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Conserved domains on  [gi|17533087|ref|NP_494839|]
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Staphylococcal nuclease domain-containing protein 1 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SNc smart00318
Staphylococcal nuclease homologues;
193-328 1.87e-39

Staphylococcal nuclease homologues;


:

Pssm-ID: 214615  Cd Length: 137  Bit Score: 142.79  E-value: 1.87e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087    193 KPIDAVIEMVRDGSTVRAFLLPNfEYITLQLSGVRAPSTRNPNAAD-SRAEAFSEEAKFFAESRLLQRDVQIILES-TSN 270
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPETARPNKGDgTPDEPFGEEAKEFLKKLLLGKKVQVEVDSkDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 17533087    271 QNFVGSIVHPKG-NIAESLLREGYAKCVDWSIGLCtGGAQKLRDAERQAKEKRLRLWKS 328
Cdd:smart00318  80 GRFLGTVYLNGGnNIAEELVKEGLAKVYRYADKDE-YVYDELLEAEEAAKKARKGLWSD 137
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
 714-796 9.86e-39

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: 138.59  E-value: 9.86e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 714 DGPKIEKMTTEMRQALAEHPPLAGSYTTKRGDLCVAKFSQDGQWYRCKVESVRA-GQAEIVYIDYGNRETIEAVKLAQIP 792
Cdd:cd20433   1 TGPQLEKLMEKLRFEIASNPPLPGSYTPRKGDLCAAKFVEDGEWYRAKVEKVEGdKKVHVLYIDYGNREVLPSTRLAALP 80


                ....
gi 17533087 793 AGFA 796
Cdd:cd20433  81 PAFS 84
SNc smart00318
Staphylococcal nuclease homologues;
341-492 5.92e-36

Staphylococcal nuclease homologues;


:

Pssm-ID: 214615  Cd Length: 137  Bit Score: 132.77  E-value: 5.92e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087    341 KAFTGKVVEIVLSDAVVVQKDDGSEVKLHLSSIRLPRESGDDKATGGpgrqfrplYDIPFMFQAREFLRKRLLGKKVQIQ 420
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKGPLITIRLSGIDAPETARPNKGDGT--------PDEPFGEEAKEFLKKLLLGKKVQVE 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17533087    421 IDYVqpkseNFPEKTCATIKIGDQ-NIAEGLISRGLSKVVRHRADDENRsseYDTLLAAEANAEKGKKGLFAD 492
Cdd:smart00318  73 VDSK-----DRYGRFLGTVYLNGGnNIAEELVKEGLAKVYRYADKDEYV---YDELLEAEEAAKKARKGLWSD 137
SNc smart00318
Staphylococcal nuclease homologues;
22-168 2.65e-34

Staphylococcal nuclease homologues;


:

Pssm-ID: 214615  Cd Length: 137  Bit Score: 127.76  E-value: 2.65e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087     22 AVRRGLVKSVLSGDAVILQGQPHngppPEWTVYLSNVTAPRLGRRPTDSAsaTPDEPYAWDSREYLRQKLVGQFVTFVRD 101
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG----PLITIRLSGIDAPETARPNKGDG--TPDEPFGEEAKEFLKKLLLGKKVQVEVD 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17533087    102 FTATSGRDHGRIYLGGTSpadaeNVAEGAVSAGLLEVRQGKVADEYS-TKLLELQEQAKSAGRGKWNS 168
Cdd:smart00318  75 SKDRYGRFLGTVYLNGGN-----NIAEELVKEGLAKVYRYADKDEYVyDELLEAEEAAKKARKGLWSD 137
SNc smart00318
Staphylococcal nuclease homologues;
524-668 1.42e-32

Staphylococcal nuclease homologues;


:

Pssm-ID: 214615  Cd Length: 137  Bit Score: 122.76  E-value: 1.42e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087    524 GRAEGVVEFLSGGSRLRIYIPKEtVLITFLLGGINCPKGARVGPGGVSTGaaEPFADEAAAFTRKLVLQHEVQLEVESTD 603
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPETARPNKGDGTPD--EPFGEEAKEFLKKLLLGKKVQVEVDSKD 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17533087    604 KNGNFVGYLYVsPDGNtsraiNLSEALVENGLASLHFTAERS-GHYNALLSAENKAKKAKKNIWAN 668
Cdd:smart00318  78 RYGRFLGTVYL-NGGN-----NIAEELVKEGLAKVYRYADKDeYVYDELLEAEEAAKKARKGLWSD 137
SNc super family cl00140
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 758-904 1.11e-03

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 smart00318:

Pssm-ID: 469627  Cd Length: 137  Bit Score: 39.94  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087    758 YRCKVESVRAGQAEIVYIDYGNRETIeavKLAQIPAgfanfPAGVReyNLALAKLPNEDYVQLTSDAFAQYLFGHS-SVF 836
Cdd:smart00318   3 IRGVVERVIDGDTIRVRLPKGPLITI---RLSGIDA-----PETAR--PNKGDGTPDEPFGEEAKEFLKKLLLGKKvQVE 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17533087    837 INSEYKVGtSEYVTVYYDSGNkkvDIGKSLIAEGLALAdHRREPRLQTLVNDYNTTEEVARKSRKNIW 904
Cdd:smart00318  73 VDSKDRYG-RFLGTVYLNGGN---NIAEELVKEGLAKV-YRYADKDEYVYDELLEAEEAAKKARKGLW 135
 
Name Accession Description Interval E-value
SNc smart00318
Staphylococcal nuclease homologues;
193-328 1.87e-39

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 142.79  E-value: 1.87e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087    193 KPIDAVIEMVRDGSTVRAFLLPNfEYITLQLSGVRAPSTRNPNAAD-SRAEAFSEEAKFFAESRLLQRDVQIILES-TSN 270
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPETARPNKGDgTPDEPFGEEAKEFLKKLLLGKKVQVEVDSkDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 17533087    271 QNFVGSIVHPKG-NIAESLLREGYAKCVDWSIGLCtGGAQKLRDAERQAKEKRLRLWKS 328
Cdd:smart00318  80 GRFLGTVYLNGGnNIAEELVKEGLAKVYRYADKDE-YVYDELLEAEEAAKKARKGLWSD 137
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
 714-796 9.86e-39

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: 138.59  E-value: 9.86e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 714 DGPKIEKMTTEMRQALAEHPPLAGSYTTKRGDLCVAKFSQDGQWYRCKVESVRA-GQAEIVYIDYGNRETIEAVKLAQIP 792
Cdd:cd20433   1 TGPQLEKLMEKLRFEIASNPPLPGSYTPRKGDLCAAKFVEDGEWYRAKVEKVEGdKKVHVLYIDYGNREVLPSTRLAALP 80


                ....
gi 17533087 793 AGFA 796
Cdd:cd20433  81 PAFS 84
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 201-328 1.60e-38

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


Pssm-ID: 238102  Cd Length: 129  Bit Score: 139.72  E-value: 1.60e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 201 MVRDGSTVRAFLLPNfEYITLQLSGVRAPST-RNPNAADSRAEAFSEEAKFFAESRLLQRDVQIILEST-SNQNFVGSIV 278
Cdd:cd00175   1 RVIDGDTIRVRLPPG-PLITVRLSGIDAPETaRPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKdRYGRTLGTVY 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17533087 279 HPKG-NIAESLLREGYAKCVDWSIGLcTGGAQKLRDAERQAKEKRLRLWKS 328
Cdd:cd00175  80 LNGGeNIAEELVKEGLARVYRYYPDD-SEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
341-492 5.92e-36

