 85
Tudor_TDRD15_rpt6 cd20441
sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 696-787 4.67e-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: 40.49  E-value: 4.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 696 FYVQDVETGTQLEKLMENMrNDIASHPPVEGSYAPRRGEFCIAKFV-DGEWYRARVEKVESPAKIHVFYIDYGNREVLPS 774
Cdd:cd20441   5 FFIQLSEDEKVILQLAEEL-NETSEKSRENAAVKLKVGDLVAAEYDeDLALYRAVITAVLPGKSFKVEFIDYGNTAVVDK 83

                        90
                ....*....|....*....
gi 77404397 775 TRLGTLS------PAFSTR 787
Cdd:cd20441  84 SNIYTLQekflslPRLSIP 102
SNc smart00318
Staphylococcal nuclease homologues;
844-895 6.70e-04

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 40.71  E-value: 6.70e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 77404397    844 FADSKGDVGLGLVKEGLVmvEVRKEKQFQKV-ITEYLNAQESAKSARLNLWRY 895
Cdd:smart00318  87 YLNGGNNIAEELVKEGLA--KVYRYADKDEYvYDELLEAEEAAKKARKGLWSD 137
Tudor_SF cd04508
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
 733-777 8.99e-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: 37.95  E-value: 8.99e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 77404397 733 GEFCIAKF-VDGEWYRARVEKVESPAKIHVFYiDYGNREVLPSTRL 777
Cdd:cd04508   1 GDRVEAKWsDDGQWYPATVVAVNDDGKYTVLF-DDGNEEEVSEDDI 45
Tudor_TDRD3 cd20413
Tudor domain found in Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is ...
 731-772 9.46e-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: 38.09  E-value: 9.46e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 77404397 731 RRGEFCIAKF-VDGEWYRARVEKVESPAKIH-VFYIDYGN-REVL 772
Cdd:cd20413   2 KPGDECLAKYwEDNKFYRAEVTAVHPSGKTAvVKFMEYGNyEEVL 46
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 850-893 1.20e-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: 39.23  E-value: 1.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 77404397   850 DVGLGLVKEGLVMVEVRKEKQFQKvITEYLNAQESAKSARLNLW 893
Cdd:pfam00565  62 NINEELVKEGLAWVYKAYPPNFKH-YDELLAAEEEAKKKKKGLW 104
Tudor_TDRD6_rpt7 cd20426
seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 686-770 2.09e-03

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: 39.40  E-value: 2.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404397 686 FVTEITDDLHFYVQDVETGtqLEKLMENMRnDIASHPPVEGSYAP--RRGEFCIAKFV-DGEWYRARVEKVESpAKIHVF 762
Cdd:cd20426   4 YATAVDSPEYFWCQFATEK--IQCLAVKVQ-EAGEQVADRGNFIPsiYVGDPCIVKYSeDNHWYRALVTKIND-NLVSVR 79


                ....*...
gi 77404397 763 YIDYGNRE 770
Cdd:cd20426  80 FVDYGNEE 87
Tudor_SMN_SPF30-like cd21182
Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing ...
 733-773 2.34e-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: 36.85  E-value: 2.34e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 77404397 733 GEFCIAKF-VDGEWYRARVEKV-ESPAKIHVFYIDYGNREVLP 773
Cdd:cd21182   1 GDKCLAPYsDDGKYYEATIEEItEESDTATVVFDGYGNSEEVP 43
 
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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