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Conserved domains on  [gi|15240352|ref|NP_200986|]
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TUDOR-SN protein 2 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tudor_AtTudor1-like cd20443
Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor ...
 743-858 2.35e-70

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: 228.89  E-value: 2.35e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 743 GGRFYVQTVGDQKVASIQNQLAALSLKDAPII-GSFNPKKGDIVLAQFSLDNSWNRAMIVNGPRGAVQSPEEEFEVFYID 821
Cdd:cd20443   1 GGRFYVQVVSDQRLSSIQQQLEGLSLKDKANPpGGFNPKKGELVLAQFSADNSWNRAMVVNAPRQGTQSPKDEYEVFYID 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15240352 822 YGNQEIVPYSAIRPVDPSVSSAPGLAQLCRLAYIKVP 858
Cdd:cd20443  81 YGNQETVPLSALRPLDPSVSSAPGLAQLCSLAHIKVP 117
SNc super family cl00140
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 188-368 5.40e-22

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: 92.71  E-value: 5.40e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352    188 KPMEGIVEQVRDGSTIRVYLLPEfQFVQVFVAGLQAPSMGRRQStqeavvdpdvtatsngdasaetrGPLTTAQrlaasa 267
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPETARPNK-----------------------GDGTPDE------ 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352    268 assvevssdPFAMEAKYFTELRVLNRDVRIVLEGVDKFNNLIGSVYYSDGdtvKDLGLELVENGLAKYVEWSANmlDEEA 347
Cdd:smart00318  51 ---------PFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRFLGTVYLNGG---NNIAEELVKEGLAKVYRYADK--DEYV 116

                          170       180
                   ....*....|....*....|.
gi 15240352    348 KKKLKATELQCKKNRVKMWAN 368
Cdd:smart00318 117 YDELLEAEEAAKKARKGLWSD 137
SNc super family cl00140
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 582-709 1.42e-21

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: 91.55  E-value: 1.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352    582 NQISAVVEYVLSGHRFKLYIPKEsCSIAFAFSGVRCP----------GRGEPYSEEAIALMRRKIMQRDVEIVVENVDRT 651
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPetarpnkgdgTPDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 15240352    652 GTFLGSMWEKNsKTNAGTYLLEAGLAKMQTGFGADRIPEAHILEmAERSAKNQKLKIW 709
Cdd:smart00318  80 GRFLGTVYLNG-GNNIAEELVKEGLAKVYRYADKDEYVYDELLE-AEEAAKKARKGLW 135
SNc super family cl00140
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 391-551 1.28e-19

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


The actual alignment was detected with superfamily member cd00175:

Pssm-ID: 469627  Cd Length: 129  Bit Score: 85.79  E-value: 1.28e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 391 VVSGDCLVVaddsipFGSPMAERRVCLSSIRSP--KMGNPRREEKPAPYAREAKEFLRQKLIGMEVIVQMEYSRKisPGd 468
Cdd:cd00175   2 VIDGDTIRV------RLPPGPLITVRLSGIDAPetARPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDR--YG- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 469 gvttsgagdrvMDFGSVFLPsptkgdtavaaaatPGANIAELIISRGLGTVVRHRDFeeRSNHYDALLAAEARAIAGKKN 548
Cdd:cd00175  73 -----------RTLGTVYLN--------------GGENIAEELVKEGLARVYRYYPD--DSEYYDELLEAEEAAKKARKG 125


                ...
gi 15240352 549 IHS 551
Cdd:cd00175 126 LWS 128
SNc super family cl00140
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 12-120 1.65e-17

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: 80.00  E-value: 1.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352     12 LKGRVKAVTSGDCLVItalthnRAGPPPEKTITLSSLMAPKMARRG----GIDEPFAWESREFLRKLCIGKEVAFKVDYK 87
Cdd:smart00318   3 IRGVVERVIDGDTIRV------RLPKGPLITIRLSGIDAPETARPNkgdgTPDEPFGEEAKEFLKKLLLGKKVQVEVDSK 76

                           90       100       110
                   ....*....|....*....|....*....|....
gi 15240352     88 veAIAGREFGSVYLGNE-NLAKLVVQNGWAKVRR 120
Cdd:smart00318  77 --DRYGRFLGTVYLNGGnNIAEELVKEGLAKVYR 108
SNc super family cl00140
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 856-966 3.24e-08

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 pfam00565:

Pssm-ID: 469627  Cd Length: 106  Bit Score: 52.32  E-value: 3.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352   856 KVPGKEEDFGRDAGEYLHTVTLesGKEFRAVVEERDTSGGkvkgqgtgteLVVTLIAvdDEISVNAAMLQEGIARMEKRR 935
Cdd:pfam00565  14 KPNTPVQPFGKEAKEFLKKLVL--GKKVVVLEFDKDKYGR----------TLGYVYL--NGKNINEELVKEGLAWVYKAY 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 15240352   936 RWEPKDKqaalDALEKFQDEARKSRTGIWEY 966
Cdd:pfam00565  80 PPNFKHY----DELLAAEEEAKKKKKGLWSD 106
 
Name Accession Description Interval E-value
Tudor_AtTudor1-like cd20443
Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor ...
 743-858 2.35e-70

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: 228.89  E-value: 2.35e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 743 GGRFYVQTVGDQKVASIQNQLAALSLKDAPII-GSFNPKKGDIVLAQFSLDNSWNRAMIVNGPRGAVQSPEEEFEVFYID 821
Cdd:cd20443   1 GGRFYVQVVSDQRLSSIQQQLEGLSLKDKANPpGGFNPKKGELVLAQFSADNSWNRAMVVNAPRQGTQSPKDEYEVFYID 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15240352 822 YGNQEIVPYSAIRPVDPSVSSAPGLAQLCRLAYIKVP 858
Cdd:cd20443  81 YGNQETVPLSALRPLDPSVSSAPGLAQLCSLAHIKVP 117
TUDOR pfam00567
Tudor domain;
731-853 1.58e-22

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 93.57  E-value: 1.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352   731 ETLKVVVTEVLGGGRFYVQTV-GDQKVASIQNQLaaLSLKDAPIIGSFNPKKGDIVLAQFSLDNSWNRAMIVNGPrgavq 809
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQPKsDSKKLEKLTEEL--QEYYASKPPESLPPAVGDGCVAAFSEDGKWYRAKITESL----- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15240352   810 sPEEEFEVFYIDYGNQEIVPYSAIRPVDPSVSSAPGLAQLCRLA 853
Cdd:pfam00567  74 -DDGLVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
SNc smart00318
Staphylococcal nuclease homologues;
188-368 5.40e-22

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 92.71  E-value: 5.40e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352    188 KPMEGIVEQVRDGSTIRVYLLPEfQFVQVFVAGLQAPSMGRRQStqeavvdpdvtatsngdasaetrGPLTTAQrlaasa 267
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPETARPNK-----------------------GDGTPDE------ 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352    268 assvevssdPFAMEAKYFTELRVLNRDVRIVLEGVDKFNNLIGSVYYSDGdtvKDLGLELVENGLAKYVEWSANmlDEEA 347
Cdd:smart00318  51 ---------PFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRFLGTVYLNGG---NNIAEELVKEGLAKVYRYADK--DEYV 116

