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Conserved domains on  [gi|22326646|ref|NP_196352|]
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TUDOR-SN protein 1 [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 ...
 747-862 4.19e-69

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: 225.42  E-value: 4.19e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 747 GGRFYVQSAGDQKIASIQNQLASLSIKDAPII-GSFNPKRGDIVLAQFSLDNSWNRAMIVTAPRAAVQSPDEKFEVFYID 825
Cdd:cd20443   1 GGRFYVQVVSDQRLSSIQQQLEGLSLKDKANPpGGFNPKKGELVLAQFSADNSWNRAMVVNAPRQGTQSPKDEYEVFYID 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 22326646 826 YGNQETVPYSAIRPIDPSVSAAPGLAQLCRLAYIKVP 862
Cdd:cd20443  81 YGNQETVPLSALRPLDPSVSSAPGLAQLCSLAHIKVP 117
SNc super family cl00140
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 37-151 1.29e-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 cd00175:

Pssm-ID: 469627  Cd Length: 129  Bit Score: 94.26  E-value: 1.29e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646  37 PEKTITFSSLMAPKMARRG----GIDEPFAWESKEFLRKLCIGKEVAFKVDYKveAIAGREFGSVFLGN-ENLAKLVVKT 111
Cdd:cd00175  16 PLITVRLSGIDAPETARPNkgksETDEPFGEEAKEFLKKLLLGKKVQVEVDSK--DRYGRTLGTVYLNGgENIAEELVKE 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 22326646 112 GWAKVREpgqqNQDKVSPYIKELLQLEELAKQEGYGRWSK 151
Cdd:cd00175  94 GLARVYR----YYPDDSEYYDELLEAEEAAKKARKGLWSD 129
SNc super family cl00140
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 587-712 1.39e-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: 94.64  E-value: 1.39e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    587 RRIPAVVEYVLSGHRFKLYIPKiTCSIAFSFSGVRCP----------GRGEPYSEEAISVMRRRIMQRDVEIEVETVDRT 656
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPK-GPLITIRLSGIDAPetarpnkgdgTPDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 22326646    657 GTFLGSMWESRT-NVATVLLEAGLAKMQTSFGADRIAEAHLLEqAERSAKNQKLKIW 712
Cdd:smart00318  80 GRFLGTVYLNGGnNIAEELVKEGLAKVYRYADKDEYVYDELLE-AEEAAKKARKGLW 135
SNc super family cl00140
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 186-364 1.59e-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: 94.25  E-value: 1.59e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    186 KPMEGIVEQVRDGSTIRVYLLPEfQFVQVFVAGVQAPSMGRRTTngsvvetvpdepngdvsaesrGPLTTAQrlaasaas 265
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPETARPNK---------------------GDGTPDE-------- 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    266 svevssdPFATEAKYFTEHRVLSRDVRIVLEGVDKFNNLIGSVHYSDGEtvkDLGLELVENGLAKFVEWSANMmeEEAKK 345
Cdd:smart00318  51 -------PFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRFLGTVYLNGGN---NIAEELVKEGLAKVYRYADKD--EYVYD 118

                          170
                   ....*....|....*....
gi 22326646    346 KLKAAELQCKKDKVKMWAN 364
Cdd:smart00318 119 ELLEAEEAAKKARKGLWSD 137
SNc super family cl00140
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 378-556 9.68e-12

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: 63.43  E-value: 9.68e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    378 QNFTGKVVEVVSGDCLIVaddavpFGSPAAERRVCLSSIRSP--KMGNPRREEKPAPYAREAREFLRQRLIGKQVIVQME 455
Cdd:smart00318   1 KEIRGVVERVIDGDTIRV------RLPKGPLITIRLSGIDAPetARPNKGDGTPDEPFGEEAKEFLKKLLLGKKVQVEVD 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    456 YSRKvtqgdgpttsgaADRFMdfGSVFLPSaakadsdevtappaaaiagsqpvGVNIAELVLVRGFGNVVRHRDFEErsN 535
Cdd:smart00318  75 SKDR------------YGRFL--GTVYLNG-----------------------GNNIAEELVKEGLAKVYRYADKDE--Y 115

                          170       180
                   ....*....|....*....|.
gi 22326646    536 HYDALLAAEARALAGKKGIHS 556
Cdd:smart00318 116 VYDELLEAEEAAKKARKGLWS 136
SNc super family cl00140
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 860-968 4.64e-07

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: 49.24  E-value: 4.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646   860 KVPSLEDDFGPEAGEYLHTVTLGsgKEFKAVIEERDTSGGkvkgqgtgteFVVTLIAvdDEISVNAAMLQEGIARMEKRq 939
Cdd:pfam00565  14 KPNTPVQPFGKEAKEFLKKLVLG--KKVVVLEFDKDKYGR----------TLGYVYL--NGKNINEELVKEGLAWVYKA- 78

                          90       100
                  ....*....|....*....|....*....
gi 22326646   940 kwgHKGKQAALDALEKFQEEARKSRIGIW 968
Cdd:pfam00565  79 ---YPPNFKHYDELLAAEEEAKKKKKGLW 104
 
Name Accession Description Interval E-value
Tudor_AtTudor1-like cd20443
Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor ...
 747-862 4.19e-69

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: 225.42  E-value: 4.19e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 747 GGRFYVQSAGDQKIASIQNQLASLSIKDAPII-GSFNPKRGDIVLAQFSLDNSWNRAMIVTAPRAAVQSPDEKFEVFYID 825
Cdd:cd20443   1 GGRFYVQVVSDQRLSSIQQQLEGLSLKDKANPpGGFNPKKGELVLAQFSADNSWNRAMVVNAPRQGTQSPKDEYEVFYID 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 22326646 826 YGNQETVPYSAIRPIDPSVSAAPGLAQLCRLAYIKVP 862
Cdd:cd20443  81 YGNQETVPLSALRPLDPSVSSAPGLAQLCSLAHIKVP 117
TUDOR pfam00567
Tudor domain;
735-857 2.88e-24

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 98.58  E-value: 2.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646   735 ETLKVVVTEVLGGGRFYVQS-AGDQKIASIQNQLasLSIKDAPIIGSFNPKRGDIVLAQFSLDNSWNRAMIvtapraAVQ 813
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQPkSDSKKLEKLTEEL--QEYYASKPPESLPPAVGDGCVAAFSEDGKWYRAKI------TES 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 22326646   814 SPDEKFEVFYIDYGNQETVPYSAIRPIDPSVSAAPGLAQLCRLA 857
Cdd:pfam00567  73 LDDGLVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 37-151 1.29e-22

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: 94.26  E-value: 1.29e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646  37 PEKTITFSSLMAPKMARRG----GIDEPFAWESKEFLRKLCIGKEVAFKVDYKveAIAGREFGSVFLGN-ENLAKLVVKT 111
Cdd:cd00175  16 PLITVRLSGIDAPETARPNkgksETDEPFGEEAKEFLKKLLLGKKVQVEVDSK--DRYGRTLGTVYLNGgENIAEELVKE 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 22326646 112 GWAKVREpgqqNQDKVSPYIKELLQLEELAKQEGYGRWSK 151
Cdd:cd00175  94 GLARVYR----YYPDDSEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
587-712 1.39e-22

