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Conserved domains on  [gi|19075617|ref|NP_588117|]
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tudor domain and nuclease, Snd1 [Schizosaccharomyces pombe]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SNc smart00318
Staphylococcal nuclease homologues;
493-626 1.62e-41

Staphylococcal nuclease homologues;


:

Pssm-ID: 214615  Cd Length: 137  Bit Score: 148.56  E-value: 1.62e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617    493 RKLSVIIENVISGSRFRCFCPKeNCYFMFACAGIRTPRTARN---DQEKGEPFAEESLS-LAKSLLQHDAQVEILSVDNN 568
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPK-GPLITIRLSGIDAPETARPnkgDGTPDEPFGEEAKEfLKKLLLGKKVQVEVDSKDRY 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 19075617    569 GCFLGDIYVNHDTNFALKLLSQGLAWCQGYASQSNVQYSQYHDTEAAAKEQKVGMWHD 626
Cdd:smart00318  80 GRFLGTVYLNGGNNIAEELVKEGLAKVYRYADKDEYVYDELLEAEEAAKKARKGLWSD 137
SNc smart00318
Staphylococcal nuclease homologues;
326-463 1.39e-40

Staphylococcal nuclease homologues;


:

Pssm-ID: 214615  Cd Length: 137  Bit Score: 145.87  E-value: 1.39e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617    326 KDYSAVVSRVISTDTLEVRKDNGVECRIQLSSIRHPRPSNEKEA------PYQLEAREFLRKKIIGKRVQVSLDFIRPGQ 399
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKGPLITIRLSGIDAPETARPNKGdgtpdePFGEEAKEFLKKLLLGKKVQVEVDSKDRYG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19075617    400 NDLpainnCTVKLSDGTNVALMVVKSGYATVIRYRMDSVDRspiYDFLIEAEKAAQEGRKGMWS 463
Cdd:smart00318  81 RFL-----GTVYLNGGNNIAEELVKEGLAKVYRYADKDEYV---YDELLEAEEAAKKARKGLWS 136
SNc smart00318
Staphylococcal nuclease homologues;
167-312 3.97e-35

Staphylococcal nuclease homologues;


:

Pssm-ID: 214615  Cd Length: 137  Bit Score: 130.07  E-value: 3.97e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617    167 KKLNGIVETIRNGDQVRVRLflspKQHQLVTISLAGVRCPRSTFTATSPEQTsseQEPCGDEAKQFVVTRLLQRNVVIEL 246
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRL----PKGPLITIRLSGIDAPETARPNKGDGTP---DEPFGEEAKEFLKKLLLGKKVQVEV 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19075617    247 LDLAPNGVsFLGNVLHPAG-NIATFLLSSGLGRVADNHISALGPetMQSLRTIERKAKISRLGIWKN 312
Cdd:smart00318  74 DSKDRYGR-FLGTVYLNGGnNIAEELVKEGLAKVYRYADKDEYV--YDELLEAEEAAKKARKGLWSD 137
SNc smart00318
Staphylococcal nuclease homologues;
3-140 1.11e-27

Staphylococcal nuclease homologues;


:

Pssm-ID: 214615  Cd Length: 137  Bit Score: 108.89  E-value: 1.11e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617      3 QYVSSMIKYAQSGDSFNILIKDNakkiTEKQFSLAYVECPRFRREG------DEPFAFEAQEFSRRLVVGRPASVSTLYv 76
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG----PLITIRLSGIDAPETARPNkgdgtpDEPFGEEAKEFLKKLLLGKKVQVEVDS- 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075617     77 iptsKREYGRIRTSEF-----DLAESLLREGLAKLRPEATRNEGtsensYFVSLEEAQDHAQQYKLGIW 140
Cdd:smart00318  76 ----KDRYGRFLGTVYlnggnNIAEELVKEGLAKVYRYADKDEY-----VYDELLEAEEAAKKARKGLW 135
TUDOR pfam00567
Tudor domain;
649-765 2.41e-23

Tudor domain;


:

Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 95.88  E-value: 2.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617   649 IYLDIVLSDIAEDGKFSFQIIgTGIQQLETLMSDLGSLKKSFKP-SEKINVGMNVAAISALDNAMYRGRVLrCDRENQAA 727
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQPK-SDSKKLEKLTEELQEYYASKPPeSLPPAVGDGCVAAFSEDGKWYRAKIT-ESLDDGLV 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 19075617   728 DVLLYDYGSVEQIPFKNISSLPDTYTKLKPQAQLARLS 765
Cdd:pfam00567  79 EVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
 
Name Accession Description Interval E-value
SNc smart00318
Staphylococcal nuclease homologues;
493-626 1.62e-41

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 148.56  E-value: 1.62e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617    493 RKLSVIIENVISGSRFRCFCPKeNCYFMFACAGIRTPRTARN---DQEKGEPFAEESLS-LAKSLLQHDAQVEILSVDNN 568
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPK-GPLITIRLSGIDAPETARPnkgDGTPDEPFGEEAKEfLKKLLLGKKVQVEVDSKDRY 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 19075617    569 GCFLGDIYVNHDTNFALKLLSQGLAWCQGYASQSNVQYSQYHDTEAAAKEQKVGMWHD 626
Cdd:smart00318  80 GRFLGTVYLNGGNNIAEELVKEGLAKVYRYADKDEYVYDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
502-626 3.45e-41

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


Pssm-ID: 238102  Cd Length: 129  Bit Score: 147.04  E-value: 3.45e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617 502 VISGSRFRCFCPKeNCYFMFACAGIRTPRTARND---QEKGEPFAEESLSLAKSLL-QHDAQVEILSVDNNGCFLGDIYV 577
Cdd:cd00175   2 VIDGDTIRVRLPP-GPLITVRLSGIDAPETARPNkgkSETDEPFGEEAKEFLKKLLlGKKVQVEVDSKDRYGRTLGTVYL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 19075617 578 NHDTNFALKLLSQGLAWCQGYASQSNVQYSQYHDTEAAAKEQKVGMWHD 626
Cdd:cd00175  81 NGGENIAEELVKEGLARVYRYYPDDSEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
326-463 1.39e-40

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 145.87  E-value: 1.39e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617    326 KDYSAVVSRVISTDTLEVRKDNGVECRIQLSSIRHPRPSNEKEA------PYQLEAREFLRKKIIGKRVQVSLDFIRPGQ 399
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKGPLITIRLSGIDAPETARPNKGdgtpdePFGEEAKEFLKKLLLGKKVQVEVDSKDRYG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19075617    400 NDLpainnCTVKLSDGTNVALMVVKSGYATVIRYRMDSVDRspiYDFLIEAEKAAQEGRKGMWS 463
Cdd:smart00318  81 RFL-----GTVYLNGGNNIAEELVKEGLAKVYRYADKDEYV---YDELLEAEEAAKKARKGLWS 136
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
334-463 1.52e-39

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


Pssm-ID: 238102  Cd Length: 129  Bit Score: 142.41  E-value: 1.52e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617 334 RVISTDTLEVRKDNGVECRIQLSSIRHPRPSN------EKEAPYQLEAREFLRKKIIGKRVQVSLDFIRPGQNDLpainn 407
Cdd:cd00175   1 RVIDGDTIRVRLPPGPLITVRLSGIDAPETARpnkgksETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTL----- 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19075617 408 CTVKLSDGTNVALMVVKSGYATVIRYRMDSvdrSPIYDFLIEAEKAAQEGRKGMWS 463
Cdd:cd00175  76 GTVYLNGGENIAEELVKEGLARVYRYYPDD---SEYYDELLEAEEAAKKARKGLWS 128
SNc smart00318
Staphylococcal nuclease homologues;
167-312 3.97e-35

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 130.07  E-value: 3.97e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617    167 KKLNGIVETIRNGDQVRVRLflspKQHQLVTISLAGVRCPRSTFTATSPEQTsseQEPCGDEAKQFVVTRLLQRNVVIEL 246
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRL----PKGPLITIRLSGIDAPETARPNKGDGTP---DEPFGEEAKEFLKKLLLGKKVQVEV 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19075617    247 LDLAPNGVsFLGNVLHPAG-NIATFLLSSGLGRVADNHISALGPetMQSLRTIERKAKISRLGIWKN 312
Cdd:smart00318  74 DSKDRYGR-FLGTVYLNGGnNIAEELVKEGLAKVYRYADKDEYV--YDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
176-312 9.14e-35