                          170       180
                   ....*....|....*....|.
gi 15240352    348 KKKLKATELQCKKNRVKMWAN 368
Cdd:smart00318 117 YDELLEAEEAAKKARKGLWSD 137
SNc smart00318
Staphylococcal nuclease homologues;
582-709 1.42e-21

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 91.55  E-value: 1.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352    582 NQISAVVEYVLSGHRFKLYIPKEsCSIAFAFSGVRCP----------GRGEPYSEEAIALMRRKIMQRDVEIVVENVDRT 651
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPetarpnkgdgTPDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 15240352    652 GTFLGSMWEKNsKTNAGTYLLEAGLAKMQTGFGADRIPEAHILEmAERSAKNQKLKIW 709
Cdd:smart00318  80 GRFLGTVYLNG-GNNIAEELVKEGLAKVYRYADKDEYVYDELLE-AEEAAKKARKGLW 135
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 391-551 1.28e-19

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: 85.79  E-value: 1.28e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 391 VVSGDCLVVaddsipFGSPMAERRVCLSSIRSP--KMGNPRREEKPAPYAREAKEFLRQKLIGMEVIVQMEYSRKisPGd 468
Cdd:cd00175   2 VIDGDTIRV------RLPPGPLITVRLSGIDAPetARPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDR--YG- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 469 gvttsgagdrvMDFGSVFLPsptkgdtavaaaatPGANIAELIISRGLGTVVRHRDFeeRSNHYDALLAAEARAIAGKKN 548
Cdd:cd00175  73 -----------RTLGTVYLN--------------GGENIAEELVKEGLARVYRYYPD--DSEYYDELLEAEEAAKKARKG 125


                ...
gi 15240352 549 IHS 551
Cdd:cd00175 126 LWS 128
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 197-368 1.34e-19

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: 85.79  E-value: 1.34e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 197 VRDGSTIRVYLLPEfQFVQVFVAGLQAPsmgrrqstqeavvdpdvtatsngdasaETRGPLTTAQRlaasaassvevSSD 276
Cdd:cd00175   2 VIDGDTIRVRLPPG-PLITVRLSGIDAP---------------------------ETARPNKGKSE-----------TDE 42

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 277 PFAMEAKYFTELRVLNRDVRIVLEGVDKFNNLIGSVYYSDGdtvKDLGLELVENGLAKYVEWSANmlDEEAKKKLKATEL 356
Cdd:cd00175  43 PFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTVYLNGG---ENIAEELVKEGLARVYRYYPD--DSEYYDELLEAEE 117

                       170
                ....*....|..
gi 15240352 357 QCKKNRVKMWAN 368
Cdd:cd00175 118 AAKKARKGLWSD 129
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 590-709 6.90e-19

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: 83.48  E-value: 6.90e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 590 YVLSGHRFKLYIPKEsCSIAFAFSGVRCP----------GRGEPYSEEAIALMRRKIMQRDVEIVVENVDRTGTFLGSMW 659
Cdd:cd00175   1 RVIDGDTIRVRLPPG-PLITVRLSGIDAPetarpnkgksETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTVY 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15240352 660 eKNSKTNAGTYLLEAGLAKMQTGFGADRIPEAHILEmAERSAKNQKLKIW 709
Cdd:cd00175  80 -LNGGENIAEELVKEGLARVYRYYPDDSEYYDELLE-AEEAAKKARKGLW 127
SNc smart00318
Staphylococcal nuclease homologues;
382-551 8.35e-19

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 83.46  E-value: 8.35e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352    382 QNFTGKVVEVVSGDCLVVaddsipFGSPMAERRVCLSSIRSP--KMGNPRREEKPAPYAREAKEFLRQKLIGMEVIVQME 459
Cdd:smart00318   1 KEIRGVVERVIDGDTIRV------RLPKGPLITIRLSGIDAPetARPNKGDGTPDEPFGEEAKEFLKKLLLGKKVQVEVD 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352    460 YSRKisPGDGVttsgagdrvmdfGSVFLPsptkgdtavaaaatPGANIAELIISRGLGTVVRHRDFEErsNHYDALLAAE 539
Cdd:smart00318  75 SKDR--YGRFL------------GTVYLN--------------GGNNIAEELVKEGLAKVYRYADKDE--YVYDELLEAE 124

                          170
                   ....*....|..
gi 15240352    540 ARAIAGKKNIHS 551
Cdd:smart00318 125 EAAKKARKGLWS 136
SNc smart00318
Staphylococcal nuclease homologues;
12-120 1.65e-17

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 80.00  E-value: 1.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352     12 LKGRVKAVTSGDCLVItalthnRAGPPPEKTITLSSLMAPKMARRG----GIDEPFAWESREFLRKLCIGKEVAFKVDYK 87
Cdd:smart00318   3 IRGVVERVIDGDTIRV------RLPKGPLITIRLSGIDAPETARPNkgdgTPDEPFGEEAKEFLKKLLLGKKVQVEVDSK 76

                           90       100       110
                   ....*....|....*....|....*....|....
gi 15240352     88 veAIAGREFGSVYLGNE-NLAKLVVQNGWAKVRR 120
Cdd:smart00318  77 --DRYGRFLGTVYLNGGnNIAEELVKEGLAKVYR 108
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 39-120 1.83e-17

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: 79.63  E-value: 1.83e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352  39 PEKTITLSSLMAPKMARRG----GIDEPFAWESREFLRKLCIGKEVAFKVDYKveAIAGREFGSVYLGN-ENLAKLVVQN 113
Cdd:cd00175  16 PLITVRLSGIDAPETARPNkgksETDEPFGEEAKEFLKKLLLGKKVQVEVDSK--DRYGRTLGTVYLNGgENIAEELVKE 93


                ....*..
gi 15240352 114 GWAKVRR 120
Cdd:cd00175  94 GLARVYR 100
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 277-368 3.92e-13

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: 66.58  E-value: 3.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352   277 PFAMEAKYFTELRVLNRDVRIVLEGVDKFNNLIGSVYYSDgdtvKDLGLELVENGLAK-YVEWSANmldEEAKKKLKATE 355
Cdd:pfam00565  21 PFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYLNG----KNINEELVKEGLAWvYKAYPPN---FKHYDELLAAE 93

                          90
                  ....*....|...
gi 15240352   356 LQCKKNRVKMWAN 368
Cdd:pfam00565  94 EEAKKKKKGLWSD 106
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 612-711 3.50e-11

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: 60.80  E-value: 3.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352   612 FSGVRCP------GRGEPYSEEAIALMRRKIMQRDVEIVVENVDRTGTFLGSMWEknSKTNAGTYLLEAGLAKMQTGFGa 685
Cdd:pfam00565   4 LVGIDAPetakpnTPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYL--NGKNINEELVKEGLAWVYKAYP- 80