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 94.64  E-value: 1.39e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    587 RRIPAVVEYVLSGHRFKLYIPKiTCSIAFSFSGVRCP----------GRGEPYSEEAISVMRRRIMQRDVEIEVETVDRT 656
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPK-GPLITIRLSGIDAPetarpnkgdgTPDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 22326646    657 GTFLGSMWESRT-NVATVLLEAGLAKMQTSFGADRIAEAHLLEqAERSAKNQKLKIW 712
Cdd:smart00318  80 GRFLGTVYLNGGnNIAEELVKEGLAKVYRYADKDEYVYDELLE-AEEAAKKARKGLW 135
SNc smart00318
Staphylococcal nuclease homologues;
186-364 1.59e-22

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 94.25  E-value: 1.59e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    186 KPMEGIVEQVRDGSTIRVYLLPEfQFVQVFVAGVQAPSMGRRTTngsvvetvpdepngdvsaesrGPLTTAQrlaasaas 265
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPETARPNK---------------------GDGTPDE-------- 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    266 svevssdPFATEAKYFTEHRVLSRDVRIVLEGVDKFNNLIGSVHYSDGEtvkDLGLELVENGLAKFVEWSANMmeEEAKK 345
Cdd:smart00318  51 -------PFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRFLGTVYLNGGN---NIAEELVKEGLAKVYRYADKD--EYVYD 118

                          170
                   ....*....|....*....
gi 22326646    346 KLKAAELQCKKDKVKMWAN 364
Cdd:smart00318 119 ELLEAEEAAKKARKGLWSD 137
SNc smart00318
Staphylococcal nuclease homologues;
10-150 9.62e-22

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 91.94  E-value: 9.62e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646     10 LKGRVKAVTSGDCLVItalshnRAGPPPEKTITFSSLMAPKMARRG----GIDEPFAWESKEFLRKLCIGKEVAFKVDYK 85
Cdd:smart00318   3 IRGVVERVIDGDTIRV------RLPKGPLITIRLSGIDAPETARPNkgdgTPDEPFGEEAKEFLKKLLLGKKVQVEVDSK 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22326646     86 veAIAGREFGSVFLGNE-NLAKLVVKTGWAKVREpgqqNQDKVSPYIKELLQLEELAKQEGYGRWS 150
Cdd:smart00318  77 --DRYGRFLGTVYLNGGnNIAEELVKEGLAKVYR----YADKDEYVYDELLEAEEAAKKARKGLWS 136
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 195-364 1.37e-20

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: 88.49  E-value: 1.37e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 195 VRDGSTIRVYLLPEfQFVQVFVAGVQAPsmgrRTTNGSVVETVPDEPngdvsaesrgplttaqrlaasaassvevssdpF 274
Cdd:cd00175   2 VIDGDTIRVRLPPG-PLITVRLSGIDAP----ETARPNKGKSETDEP--------------------------------F 44

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 275 ATEAKYFTEHRVLSRDVRIVLEGVDKFNNLIGSVHYSDGEtvkDLGLELVENGLAKFVEWSANMMEEeaKKKLKAAELQC 354
Cdd:cd00175  45 GEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTVYLNGGE---NIAEELVKEGLARVYRYYPDDSEY--YDELLEAEEAA 119

                       170
                ....*....|
gi 22326646 355 KKDKVKMWAN 364
Cdd:cd00175 120 KKARKGLWSD 129
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 595-712 1.92e-20

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: 88.10  E-value: 1.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 595 YVLSGHRFKLYIPKiTCSIAFSFSGVRCP----------GRGEPYSEEAISVMRRRIMQRDVEIEVETVDRTGTFLGSMW 664
Cdd:cd00175   1 RVIDGDTIRVRLPP-GPLITVRLSGIDAPetarpnkgksETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTVY 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 22326646 665 -ESRTNVATVLLEAGLAKMQTSFGADRIAEAHLLEqAERSAKNQKLKIW 712
Cdd:cd00175  80 lNGGENIAEELVKEGLARVYRYYPDDSEYYDELLE-AEEAAKKARKGLW 127
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 40-151 5.01e-15

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


Pssm-ID: 395448  Cd Length: 106  Bit Score: 71.97  E-value: 5.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    40 TITFSSLMAPKMARRGGIDEPFAWESKEFLRKLCIGKEVA---FKVDYKveaiaGREFGSVFLGNENLAKLVVKTGWAKV 116
Cdd:pfam00565   1 RVRLVGIDAPETAKPNTPVQPFGKEAKEFLKKLVLGKKVVvleFDKDKY-----GRTLGYVYLNGKNINEELVKEGLAWV 75

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 22326646   117 REpgqqNQDKVSPYIKELLQLEELAKQEGYGRWSK 151
Cdd:pfam00565  76 YK----AYPPNFKHYDELLAAEEEAKKKKKGLWSD 106
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 615-714 8.55e-15

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


Pssm-ID: 395448  Cd Length: 106  Bit Score: 71.20  E-value: 8.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646   615 FSFSGVRCP------GRGEPYSEEAISVMRRRIMQRDVEIEVETVDRTGTFLGSMWESRTNVATVLLEAGLAKMQTSFGa 688
Cdd:pfam00565   2 VRLVGIDAPetakpnTPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYLNGKNINEELVKEGLAWVYKAYP- 80

                          90       100
                  ....*....|....*....|....*.
gi 22326646   689 DRIAEAHLLEQAERSAKNQKLKIWEN 714
Cdd:pfam00565  81 PNFKHYDELLAAEEEAKKKKKGLWSD 106
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
1-151 1.99e-13

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 68.94  E-value: 1.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646   1 MATGAENQWLKGRVKAVTSGDCLVITALSHnragpppEKTITFSSLMAPKMARRGGIDEPFAWESKEFLRKLCIGKEVAF 80
Cdd:COG1525  15 LAAAAAAATLTAGVVRVIDGDTLRVRDDGK-------GERVRLAGIDAPELGQPCGPEQPCGEEARQALRALLAGKTVTL 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22326646  81 KVDYKVEAiAGREFGSVFLGNENLAKLVVKTGWAKVREPGQQNqdkvsPYIKELLQLEELAKQEGYGRWSK 151
Cdd:COG1525  88 EPDEGRDR-YGRLLAYVYVDGRDLNEELVREGLAWAYRRYSPD-----KYADRYLAAEAEARAARRGLWSD 152
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 273-364 1.37e-12

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


Pssm-ID: 395448  Cd Length: 106  Bit Score: 65.04  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646   273 PFATEAKYFTEHRVLSRDVRIVLEGVDKFNNLIGSVhYSDGetvKDLGLELVENGLAKFVE-WSANmmeEEAKKKLKAAE 351
Cdd:pfam00565  21 PFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYV-YLNG---KNINEELVKEGLAWVYKaYPPN---FKHYDELLAAE 93

                          90
                  ....*....|...
gi 22326646   352 LQCKKDKVKMWAN 364
Cdd:pfam00565  94 EEAKKKKKGLWSD 106
SNc smart00318
Staphylococcal nuclease homologues;
378-556 9.68e-12