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


Pssm-ID: 238102  Cd Length: 129  Bit Score: 128.93  E-value: 9.14e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617 176 IRNGDQVRVRLflsPKQHQlVTISLAGVRCPRSTFTATspeQTSSEQEPCGDEAKQFVVTRLLQRNVVIELLDLAPNGVS 255
Cdd:cd00175   2 VIDGDTIRVRL---PPGPL-ITVRLSGIDAPETARPNK---GKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRT 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19075617 256 FLGNVLHPAGNIATFLLSSGLGRVADNHISAlgPETMQSLRTIERKAKISRLGIWKN 312
Cdd:cd00175  75 LGTVYLNGGENIAEELVKEGLARVYRYYPDD--SEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
3-140 1.11e-27

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 108.89  E-value: 1.11e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617      3 QYVSSMIKYAQSGDSFNILIKDNakkiTEKQFSLAYVECPRFRREG------DEPFAFEAQEFSRRLVVGRPASVSTLYv 76
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG----PLITIRLSGIDAPETARPNkgdgtpDEPFGEEAKEFLKKLLLGKKVQVEVDS- 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075617     77 iptsKREYGRIRTSEF-----DLAESLLREGLAKLRPEATRNEGtsensYFVSLEEAQDHAQQYKLGIW 140
Cdd:smart00318  76 ----KDRYGRFLGTVYlnggnNIAEELVKEGLAKVYRYADKDEY-----VYDELLEAEEAAKKARKGLW 135
TUDOR pfam00567
Tudor domain;
649-765 2.41e-23

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 95.88  E-value: 2.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617   649 IYLDIVLSDIAEDGKFSFQIIgTGIQQLETLMSDLGSLKKSFKP-SEKINVGMNVAAISALDNAMYRGRVLrCDRENQAA 727
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQPK-SDSKKLEKLTEELQEYYASKPPeSLPPAVGDGCVAAFSEDGKWYRAKIT-ESLDDGLV 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 19075617   728 DVLLYDYGSVEQIPFKNISSLPDTYTKLKPQAQLARLS 765
Cdd:pfam00567  79 EVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
524-626 3.03e-19

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


Pssm-ID: 395448  Cd Length: 106  Bit Score: 83.53  E-value: 3.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617   524 AGIRTPRTARNDqEKGEPFAEESLSLAKSLL-QHDAQVEILSVDNNGCFLGDIYVNhDTNFALKLLSQGLAWCQGYASQS 602
Cdd:pfam00565   5 VGIDAPETAKPN-TPVQPFGKEAKEFLKKLVlGKKVVVLEFDKDKYGRTLGYVYLN-GKNINEELVKEGLAWVYKAYPPN 82
                          90       100
                  ....*....|....*....|....
gi 19075617   603 NVQYSQYHDTEAAAKEQKVGMWHD 626
Cdd:pfam00565  83 FKHYDELLAAEEEAKKKKKGLWSD 106
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
327-467 7.54e-17

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 78.95  E-value: 7.54e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617 327 DYSAVVSRVISTDTLEVRKDNGVEcRIQLSSIRHP--RPSNEKEAPYQLEAREFLRKKIIGKRVQVSLDFIRPGQNDLPA 404
Cdd:COG1525  23 TLTAGVVRVIDGDTLRVRDDGKGE-RVRLAGIDAPelGQPCGPEQPCGEEARQALRALLAGKTVTLEPDEGRDRYGRLLA 101
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19075617 405 InnCTVklsDGTNVALMVVKSGYATVIRYrmdsVDRSPIYDFLIEAEKAAQEGRKGMWSGKKP 467
Cdd:COG1525 102 Y--VYV---DGRDLNEELVREGLAWAYRR----YSPDKYADRYLAAEAEARAARRGLWSDAFP 155
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
14-140 3.75e-15

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: 72.69  E-value: 3.75e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617  14 SGDSFNILIKDNAkkitEKQFSLAYVECPRFRR------EGDEPFAFEAQEFSRRLVVGRPASVSTLYVIPtSKREYGRI 87
Cdd:cd00175   4 DGDTIRVRLPPGP----LITVRLSGIDAPETARpnkgksETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDR-YGRTLGTV 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 19075617  88 RTSEF-DLAESLLREGLAKLRPEATRNEGTSEnsyfvSLEEAQDHAQQYKLGIW 140
Cdd:cd00175  79 YLNGGeNIAEELVKEGLARVYRYYPDDSEYYD-----ELLEAEEAAKKARKGLW 127
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
352-463 5.26e-14