                          90       100
                  ....*....|....*....|....*.
gi 15240352   686 DRIPEAHILEMAERSAKNQKLKIWEN 711
Cdd:pfam00565  81 PNFKHYDELLAAEEEAKKKKKGLWSD 106
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 42-118 1.80e-10

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: 58.87  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352    42 TITLSSLMAPKMARRGGIDEPFAWESREFLRKLCIGKEVA---FKVDYKveaiaGREFGSVYLGNENLAKLVVQNGWAKV 118
Cdd:pfam00565   1 RVRLVGIDAPETAKPNTPVQPFGKEAKEFLKKLVLGKKVVvleFDKDKY-----GRTLGYVYLNGKNINEELVKEGLAWV 75
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
2-121 3.55e-10

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 59.69  E-value: 3.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352   2 ATGAATENQWLKGRVKAVTSGDCLVITALTHnragpppEKTITLSSLMAPKMARRGGIDEPFAWESREFLRKLCIGKEVA 81
Cdd:COG1525  14 ALAAAAAAATLTAGVVRVIDGDTLRVRDDGK-------GERVRLAGIDAPELGQPCGPEQPCGEEARQALRALLAGKTVT 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15240352  82 FKVDYKVEAiAGREFGSVYLGNENLAKLVVQNGWAKVRRP 121
Cdd:COG1525  87 LEPDEGRDR-YGRLLAYVYVDGRDLNEELVREGLAWAYRR 125
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 779-838 2.34e-09

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: 54.20  E-value: 2.34e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352    779 PKKGDIVLAQFSlDNSWNRAMIVNgprgavQSPEEEFEVFYIDYGNQEIVPYSAIRPVDP 838
Cdd:smart00333   3 FKVGDKVAARWE-DGEWYRARIVK------VDGEQLYEVFFIDYGNEEVVPPSDLRQLPE 55
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
384-557 2.79e-08

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 54.30  E-value: 2.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 384 FTGKVVEVVSGDCLVVADDSipfgspmAERRVCLSSIRSPKMGNPRREEKPapYAREAKEFLRQKLIGMEVIVQMEYSRk 463
Cdd:COG1525  24 LTAGVVRVIDGDTLRVRDDG-------KGERVRLAGIDAPELGQPCGPEQP--CGEEARQALRALLAGKTVTLEPDEGR- 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 464 ispgdgvttsGAGDRVMdfGSVFLpsptkgdtavaaaatPGANIAELIISRGLGTVVRHRDfeeRSNHYDALLAAEARAI 543
Cdd:COG1525  94 ----------DRYGRLL--AYVYV---------------DGRDLNEELVREGLAWAYRRYS---PDKYADRYLAAEAEAR 143

                       170
                ....*....|....
gi 15240352 544 AGKKNIHSAKDSPA 557
Cdd:COG1525 144 AARRGLWSDAFPVP 157
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 856-966 3.24e-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: 52.32  E-value: 3.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352   856 KVPGKEEDFGRDAGEYLHTVTLesGKEFRAVVEERDTSGGkvkgqgtgteLVVTLIAvdDEISVNAAMLQEGIARMEKRR 935
Cdd:pfam00565  14 KPNTPVQPFGKEAKEFLKKLVL--GKKVVVLEFDKDKYGR----------TLGYVYL--NGKNINEELVKEGLAWVYKAY 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 15240352   936 RWEPKDKqaalDALEKFQDEARKSRTGIWEY 966
Cdd:pfam00565  80 PPNFKHY----DELLAAEEEAKKKKKGLWSD 106
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
178-372 3.25e-08

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 53.91  E-value: 3.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 178 AMGLLAASKGKPMEGIVEQVRDGSTIRVYLLPEFQFVQVfvAGLQAPsmgrrqstqeavvdpdvtatsngdasaETRGPL 257
Cdd:COG1525  12 LAALAAAAAAATLTAGVVRVIDGDTLRVRDDGKGERVRL--AGIDAP---------------------------ELGQPC 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 258 TTAQrlaasaassvevssdPFAMEAKYFTELRVLNRDVRI-VLEGVDKFNNLIGSVYYsDGdtvKDLGLELVENGLAK-Y 335
Cdd:COG1525  63 GPEQ---------------PCGEEARQALRALLAGKTVTLePDEGRDRYGRLLAYVYV-DG---RDLNEELVREGLAWaY 123

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15240352 336 VEWSanmlDEEAKKKLKATELQCKKNRVKMWA--NYVPP 372
Cdd:COG1525 124 RRYS----PDKYADRYLAAEAEARAARRGLWSdaFPVPP 158
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 414-549 2.23e-06

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: 47.32  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352   414 RVCLSSIRSPKMGNPRREEKPapYAREAKEFLRQKLIGMEVIVqMEYSRkispgdgvttsgagDRVMDF-GSVFLpsptk 492
Cdd:pfam00565   1 RVRLVGIDAPETAKPNTPVQP--FGKEAKEFLKKLVLGKKVVV-LEFDK--------------DKYGRTlGYVYL----- 58

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15240352   493 gdtavaaaatPGANIAELIISRGLGTVvrHRDFEERSNHYDALLAAEARAIAGKKNI 549
Cdd:pfam00565  59 ----------NGKNINEELVKEGLAWV--YKAYPPNFKHYDELLAAEEEAKKKKKGL 103
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
851-964 6.60e-06

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 47.37  E-value: 6.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 851 RLAYIKVP------GKEEDFGRDAGEYL------HTVTLEsgkefraVVEERDTSGgkvkgqgtgtELVVTLIAvdDEIS 918
Cdd:COG1525  49 RLAGIDAPelgqpcGPEQPCGEEARQALrallagKTVTLE-------PDEGRDRYG----------RLLAYVYV--DGRD 109

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15240352 919 VNAAMLQEGIARMekRRRWEPKDKQAALDALEKfqdEARKSRTGIW 964
Cdd:COG1525 110 LNEELVREGLAWA--YRRYSPDKYADRYLAAEA---EARAARRGLW 150
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
574-709 8.44e-06

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 46.98  E-value: 8.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 574 FLPSLQRINQISAVVEYVLSGHRFKLYIPKESCSIAFAfsGVRCP------GRGEPYSEEAIALMRRKIMQRDVEI-VVE 646
Cdd:COG1525  14 ALAAAAAAATLTAGVVRVIDGDTLRVRDDGKGERVRLA--GIDAPelgqpcGPEQPCGEEARQALRALLAGKTVTLePDE 91

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240352 647 NVDRTGTFLGSMWekNSKTNAGTYLLEAGLAKMQTGFGADRIPEAhiLEMAERSAKNQKLKIW 709
Cdd:COG1525  92 GRDRYGRLLAYVY--VDGRDLNEELVREGLAWAYRRYSPDKYADR--YLAAEAEARAARRGLW 150
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 858-964 2.30e-05