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 63.43  E-value: 9.68e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    378 QNFTGKVVEVVSGDCLIVaddavpFGSPAAERRVCLSSIRSP--KMGNPRREEKPAPYAREAREFLRQRLIGKQVIVQME 455
Cdd:smart00318   1 KEIRGVVERVIDGDTIRV------RLPKGPLITIRLSGIDAPetARPNKGDGTPDEPFGEEAKEFLKKLLLGKKVQVEVD 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    456 YSRKvtqgdgpttsgaADRFMdfGSVFLPSaakadsdevtappaaaiagsqpvGVNIAELVLVRGFGNVVRHRDFEErsN 535
Cdd:smart00318  75 SKDR------------YGRFL--GTVYLNG-----------------------GNNIAEELVKEGLAKVYRYADKDE--Y 115

                          170       180
                   ....*....|....*....|.
gi 22326646    536 HYDALLAAEARALAGKKGIHS 556
Cdd:smart00318 116 VYDELLEAEEAAKKARKGLWS 136
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 387-556 9.93e-12

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: 63.06  E-value: 9.93e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 387 VVSGDCLIVaddavpFGSPAAERRVCLSSIRSP--KMGNPRREEKPAPYAREAREFLRQRLIGKQVIVQMEYSRKvtqgd 464
Cdd:cd00175   2 VIDGDTIRV------RLPPGPLITVRLSGIDAPetARPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDR----- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 465 gpttsgaADRFMdfGSVFLPSAAkadsdevtappaaaiagsqpvgvNIAELVLVRGFGNVVRHRDFeeRSNHYDALLAAE 544
Cdd:cd00175  71 -------YGRTL--GTVYLNGGE-----------------------NIAEELVKEGLARVYRYYPD--DSEYYDELLEAE 116

                       170
                ....*....|..
gi 22326646 545 ARALAGKKGIHS 556
Cdd:cd00175 117 EAAKKARKGLWS 128
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 783-842 3.79e-11

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: 59.21  E-value: 3.79e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    783 PKRGDIVLAQFSlDNSWNRAMIVTapraavQSPDEKFEVFYIDYGNQETVPYSAIRPIDP 842
Cdd:smart00333   3 FKVGDKVAARWE-DGEWYRARIVK------VDGEQLYEVFFIDYGNEEVVPPSDLRQLPE 55
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
589-712 3.56e-08

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 53.91  E-value: 3.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 589 IPAVVEYVLSGHRFKLYIPKITcsIAFSFSGVRCP------GRGEPYSEEAISVMRRRIMQRDVEIEV-ETVDRTGTFLG 661
Cdd:COG1525  24 LTAGVVRVIDGDTLRVRDDGKG--ERVRLAGIDAPelgqpcGPEQPCGEEARQALRALLAGKTVTLEPdEGRDRYGRLLA 101

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 22326646 662 SMWESRTNVATVLLEAGLAKMQTSFGADRIAEAhlLEQAERSAKNQKLKIW 712
Cdd:COG1525 102 YVYVDGRDLNEELVREGLAWAYRRYSPDKYADR--YLAAEAEARAARRGLW 150
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
176-368 4.15e-08

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 53.53  E-value: 4.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 176 AMGLLAANKGKPMEGIVEQVRDGSTIRVYLLPEFQFVQVfvAGVQAPsmgrrttngsvvetvpdepngdvsaESRGPLTT 255
Cdd:COG1525  12 LAALAAAAAAATLTAGVVRVIDGDTLRVRDDGKGERVRL--AGIDAP-------------------------ELGQPCGP 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 256 AQrlaasaassvevssdPFATEAKYFTEHRVLSRDVRI-VLEGVDKFNNLIGSVhYSDGetvKDLGLELVENGLAKFVEW 334
Cdd:COG1525  65 EQ---------------PCGEEARQALRALLAGKTVTLePDEGRDRYGRLLAYV-YVDG---RDLNEELVREGLAWAYRR 125

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 22326646 335 SANmmeEEAKKKLKAAELQCKKDKVKMWA--NYVPP 368
Cdd:COG1525 126 YSP---DKYADRYLAAEAEARAARRGLWSdaFPVPP 158
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
380-453 8.10e-08

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 52.76  E-value: 8.10e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22326646 380 FTGKVVEVVSGDCLIVADDAVpfgspaaERRVCLSSIRSPKMGNPRREEKPapYAREAREFLRQRLIGKQVIVQ 453
Cdd:COG1525  24 LTAGVVRVIDGDTLRVRDDGK-------GERVRLAGIDAPELGQPCGPEQP--CGEEARQALRALLAGKTVTLE 88
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 860-968 4.64e-07

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: 49.24  E-value: 4.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646   860 KVPSLEDDFGPEAGEYLHTVTLGsgKEFKAVIEERDTSGGkvkgqgtgteFVVTLIAvdDEISVNAAMLQEGIARMEKRq 939
Cdd:pfam00565  14 KPNTPVQPFGKEAKEFLKKLVLG--KKVVVLEFDKDKYGR----------TLGYVYL--NGKNINEELVKEGLAWVYKA- 78

                          90       100
                  ....*....|....*....|....*....
gi 22326646   940 kwgHKGKQAALDALEKFQEEARKSRIGIW 968
Cdd:pfam00565  79 ---YPPNFKHYDELLAAEEEAKKKKKGLW 104
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 822-968 5.21e-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: 43.80  E-value: 5.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 822 FYIDYGNQETVPYSAIRpidpsvsaAPGLAQLCRLAyikvPSLEDDFGPEAGEYLHTVTLGsgKEFKAVIEERDTSGGkv 901
Cdd:cd00175  10 VRLPPGPLITVRLSGID--------APETARPNKGK----SETDEPFGEEAKEFLKKLLLG--KKVQVEVDSKDRYGR-- 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22326646 902 kgqgtgteFVVTLIaVDDEISVNAAMLQEGIARMEKrqkwGHKGKQAALDALEKFQEEARKSRIGIW 968
Cdd:cd00175  74 --------TLGTVY-LNGGENIAEELVKEGLARVYR----YYPDDSEYYDELLEAEEAAKKARKGLW 127
SNc smart00318
Staphylococcal nuclease homologues;
855-968 2.37e-04

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 42.25  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    855 RLAYIKVPSLEDD----------FGPEAGEYLHTVTLGsgKEFKAVIEERDTSGGkvkgqgtgteFVVTLIaVDDEISVN 924
Cdd:smart00318  29 RLSGIDAPETARPnkgdgtpdepFGEEAKEFLKKLLLG--KKVQVEVDSKDRYGR----------FLGTVY-LNGGNNIA 95

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 22326646    925 AAMLQEGIARMekRQKWGHKGKQAalDALEKFQEEARKSRIGIW 968
Cdd:smart00318  96 EELVKEGLAKV--YRYADKDEYVY--DELLEAEEAAKKARKGLW 135
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
855-969 1.16e-03

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 40.82  E-value: 1.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 855 RLAYIKVPSL------EDDFGPEAGEYL------HTVTLgsgkefkAVIEERDTSGGkvkgqgtgtefVVTLIAVDDEiS 922
Cdd:COG1525  49 RLAGIDAPELgqpcgpEQPCGEEARQALrallagKTVTL-------EPDEGRDRYGR-----------LLAYVYVDGR-D 109

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 22326646 923 VNAAMLQEGIARMekrqkWGHKGKQAALDALEKFQEEARKSRIGIWQ 969
Cdd:COG1525 110 LNEELVREGLAWA-----YRRYSPDKYADRYLAAEAEARAARRGLWS 151
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 410-452 1.16e-03