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


Pssm-ID: 395448  Cd Length: 106  Bit Score: 68.89  E-value: 5.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617   352 RIQLSSIRHPRPS--NEKEAPYQLEAREFLRKKIIGKRVQVSLDFIRPGQNDLPAInnctvkLSDGTNVALMVVKSGYAT 429
Cdd:pfam00565   1 RVRLVGIDAPETAkpNTPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYV------YLNGKNINEELVKEGLAW 74
                          90       100       110
                  ....*....|....*....|....*....|....
gi 19075617   430 VIRYRMDsvdRSPIYDFLIEAEKAAQEGRKGMWS 463
Cdd:pfam00565  75 VYKAYPP---NFKHYDELLAAEEEAKKKKKGLWS 105
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
524-636 3.07e-12

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 65.47  E-value: 3.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617 524 AGIRTPRTARNDQeKGEPFAEESLSLAKSLLQhDAQVEILSV---DNNGCFLGDIYVNhDTNFALKLLSQGLAW-CQGYA 599
Cdd:COG1525  51 AGIDAPELGQPCG-PEQPCGEEARQALRALLA-GKTVTLEPDegrDRYGRLLAYVYVD-GRDLNEELVREGLAWaYRRYS 127
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 19075617 600 SQSNVQysQYHDTEAAAKEQKVGMWHD--YVPPEKKAAS 636
Cdd:COG1525 128 PDKYAD--RYLAAEAEARAARRGLWSDafPVPPEWRRRK 164
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
197-312 2.55e-11

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


Pssm-ID: 395448  Cd Length: 106  Bit Score: 61.18  E-value: 2.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617   197 TISLAGVRCPRStftatspEQTSSEQEPCGDEAKQFVVTRLLQRNVVIELLDLAPNGvSFLGNVLHPAGNIATFLLSSGL 276
Cdd:pfam00565   1 RVRLVGIDAPET-------AKPNTPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYG-RTLGYVYLNGKNINEELVKEGL 72
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 19075617   277 GRVADNHISAlgPETMQSLRTIERKAKISRLGIWKN 312
Cdd:pfam00565  73 AWVYKAYPPN--FKHYDELLAAEEEAKKKKKGLWSD 106
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
15-146 3.29e-11

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 62.39  E-value: 3.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617  15 GDSFNILIKDNAKKITekqfsLAYVECP--RFRREGDEPFAFEAQEFSRRLVVGRpasvsTLYVIPTSKR-EYGR----I 87
Cdd:COG1525  34 GDTLRVRDDGKGERVR-----LAGIDAPelGQPCGPEQPCGEEARQALRALLAGK-----TVTLEPDEGRdRYGRllayV 103
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19075617  88 RTSEFDLAESLLREGLAKLRPEATRNEgtsensYFVSLEEAQDHAQQYKLGIWGPSDDV 146
Cdd:COG1525 104 YVDGRDLNEELVREGLAWAYRRYSPDK------YADRYLAAEAEARAARRGLWSDAFPV 156
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
163-310 3.28e-10

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 59.69  E-value: 3.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617 163 AHKGKKLNGIVETIRNGDQVRVRLflspkQHQLVTISLAGVRCPRSTftatspeQTSSEQEPCGDEAKQFVVTRLLQRNV 242
Cdd:COG1525  18 AAAAATLTAGVVRVIDGDTLRVRD-----DGKGERVRLAGIDAPELG-------QPCGPEQPCGEEARQALRALLAGKTV 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19075617 243 VIELLD--------LApngVSFLGNVlhpagNIATFLLSSGLGRVADNHisaLGPETMQSLRTIERKAKISRLGIW 310
Cdd:COG1525  86 TLEPDEgrdrygrlLA---YVYVDGR-----DLNEELVREGLAWAYRRY---SPDKYADRYLAAEAEARAARRGLW 150
Tudor_AtTudor1-like cd20443
Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor ...
662-770 3.99e-10