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: 44.96  E-value: 2.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 858 PGKEEDFGRDAGEYLHTVTLesGKEFRAVVEERDTSGGkvkgqgtgteLVVTLIaVDDEISVNAAMLQEGIARmekRRRW 937
Cdd:cd00175  38 SETDEPFGEEAKEFLKKLLL--GKKVQVEVDSKDRYGR----------TLGTVY-LNGGENIAEELVKEGLAR---VYRY 101

                        90       100
                ....*....|....*....|....*..
gi 15240352 938 EPKDKqAALDALEKFQDEARKSRTGIW 964
Cdd:cd00175 102 YPDDS-EYYDELLEAEEAAKKARKGLW 127
SNc smart00318
Staphylococcal nuclease homologues;
851-964 5.93e-05

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 43.79  E-value: 5.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352    851 RLAYIKVP----------GKEEDFGRDAGEYLHTVTLesGKEFRAVVEERDTSGGKVkgqgtGTelvvtlIAVDDEISVN 920
Cdd:smart00318  29 RLSGIDAPetarpnkgdgTPDEPFGEEAKEFLKKLLL--GKKVQVEVDSKDRYGRFL-----GT------VYLNGGNNIA 95

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 15240352    921 AAMLQEGIARmekRRRWEPKDKQAAlDALEKFQDEARKSRTGIW 964
Cdd:smart00318  96 EELVKEGLAK---VYRYADKDEYVY-DELLEAEEAAKKARKGLW 135
 
Name Accession Description Interval E-value
Tudor_AtTudor1-like cd20443
Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor ...
 743-858 2.35e-70

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: 228.89  E-value: 2.35e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 743 GGRFYVQTVGDQKVASIQNQLAALSLKDAPII-GSFNPKKGDIVLAQFSLDNSWNRAMIVNGPRGAVQSPEEEFEVFYID 821
Cdd:cd20443   1 GGRFYVQVVSDQRLSSIQQQLEGLSLKDKANPpGGFNPKKGELVLAQFSADNSWNRAMVVNAPRQGTQSPKDEYEVFYID 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15240352 822 YGNQEIVPYSAIRPVDPSVSSAPGLAQLCRLAYIKVP 858
Cdd:cd20443  81 YGNQETVPLSALRPLDPSVSSAPGLAQLCSLAHIKVP 117
TUDOR pfam00567
Tudor domain;
731-853 1.58e-22

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 93.57  E-value: 1.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352   731 ETLKVVVTEVLGGGRFYVQTV-GDQKVASIQNQLaaLSLKDAPIIGSFNPKKGDIVLAQFSLDNSWNRAMIVNGPrgavq 809
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQPKsDSKKLEKLTEEL--QEYYASKPPESLPPAVGDGCVAAFSEDGKWYRAKITESL----- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15240352   810 sPEEEFEVFYIDYGNQEIVPYSAIRPVDPSVSSAPGLAQLCRLA 853
Cdd:pfam00567  74 -DDGLVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
SNc smart00318
Staphylococcal nuclease homologues;
188-368 5.40e-22

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 92.71  E-value: 5.40e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352    188 KPMEGIVEQVRDGSTIRVYLLPEfQFVQVFVAGLQAPSMGRRQStqeavvdpdvtatsngdasaetrGPLTTAQrlaasa 267
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPETARPNK-----------------------GDGTPDE------ 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352    268 assvevssdPFAMEAKYFTELRVLNRDVRIVLEGVDKFNNLIGSVYYSDGdtvKDLGLELVENGLAKYVEWSANmlDEEA 347
Cdd:smart00318  51 ---------PFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRFLGTVYLNGG---NNIAEELVKEGLAKVYRYADK--DEYV 116

                          170       180
                   ....*....|....*....|.
gi 15240352    348 KKKLKATELQCKKNRVKMWAN 368
Cdd:smart00318 117 YDELLEAEEAAKKARKGLWSD 137
SNc smart00318
Staphylococcal nuclease homologues;
582-709 1.42e-21

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 91.55  E-value: 1.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352    582 NQISAVVEYVLSGHRFKLYIPKEsCSIAFAFSGVRCP----------GRGEPYSEEAIALMRRKIMQRDVEIVVENVDRT 651
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPetarpnkgdgTPDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 15240352    652 GTFLGSMWEKNsKTNAGTYLLEAGLAKMQTGFGADRIPEAHILEmAERSAKNQKLKIW 709
Cdd:smart00318  80 GRFLGTVYLNG-GNNIAEELVKEGLAKVYRYADKDEYVYDELLE-AEEAAKKARKGLW 135
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 391-551 1.28e-19

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: 85.79  E-value: 1.28e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 391 VVSGDCLVVaddsipFGSPMAERRVCLSSIRSP--KMGNPRREEKPAPYAREAKEFLRQKLIGMEVIVQMEYSRKisPGd 468
Cdd:cd00175   2 VIDGDTIRV------RLPPGPLITVRLSGIDAPetARPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDR--YG- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 469 gvttsgagdrvMDFGSVFLPsptkgdtavaaaatPGANIAELIISRGLGTVVRHRDFeeRSNHYDALLAAEARAIAGKKN 548
Cdd:cd00175  73 -----------RTLGTVYLN--------------GGENIAEELVKEGLARVYRYYPD--DSEYYDELLEAEEAAKKARKG 125


                ...
gi 15240352 549 IHS 551
Cdd:cd00175 126 LWS 128
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 197-368 1.34e-19

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: 85.79  E-value: 1.34e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 197 VRDGSTIRVYLLPEfQFVQVFVAGLQAPsmgrrqstqeavvdpdvtatsngdasaETRGPLTTAQRlaasaassvevSSD 276
Cdd:cd00175   2 VIDGDTIRVRLPPG-PLITVRLSGIDAP---------------------------ETARPNKGKSE-----------TDE 42

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 277 PFAMEAKYFTELRVLNRDVRIVLEGVDKFNNLIGSVYYSDGdtvKDLGLELVENGLAKYVEWSANmlDEEAKKKLKATEL 356
Cdd:cd00175  43 PFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTVYLNGG---ENIAEELVKEGLARVYRYYPD--DSEYYDELLEAEE 117

                       170
                ....*....|..
gi 15240352 357 QCKKNRVKMWAN 368
Cdd:cd00175 118 AAKKARKGLWSD 129
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 590-709 6.90e-19