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 132.77  E-value: 5.92e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087    341 KAFTGKVVEIVLSDAVVVQKDDGSEVKLHLSSIRLPRESGDDKATGGpgrqfrplYDIPFMFQAREFLRKRLLGKKVQIQ 420
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKGPLITIRLSGIDAPETARPNKGDGT--------PDEPFGEEAKEFLKKLLLGKKVQVE 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17533087    421 IDYVqpkseNFPEKTCATIKIGDQ-NIAEGLISRGLSKVVRHRADDENRsseYDTLLAAEANAEKGKKGLFAD 492
Cdd:smart00318  73 VDSK-----DRYGRFLGTVYLNGGnNIAEELVKEGLAKVYRYADKDEYV---YDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 350-492 3.07e-35

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


Pssm-ID: 238102  Cd Length: 129  Bit Score: 130.09  E-value: 3.07e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 350 IVLSDAVVVQKDDGSEVKLHLSSIRLPRESGDDKAtggpgrqfRPLYDIPFMFQAREFLRKRLLGKKVQIQIDYVqpkse 429
Cdd:cd00175   2 VIDGDTIRVRLPPGPLITVRLSGIDAPETARPNKG--------KSETDEPFGEEAKEFLKKLLLGKKVQVEVDSK----- 68

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17533087 430 NFPEKTCATIKIGD-QNIAEGLISRGLSKVVRHRADDenrSSEYDTLLAAEANAEKGKKGLFAD 492
Cdd:cd00175  69 DRYGRTLGTVYLNGgENIAEELVKEGLARVYRYYPDD---SEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
22-168 2.65e-34

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 127.76  E-value: 2.65e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087     22 AVRRGLVKSVLSGDAVILQGQPHngppPEWTVYLSNVTAPRLGRRPTDSAsaTPDEPYAWDSREYLRQKLVGQFVTFVRD 101
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG----PLITIRLSGIDAPETARPNKGDG--TPDEPFGEEAKEFLKKLLLGKKVQVEVD 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17533087    102 FTATSGRDHGRIYLGGTSpadaeNVAEGAVSAGLLEVRQGKVADEYS-TKLLELQEQAKSAGRGKWNS 168
Cdd:smart00318  75 SKDRYGRFLGTVYLNGGN-----NIAEELVKEGLAKVYRYADKDEYVyDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 30-168 6.52e-34

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


Pssm-ID: 238102  Cd Length: 129  Bit Score: 126.62  E-value: 6.52e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087  30 SVLSGDAVILQGQPHngppPEWTVYLSNVTAPRLGRRPTDSAsaTPDEPYAWDSREYLRQKLVGQFVTFVRDFTATSGRD 109
Cdd:cd00175   1 RVIDGDTIRVRLPPG----PLITVRLSGIDAPETARPNKGKS--ETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRT 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 110 HGRIYLGGtspadAENVAEGAVSAGLLEVRQGKVAD-EYSTKLLELQEQAKSAGRGKWNS 168
Cdd:cd00175  75 LGTVYLNG-----GENIAEELVKEGLARVYRYYPDDsEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
524-668 1.42e-32

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 122.76  E-value: 1.42e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087    524 GRAEGVVEFLSGGSRLRIYIPKEtVLITFLLGGINCPKGARVGPGGVSTGaaEPFADEAAAFTRKLVLQHEVQLEVESTD 603
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPETARPNKGDGTPD--EPFGEEAKEFLKKLLLGKKVQVEVDSKD 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17533087    604 KNGNFVGYLYVsPDGNtsraiNLSEALVENGLASLHFTAERS-GHYNALLSAENKAKKAKKNIWAN 668
Cdd:smart00318  78 RYGRFLGTVYL-NGGN-----NIAEELVKEGLAKVYRYADKDeYVYDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 536-668 5.38e-32

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: 120.84  E-value: 5.38e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 536 GSRLRIYIPKEtVLITFLLGGINCPKGARVGPGGVSTGaaEPFADEAAAFTRKLVLQHEVQLEVESTDKNGNFVGYLYVS 615
Cdd:cd00175   5 GDTIRVRLPPG-PLITVRLSGIDAPETARPNKGKSETD--EPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTVYLN 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 17533087 616 PdgntsrAINLSEALVENGLASLHFTAER-SGHYNALLSAENKAKKAKKNIWAN 668
Cdd:cd00175  82 G------GENIAEELVKEGLARVYRYYPDdSEYYDELLEAEEAAKKARKGLWSD 129
TUDOR pfam00567
Tudor domain;
691-808 1.13e-27

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 108.21  E-value: 1.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087   691 NFRQVAVTDIApGALRFSAQNIEDGPKIEKMTTEMRQALAEHPPlaGSYTTKRGDLCVAKFSQDGQWYRCKV-ESVRAGQ 769
Cdd:pfam00567   1 STIDVVVSHIE-SPSTFYIQPKSDSKKLEKLTEELQEYYASKPP--ESLPPAVGDGCVAAFSEDGKWYRAKItESLDDGL 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 17533087   770 AEIVYIDYGNRETIEAVKLAQIPAGFANFPAGVREYNLA 808
Cdd:pfam00567  78 VEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 551-668 5.17e-23

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: 94.31  E-value: 5.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087   551 TFLLGGINCPKGARVGpggvstGAAEPFADEAAAFTRKLVLQHEVQLEVESTDKNGNFVGYLYVSPdgntsraINLSEAL 630
Cdd:pfam00565   1 RVRLVGIDAPETAKPN------TPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYLNG-------KNINEEL 67

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 17533087   631 VENGLASLHFTAE-RSGHYNALLSAENKAKKAKKNIWAN 668
Cdd:pfam00565  68 VKEGLAWVYKAYPpNFKHYDELLAAEEEAKKKKKGLWSD 106
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 220-328 1.30e-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: 76.21  E-value: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087   220 TLQLSGVRAPSTRNPNAAdsrAEAFSEEAKFFAESRLLQRDVQIILEST-SNQNFVGSIVHPKGNIAESLLREGYAKcVD 298
Cdd:pfam00565   1 RVRLVGIDAPETAKPNTP---VQPFGKEAKEFLKKLVLGKKVVVLEFDKdKYGRTLGYVYLNGKNINEELVKEGLAW-VY 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 17533087   299 WSIGLCTGGAQKLRDAERQAKEKRLRLWKS 328
Cdd:pfam00565  77 KAYPPNFKHYDELLAAEEEAKKKKKGLWSD 106
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 739-795 7.73e-13

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: 63.83  E-value: 7.73e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 17533087    739 YTTKRGDLCVAKFSqDGQWYRCKVESV-RAGQAEIVYIDYGNRETIEAVKLAQIPAGF 795
Cdd:smart00333   1 PTFKVGDKVAARWE-DGEWYRARIVKVdGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
191-336 5.99e-12