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


Pssm-ID: 395448  Cd Length: 106  Bit Score: 39.61  E-value: 1.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 22326646   410 RVCLSSIRSPKMGNPRREEKPapYAREAREFLRQRLIGKQVIV 452
Cdd:pfam00565   1 RVRLVGIDAPETAKPNTPVQP--FGKEAKEFLKKLVLGKKVVV 41
 
Name Accession Description Interval E-value
Tudor_AtTudor1-like cd20443
Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor ...
 747-862 4.19e-69

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: 225.42  E-value: 4.19e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 747 GGRFYVQSAGDQKIASIQNQLASLSIKDAPII-GSFNPKRGDIVLAQFSLDNSWNRAMIVTAPRAAVQSPDEKFEVFYID 825
Cdd:cd20443   1 GGRFYVQVVSDQRLSSIQQQLEGLSLKDKANPpGGFNPKKGELVLAQFSADNSWNRAMVVNAPRQGTQSPKDEYEVFYID 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 22326646 826 YGNQETVPYSAIRPIDPSVSAAPGLAQLCRLAYIKVP 862
Cdd:cd20443  81 YGNQETVPLSALRPLDPSVSSAPGLAQLCSLAHIKVP 117
TUDOR pfam00567
Tudor domain;
735-857 2.88e-24

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 98.58  E-value: 2.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646   735 ETLKVVVTEVLGGGRFYVQS-AGDQKIASIQNQLasLSIKDAPIIGSFNPKRGDIVLAQFSLDNSWNRAMIvtapraAVQ 813
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQPkSDSKKLEKLTEEL--QEYYASKPPESLPPAVGDGCVAAFSEDGKWYRAKI------TES 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 22326646   814 SPDEKFEVFYIDYGNQETVPYSAIRPIDPSVSAAPGLAQLCRLA 857
Cdd:pfam00567  73 LDDGLVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 37-151 1.29e-22

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: 94.26  E-value: 1.29e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646  37 PEKTITFSSLMAPKMARRG----GIDEPFAWESKEFLRKLCIGKEVAFKVDYKveAIAGREFGSVFLGN-ENLAKLVVKT 111
Cdd:cd00175  16 PLITVRLSGIDAPETARPNkgksETDEPFGEEAKEFLKKLLLGKKVQVEVDSK--DRYGRTLGTVYLNGgENIAEELVKE 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 22326646 112 GWAKVREpgqqNQDKVSPYIKELLQLEELAKQEGYGRWSK 151
Cdd:cd00175  94 GLARVYR----YYPDDSEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
587-712 1.39e-22

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 94.64  E-value: 1.39e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    587 RRIPAVVEYVLSGHRFKLYIPKiTCSIAFSFSGVRCP----------GRGEPYSEEAISVMRRRIMQRDVEIEVETVDRT 656
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPK-GPLITIRLSGIDAPetarpnkgdgTPDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 22326646    657 GTFLGSMWESRT-NVATVLLEAGLAKMQTSFGADRIAEAHLLEqAERSAKNQKLKIW 712
Cdd:smart00318  80 GRFLGTVYLNGGnNIAEELVKEGLAKVYRYADKDEYVYDELLE-AEEAAKKARKGLW 135
SNc smart00318
Staphylococcal nuclease homologues;
186-364 1.59e-22

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 94.25  E-value: 1.59e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    186 KPMEGIVEQVRDGSTIRVYLLPEfQFVQVFVAGVQAPSMGRRTTngsvvetvpdepngdvsaesrGPLTTAQrlaasaas 265
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG-PLITIRLSGIDAPETARPNK---------------------GDGTPDE-------- 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    266 svevssdPFATEAKYFTEHRVLSRDVRIVLEGVDKFNNLIGSVHYSDGEtvkDLGLELVENGLAKFVEWSANMmeEEAKK 345
Cdd:smart00318  51 -------PFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRFLGTVYLNGGN---NIAEELVKEGLAKVYRYADKD--EYVYD 118

                          170
                   ....*....|....*....
gi 22326646    346 KLKAAELQCKKDKVKMWAN 364
Cdd:smart00318 119 ELLEAEEAAKKARKGLWSD 137
SNc smart00318
Staphylococcal nuclease homologues;
10-150 9.62e-22

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 91.94  E-value: 9.62e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646     10 LKGRVKAVTSGDCLVItalshnRAGPPPEKTITFSSLMAPKMARRG----GIDEPFAWESKEFLRKLCIGKEVAFKVDYK 85
Cdd:smart00318   3 IRGVVERVIDGDTIRV------RLPKGPLITIRLSGIDAPETARPNkgdgTPDEPFGEEAKEFLKKLLLGKKVQVEVDSK 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22326646     86 veAIAGREFGSVFLGNE-NLAKLVVKTGWAKVREpgqqNQDKVSPYIKELLQLEELAKQEGYGRWS 150
Cdd:smart00318  77 --DRYGRFLGTVYLNGGnNIAEELVKEGLAKVYR----YADKDEYVYDELLEAEEAAKKARKGLWS 136
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 739-872 3.59e-21

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: 90.12  E-value: 3.59e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 739 VVVTEVLGGGRFYVQSAGDQKI-------ASIQNQLASLSIKDapiigSFNPKRGDIVLAQFSLDNSWNRAMIVTapraa 811
Cdd:cd20408   1 GTVTEFKNPGEFYIQIYTLEVLeslvkltSQLKKTYASVNNHK-----EYIPEVGEVCVAKYSEDQNWYRALVQT----- 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22326646 812 VQSPDEKFEVFYIDYGNQETVPYSAIRPIDPSVSAAPGLAQLCRLAyiKVPSLEDDFGPEA 872
Cdd:cd20408  71 VDVQQKKAGVFYIDYGNEETVPLNRIQPLKKDIELFPPCAIKCCLA--NVKPPSGSWSEEC 129
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 195-364 1.37e-20

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: 88.49  E-value: 1.37e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 195 VRDGSTIRVYLLPEfQFVQVFVAGVQAPsmgrRTTNGSVVETVPDEPngdvsaesrgplttaqrlaasaassvevssdpF 274
Cdd:cd00175   2 VIDGDTIRVRLPPG-PLITVRLSGIDAP----ETARPNKGKSETDEP--------------------------------F 44

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 275 ATEAKYFTEHRVLSRDVRIVLEGVDKFNNLIGSVHYSDGEtvkDLGLELVENGLAKFVEWSANMMEEeaKKKLKAAELQC 354
Cdd:cd00175  45 GEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTVYLNGGE---NIAEELVKEGLARVYRYYPDDSEY--YDELLEAEEAA 119

                       170
                ....*....|
gi 22326646 355 KKDKVKMWAN 364
Cdd:cd00175 120 KKARKGLWSD 129
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 595-712 1.92e-20

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: 88.10  E-value: 1.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 595 YVLSGHRFKLYIPKiTCSIAFSFSGVRCP----------GRGEPYSEEAISVMRRRIMQRDVEIEVETVDRTGTFLGSMW 664
Cdd:cd00175   1 RVIDGDTIRVRLPP-GPLITVRLSGIDAPetarpnkgksETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTLGTVY 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 22326646 665 -ESRTNVATVLLEAGLAKMQTSFGADRIAEAHLLEqAERSAKNQKLKIW 712
Cdd:cd00175  80 lNGGENIAEELVKEGLARVYRYYPDDSEYYDELLE-AEEAAKKARKGLW 127
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
 759-845 5.57e-19