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: 83.48  E-value: 6.90e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 590 YVLSGHRFKLYIPKEsCSIAFAFSGVRCP----------GRGEPYSEEAIALMRRKIMQRDVEIVVENVDRTGTFLGSMW 659
Cdd:cd00175   1 RVIDGDTIRVRLPPG-PLITVRLSGIDAPetarpnkgksETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTVY 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15240352 660 eKNSKTNAGTYLLEAGLAKMQTGFGADRIPEAHILEmAERSAKNQKLKIW 709
Cdd:cd00175  80 -LNGGENIAEELVKEGLARVYRYYPDDSEYYDELLE-AEEAAKKARKGLW 127
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 735-858 8.14e-19

first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410479  Cd Length: 130  Bit Score: 83.57  E-value: 8.14e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 735 VVVTEVLGGGRFYVQtVGDQKVASIQNQLAAlSLKDAPIIGS----FNPKKGDIVLAQFSLDNSWNRAMIVngprgAVQS 810
Cdd:cd20408   1 GTVTEFKNPGEFYIQ-IYTLEVLESLVKLTS-QLKKTYASVNnhkeYIPEVGEVCVAKYSEDQNWYRALVQ-----TVDV 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15240352 811 PEEEFEVFYIDYGNQEIVPYSAIRPVDPSVSSAPGLAQLCRLAYIKVP 858
Cdd:cd20408  74 QQKKAGVFYIDYGNEETVPLNRIQPLKKDIELFPPCAIKCCLANVKPP 121
SNc smart00318
Staphylococcal nuclease homologues;
382-551 8.35e-19

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 83.46  E-value: 8.35e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352    382 QNFTGKVVEVVSGDCLVVaddsipFGSPMAERRVCLSSIRSP--KMGNPRREEKPAPYAREAKEFLRQKLIGMEVIVQME 459
Cdd:smart00318   1 KEIRGVVERVIDGDTIRV------RLPKGPLITIRLSGIDAPetARPNKGDGTPDEPFGEEAKEFLKKLLLGKKVQVEVD 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352    460 YSRKisPGDGVttsgagdrvmdfGSVFLPsptkgdtavaaaatPGANIAELIISRGLGTVVRHRDFEErsNHYDALLAAE 539
Cdd:smart00318  75 SKDR--YGRFL------------GTVYLN--------------GGNNIAEELVKEGLAKVYRYADKDE--YVYDELLEAE 124

                          170
                   ....*....|..
gi 15240352    540 ARAIAGKKNIHS 551
Cdd:smart00318 125 EAAKKARKGLWS 136
SNc smart00318
Staphylococcal nuclease homologues;
12-120 1.65e-17

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 80.00  E-value: 1.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352     12 LKGRVKAVTSGDCLVItalthnRAGPPPEKTITLSSLMAPKMARRG----GIDEPFAWESREFLRKLCIGKEVAFKVDYK 87
Cdd:smart00318   3 IRGVVERVIDGDTIRV------RLPKGPLITIRLSGIDAPETARPNkgdgTPDEPFGEEAKEFLKKLLLGKKVQVEVDSK 76

                           90       100       110
                   ....*....|....*....|....*....|....
gi 15240352     88 veAIAGREFGSVYLGNE-NLAKLVVQNGWAKVRR 120
Cdd:smart00318  77 --DRYGRFLGTVYLNGGnNIAEELVKEGLAKVYR 108
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 39-120 1.83e-17

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: 79.63  E-value: 1.83e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352  39 PEKTITLSSLMAPKMARRG----GIDEPFAWESREFLRKLCIGKEVAFKVDYKveAIAGREFGSVYLGN-ENLAKLVVQN 113
Cdd:cd00175  16 PLITVRLSGIDAPETARPNkgksETDEPFGEEAKEFLKKLLLGKKVQVEVDSK--DRYGRTLGTVYLNGgENIAEELVKE 93


                ....*..
gi 15240352 114 GWAKVRR 120
Cdd:cd00175  94 GLARVYR 100
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
 755-841 1.41e-16

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: 75.41  E-value: 1.41e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 755 KVASIQNQLAALSLKDAPIIGSFNPKKGDIVLAQFSLDNSWNRAMIVngprgAVQSPeEEFEVFYIDYGNQEIVPYSAIR 834
Cdd:cd20433   4 QLEKLMEKLRFEIASNPPLPGSYTPRKGDLCAAKFVEDGEWYRAKVE-----KVEGD-KKVHVLYIDYGNREVLPSTRLA 77


                ....*..
gi 15240352 835 PVDPSVS 841
Cdd:cd20433  78 ALPPAFS 84
Tudor_TDRD1_rpt2 cd20409
second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 768-840 1.13e-13

second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410480  Cd Length: 82  Bit Score: 67.10  E-value: 1.13e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240352 768 LKDAPIIGSFNPKKGDIVLAQFSLDNSWNRAMIVNgprgavQSPEEEFEVFYIDYGNQEIVPYSAIRPVDPSV 840
Cdd:cd20409  15 CKVAPASSDFSPAVGEVCCAQFTEDNQWYRASVLA------YSSEDSVLVGYIDFGNSEEVALSRLRPIPPSL 81
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 277-368 3.92e-13

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: 66.58  E-value: 3.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352   277 PFAMEAKYFTELRVLNRDVRIVLEGVDKFNNLIGSVYYSDgdtvKDLGLELVENGLAK-YVEWSANmldEEAKKKLKATE 355
Cdd:pfam00565  21 PFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYLNG----KNINEELVKEGLAWvYKAYPPN---FKHYDELLAAE 93

                          90
                  ....*....|...
gi 15240352   356 LQCKKNRVKMWAN 368
Cdd:pfam00565  94 EEAKKKKKGLWSD 106
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 781-835 4.92e-13

Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar proteins; dTUD is required during oogenesis for the formation of primordial germ cells and for normal abdominal segmentation. It contains 11 Tudor domains. The family also includes mitochondrial A-kinase anchor protein 1 (AKAP1) and Tudor domain-containing proteins (TDRDs). AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), or dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), or protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. TDRDs have diverse biological functions and may contain one or more copies of the Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410450  Cd Length: 50  Bit Score: 64.07  E-value: 4.92e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15240352 781 KGDIVLAQFSLDNSWNRAMIVNgprgavQSPEEEFEVFYIDYGNQEIVPYSAIRP 835
Cdd:cd20379   1 VGDLCAAKYEEDGKWYRARVLE------VLSNDKVEVFFVDYGNTETVPLSDLRP 49
Tudor_TDRD1_rpt4 cd20411
fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 735-853 8.09e-13

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: 65.93  E-value: 8.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 735 VVVTEVLGGGRFYV----QTVGDQKVASIQNQLAALSLKdAPIIGSFNPKKGDIVLAQFSLDNSWNRAMivngprgAVQS 810
Cdd:cd20411   1 ALVLEVISPDLFYAlpktGQVNVEKLKALMTELAEYCSK-QSVPQQFRPRIGDACCARFTGDKNWYRAV-------VLET 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15240352 811 PEEEFEVFYIDYGNQEIVPYSAIRPVDPSVSSAPGLAQLCRLA 853
Cdd:cd20411  73 SDSEVKVLYADYGNTETLPLSRILPITKSHLELPFQIIRCSLA 115
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 612-711 3.50e-11

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: 60.80  E-value: 3.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352   612 FSGVRCP------GRGEPYSEEAIALMRRKIMQRDVEIVVENVDRTGTFLGSMWEknSKTNAGTYLLEAGLAKMQTGFGa 685
Cdd:pfam00565   4 LVGIDAPetakpnTPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYL--NGKNINEELVKEGLAWVYKAYP- 80