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 64.70  E-value: 5.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 191 AQKPIDAVIEMVRDGSTVRafLLPNFEYITLQLSGVRAPSTRNPNaadSRAEAFSEEAKFFAESRLLQRDVQIILESTSN 270
Cdd:COG1525  20 AAATLTAGVVRVIDGDTLR--VRDDGKGERVRLAGIDAPELGQPC---GPEQPCGEEARQALRALLAGKTVTLEPDEGRD 94

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17533087 271 QNF--VGSIVHPKGNIAESLLREGYAkcVDWSIGLCTGGAQKLRDAERQAKEKRLRLWKSYQPTSSAY 336
Cdd:COG1525  95 RYGrlLAYVYVDGRDLNEELVREGLA--WAYRRYSPDKYADRYLAAEAEARAARRGLWSDAFPVPPEW 160
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
528-667 6.41e-11

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 61.62  E-value: 6.41e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 528 GVVEFLSGGSrLRIYIPKETVLITFLlgGINCPKGARvgpggvSTGAAEPFADEAAAFTRKLVLQHEVQLEV-ESTDKNG 606
Cdd:COG1525  27 GVVRVIDGDT-LRVRDDGKGERVRLA--GIDAPELGQ------PCGPEQPCGEEARQALRALLAGKTVTLEPdEGRDRYG 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17533087 607 NFVGYLYVspDGntsraINLSEALVENGLASLHFTAERSGHYNALLSAENKAKKAKKNIWA 667
Cdd:COG1525  98 RLLAYVYV--DG-----RDLNEELVREGLAWAYRRYSPDKYADRYLAAEAEARAARRGLWS 151
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
1-178 1.10e-10

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 61.23  E-value: 1.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087   1 MTDAAAATPTVPPPAASSANPAVRRGLVKSVLSGD--AVILQGQPHngpppewTVYLSNVTAPRLGRrptdsaSATPDEP 78
Cdd:COG1525   1 MRKLLLALLLALAALAAAAAAATLTAGVVRVIDGDtlRVRDDGKGE-------RVRLAGIDAPELGQ------PCGPEQP 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087  79 YAWDSREYLRQKLVGQFVTFVRDftatSGRDH-----GRIYLGGTspadaeNVAEGAVSAGLLEVRQGKVADEYSTKLLE 153
Cdd:COG1525  68 CGEEARQALRALLAGKTVTLEPD----EGRDRygrllAYVYVDGR------DLNEELVREGLAWAYRRYSPDKYADRYLA 137

                       170       180
                ....*....|....*....|....*
gi 17533087 154 LQEQAKSAGRGKWNSNAGTIRDIRW 178
Cdd:COG1525 138 AEAEARAARRGLWSDAFPVPPEWRR 162
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
331-495 2.50e-10

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 60.08  E-value: 2.50e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 331 PTSSAYSGDRKAFTGKVVEIVLSDAVVVqKDDGSEVKLHLSSIRLPResgddkaTGGPGRQFRPLYDipfmfQAREFLRK 410
Cdd:COG1525  12 LAALAAAAAAATLTAGVVRVIDGDTLRV-RDDGKGERVRLAGIDAPE-------LGQPCGPEQPCGE-----EARQALRA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 411 RLLGKKVQIQIDYVQPKSenfpEKTCATIKIGDQNIAEGLISRGLSKVVRHRADDENRsseyDTLLAAEANAEKGKKGLF 490
Cdd:COG1525  79 LLAGKTVTLEPDEGRDRY----GRLLAYVYVDGRDLNEELVREGLAWAYRRYSPDKYA----DRYLAAEAEARAARRGLW 150


                ....*
gi 17533087 491 ADKTA 495
Cdd:COG1525 151 SDAFP 155
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 393-492 1.71e-09

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: 55.79  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087   393 RPLYDIPFMFQAREFLRKRLLGKKVQI---QIDYVqpksenfpEKTCATIKIGDQNIAEGLISRGLSKVvrHRADDENrS 469
Cdd:pfam00565  15 PNTPVQPFGKEAKEFLKKLVLGKKVVVlefDKDKY--------GRTLGYVYLNGKNINEELVKEGLAWV--YKAYPPN-F 83

                          90       100
                  ....*....|....*....|...
gi 17533087   470 SEYDTLLAAEANAEKGKKGLFAD 492
Cdd:pfam00565  84 KHYDELLAAEEEAKKKKKGLWSD 106
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 52-168 1.50e-08

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: 53.09  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087    52 TVYLSNVTAPRLGRRPTdsasatPDEPYAWDSREYLRQKLVGQFVTFVRDFTATSGRDHGRIYLGGTspadaeNVAEGAV 131
Cdd:pfam00565   1 RVRLVGIDAPETAKPNT------PVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYLNGK------NINEELV 68

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 17533087   132 SAGLLEV-RQGKVADEYSTKLLELQEQAKSAGRGKWNS 168
Cdd:pfam00565  69 KEGLAWVyKAYPPNFKHYDELLAAEEEAKKKKKGLWSD 106
SNc smart00318
Staphylococcal nuclease homologues;
758-904 1.11e-03

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 39.94  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087    758 YRCKVESVRAGQAEIVYIDYGNRETIeavKLAQIPAgfanfPAGVReyNLALAKLPNEDYVQLTSDAFAQYLFGHS-SVF 836
Cdd:smart00318   3 IRGVVERVIDGDTIRVRLPKGPLITI---RLSGIDA-----PETAR--PNKGDGTPDEPFGEEAKEFLKKLLLGKKvQVE 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17533087    837 INSEYKVGtSEYVTVYYDSGNkkvDIGKSLIAEGLALAdHRREPRLQTLVNDYNTTEEVARKSRKNIW 904
Cdd:smart00318  73 VDSKDRYG-RFLGTVYLNGGN---NIAEELVKEGLAKV-YRYADKDEYVYDELLEAEEAAKKARKGLW 135
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 850-906 7.80e-03

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


Pssm-ID: 395448  Cd Length: 106  Bit Score: 36.92  E-value: 7.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17533087   850 TVYYDsgnkKVDIGKSLIAEGLALADHRREPRLQTLvNDYNTTEEVARKSRKNIWEY 906
Cdd:pfam00565  55 YVYLN----GKNINEELVKEGLAWVYKAYPPNFKHY-DELLAAEEEAKKKKKGLWSD 106
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
822-904 7.86e-03

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 38.12  E-value: 7.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 822 SDAFAQYLFGHSsVFInsEYKVGTSEY----VTVYYDsgnkKVDIGKSLIAEGLALADHRREPRlqTLVNDYNTTEEVAR 897
Cdd:COG1525  73 RQALRALLAGKT-VTL--EPDEGRDRYgrllAYVYVD----GRDLNEELVREGLAWAYRRYSPD--KYADRYLAAEAEAR 143


                ....*..
gi 17533087 898 KSRKNIW 904
Cdd:COG1525 144 AARRGLW 150
 
Name Accession Description Interval E-value
SNc smart00318
Staphylococcal nuclease homologues;
193-328 1.87e-39