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: 82.35  E-value: 5.57e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 759 KIASIQNQLASLSIKDAPIIGSFNPKRGDIVLAQFSLDNSWNRAMIVTApraavqSPDEKFEVFYIDYGNQETVPYSAIR 838
Cdd:cd20433   4 QLEKLMEKLRFEIASNPPLPGSYTPRKGDLCAAKFVEDGEWYRAKVEKV------EGDKKVHVLYIDYGNREVLPSTRLA 77


                ....*..
gi 22326646 839 PIDPSVS 845
Cdd:cd20433  78 ALPPAFS 84
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 40-151 5.01e-15

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


Pssm-ID: 395448  Cd Length: 106  Bit Score: 71.97  E-value: 5.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    40 TITFSSLMAPKMARRGGIDEPFAWESKEFLRKLCIGKEVA---FKVDYKveaiaGREFGSVFLGNENLAKLVVKTGWAKV 116
Cdd:pfam00565   1 RVRLVGIDAPETAKPNTPVQPFGKEAKEFLKKLVLGKKVVvleFDKDKY-----GRTLGYVYLNGKNINEELVKEGLAWV 75

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 22326646   117 REpgqqNQDKVSPYIKELLQLEELAKQEGYGRWSK 151
Cdd:pfam00565  76 YK----AYPPNFKHYDELLAAEEEAKKKKKGLWSD 106
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 615-714 8.55e-15

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


Pssm-ID: 395448  Cd Length: 106  Bit Score: 71.20  E-value: 8.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646   615 FSFSGVRCP------GRGEPYSEEAISVMRRRIMQRDVEIEVETVDRTGTFLGSMWESRTNVATVLLEAGLAKMQTSFGa 688
Cdd:pfam00565   2 VRLVGIDAPetakpnTPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYVYLNGKNINEELVKEGLAWVYKAYP- 80

                          90       100
                  ....*....|....*....|....*.
gi 22326646   689 DRIAEAHLLEQAERSAKNQKLKIWEN 714
Cdd:pfam00565  81 PNFKHYDELLAAEEEAKKKKKGLWSD 106
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 786-840 9.15e-14

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


Pssm-ID: 410450  Cd Length: 50  Bit Score: 66.38  E-value: 9.15e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 22326646 786 GDIVLAQFSLDNSWNRAMIVTapraavQSPDEKFEVFYIDYGNQETVPYSAIRPI 840
Cdd:cd20379   2 GDLCAAKYEEDGKWYRARVLE------VLSNDKVEVFFVDYGNTETVPLSDLRPL 50
Tudor_TDRD1_rpt2 cd20409
second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 762-844 1.53e-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: 66.71  E-value: 1.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 762 SIQNQLASLS--IKDAPIIGSFNPKRGDIVLAQFSLDNSWNRAMIVTapraavQSPDEKFEVFYIDYGNQETVPYSAIRP 839
Cdd:cd20409   3 QLAELQESLSayCKVAPASSDFSPAVGEVCCAQFTEDNQWYRASVLA------YSSEDSVLVGYIDFGNSEEVALSRLRP 76


                ....*
gi 22326646 840 IDPSV 844
Cdd:cd20409  77 IPPSL 81
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
1-151 1.99e-13

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 68.94  E-value: 1.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646   1 MATGAENQWLKGRVKAVTSGDCLVITALSHnragpppEKTITFSSLMAPKMARRGGIDEPFAWESKEFLRKLCIGKEVAF 80
Cdd:COG1525  15 LAAAAAAATLTAGVVRVIDGDTLRVRDDGK-------GERVRLAGIDAPELGQPCGPEQPCGEEARQALRALLAGKTVTL 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22326646  81 KVDYKVEAiAGREFGSVFLGNENLAKLVVKTGWAKVREPGQQNqdkvsPYIKELLQLEELAKQEGYGRWSK 151
Cdd:COG1525  88 EPDEGRDR-YGRLLAYVYVDGRDLNEELVREGLAWAYRRYSPD-----KYADRYLAAEAEARAARRGLWSD 152
Tudor_TDRD1_rpt4 cd20411
fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 739-857 2.59e-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: 67.47  E-value: 2.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 739 VVVTEVLGGGRFYV----QSAGDQKIASIQNQLASLSIKdAPIIGSFNPKRGDIVLAQFSLDNSWNRAMIVTAPRAAVQs 814
Cdd:cd20411   1 ALVLEVISPDLFYAlpktGQVNVEKLKALMTELAEYCSK-QSVPQQFRPRIGDACCARFTGDKNWYRAVVLETSDSEVK- 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 22326646 815 pdekfeVFYIDYGNQETVPYSAIRPIDPSVSAAPGLAQLCRLA 857
Cdd:cd20411  79 ------VLYADYGNTETLPLSRILPITKSHLELPFQIIRCSLA 115
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 273-364 1.37e-12

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


Pssm-ID: 395448  Cd Length: 106  Bit Score: 65.04  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646   273 PFATEAKYFTEHRVLSRDVRIVLEGVDKFNNLIGSVhYSDGetvKDLGLELVENGLAKFVE-WSANmmeEEAKKKLKAAE 351
Cdd:pfam00565  21 PFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYV-YLNG---KNINEELVKEGLAWVYKaYPPN---FKHYDELLAAE 93

                          90
                  ....*....|...
gi 22326646   352 LQCKKDKVKMWAN 364
Cdd:pfam00565  94 EEAKKKKKGLWSD 106
SNc smart00318
Staphylococcal nuclease homologues;
378-556 9.68e-12

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 63.43  E-value: 9.68e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    378 QNFTGKVVEVVSGDCLIVaddavpFGSPAAERRVCLSSIRSP--KMGNPRREEKPAPYAREAREFLRQRLIGKQVIVQME 455
Cdd:smart00318   1 KEIRGVVERVIDGDTIRV------RLPKGPLITIRLSGIDAPetARPNKGDGTPDEPFGEEAKEFLKKLLLGKKVQVEVD 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    456 YSRKvtqgdgpttsgaADRFMdfGSVFLPSaakadsdevtappaaaiagsqpvGVNIAELVLVRGFGNVVRHRDFEErsN 535
Cdd:smart00318  75 SKDR------------YGRFL--GTVYLNG-----------------------GNNIAEELVKEGLAKVYRYADKDE--Y 115

                          170       180
                   ....*....|....*....|.
gi 22326646    536 HYDALLAAEARALAGKKGIHS 556
Cdd:smart00318 116 VYDELLEAEEAAKKARKGLWS 136
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 387-556 9.93e-12

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: 63.06  E-value: 9.93e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 387 VVSGDCLIVaddavpFGSPAAERRVCLSSIRSP--KMGNPRREEKPAPYAREAREFLRQRLIGKQVIVQMEYSRKvtqgd 464
Cdd:cd00175   2 VIDGDTIRV------RLPPGPLITVRLSGIDAPetARPNKGKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDR----- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 465 gpttsgaADRFMdfGSVFLPSAAkadsdevtappaaaiagsqpvgvNIAELVLVRGFGNVVRHRDFeeRSNHYDALLAAE 544
Cdd:cd00175  71 -------YGRTL--GTVYLNGGE-----------------------NIAEELVKEGLARVYRYYPD--DSEYYDELLEAE 116