                          90       100
                  ....*....|....*....|....*.
gi 15240352   686 DRIPEAHILEMAERSAKNQKLKIWEN 711
Cdd:pfam00565  81 PNFKHYDELLAAEEEAKKKKKGLWSD 106
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 42-118 1.80e-10

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: 58.87  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352    42 TITLSSLMAPKMARRGGIDEPFAWESREFLRKLCIGKEVA---FKVDYKveaiaGREFGSVYLGNENLAKLVVQNGWAKV 118
Cdd:pfam00565   1 RVRLVGIDAPETAKPNTPVQPFGKEAKEFLKKLVLGKKVVvleFDKDKY-----GRTLGYVYLNGKNINEELVKEGLAWV 75
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
2-121 3.55e-10

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 59.69  E-value: 3.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352   2 ATGAATENQWLKGRVKAVTSGDCLVITALTHnragpppEKTITLSSLMAPKMARRGGIDEPFAWESREFLRKLCIGKEVA 81
Cdd:COG1525  14 ALAAAAAAATLTAGVVRVIDGDTLRVRDDGK-------GERVRLAGIDAPELGQPCGPEQPCGEEARQALRALLAGKTVT 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15240352  82 FKVDYKVEAiAGREFGSVYLGNENLAKLVVQNGWAKVRRP 121
Cdd:COG1525  87 LEPDEGRDR-YGRLLAYVYVDGRDLNEELVREGLAWAYRR 125
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 784-852 8.53e-10

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


Pssm-ID: 410494  Cd Length: 80  Bit Score: 55.95  E-value: 8.53e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240352 784 IVLAQFSLDNSWNRAMIVNgprgaVQSPEEEFEVFYIDYGNQEIVPYSAIRPVDPSVSSAPGLAQLCRL 852
Cdd:cd20423   8 VCLAKYSEDGKWCRALIDN-----VYEPVEMVEVTYVDYGNKELVSLKNLRSISEEFLKLKAQAFRCSL 71
Tudor_TDRD15_rpt7 cd20442
seventh Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 730-863 1.76e-09

seventh Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the seventh one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410513  Cd Length: 160  Bit Score: 57.74  E-value: 1.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 730 KETLKVVVTEVLGGGRFYVQTVGDQKVASIQNQLAALSLKDAPIIGSFNPKKGDIVLAQFSLDNSWNRAMIVNgprgaVQ 809
Cdd:cd20442   1 GQIEKGTLLSVSKNGTFYVRLLRNSEQLTDLESLIAKEAKKCKFVPVEDIKEGLECLAKSKKNLKWYRAVVEH-----LY 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15240352 810 SPEEEFEVFYIDYGNQEIVPYSAIRPVDPSVSSAPGLAQLCRLAYIKVPGKEED 863
Cdd:cd20442  76 PETEKMLVFFVDHGITEVVSMGNIKQLSNDLLQIPRQAVLCRWNWPESSKELSF 129
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 779-838 2.34e-09

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: 54.20  E-value: 2.34e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352    779 PKKGDIVLAQFSlDNSWNRAMIVNgprgavQSPEEEFEVFYIDYGNQEIVPYSAIRPVDP 838
Cdd:smart00333   3 FKVGDKVAARWE-DGEWYRARIVK------VDGEQLYEVFFIDYGNEEVVPPSDLRQLPE 55
Tudor_TDRD6_rpt6 cd20425
sixth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 746-852 8.17e-09

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: 54.39  E-value: 8.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 746 FYVQTVGDQ-KVASIQNQLAALSLKDAPIIG-SFNpkKGDIVLAQFSLDNSWNRAMIVNgprgavQSPEEEFEVFYIDYG 823
Cdd:cd20425  15 FYVQLAQDEdELSMISEKLNASKANDEEVECeSLQ--LGDLICAEYPEDGLWYRAVVKE------KIPNNLVSVQFIDYG 86

                        90       100
                ....*....|....*....|....*....
gi 15240352 824 NQEIVPYSAIRPVDPSVSSAPGLAQLCRL 852
Cdd:cd20425  87 NTSVVQPSKIHRLPKELLSIPALSIHCFL 115
Tudor_TDRD15_rpt6 cd20441
sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 744-853 2.67e-08

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: 52.82  E-value: 2.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 744 GRFYVQTVGDQKV-ASIQNQLAALSLKDAPIIGSfNPKKGDIVLAQFSLDNSWNRAMIVNgprgavQSPEEEFEVFYIDY 822
Cdd:cd20441   3 SRFFIQLSEDEKViLQLAEELNETSEKSRENAAV-KLKVGDLVAAEYDEDLALYRAVITA------VLPGKSFKVEFIDY 75

                        90       100       110
                ....*....|....*....|....*....|.
gi 15240352 823 GNQEIVPYSAIRPVDPSVSSAPGLAQLCRLA 853
Cdd:cd20441  76 GNTAVVDKSNIYTLQEKFLSLPRLSIPCSLS 106
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
384-557 2.79e-08

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 54.30  E-value: 2.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 384 FTGKVVEVVSGDCLVVADDSipfgspmAERRVCLSSIRSPKMGNPRREEKPapYAREAKEFLRQKLIGMEVIVQMEYSRk 463
Cdd:COG1525  24 LTAGVVRVIDGDTLRVRDDG-------KGERVRLAGIDAPELGQPCGPEQP--CGEEARQALRALLAGKTVTLEPDEGR- 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 464 ispgdgvttsGAGDRVMdfGSVFLpsptkgdtavaaaatPGANIAELIISRGLGTVVRHRDfeeRSNHYDALLAAEARAI 543
Cdd:COG1525  94 ----------DRYGRLL--AYVYV---------------DGRDLNEELVREGLAWAYRRYS---PDKYADRYLAAEAEAR 143

                       170
                ....*....|....
gi 15240352 544 AGKKNIHSAKDSPA 557
Cdd:COG1525 144 AARRGLWSDAFPVP 157
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 856-966 3.24e-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: 52.32  E-value: 3.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352   856 KVPGKEEDFGRDAGEYLHTVTLesGKEFRAVVEERDTSGGkvkgqgtgteLVVTLIAvdDEISVNAAMLQEGIARMEKRR 935
Cdd:pfam00565  14 KPNTPVQPFGKEAKEFLKKLVL--GKKVVVLEFDKDKYGR----------TLGYVYL--NGKNINEELVKEGLAWVYKAY 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 15240352   936 RWEPKDKqaalDALEKFQDEARKSRTGIWEY 966
Cdd:pfam00565  80 PPNFKHY----DELLAAEEEAKKKKKGLWSD 106
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
178-372 3.25e-08