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 142.79  E-value: 1.87e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087    193 KPIDAVIEMVRDGSTVRAFLLPNfEYITLQLSGVRAPSTRNPNAAD-SRAEAFSEEAKFFAESRLLQRDVQIILES-TSN 270
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPETARPNKGDgTPDEPFGEEAKEFLKKLLLGKKVQVEVDSkDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 17533087    271 QNFVGSIVHPKG-NIAESLLREGYAKCVDWSIGLCtGGAQKLRDAERQAKEKRLRLWKS 328
Cdd:smart00318  80 GRFLGTVYLNGGnNIAEELVKEGLAKVYRYADKDE-YVYDELLEAEEAAKKARKGLWSD 137
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
 714-796 9.86e-39

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: 138.59  E-value: 9.86e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 714 DGPKIEKMTTEMRQALAEHPPLAGSYTTKRGDLCVAKFSQDGQWYRCKVESVRA-GQAEIVYIDYGNRETIEAVKLAQIP 792
Cdd:cd20433   1 TGPQLEKLMEKLRFEIASNPPLPGSYTPRKGDLCAAKFVEDGEWYRAKVEKVEGdKKVHVLYIDYGNREVLPSTRLAALP 80


                ....
gi 17533087 793 AGFA 796
Cdd:cd20433  81 PAFS 84
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 201-328 1.60e-38

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


Pssm-ID: 238102  Cd Length: 129  Bit Score: 139.72  E-value: 1.60e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 201 MVRDGSTVRAFLLPNfEYITLQLSGVRAPST-RNPNAADSRAEAFSEEAKFFAESRLLQRDVQIILEST-SNQNFVGSIV 278
Cdd:cd00175   1 RVIDGDTIRVRLPPG-PLITVRLSGIDAPETaRPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKdRYGRTLGTVY 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17533087 279 HPKG-NIAESLLREGYAKCVDWSIGLcTGGAQKLRDAERQAKEKRLRLWKS 328
Cdd:cd00175  80 LNGGeNIAEELVKEGLARVYRYYPDD-SEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
341-492 5.92e-36

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 132.77  E-value: 5.92e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087    341 KAFTGKVVEIVLSDAVVVQKDDGSEVKLHLSSIRLPRESGDDKATGGpgrqfrplYDIPFMFQAREFLRKRLLGKKVQIQ 420
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKGPLITIRLSGIDAPETARPNKGDGT--------PDEPFGEEAKEFLKKLLLGKKVQVE 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17533087    421 IDYVqpkseNFPEKTCATIKIGDQ-NIAEGLISRGLSKVVRHRADDENRsseYDTLLAAEANAEKGKKGLFAD 492
Cdd:smart00318  73 VDSK-----DRYGRFLGTVYLNGGnNIAEELVKEGLAKVYRYADKDEYV---YDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 350-492 3.07e-35

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


Pssm-ID: 238102  Cd Length: 129  Bit Score: 130.09  E-value: 3.07e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 350 IVLSDAVVVQKDDGSEVKLHLSSIRLPRESGDDKAtggpgrqfRPLYDIPFMFQAREFLRKRLLGKKVQIQIDYVqpkse 429
Cdd:cd00175   2 VIDGDTIRVRLPPGPLITVRLSGIDAPETARPNKG--------KSETDEPFGEEAKEFLKKLLLGKKVQVEVDSK----- 68

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17533087 430 NFPEKTCATIKIGD-QNIAEGLISRGLSKVVRHRADDenrSSEYDTLLAAEANAEKGKKGLFAD 492
Cdd:cd00175  69 DRYGRTLGTVYLNGgENIAEELVKEGLARVYRYYPDD---SEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
22-168 2.65e-34

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 127.76  E-value: 2.65e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087     22 AVRRGLVKSVLSGDAVILQGQPHngppPEWTVYLSNVTAPRLGRRPTDSAsaTPDEPYAWDSREYLRQKLVGQFVTFVRD 101
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG----PLITIRLSGIDAPETARPNKGDG--TPDEPFGEEAKEFLKKLLLGKKVQVEVD 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17533087    102 FTATSGRDHGRIYLGGTSpadaeNVAEGAVSAGLLEVRQGKVADEYS-TKLLELQEQAKSAGRGKWNS 168
Cdd:smart00318  75 SKDRYGRFLGTVYLNGGN-----NIAEELVKEGLAKVYRYADKDEYVyDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 30-168 6.52e-34

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


Pssm-ID: 238102  Cd Length: 129  Bit Score: 126.62  E-value: 6.52e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087  30 SVLSGDAVILQGQPHngppPEWTVYLSNVTAPRLGRRPTDSAsaTPDEPYAWDSREYLRQKLVGQFVTFVRDFTATSGRD 109
Cdd:cd00175   1 RVIDGDTIRVRLPPG----PLITVRLSGIDAPETARPNKGKS--ETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRT 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 110 HGRIYLGGtspadAENVAEGAVSAGLLEVRQGKVAD-EYSTKLLELQEQAKSAGRGKWNS 168
Cdd:cd00175  75 LGTVYLNG-----GENIAEELVKEGLARVYRYYPDDsEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
524-668 1.42e-32

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 122.76  E-value: 1.42e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087    524 GRAEGVVEFLSGGSRLRIYIPKEtVLITFLLGGINCPKGARVGPGGVSTGaaEPFADEAAAFTRKLVLQHEVQLEVESTD 603
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPETARPNKGDGTPD--EPFGEEAKEFLKKLLLGKKVQVEVDSKD 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17533087    604 KNGNFVGYLYVsPDGNtsraiNLSEALVENGLASLHFTAERS-GHYNALLSAENKAKKAKKNIWAN 668
Cdd:smart00318  78 RYGRFLGTVYL-NGGN-----NIAEELVKEGLAKVYRYADKDeYVYDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 536-668 5.38e-32

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: 120.84  E-value: 5.38e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 536 GSRLRIYIPKEtVLITFLLGGINCPKGARVGPGGVSTGaaEPFADEAAAFTRKLVLQHEVQLEVESTDKNGNFVGYLYVS 615
Cdd:cd00175   5 GDTIRVRLPPG-PLITVRLSGIDAPETARPNKGKSETD--EPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTVYLN 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 17533087 616 PdgntsrAINLSEALVENGLASLHFTAER-SGHYNALLSAENKAKKAKKNIWAN 668
Cdd:cd00175  82 G------GENIAEELVKEGLARVYRYYPDdSEYYDELLEAEEAAKKARKGLWSD 129
TUDOR pfam00567
Tudor domain;
691-808 1.13e-27

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 108.21  E-value: 1.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087   691 NFRQVAVTDIApGALRFSAQNIEDGPKIEKMTTEMRQALAEHPPlaGSYTTKRGDLCVAKFSQDGQWYRCKV-ESVRAGQ 769
Cdd:pfam00567   1 STIDVVVSHIE-SPSTFYIQPKSDSKKLEKLTEELQEYYASKPP--ESLPPAVGDGCVAAFSEDGKWYRAKItESLDDGL 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 17533087   770 AEIVYIDYGNRETIEAVKLAQIPAGFANFPAGVREYNLA 808
Cdd:pfam00567  78 VEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 551-668 5.17e-23

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: 94.31  E-value: 5.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087   551 TFLLGGINCPKGARVGpggvstGAAEPFADEAAAFTRKLVLQHEVQLEVESTDKNGNFVGYLYVSPdgntsraINLSEAL 630
Cdd:pfam00565   1 RVRLVGIDAPETAKPN------TPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYLNG-------KNINEEL 67