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: 58.25  E-value: 3.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617 662 GKFSFQIIGTGI-----QQLETL-MSDLGSLKKSFKPSEkinvGMNVAAISALDNAMYRGRVLRCDRENQAA-----DVL 730
Cdd:cd20443   2 GRFYVQVVSDQRlssiqQQLEGLsLKDKANPPGGFNPKK----GELVLAQFSADNSWNRAMVVNAPRQGTQSpkdeyEVF 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 19075617 731 LYDYGSVEQIPFKNISSLPDTYTKLKPQAQLARLSYVQLP 770
Cdd:cd20443  78 YIDYGNQETVPLSALRPLDPSVSSAPGLAQLCSLAHIKVP 117
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
34-140 1.97e-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: 50.01  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617    34 FSLAYVECPRFRREGD--EPFAFEAQEFSRRLVVGRpasvsTLYVIPTSKREYGR----IRTSEFDLAESLLREGLAKLR 107
Cdd:pfam00565   2 VRLVGIDAPETAKPNTpvQPFGKEAKEFLKKLVLGK-----KVVVLEFDKDKYGRtlgyVYLNGKNINEELVKEGLAWVY 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 19075617   108 PEATRNEGTSEnsyfvSLEEAQDHAQQYKLGIW 140
Cdd:pfam00565  77 KAYPPNFKHYD-----ELLAAEEEAKKKKKGLW 104
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
695-749 4.64e-07

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: 47.27  E-value: 4.64e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 19075617    695 KINVGMNVAAISaLDNAMYRGRVLRCDRENQaADVLLYDYGSVEQIPFKNISSLP 749
Cdd:smart00333   2 TFKVGDKVAARW-EDGEWYRARIVKVDGEQL-YEVFFIDYGNEEVVPPSDLRQLP 54
 
Name Accession Description Interval E-value
SNc smart00318
Staphylococcal nuclease homologues;
493-626 1.62e-41

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 148.56  E-value: 1.62e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617    493 RKLSVIIENVISGSRFRCFCPKeNCYFMFACAGIRTPRTARN---DQEKGEPFAEESLS-LAKSLLQHDAQVEILSVDNN 568
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPK-GPLITIRLSGIDAPETARPnkgDGTPDEPFGEEAKEfLKKLLLGKKVQVEVDSKDRY 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 19075617    569 GCFLGDIYVNHDTNFALKLLSQGLAWCQGYASQSNVQYSQYHDTEAAAKEQKVGMWHD 626
Cdd:smart00318  80 GRFLGTVYLNGGNNIAEELVKEGLAKVYRYADKDEYVYDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
502-626 3.45e-41

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


Pssm-ID: 238102  Cd Length: 129  Bit Score: 147.04  E-value: 3.45e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617 502 VISGSRFRCFCPKeNCYFMFACAGIRTPRTARND---QEKGEPFAEESLSLAKSLL-QHDAQVEILSVDNNGCFLGDIYV 577
Cdd:cd00175   2 VIDGDTIRVRLPP-GPLITVRLSGIDAPETARPNkgkSETDEPFGEEAKEFLKKLLlGKKVQVEVDSKDRYGRTLGTVYL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 19075617 578 NHDTNFALKLLSQGLAWCQGYASQSNVQYSQYHDTEAAAKEQKVGMWHD 626
Cdd:cd00175  81 NGGENIAEELVKEGLARVYRYYPDDSEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
326-463 1.39e-40

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 145.87  E-value: 1.39e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617    326 KDYSAVVSRVISTDTLEVRKDNGVECRIQLSSIRHPRPSNEKEA------PYQLEAREFLRKKIIGKRVQVSLDFIRPGQ 399
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKGPLITIRLSGIDAPETARPNKGdgtpdePFGEEAKEFLKKLLLGKKVQVEVDSKDRYG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19075617    400 NDLpainnCTVKLSDGTNVALMVVKSGYATVIRYRMDSVDRspiYDFLIEAEKAAQEGRKGMWS 463
Cdd:smart00318  81 RFL-----GTVYLNGGNNIAEELVKEGLAKVYRYADKDEYV---YDELLEAEEAAKKARKGLWS 136
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
334-463 1.52e-39