                       170
                ....*....|..
gi 22326646 545 ARALAGKKGIHS 556
Cdd:cd00175 117 EAAKKARKGLWS 128
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 783-842 3.79e-11

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: 59.21  E-value: 3.79e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    783 PKRGDIVLAQFSlDNSWNRAMIVTapraavQSPDEKFEVFYIDYGNQETVPYSAIRPIDP 842
Cdd:smart00333   3 FKVGDKVAARWE-DGEWYRARIVK------VDGEQLYEVFFIDYGNEEVVPPSDLRQLPE 55
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 783-860 1.03e-09

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: 56.29  E-value: 1.03e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22326646 783 PKRGDIVLAQFSlDNSWNRAMIVTAPRAavqspdEKFEVFYIDYGNQETVPYSAIRPIDPSVSAAPGLAQLCRLAYIK 860
Cdd:cd20415  25 PVQGQACVALFE-DGAWYRARIIGLPGH------REVEVKYVDFGNTATVTIKHVRKIKDDFLSLPEKARECRLAFIE 95
Tudor_TDRD6_rpt6 cd20425
sixth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 750-856 2.01e-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: 56.31  E-value: 2.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 750 FYVQSAGDQ-KIASIQNQLASLSIKDAPIIG-SFNpkRGDIVLAQFSLDNSWNRAMIVTapraavQSPDEKFEVFYIDYG 827
Cdd:cd20425  15 FYVQLAQDEdELSMISEKLNASKANDEEVECeSLQ--LGDLICAEYPEDGLWYRAVVKE------KIPNNLVSVQFIDYG 86

                        90       100
                ....*....|....*....|....*....
gi 22326646 828 NQETVPYSAIRPIDPSVSAAPGLAQLCRL 856
Cdd:cd20425  87 NTSVVQPSKIHRLPKELLSIPALSIHCFL 115
Tudor_TDRD15_rpt6 cd20441
sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 748-857 3.74e-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: 3.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 748 GRFYVQSAGDQK-IASIQNQLASLSIKDAPIIGSfNPKRGDIVLAQFSLDNSWNRAMIVTApraavqSPDEKFEVFYIDY 826
Cdd:cd20441   3 SRFFIQLSEDEKvILQLAEELNETSEKSRENAAV-KLKVGDLVAAEYDEDLALYRAVITAV------LPGKSFKVEFIDY 75

                        90       100       110
                ....*....|....*....|....*....|.
gi 22326646 827 GNQETVPYSAIRPIDPSVSAAPGLAQLCRLA 857
Cdd:cd20441  76 GNTAVVDKSNIYTLQEKFLSLPRLSIPCSLS 106
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 788-856 2.05e-08

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


Pssm-ID: 410494  Cd Length: 80  Bit Score: 52.10  E-value: 2.05e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22326646 788 IVLAQFSLDNSWNRAMIVTapraaVQSPDEKFEVFYIDYGNQETVPYSAIRPIDPSVSAAPGLAQLCRL 856
Cdd:cd20423   8 VCLAKYSEDGKWCRALIDN-----VYEPVEMVEVTYVDYGNKELVSLKNLRSISEEFLKLKAQAFRCSL 71
Tudor_TDRD1_rpt3 cd20410
third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 781-843 2.48e-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: 51.19  E-value: 2.48e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22326646 781 FNPKRGDIVLAQFSLDNSWNRAMIVTapraavQSPDEKFEVFYIDYGNQETVPYSAIRPIDPS 843
Cdd:cd20410   1 FKPIVGEPCCAFFSGDGNWYRAMVKE------ILPGGAVKVHFVDYGNVEEVTLDKLRKITST 57
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
589-712 3.56e-08

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 53.91  E-value: 3.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 589 IPAVVEYVLSGHRFKLYIPKITcsIAFSFSGVRCP------GRGEPYSEEAISVMRRRIMQRDVEIEV-ETVDRTGTFLG 661
Cdd:COG1525  24 LTAGVVRVIDGDTLRVRDDGKG--ERVRLAGIDAPelgqpcGPEQPCGEEARQALRALLAGKTVTLEPdEGRDRYGRLLA 101

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 22326646 662 SMWESRTNVATVLLEAGLAKMQTSFGADRIAEAhlLEQAERSAKNQKLKIW 712
Cdd:COG1525 102 YVYVDGRDLNEELVREGLAWAYRRYSPDKYADR--YLAAEAEARAARRGLW 150
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
176-368 4.15e-08

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 53.53  E-value: 4.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 176 AMGLLAANKGKPMEGIVEQVRDGSTIRVYLLPEFQFVQVfvAGVQAPsmgrrttngsvvetvpdepngdvsaESRGPLTT 255
Cdd:COG1525  12 LAALAAAAAAATLTAGVVRVIDGDTLRVRDDGKGERVRL--AGIDAP-------------------------ELGQPCGP 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 256 AQrlaasaassvevssdPFATEAKYFTEHRVLSRDVRI-VLEGVDKFNNLIGSVhYSDGetvKDLGLELVENGLAKFVEW 334
Cdd:COG1525  65 EQ---------------PCGEEARQALRALLAGKTVTLePDEGRDRYGRLLAYV-YVDG---RDLNEELVREGLAWAYRR 125

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 22326646 335 SANmmeEEAKKKLKAAELQCKKDKVKMWA--NYVPP 368
Cdd:COG1525 126 YSP---DKYADRYLAAEAEARAARRGLWSdaFPVPP 158
Tudor_TDRD15_rpt3 cd20438
third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 782-859 5.85e-08

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: 52.86  E-value: 5.85e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22326646 782 NPKRGDIVLAQFSLDNSWNRAMIVtapraavQSPDEKFEVFYIDYGNQETVPYSAIRPIDPSVSAAPGLAQLCRLAYI 859
Cdd:cd20438  54 KPEPGLLCCARYSKDRHYYRAVIT-------EVLDLKVSVYFLDFGNTDTVPFYDVKTLLPEFSELPALAMCCSLAHV 124
Tudor_TDRD15_rpt2 cd20437
second Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 736-857 7.52e-08

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: 51.65  E-value: 7.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 736 TLKVVVTEVLGGGRFYVQ-SAGDQKIASIQNQLA----SLSIKDAPIIGSFnpkrgDIVLAQFSLDNSWNRAMIVTAPra 810
Cdd:cd20437   4 TEKVKITAAVSPSKFYCQlLSWEPELSKLTTQMTlhyeSVSKELNPSCENF-----GLLCAAKGKDGQWHRGFLQQLL-- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 22326646 811 avqsPDEKFEVFYIDYGNQETVPYSAIRPIDPSVSAAPGLAQLCRLA 857
Cdd:cd20437  77 ----PPSQVKVWFIDYGNSEAVSSHSVLKLPPDFFSLPLMSFPCSLS 119
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
380-453 8.10e-08