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 17533087   631 VENGLASLHFTAE-RSGHYNALLSAENKAKKAKKNIWAN 668
Cdd:pfam00565  68 VKEGLAWVYKAYPpNFKHYDELLAAEEEAKKKKKGLWSD 106
Tudor_AtTudor1-like cd20443
Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor ...
 706-813 4.50e-17

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: 77.89  E-value: 4.50e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 706 RFSAQNIEDGPKIEKMTTEMRQALAEHPPLAGSYTTKRGDLCVAKFSQDGQWYRCK-VESVRAG------QAEIVYIDYG 778
Cdd:cd20443   3 RFYVQVVSDQRLSSIQQQLEGLSLKDKANPPGGFNPKKGELVLAQFSADNSWNRAMvVNAPRQGtqspkdEYEVFYIDYG 82

                        90       100       110
                ....*....|....*....|....*....|....*
gi 17533087 779 NRETIEAVKLAQIPAGFANFPAGVREYNLALAKLP 813
Cdd:cd20443  83 NQETVPLSALRPLDPSVSSAPGLAQLCSLAHIKVP 117
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 220-328 1.30e-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: 76.21  E-value: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087   220 TLQLSGVRAPSTRNPNAAdsrAEAFSEEAKFFAESRLLQRDVQIILEST-SNQNFVGSIVHPKGNIAESLLREGYAKcVD 298
Cdd:pfam00565   1 RVRLVGIDAPETAKPNTP---VQPFGKEAKEFLKKLVLGKKVVVLEFDKdKYGRTLGYVYLNGKNINEELVKEGLAW-VY 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 17533087   299 WSIGLCTGGAQKLRDAERQAKEKRLRLWKS 328
Cdd:pfam00565  77 KAYPPNFKHYDELLAAEEEAKKKKKGLWSD 106
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 695-800 1.28e-15

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: 74.33  E-value: 1.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 695 VAVTDI-APGALRFSAQNIEDGPKIEKMTTEMRQALAEhPPLAGSYTTKRGDLCVAKFSQDGQWYRCKVESVRAGQ--AE 771
Cdd:cd20408   1 GTVTEFkNPGEFYIQIYTLEVLESLVKLTSQLKKTYAS-VNNHKEYIPEVGEVCVAKYSEDQNWYRALVQTVDVQQkkAG 79

                        90       100
                ....*....|....*....|....*....
gi 17533087 772 IVYIDYGNRETIEAVKLAQIPAGFANFPA 800
Cdd:cd20408  80 VFYIDYGNEETVPLNRIQPLKKDIELFPP 108
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 739-795 7.73e-13

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: 63.83  E-value: 7.73e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 17533087    739 YTTKRGDLCVAKFSqDGQWYRCKVESV-RAGQAEIVYIDYGNRETIEAVKLAQIPAGF 795
Cdd:smart00333   1 PTFKVGDKVAARWE-DGEWYRARIVKVdGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 744-791 3.01e-12

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: 61.76  E-value: 3.01e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 17533087 744 GDLCVAKFSQDGQWYRCKVESV-RAGQAEIVYIDYGNRETIEAVKLAQI 791
Cdd:cd20379   2 GDLCAAKYEEDGKWYRARVLEVlSNDKVEVFFVDYGNTETVPLSDLRPL 50
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
191-336 5.99e-12

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 64.70  E-value: 5.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 191 AQKPIDAVIEMVRDGSTVRafLLPNFEYITLQLSGVRAPSTRNPNaadSRAEAFSEEAKFFAESRLLQRDVQIILESTSN 270
Cdd:COG1525  20 AAATLTAGVVRVIDGDTLR--VRDDGKGERVRLAGIDAPELGQPC---GPEQPCGEEARQALRALLAGKTVTLEPDEGRD 94

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17533087 271 QNF--VGSIVHPKGNIAESLLREGYAkcVDWSIGLCTGGAQKLRDAERQAKEKRLRLWKSYQPTSSAY 336
Cdd:COG1525  95 RYGrlLAYVYVDGRDLNEELVREGLA--WAYRRYSPDKYADRYLAAEAEARAARRGLWSDAFPVPPEW 160
Tudor_TDRD8 cd20430
Tudor domain found in Tudor domain-containing protein 8 (TDRD8) and similar proteins; TDRD8, ...
 749-796 3.49e-11

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: 59.61  E-value: 3.49e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 17533087 749 AKFSQDGQWYRCKVESV-RAGQAEIVYIDYGNRETIEAVKLAQIPAGFA 796
Cdd:cd20430  27 GKFSEDNCWYRCKVKSIlSDEKCTVQYIDYGNTETVSRSSIVELPPDLQ 75
Tudor_TDRD1_rpt2 cd20409
second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 724-793 4.58e-11

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: 59.78  E-value: 4.58e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17533087 724 EMRQALAEHPPLAGS---YTTKRGDLCVAKFSQDGQWYRCKVESVRAGQAEIV-YIDYGNRETIEAVKLAQIPA 793
Cdd:cd20409   6 ELQESLSAYCKVAPAssdFSPAVGEVCCAQFTEDNQWYRASVLAYSSEDSVLVgYIDFGNSEEVALSRLRPIPP 79
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
528-667 6.41e-11

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 61.62  E-value: 6.41e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 528 GVVEFLSGGSrLRIYIPKETVLITFLlgGINCPKGARvgpggvSTGAAEPFADEAAAFTRKLVLQHEVQLEV-ESTDKNG 606
Cdd:COG1525  27 GVVRVIDGDT-LRVRDDGKGERVRLA--GIDAPELGQ------PCGPEQPCGEEARQALRALLAGKTVTLEPdEGRDRYG 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17533087 607 NFVGYLYVspDGntsraINLSEALVENGLASLHFTAERSGHYNALLSAENKAKKAKKNIWA 667
Cdd:COG1525  98 RLLAYVYV--DG-----RDLNEELVREGLAWAYRRYSPDKYADRYLAAEAEARAARRGLWS 151
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
1-178 1.10e-10

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 61.23  E-value: 1.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087   1 MTDAAAATPTVPPPAASSANPAVRRGLVKSVLSGD--AVILQGQPHngpppewTVYLSNVTAPRLGRrptdsaSATPDEP 78
Cdd:COG1525   1 MRKLLLALLLALAALAAAAAAATLTAGVVRVIDGDtlRVRDDGKGE-------RVRLAGIDAPELGQ------PCGPEQP 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087  79 YAWDSREYLRQKLVGQFVTFVRDftatSGRDH-----GRIYLGGTspadaeNVAEGAVSAGLLEVRQGKVADEYSTKLLE 153
Cdd:COG1525  68 CGEEARQALRALLAGKTVTLEPD----EGRDRygrllAYVYVDGR------DLNEELVREGLAWAYRRYSPDKYADRYLA 137