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 53.91  E-value: 3.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 178 AMGLLAASKGKPMEGIVEQVRDGSTIRVYLLPEFQFVQVfvAGLQAPsmgrrqstqeavvdpdvtatsngdasaETRGPL 257
Cdd:COG1525  12 LAALAAAAAAATLTAGVVRVIDGDTLRVRDDGKGERVRL--AGIDAP---------------------------ELGQPC 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 258 TTAQrlaasaassvevssdPFAMEAKYFTELRVLNRDVRI-VLEGVDKFNNLIGSVYYsDGdtvKDLGLELVENGLAK-Y 335
Cdd:COG1525  63 GPEQ---------------PCGEEARQALRALLAGKTVTLePDEGRDRYGRLLAYVYV-DG---RDLNEELVREGLAWaY 123

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15240352 336 VEWSanmlDEEAKKKLKATELQCKKNRVKMWA--NYVPP 372
Cdd:COG1525 124 RRYS----PDKYADRYLAAEAEARAARRGLWSdaFPVPP 158
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 779-856 3.60e-08

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: 52.05  E-value: 3.60e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15240352 779 PKKGDIVLAQFSlDNSWNRAMIVNGPRgavqspEEEFEVFYIDYGNQEIVPYSAIRPVDPSVSSAPGLAQLCRLAYIK 856
Cdd:cd20415  25 PVQGQACVALFE-DGAWYRARIIGLPG------HREVEVKYVDFGNTATVTIKHVRKIKDDFLSLPEKARECRLAFIE 95
Tudor_TDRD1_rpt3 cd20410
third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 777-839 4.75e-08

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: 50.42  E-value: 4.75e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240352 777 FNPKKGDIVLAQFSLDNSWNRAMIVNgprgavQSPEEEFEVFYIDYGNQEIVPYSAIRPVDPS 839
Cdd:cd20410   1 FKPIVGEPCCAFFSGDGNWYRAMVKE------ILPGGAVKVHFVDYGNVEEVTLDKLRKITST 57
Tudor_TDRD15_rpt3 cd20438
third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 778-855 2.44e-07

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: 50.94  E-value: 2.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 778 NPKKGDIVLAQFSLDNSWNRAMI--VNGprgavqspeEEFEVFYIDYGNQEIVPYSAIRPVDPSVSSAPGLAQLCRLAYI 855
Cdd:cd20438  54 KPEPGLLCCARYSKDRHYYRAVIteVLD---------LKVSVYFLDFGNTDTVPFYDVKTLLPEFSELPALAMCCSLAHV 124
Tudor_TDRD8 cd20430
Tudor domain found in Tudor domain-containing protein 8 (TDRD8) and similar proteins; TDRD8, ...
 761-833 9.00e-07

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: 47.29  E-value: 9.00e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15240352 761 NQLAALSLKDAPIIGsfNPKKGDIVLAQFSLDNSWNRAmivngprgAVQS--PEEEFEVFYIDYGNQEIVPYSAI 833
Cdd:cd20430   3 DELAEVCPTAPPLFG--TPDPNKIYGGKFSEDNCWYRC--------KVKSilSDEKCTVQYIDYGNTETVSRSSI 67
Tudor_vreteno-like_rpt1 cd20444
first Tudor domain found in Drosophila melanogaster protein vreteno and similar proteins; ...
 779-828 1.08e-06

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: 46.53  E-value: 1.08e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15240352 779 PKKGDIVLAQFslDNSWNRAMIVNgprgaVQSPEEEFEVFYIDYGNQEIV 828
Cdd:cd20444   1 PTPGQMVIAKF--DGNHYRAIVLR-----VLNPDLKILVRFVDFGNVEVM 43
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 414-549 2.23e-06

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: 47.32  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352   414 RVCLSSIRSPKMGNPRREEKPapYAREAKEFLRQKLIGMEVIVqMEYSRkispgdgvttsgagDRVMDF-GSVFLpsptk 492
Cdd:pfam00565   1 RVRLVGIDAPETAKPNTPVQP--FGKEAKEFLKKLVLGKKVVV-LEFDK--------------DKYGRTlGYVYL----- 58

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15240352   493 gdtavaaaatPGANIAELIISRGLGTVvrHRDFEERSNHYDALLAAEARAIAGKKNI 549
Cdd:pfam00565  59 ----------NGKNINEELVKEGLAWV--YKAYPPNFKHYDELLAAEEEAKKKKKGL 103
Tudor_TDRD2 cd20412
Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, ...
 778-835 2.26e-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: 46.90  E-value: 2.26e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15240352 778 NPKKGDIVLAQFSLDNSWNRAMIVNgprgavQSPEEEFEVFYIDYGNQEIVPYSAIRP 835
Cdd:cd20412  28 TVQVGDIVAAPFRHDGSWYRARVLG------FLENGNLDLYFVDYGDSGYVPLEDLRA 79
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
851-964 6.60e-06

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 47.37  E-value: 6.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 851 RLAYIKVP------GKEEDFGRDAGEYL------HTVTLEsgkefraVVEERDTSGgkvkgqgtgtELVVTLIAvdDEIS 918
Cdd:COG1525  49 RLAGIDAPelgqpcGPEQPCGEEARQALrallagKTVTLE-------PDEGRDRYG----------RLLAYVYV--DGRD 109

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15240352 919 VNAAMLQEGIARMekRRRWEPKDKQAALDALEKfqdEARKSRTGIW 964
Cdd:COG1525 110 LNEELVREGLAWA--YRRYSPDKYADRYLAAEA---EARAARRGLW 150
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
574-709 8.44e-06

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 46.98  E-value: 8.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 574 FLPSLQRINQISAVVEYVLSGHRFKLYIPKESCSIAFAfsGVRCP------GRGEPYSEEAIALMRRKIMQRDVEI-VVE 646
Cdd:COG1525  14 ALAAAAAAATLTAGVVRVIDGDTLRVRDDGKGERVRLA--GIDAPelgqpcGPEQPCGEEARQALRALLAGKTVTLePDE 91

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240352 647 NVDRTGTFLGSMWekNSKTNAGTYLLEAGLAKMQTGFGADRIPEAhiLEMAERSAKNQKLKIW 709
Cdd:COG1525  92 GRDRYGRLLAYVY--VDGRDLNEELVREGLAWAYRRYSPDKYADR--YLAAEAEARAARRGLW 150
Tudor_TDRD6_rpt5 cd20424
fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 735-839 1.07e-05

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: 45.96  E-value: 1.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 735 VVVTEVLGGGRFYVQTVGDQKV-ASIQNQLAALSLKDAPIIGSFNPkkGDIVLAQFSlDNSWNRamivngprGAVQSPEE 813
Cdd:cd20424  16 VYITYVNDPWTFYCQLARNAGVlDQLASAISRLSSEIRKLELSVNP--GTLCLAKYS-DQHWYR--------GIIITNKN 84

                        90       100
                ....*....|....*....|....*.
gi 15240352 814 EFEVFYIDYGNQEIVPYSAIRPVdPS 839
Cdd:cd20424  85 STEVFFVDYGNTEKVEKEDMLPI-PS 109
Tudor_TDRD15_rpt2 cd20437
second Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 732-853 1.49e-05