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 52.76  E-value: 8.10e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22326646 380 FTGKVVEVVSGDCLIVADDAVpfgspaaERRVCLSSIRSPKMGNPRREEKPapYAREAREFLRQRLIGKQVIVQ 453
Cdd:COG1525  24 LTAGVVRVIDGDTLRVRDDGK-------GERVRLAGIDAPELGQPCGPEQP--CGEEARQALRALLAGKTVTLE 88
Tudor_TDRD8 cd20430
Tudor domain found in Tudor domain-containing protein 8 (TDRD8) and similar proteins; TDRD8, ...
 765-837 1.65e-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: 49.60  E-value: 1.65e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22326646 765 NQLASLSIKDAPIIGsfNPKRGDIVLAQFSLDNSWNRAmivtapraAVQS--PDEKFEVFYIDYGNQETVPYSAI 837
Cdd:cd20430   3 DELAEVCPTAPPLFG--TPDPNKIYGGKFSEDNCWYRC--------KVKSilSDEKCTVQYIDYGNTETVSRSSI 67
Tudor_TDRD6_rpt5 cd20424
fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 739-843 4.34e-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: 49.81  E-value: 4.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 739 VVVTEVLGGGRFYVQSAGDQKI-ASIQNQLASLSIKDAPIIGSFNPkrGDIVLAQFSlDNSWNRAMIVTAPraavqspdE 817
Cdd:cd20424  16 VYITYVNDPWTFYCQLARNAGVlDQLASAISRLSSEIRKLELSVNP--GTLCLAKYS-DQHWYRGIIITNK--------N 84

                        90       100
                ....*....|....*....|....*.
gi 22326646 818 KFEVFYIDYGNQETVPYSAIRPIdPS 843
Cdd:cd20424  85 STEVFFVDYGNTEKVEKEDMLPI-PS 109
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 860-968 4.64e-07

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: 49.24  E-value: 4.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646   860 KVPSLEDDFGPEAGEYLHTVTLGsgKEFKAVIEERDTSGGkvkgqgtgteFVVTLIAvdDEISVNAAMLQEGIARMEKRq 939
Cdd:pfam00565  14 KPNTPVQPFGKEAKEFLKKLVLG--KKVVVLEFDKDKYGR----------TLGYVYL--NGKNINEELVKEGLAWVYKA- 78

                          90       100
                  ....*....|....*....|....*....
gi 22326646   940 kwgHKGKQAALDALEKFQEEARKSRIGIW 968
Cdd:pfam00565  79 ---YPPNFKHYDELLAAEEEAKKKKKGLW 104
Tudor_TDRD15_rpt7 cd20442
seventh Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 734-857 2.81e-06

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: 48.11  E-value: 2.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 734 KETLKVVVTEVLGGGRFYVQSAGDQKIASIQNQLASLSIKDAPIIGSFNPKRGDIVLAQFSLDNSWNRAMIVTApraavQ 813
Cdd:cd20442   1 GQIEKGTLLSVSKNGTFYVRLLRNSEQLTDLESLIAKEAKKCKFVPVEDIKEGLECLAKSKKNLKWYRAVVEHL-----Y 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 22326646 814 SPDEKFEVFYIDYGNQETVPYSAIRPIDPSVSAAPGLAQLCRLA 857
Cdd:cd20442  76 PETEKMLVFFVDHGITEVVSMGNIKQLSNDLLQIPRQAVLCRWN 119
Tudor_vreteno-like_rpt1 cd20444
first Tudor domain found in Drosophila melanogaster protein vreteno and similar proteins; ...
 783-832 4.57e-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: 44.60  E-value: 4.57e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 22326646 783 PKRGDIVLAQFslDNSWNRAMIVTapraaVQSPDEKFEVFYIDYGNQETV 832
Cdd:cd20444   1 PTPGQMVIAKF--DGNHYRAIVLR-----VLNPDLKILVRFVDFGNVEVM 43
Tudor_TDRD2 cd20412
Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, ...
 782-840 8.31e-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: 45.36  E-value: 8.31e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 22326646 782 NPKRGDIVLAQFSLDNSWNRAMIVTapraavQSPDEKFEVFYIDYGNQETVPYSAIRPI 840
Cdd:cd20412  28 TVQVGDIVAAPFRHDGSWYRARVLG------FLENGNLDLYFVDYGDSGYVPLEDLRAL 80
Tudor_TDRD6_rpt7 cd20426
seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 752-857 3.65e-05

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: 44.80  E-value: 3.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 752 VQSAGDQKIASiQNQLASLSIKDAPIIgsfnpkrgdivlaQFSLDNSWNRAMIVtapraavQSPDEKFEVFYIDYGNQET 831
Cdd:cd20426  30 VQEAGEQVADR-GNFIPSIYVGDPCIV-------------KYSEDNHWYRALVT-------KINDNLVSVRFVDYGNEED 88

                        90       100
                ....*....|....*....|....*.
gi 22326646 832 VPYSAIRPIDPSVSAAPGLAQLCRLA 857
Cdd:cd20426  89 VVREQVRALPSELLKIPVQAFPCCLS 114
Tudor_SMN_SPF30-like cd21182
Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing ...
 786-840 3.73e-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: 41.85  E-value: 3.73e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 22326646 786 GDIVLAQFSLDNSWNRAMIVtapraAVQSPDEKFEVFYIDYGNQETVPYSAIRPI 840
Cdd:cd21182   1 GDKCLAPYSDDGKYYEATIE-----EITEESDTATVVFDGYGNSEEVPLSDLKPL 50
Tudor_TDRD15_rpt5 cd20440
fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 738-840 4.81e-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: 43.98  E-value: 4.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 738 KVVVTEVLGGGRFYVQSAGDQKIasiqnqLASLSIKDAPIIGSFNPKRGD-----IVLAQFSLDNSWNRAMIVTapraaV 812
Cdd:cd20440  13 EVYITHVYSPAKFYCQLDRNTEI------LEALMEKIAEISKLFNSQILDncktrLCLAKYFEDGQWYRALAHP-----V 81

                        90       100
                ....*....|....*....|....*...
gi 22326646 813 QSPDEkFEVFYIDYGNQETVPYSAIRPI 840
Cdd:cd20440  82 ESSSH-LSVYFVDYGNKQIVEKNEVLPI 108
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
 822-968 5.21e-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: 43.80  E-value: 5.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 822 FYIDYGNQETVPYSAIRpidpsvsaAPGLAQLCRLAyikvPSLEDDFGPEAGEYLHTVTLGsgKEFKAVIEERDTSGGkv 901
Cdd:cd00175  10 VRLPPGPLITVRLSGID--------APETARPNKGK----SETDEPFGEEAKEFLKKLLLG--KKVQVEVDSKDRYGR-- 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22326646 902 kgqgtgteFVVTLIaVDDEISVNAAMLQEGIARMEKrqkwGHKGKQAALDALEKFQEEARKSRIGIW 968
Cdd:cd00175  74 --------TLGTVY-LNGGENIAEELVKEGLARVYR----YYPDDSEYYDELLEAEEAAKKARKGLW 127
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
 742-842 2.07e-04

Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is an ATP-dependent DEAD-like RNA helicase required during spermatogenesis. It is involved in the biosynthesis of PIWI-interacting RNAs (piRNAs). A recessive deleterious mutation mutation in TDRD9 causes non-obstructive azoospermia in infertile men. TDRD9 contains an N-terminal HrpA-like RNA helicase module and a Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410502  Cd Length: 101  Bit Score: 41.60  E-value: 2.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 742 TEVLGGGRFYVQSAGD------QKI-ASI-QNQLASLSIKDAPiigsfnpkrGDIVLAQFS--LDNSWNRAMIVTAPRAA 811
Cdd:cd20431   1 TEVVEVGHFWGYRIDEnsseilQQLtAEInQRQLVPLTTKPVP---------NLLCLAPFTdaDMKKYYRAKILYVSGSS 71