                       170       180
                ....*....|....*....|....*
gi 17533087 154 LQEQAKSAGRGKWNSNAGTIRDIRW 178
Cdd:COG1525 138 AEAEARAARRGLWSDAFPVPPEWRR 162
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 743-811 2.24e-10

second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410486  Cd Length: 96  Bit Score: 58.21  E-value: 2.24e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 743 RGDLCVAKFSqDGQWYRCKVESV-RAGQAEIVYIDYGNRETIEAVKLAQIPAGFANFPAGVREYNLALAK 811
Cdd:cd20415  27 QGQACVALFE-DGAWYRARIIGLpGHREVEVKYVDFGNTATVTIKHVRKIKDDFLSLPEKARECRLAFIE 95
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
331-495 2.50e-10

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 60.08  E-value: 2.50e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 331 PTSSAYSGDRKAFTGKVVEIVLSDAVVVqKDDGSEVKLHLSSIRLPResgddkaTGGPGRQFRPLYDipfmfQAREFLRK 410
Cdd:COG1525  12 LAALAAAAAAATLTAGVVRVIDGDTLRV-RDDGKGERVRLAGIDAPE-------LGQPCGPEQPCGE-----EARQALRA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 411 RLLGKKVQIQIDYVQPKSenfpEKTCATIKIGDQNIAEGLISRGLSKVVRHRADDENRsseyDTLLAAEANAEKGKKGLF 490
Cdd:COG1525  79 LLAGKTVTLEPDEGRDRY----GRLLAYVYVDGRDLNEELVREGLAWAYRRYSPDKYA----DRYLAAEAEARAARRGLW 150


                ....*
gi 17533087 491 ADKTA 495
Cdd:COG1525 151 SDAFP 155
Tudor_TDRD1_rpt4 cd20411
fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 700-799 2.68e-10

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: 58.61  E-value: 2.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 700 IAPG---ALRFSAQniEDGPKIEKMTTEMRQaLAEHPPLAGSYTTKRGDLCVAKFSQDGQWYRCKVESVRAGQAEIVYID 776
Cdd:cd20411   7 ISPDlfyALPKTGQ--VNVEKLKALMTELAE-YCSKQSVPQQFRPRIGDACCARFTGDKNWYRAVVLETSDSEVKVLYAD 83

                        90       100
                ....*....|....*....|...
gi 17533087 777 YGNRETIEAVKLAQIPAGFANFP 799
Cdd:cd20411  84 YGNTETLPLSRILPITKSHLELP 106
Tudor_TDRD1_rpt3 cd20410
third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 739-795 3.20e-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: 3.20e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17533087 739 YTTKRGDLCVAKFSQDGQWYRCKV-ESVRAGQAEIVYIDYGNRETIEAVKLAQIPAGF 795
Cdd:cd20410   1 FKPIVGEPCCAFFSGDGNWYRAMVkEILPGGAVKVHFVDYGNVEEVTLDKLRKITSTF 58
Tudor_TDRD15_rpt2 cd20437
second Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 700-799 1.11e-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: 57.04  E-value: 1.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 700 IAPGalRFSAQNIEDGPKIEKMTTEMrqALA------EHPPLAGSYttkrGDLCVAKfSQDGQWYRCKVESVRAG-QAEI 772
Cdd:cd20437  13 VSPS--KFYCQLLSWEPELSKLTTQM--TLHyesvskELNPSCENF----GLLCAAK-GKDGQWHRGFLQQLLPPsQVKV 83

                        90       100
                ....*....|....*....|....*..
gi 17533087 773 VYIDYGNRETIEAVKLAQIPAGFANFP 799
Cdd:cd20437  84 WFIDYGNSEAVSSHSVLKLPPDFFSLP 110
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 393-492 1.71e-09

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: 55.79  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087   393 RPLYDIPFMFQAREFLRKRLLGKKVQI---QIDYVqpksenfpEKTCATIKIGDQNIAEGLISRGLSKVvrHRADDENrS 469
Cdd:pfam00565  15 PNTPVQPFGKEAKEFLKKLVLGKKVVVlefDKDKY--------GRTLGYVYLNGKNINEELVKEGLAWV--YKAYPPN-F 83

                          90       100
                  ....*....|....*....|...
gi 17533087   470 SEYDTLLAAEANAEKGKKGLFAD 492
Cdd:pfam00565  84 KHYDELLAAEEEAKKKKKGLWSD 106
Tudor_TDRD15_rpt6 cd20441
sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 706-800 3.46e-09

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: 55.13  E-value: 3.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 706 RFSAQNIEDGPKIEKMTTEMrQALAEHPPLAGSYTTKRGDLCVAKFSQDGQWYRCKVESVRAGQA-EIVYIDYGNRETIE 784
Cdd:cd20441   4 RFFIQLSEDEKVILQLAEEL-NETSEKSRENAAVKLKVGDLVAAEYDEDLALYRAVITAVLPGKSfKVEFIDYGNTAVVD 82

                        90
                ....*....|....*.
gi 17533087 785 AVKLAQIPAGFANFPA 800
Cdd:cd20441  83 KSNIYTLQEKFLSLPR 98
Tudor_TDRD6_rpt7 cd20426
seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 706-808 5.89e-09

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: 55.58  E-value: 5.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 706 RFSAQNIEdgpkiekMTTEMRQALAEHPPLAGSYTT--KRGDLCVAKFSQDGQWYRCKVESVRAGQAEIVYIDYGNRETI 783
Cdd:cd20426  17 QFATEKIQ-------CLAVKVQEAGEQVADRGNFIPsiYVGDPCIVKYSEDNHWYRALVTKINDNLVSVRFVDYGNEEDV 89

                        90       100       110
                ....*....|....*....|....*....|
gi 17533087 784 EAVKLAQIPAGFAN-----FPAGVREYNLA 808
Cdd:cd20426  90 VREQVRALPSELLKipvqaFPCCLSGFNLS 119
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 746-816 8.72e-09

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: 53.95  E-value: 8.72e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17533087 746 LCVAKFSqDGQWYRCKVESVRAGQAEIV---YIDYGNRETIEAVKLAQIPAGFANFPAGVREYNLALAKLPNED 816
Cdd:cd20418   9 PCLAEYS-DGKWYRAKLLSILEFNPVKIlvrHVDYGSTAALPTSRLRQIPAELMQYPCQAIKVKLAGFKPPLND 81
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 52-168 1.50e-08

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: 53.09  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087    52 TVYLSNVTAPRLGRRPTdsasatPDEPYAWDSREYLRQKLVGQFVTFVRDFTATSGRDHGRIYLGGTspadaeNVAEGAV 131
Cdd:pfam00565   1 RVRLVGIDAPETAKPNT------PVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYLNGK------NINEELV 68

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 17533087   132 SAGLLEV-RQGKVADEYSTKLLELQEQAKSAGRGKWNS 168
Cdd:pfam00565  69 KEGLAWVyKAYPPNFKHYDELLAAEEEAKKKKKGLWSD 106
Tudor_TDRD6_rpt5 cd20424
fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 742-793 1.41e-07

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: 50.97  E-value: 1.41e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 17533087 742 KRGDLCVAKFSqDGQWYRCKVESvRAGQAEIVYIDYGNRETIEAVKLAQIPA 793
Cdd:cd20424  60 NPGTLCLAKYS-DQHWYRGIIIT-NKNSTEVFFVDYGNTEKVEKEDMLPIPS 109
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 747-800 2.27e-07