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: 45.10  E-value: 1.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 732 TLKVVVTEVLGGGRFYVQTVGDQK-----VASIQNQLAALSLKDAPIIGSFnpkkgDIVLAQFSLDNSWNRamivngprG 806
Cdd:cd20437   4 TEKVKITAAVSPSKFYCQLLSWEPelsklTTQMTLHYESVSKELNPSCENF-----GLLCAAKGKDGQWHR--------G 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15240352 807 AVQS--PEEEFEVFYIDYGNQEIVPYSAIRPVDPSVSSAPGLAQLCRLA 853
Cdd:cd20437  71 FLQQllPPSQVKVWFIDYGNSEAVSSHSVLKLPPDFFSLPLMSFPCSLS 119
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 858-964 2.30e-05

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: 44.96  E-value: 2.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 858 PGKEEDFGRDAGEYLHTVTLesGKEFRAVVEERDTSGGkvkgqgtgteLVVTLIaVDDEISVNAAMLQEGIARmekRRRW 937
Cdd:cd00175  38 SETDEPFGEEAKEFLKKLLL--GKKVQVEVDSKDRYGR----------TLGTVY-LNGGENIAEELVKEGLAR---VYRY 101

                        90       100
                ....*....|....*....|....*..
gi 15240352 938 EPKDKqAALDALEKFQDEARKSRTGIW 964
Cdd:cd00175 102 YPDDS-EYYDELLEAEEAAKKARKGLW 127
Tudor_TDRD15_rpt5 cd20440
fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 734-836 3.07e-05

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: 44.37  E-value: 3.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 734 KVVVTEVLGGGRFYVQTVGDQKVasiqnqLAALSLKDAPIIGSFN-----PKKGDIVLAQFSLDNSWNRAMIVngprgAV 808
Cdd:cd20440  13 EVYITHVYSPAKFYCQLDRNTEI------LEALMEKIAEISKLFNsqildNCKTRLCLAKYFEDGQWYRALAH-----PV 81

                        90       100
                ....*....|....*....|....*...
gi 15240352 809 QSPEEeFEVFYIDYGNQEIVPYSAIRPV 836
Cdd:cd20440  82 ESSSH-LSVYFVDYGNKQIVEKNEVLPI 108
Tudor_SMN_SPF30-like cd21182
Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing ...
 782-836 3.40e-05

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: 42.24  E-value: 3.40e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15240352 782 GDIVLAQFSLDNSWNRAMIVngprgAVQSPEEEFEVFYIDYGNQEIVPYSAIRPV 836
Cdd:cd21182   1 GDKCLAPYSDDGKYYEATIE-----EITEESDTATVVFDGYGNSEEVPLSDLKPL 50
SNc smart00318
Staphylococcal nuclease homologues;
851-964 5.93e-05

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 43.79  E-value: 5.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352    851 RLAYIKVP----------GKEEDFGRDAGEYLHTVTLesGKEFRAVVEERDTSGGKVkgqgtGTelvvtlIAVDDEISVN 920
Cdd:smart00318  29 RLSGIDAPetarpnkgdgTPDEPFGEEAKEFLKKLLL--GKKVQVEVDSKDRYGRFL-----GT------VYLNGGNNIA 95

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 15240352    921 AAMLQEGIARmekRRRWEPKDKQAAlDALEKFQDEARKSRTGIW 964
Cdd:smart00318  96 EELVKEGLAK---VYRYADKDEYVY-DELLEAEEAAKKARKGLW 135
Tudor_TDRD15_rpt4 cd20439
fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 786-852 9.14e-04

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: 40.17  E-value: 9.14e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240352 786 LAQFSLDNSWNRAMIVNgprgavQSPEEEFEVFYIDYGNQEIVPYSAIRPVDPSVSSAPGLAQLCRL 852
Cdd:cd20439  62 VAKYSKDGKWYRAAVLK------QVSAKEVDVIFVDYGNQERVLISDLRAIKPQFLLLEGQAFRCSL 122
Tudor_TDRD6_rpt2 cd20421
second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 731-852 1.44e-03

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: 39.71  E-value: 1.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 731 ETLKVVVTEVLGGGRFYVQtvgdqkVASIQNQLAALSLKDAPI----IGSFN---PKKGDIVLAQFSLDNSWNRAMIVNg 803
Cdd:cd20421  11 VTETVVVTEVTDPHRIFCQ------LRSLSQELKRLSESMHQYyegrVGSGYetrPEKLGSPCAARGSDGRWYRAVLQQ- 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15240352 804 prgaVQSPEEEFEVFYIDYGNQEIVPYSAIRPVDPSVSSAPGLAQLCRL 852
Cdd:cd20421  84 ----VFSANRVVEVLHVDYGRKEVVSVSNLRYLAPEYFRMPVVTYPCAL 128
Tudor_TDRD3 cd20413
Tudor domain found in Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is ...
 780-836 1.49e-03

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: 37.71  E-value: 1.49e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 780 KKGDIVLAQFSLDNSWNRAMIVN-GPRG--AVqspeeefeVFYIDYGNQEIVPYSAIRPV 836
Cdd:cd20413   2 KPGDECLAKYWEDNKFYRAEVTAvHPSGktAV--------VKFMEYGNYEEVLLSDIKPI 53
Tudor_TDRD6_rpt3 cd20422
third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 779-855 2.12e-03

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: 39.42  E-value: 2.12e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240352 779 PKKGDIVLAQFSlDNSWNRAMIVngprgAVQSpeEEFEVFYIDYGNQEIVPYSAIRPVDPSVSSAPGLAQLCRLAYI 855
Cdd:cd20422  50 PQPGQLCCAKWK-EDRYYRAIVT-----AVKG--KMVEVFLVDRGNTEMVDWYDVKKLLPQFRELPALALKCCLADI 118
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
 738-838 3.12e-03

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: 38.14  E-value: 3.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240352 738 TEVLGGGRFYVQTVGDQKV-------ASI-QNQLAALSLKDAPiigsfnpkkGDIVLAQFS--LDNSWNRAMI--VNGpr 805
Cdd:cd20431   1 TEVVEVGHFWGYRIDENSSeilqqltAEInQRQLVPLTTKPVP---------NLLCLAPFTdaDMKKYYRAKIlyVSG-- 69

                        90       100       110
                ....*....|....*....|....*....|...
gi 15240352 806 gavqspeEEFEVFYIDYGNQEIVPYSAIRPVDP 838
Cdd:cd20431  70 -------SSAEVFFVDYGNTSQVPSSLLREIPE 95
Tudor_TDRD7_rpt1 cd20427
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 779-853 8.61e-03

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: 36.64  E-value: 8.61e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15240352 779 PKKGDIVlAQFSLDNSWNRAMIVngprgavQSPEEEFEVFYIDYGNQEIVPYSAIRPVDPSVSSAPGLAQLCRLA 853
Cdd:cd20427  23 PSVGQLV-AVKAEEDAWLRAQVI-------EVEEDKVKVYYVDHGFSEVVERSKLFKLNKQFYSLPFQATKCKLA 89
 
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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