                        90       100       110
                ....*....|....*....|....*....|.
gi 22326646 812 VqspdekfEVFYIDYGNQETVPYSAIRPIDP 842
Cdd:cd20431  72 A-------EVFFVDYGNTSQVPSSLLREIPE 95
SNc smart00318
Staphylococcal nuclease homologues;
855-968 2.37e-04

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 42.25  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646    855 RLAYIKVPSLEDD----------FGPEAGEYLHTVTLGsgKEFKAVIEERDTSGGkvkgqgtgteFVVTLIaVDDEISVN 924
Cdd:smart00318  29 RLSGIDAPETARPnkgdgtpdepFGEEAKEFLKKLLLG--KKVQVEVDSKDRYGR----------FLGTVY-LNGGNNIA 95

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 22326646    925 AAMLQEGIARMekRQKWGHKGKQAalDALEKFQEEARKSRIGIW 968
Cdd:smart00318  96 EELVKEGLAKV--YRYADKDEYVY--DELLEAEEAAKKARKGLW 135
Tudor_TDRD6_rpt3 cd20422
third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 783-859 2.69e-04

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: 42.11  E-value: 2.69e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22326646 783 PKRGDIVLAQFSlDNSWNRAMIVtapraAVQspDEKFEVFYIDYGNQETVPYSAIRPIDPSVSAAPGLAQLCRLAYI 859
Cdd:cd20422  50 PQPGQLCCAKWK-EDRYYRAIVT-----AVK--GKMVEVFLVDRGNTEMVDWYDVKKLLPQFRELPALALKCCLADI 118
Tudor_TDRD6_rpt2 cd20421
second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 735-842 2.92e-04

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: 41.64  E-value: 2.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 735 ETLKVVVTEVLGGGRFYVQsagdqkIASIQNQLASLSIKDAPI----IGSFNPKRGDIV---LAQFSLDNSWNRAMIVTa 807
Cdd:cd20421  11 VTETVVVTEVTDPHRIFCQ------LRSLSQELKRLSESMHQYyegrVGSGYETRPEKLgspCAARGSDGRWYRAVLQQ- 83

                        90       100       110
                ....*....|....*....|....*....|....*
gi 22326646 808 praaVQSPDEKFEVFYIDYGNQETVPYSAIRPIDP 842
Cdd:cd20421  84 ----VFSANRVVEVLHVDYGRKEVVSVSNLRYLAP 114
Tudor_SF cd04508
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
 786-839 3.62e-04

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


Pssm-ID: 410449 [Multi-domain]  Cd Length: 47  Bit Score: 39.11  E-value: 3.62e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 22326646 786 GDIVLAQFSLDNSWNRAMIVTapraavQSPDEKFEVFYiDYGNQETVPYSAIRP 839
Cdd:cd04508   1 GDRVEAKWSDDGQWYPATVVA------VNDDGKYTVLF-DDGNEEEVSEDDIRP 47
Tudor_TDRD3 cd20413
Tudor domain found in Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is ...
 784-840 4.05e-04

Tudor domain found in Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is a scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. In the nucleus, it acts as a coactivator; it recognizes and binds asymmetric dimethylation on the core histone tails associated with transcriptional activation (H3R17me2a and H4R3me2a) and recruits proteins at these arginine-methylated loci. In the cytoplasm, it may play a role in the assembly and/or disassembly of mRNA stress granules and in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins. TDRD3 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410484  Cd Length: 53  Bit Score: 39.25  E-value: 4.05e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 22326646 784 KRGDIVLAQFSLDNSWNRAMIvtaprAAVQSPDEKFEVFYIDYGNQETVPYSAIRPI 840
Cdd:cd20413   2 KPGDECLAKYWEDNKFYRAEV-----TAVHPSGKTAVVKFMEYGNYEEVLLSDIKPI 53
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
855-969 1.16e-03

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 40.82  E-value: 1.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 855 RLAYIKVPSL------EDDFGPEAGEYL------HTVTLgsgkefkAVIEERDTSGGkvkgqgtgtefVVTLIAVDDEiS 922
Cdd:COG1525  49 RLAGIDAPELgqpcgpEQPCGEEARQALrallagKTVTL-------EPDEGRDRYGR-----------LLAYVYVDGR-D 109

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 22326646 923 VNAAMLQEGIARMekrqkWGHKGKQAALDALEKFQEEARKSRIGIWQ 969
Cdd:COG1525 110 LNEELVREGLAWA-----YRRYSPDKYADRYLAAEAEARAARRGLWS 151
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
 410-452 1.16e-03

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


Pssm-ID: 395448  Cd Length: 106  Bit Score: 39.61  E-value: 1.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 22326646   410 RVCLSSIRSPKMGNPRREEKPapYAREAREFLRQRLIGKQVIV 452
Cdd:pfam00565   1 RVRLVGIDAPETAKPNTPVQP--FGKEAKEFLKKLVLGKKVVV 41
Tudor_TDRD15_rpt4 cd20439
fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 790-856 1.42e-03

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: 39.78  E-value: 1.42e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22326646 790 LAQFSLDNSWNRAMIVTapraavQSPDEKFEVFYIDYGNQETVPYSAIRPIDPSVSAAPGLAQLCRL 856
Cdd:cd20439  62 VAKYSKDGKWYRAAVLK------QVSAKEVDVIFVDYGNQERVLISDLRAIKPQFLLLEGQAFRCSL 122
Tudor_TDRD10 cd20432
Tudor domain found in Tudor domain-containing protein 10 (TDRD10) and similar proteins; TDRD10 ...
 758-852 1.57e-03

Tudor domain found in Tudor domain-containing protein 10 (TDRD10) and similar proteins; TDRD10 is widely expressed and localized both to the nucleus and cytoplasm, and may play general roles like regulation of RNA metabolism. It contains a Tudor domain and an RNA recognition motif (RRM). 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: 410503  Cd Length: 139  Bit Score: 39.72  E-value: 1.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22326646 758 QKIASIQNQLASLSiKDAPIIGSFNPKRGDIVLAQFSLDN---SWNRAMIV-TAPRAAVqspdekfeVFYIDYGNQETVP 833
Cdd:cd20432  47 QNMQQLFSTLAEVE-SQQPFLAKEDVHRGRRCLAECPLGEeggAWNRCWVLdVVEDFAV--------VFFVDFGSTANIP 117

                        90       100
                ....*....|....*....|
gi 22326646 834 YSAIRPIDPS-VSAAPGLAQ 852
Cdd:cd20432 118 LPSLRSLDEDeFWQIPPLAQ 137
Tudor_SpSPF30-like cd20446
Tudor domain found in Schizosaccharomyces pombe splicing factor spf30 (SpSPF30) and similar ...
 784-840 2.80e-03

Tudor domain found in Schizosaccharomyces pombe splicing factor spf30 (SpSPF30) and similar proteins; SpSPF30, also called survival of motor neuron-related-splicing factor 30, is necessary for spliceosome assembly. 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: 410517  Cd Length: 56  Bit Score: 37.08  E-value: 2.80e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 22326646 784 KRGDIVLAQF-SLDNSWNRAMIvTAPRAAVQSPdeKFEVFYIDYGNQETVPYSAIRPI 840
Cdd:cd20446   2 KPGEVVMARWkSGDGKFYPARI-TSITGSSINP--IYTVKFLDYGEIDTVYLKDIRPL 56
 
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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