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: 49.02  E-value: 2.27e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17533087 747 CVAKFSQDGQWYRCKVESVRAG--QAEIVYIDYGNRETIEAVKLAQIPAGFANFPA 800
Cdd:cd20423   9 CLAKYSEDGKWCRALIDNVYEPveMVEVTYVDYGNKELVSLKNLRSISEEFLKLKA 64
Tudor_TDRD6_rpt6 cd20425
sixth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 742-800 3.59e-07

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: 49.76  E-value: 3.59e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 742 KRGDLCVAKFSQDGQWYRCKV-ESVRAGQAEIVYIDYGNRETIEAVKLAQIPAGFANFPA 800
Cdd:cd20425  49 QLGDLICAEYPEDGLWYRAVVkEKIPNNLVSVQFIDYGNTSVVQPSKIHRLPKELLSIPA 108
Tudor_SMN_SPF30-like cd21182
Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing ...
 744-791 3.62e-07

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: 47.63  E-value: 3.62e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 17533087 744 GDLCVAKFSQDGQWYRCKVESVRA--GQAEIVYIDYGNRETIEAVKLAQI 791
Cdd:cd21182   1 GDKCLAPYSDDGKYYEATIEEITEesDTATVVFDGYGNSEEVPLSDLKPL 50
Tudor_TDRD15_rpt5 cd20440
fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 694-795 7.15e-07

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: 48.99  E-value: 7.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 694 QVAVTDI-APGALRFS-AQNIEDGPKIEKMTTEMRQAlaehpPLAGSYTTKRGDLCVAKFSQDGQWYRCKVESVRAGQAE 771
Cdd:cd20440  13 EVYITHVySPAKFYCQlDRNTEILEALMEKIAEISKL-----FNSQILDNCKTRLCLAKYFEDGQWYRALAHPVESSSHL 87

                        90       100
                ....*....|....*....|....*
gi 17533087 772 IVY-IDYGNRETIEAVKLAQIPAGF 795
Cdd:cd20440  88 SVYfVDYGNKQIVEKNEVLPIPDTA 112
Tudor_TDRD2 cd20412
Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, ...
 717-799 1.08e-06

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


Pssm-ID: 410483  Cd Length: 95  Bit Score: 47.68  E-value: 1.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 717 KIEKMTTEMRQALAEHPPLAGSYTTKRGDLCVAKFSQDGQWYRCKVESVR-AGQAEIVYIDYGNRETIEAVKLAQIPAGF 795
Cdd:cd20412   5 QLDKLVQEMTQYYESEENRHTLLTVQVGDIVAAPFRHDGSWYRARVLGFLeNGNLDLYFVDYGDSGYVPLEDLRALRSDF 84


                ....
gi 17533087 796 ANFP 799
Cdd:cd20412  85 LSLP 88
Tudor_TDRD6_rpt2 cd20421
second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 716-809 5.07e-06

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: 46.65  E-value: 5.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 716 PKIEKMTTEMRQAL-AEHPPLAGSYTTKRGDLCVAKfSQDGQWYRCKVESVRAGQ--AEIVYIDYGNRETIEAVKLAQIP 792
Cdd:cd20421  35 QELKRLSESMHQYYeGRVGSGYETRPEKLGSPCAAR-GSDGRWYRAVLQQVFSANrvVEVLHVDYGRKEVVSVSNLRYLA 113

                        90
                ....*....|....*..
gi 17533087 793 AGFANFPagVREYNLAL 809
Cdd:cd20421 114 PEYFRMP--VVTYPCAL 128
Tudor_AKAP1 cd20407
Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; ...
 744-799 6.12e-06

Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope, where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. It contains a C-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410478  Cd Length: 76  Bit Score: 44.89  E-value: 6.12e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17533087 744 GDLCVAkfSQDGQWYRCKVESV--RAGQAEIVYIDYGNRETIEAVKLAQIPAGFANFP 799
Cdd:cd20407   8 GVICAA--PVMNAWYRAQVVGVfeETDEVEIKYLDYGGYERVPVDDLRQIRSDFMTLP 63
Tudor_SPF30 cd20399
Tudor domain found in survival of motor neuron-related-splicing factor 30 (SPF30) and similar ...
 742-782 6.22e-06

Tudor domain found in survival of motor neuron-related-splicing factor 30 (SPF30) and similar proteins; 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. Overexpression of SPF30 causes apoptosis. It 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: 410470 [Multi-domain]  Cd Length: 55  Bit Score: 44.22  E-value: 6.22e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 17533087 742 KRGDLCVAKFSQDGQWYRCKVESVRA-GQAEIVYIDYGNRET 782
Cdd:cd20399   2 KVGDKCMAVWSEDGQYYEATIEEISEdGTCTVTFDGYGNTEV 43
Tudor_TDRD15_rpt4 cd20439
fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 747-795 6.47e-06

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: 46.33  E-value: 6.47e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 17533087 747 CVAKFSQDGQWYRCKVES-VRAGQAEIVYIDYGNRETIEAVKLAQIPAGF 795
Cdd:cd20439  61 CVAKYSKDGKWYRAAVLKqVSAKEVDVIFVDYGNQERVLISDLRAIKPQF 110
Tudor_TDRD5 cd20419
Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is ...
 713-800 6.75e-06

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: 45.90  E-value: 6.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 713 EDGPKIEKMTTEMR-----QALAEHPPLAGSYTTKrGDLCVAKFSQDGQWYRCKVESV-RAGQAEIVYIDYGNRETIEAV 786
Cdd:cd20419  19 DTSEMLEDMMIEMRrcysnEHVSERYVMPEAFIQP-GQVCCVRIPEDVWWYRVIIHQVlNKQEVEVFYPDFGDIGTVQKS 97

                        90
                ....*....|....
gi 17533087 787 KLAQIPAGFANFPA 800
Cdd:cd20419  98 RLRFLKCCYSKLPA 111
Tudor_SF cd04508
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
 744-783 9.80e-06

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: 43.34  E-value: 9.80e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 17533087 744 GDLCVAKFSQDGQWYRCKVESVRAGQAEIVYIDYGNRETI 783
Cdd:cd04508   1 GDRVEAKWSDDGQWYPATVVAVNDDGKYTVLFDDGNEEEV 40
Tudor_SMN cd20398
Tudor domain found in survival motor neuron protein (SMN) and similar proteins; SMN, also ...
 742-781 1.10e-05

Tudor domain found in survival motor neuron protein (SMN) 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. Mutations in human SMN lead to motor neuron degeneration and spinal muscular atrophy. SMN contains a central, highly conserved Tudor domain that is required for U snRNP assembly and Sm protein binding and has been shown to bind arginine-glycine-rich motifs in an methylarginine-dependent manner.


Pssm-ID: 410469  Cd Length: 56  Bit Score: 43.41  E-value: 1.10e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 17533087 742 KRGDLCVAKFSQDGQWYRCKVESVRAGQAE--IVYIDYGNRE 781
Cdd:cd20398   2 KVGDKCRAVYSEDGIIYEATIVSIDAERGTcvVRYTGYGNEE 43
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
 717-799 2.21e-05

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: 43.92  E-value: 2.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 717 KIEKMTTEMRQ------ALAEHPPLagsyttkrgdLCVAKFS--QDGQWYRCKVESVRAGQAEIVYIDYGNRETIEAVKL 788
Cdd:cd20431  21 ILQQLTAEINQrqlvplTTKPVPNL----------LCLAPFTdaDMKKYYRAKILYVSGSSAEVFFVDYGNTSQVPSSLL 90

                        90
                ....*....|.
gi 17533087 789 AQIPAGFANFP 799
Cdd:cd20431  91 REIPETLLTLP 101
Tudor_TDRD3 cd20413
Tudor domain found in Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is ...
 742-791 4.20e-05

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: 41.94  E-value: 4.20e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 17533087 742 KRGDLCVAKFSQDGQWYRCKVESV--RAGQAEIVYIDYGNRETIEAVKLAQI 791
Cdd:cd20413   2 KPGDECLAKYWEDNKFYRAEVTAVhpSGKTAVVKFMEYGNYEEVLLSDIKPI 53
Tudor_vreteno-like_rpt1 cd20444
first Tudor domain found in Drosophila melanogaster protein vreteno and similar proteins; ...
 742-792 7.94e-05

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: 41.14  E-value: 7.94e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 17533087 742 KRGDLCVAKFsqDGQWYRCKVESVRAGQAEIV--YIDYGNRETIEAVKLAQIP 792
Cdd:cd20444   2 TPGQMVIAKF--DGNHYRAIVLRVLNPDLKILvrFVDFGNVEVMKLENLYECP 52
Tudor_TDRD6_rpt3 cd20422
third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 744-800 8.93e-05

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: 43.27  E-value: 8.93e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17533087 744 GDLCVAKFSQDGqWYRCKVESVRAGQAEIVYIDYGNRETIEAVKLAQIPAGFANFPA 800
Cdd:cd20422  53 GQLCCAKWKEDR-YYRAIVTAVKGKMVEVFLVDRGNTEMVDWYDVKKLLPQFRELPA 108
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 742-799 2.13e-04

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: 42.24  E-value: 2.13e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17533087 742 KRGDLCVAKfSQDGQWYRCKVESV-------RAGQAEIVYIDYGNRETIEAVKLAQIPAGFANFP 799
Cdd:cd20435  51 KVGDLCAVE-DENNLYHRVKVLEItekddktKPREVLVKFIDEGRVETVVVSQLLELPEELKSLP 114
Tudor_TDRD6_rpt1 cd20420
first Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 719-808 2.14e-04

first 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 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: 410491  Cd Length: 132  Bit Score: 42.03  E-value: 2.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 719 EKMTTEMRQALAEHPPLA--GSYTTKRGDLCVAKFsqDGQWYRCKVESVRAGQAEIVYIDYGNRETIEAVKLAQIPAGFA 796
Cdd:cd20420  39 QRLTREIQAAVKMRGCGAgdGGAEPSVGDLCLVEV--GGLWHRCRVVSRQGDDYRVFLLDEGRTVVARAKSLARGRKDFF 116

                        90
                ....*....|..
gi 17533087 797 NFPAGVREYNLA 808
Cdd:cd20420 117 SLPPEVLGCVLA 128
Tudor_vreteno-like_rpt2 cd20445
second Tudor domain found in Drosophila melanogaster protein vreteno and similar proteins; ...
 745-799 2.83e-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: 39.71  E-value: 2.83e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17533087 745 DLCVAKFsqDGQWYR--CkVESVRAGQAEIVYIDYGNRETIEAVKLAQIPAGFANFP 799
Cdd:cd20445   3 ELCIAKY--MDKWYRavC-LESVGDGRPTVLFCDYGNILMARLTDIRPFPPTFATEP 56
Tudor_TDRD15_rpt3 cd20438
third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 744-827 4.81e-04

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: 41.31  E-value: 4.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 744 GDLCVAKFSQDGQWYRCKVESVRAGQAEIVYIDYGNRETIEAVKLAQIPAGFANFPAGVREYNLALAKLPNEDYVQLTSD 823
Cdd:cd20438  58 GLLCCARYSKDRHYYRAVITEVLDLKVSVYFLDFGNTDTVPFYDVKTLLPEFSELPALAMCCSLAHVFPVEEVWTKNAND 137


                ....
gi 17533087 824 AFAQ 827
Cdd:cd20438 138 FFKK 141
Tudor_TDRD7_rpt1 cd20427
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 719-799 7.99e-04

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: 39.72  E-value: 7.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 719 EKMTTEMRQALAEHPPLAGSYTTKRGDLcVAKFSQDGQWYRCKVESVRAGQAEIVYIDYGNRETIEAVKLAQIPAGFANF 798
Cdd:cd20427   1 EQMEDEMKEFYSKSSTAMCLRSPSVGQL-VAVKAEEDAWLRAQVIEVEEDKVKVYYVDHGFSEVVERSKLFKLNKQFYSL 79


                .
gi 17533087 799 P 799
Cdd:cd20427  80 P 80
SNc smart00318
Staphylococcal nuclease homologues;
758-904 1.11e-03

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 39.94  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087    758 YRCKVESVRAGQAEIVYIDYGNRETIeavKLAQIPAgfanfPAGVReyNLALAKLPNEDYVQLTSDAFAQYLFGHS-SVF 836
Cdd:smart00318   3 IRGVVERVIDGDTIRVRLPKGPLITI---RLSGIDA-----PETAR--PNKGDGTPDEPFGEEAKEFLKKLLLGKKvQVE 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17533087    837 INSEYKVGtSEYVTVYYDSGNkkvDIGKSLIAEGLALAdHRREPRLQTLVNDYNTTEEVARKSRKNIW 904
Cdd:smart00318  73 VDSKDRYG-RFLGTVYLNGGN---NIAEELVKEGLAKV-YRYADKDEYVYDELLEAEEAAKKARKGLW 135
Tudor_TDRD4_rpt4 cd20417
fourth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 742-783 1.52e-03

fourth 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 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: 410488  Cd Length: 68  Bit Score: 37.80  E-value: 1.52e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 17533087 742 KRGDLCVAKFSqDGQWYRCKVESVRAGQAEIVYIDYGNRETI 783
Cdd:cd20417   2 KKGEGCVVRGS-DTLWYRGKVLEVIGGMVRVQYVDQGYIEKI 42
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 850-906 7.80e-03

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


Pssm-ID: 395448  Cd Length: 106  Bit Score: 36.92  E-value: 7.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17533087   850 TVYYDsgnkKVDIGKSLIAEGLALADHRREPRLQTLvNDYNTTEEVARKSRKNIWEY 906
Cdd:pfam00565  55 YVYLN----GKNINEELVKEGLAWVYKAYPPNFKHY-DELLAAEEEAKKKKKGLWSD 106
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
822-904 7.86e-03

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 38.12  E-value: 7.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533087 822 SDAFAQYLFGHSsVFInsEYKVGTSEY----VTVYYDsgnkKVDIGKSLIAEGLALADHRREPRlqTLVNDYNTTEEVAR 897
Cdd:COG1525  73 RQALRALLAGKT-VTL--EPDEGRDRYgrllAYVYVD----GRDLNEELVREGLAWAYRRYSPD--KYADRYLAAEAEAR 143


                ....*..
gi 17533087 898 KSRKNIW 904
Cdd:COG1525 144 AARRGLW 150
 
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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