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


Pssm-ID: 238102  Cd Length: 129  Bit Score: 142.41  E-value: 1.52e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617 334 RVISTDTLEVRKDNGVECRIQLSSIRHPRPSN------EKEAPYQLEAREFLRKKIIGKRVQVSLDFIRPGQNDLpainn 407
Cdd:cd00175   1 RVIDGDTIRVRLPPGPLITVRLSGIDAPETARpnkgksETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRTL----- 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19075617 408 CTVKLSDGTNVALMVVKSGYATVIRYRMDSvdrSPIYDFLIEAEKAAQEGRKGMWS 463
Cdd:cd00175  76 GTVYLNGGENIAEELVKEGLARVYRYYPDD---SEYYDELLEAEEAAKKARKGLWS 128
SNc smart00318
Staphylococcal nuclease homologues;
167-312 3.97e-35

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 130.07  E-value: 3.97e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617    167 KKLNGIVETIRNGDQVRVRLflspKQHQLVTISLAGVRCPRSTFTATSPEQTsseQEPCGDEAKQFVVTRLLQRNVVIEL 246
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRL----PKGPLITIRLSGIDAPETARPNKGDGTP---DEPFGEEAKEFLKKLLLGKKVQVEV 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19075617    247 LDLAPNGVsFLGNVLHPAG-NIATFLLSSGLGRVADNHISALGPetMQSLRTIERKAKISRLGIWKN 312
Cdd:smart00318  74 DSKDRYGR-FLGTVYLNGGnNIAEELVKEGLAKVYRYADKDEYV--YDELLEAEEAAKKARKGLWSD 137
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
176-312 9.14e-35

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


Pssm-ID: 238102  Cd Length: 129  Bit Score: 128.93  E-value: 9.14e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617 176 IRNGDQVRVRLflsPKQHQlVTISLAGVRCPRSTFTATspeQTSSEQEPCGDEAKQFVVTRLLQRNVVIELLDLAPNGVS 255
Cdd:cd00175   2 VIDGDTIRVRL---PPGPL-ITVRLSGIDAPETARPNK---GKSETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDRYGRT 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19075617 256 FLGNVLHPAGNIATFLLSSGLGRVADNHISAlgPETMQSLRTIERKAKISRLGIWKN 312
Cdd:cd00175  75 LGTVYLNGGENIAEELVKEGLARVYRYYPDD--SEYYDELLEAEEAAKKARKGLWSD 129
SNc smart00318
Staphylococcal nuclease homologues;
3-140 1.11e-27

Staphylococcal nuclease homologues;


Pssm-ID: 214615  Cd Length: 137  Bit Score: 108.89  E-value: 1.11e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617      3 QYVSSMIKYAQSGDSFNILIKDNakkiTEKQFSLAYVECPRFRREG------DEPFAFEAQEFSRRLVVGRPASVSTLYv 76
Cdd:smart00318   1 KEIRGVVERVIDGDTIRVRLPKG----PLITIRLSGIDAPETARPNkgdgtpDEPFGEEAKEFLKKLLLGKKVQVEVDS- 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075617     77 iptsKREYGRIRTSEF-----DLAESLLREGLAKLRPEATRNEGtsensYFVSLEEAQDHAQQYKLGIW 140
Cdd:smart00318  76 ----KDRYGRFLGTVYlnggnNIAEELVKEGLAKVYRYADKDEY-----VYDELLEAEEAAKKARKGLW 135
TUDOR pfam00567
Tudor domain;
649-765 2.41e-23

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 95.88  E-value: 2.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617   649 IYLDIVLSDIAEDGKFSFQIIgTGIQQLETLMSDLGSLKKSFKP-SEKINVGMNVAAISALDNAMYRGRVLrCDRENQAA 727
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQPK-SDSKKLEKLTEELQEYYASKPPeSLPPAVGDGCVAAFSEDGKWYRAKIT-ESLDDGLV 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 19075617   728 DVLLYDYGSVEQIPFKNISSLPDTYTKLKPQAQLARLS 765
Cdd:pfam00567  79 EVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLA 116
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
524-626 3.03e-19

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


Pssm-ID: 395448  Cd Length: 106  Bit Score: 83.53  E-value: 3.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617   524 AGIRTPRTARNDqEKGEPFAEESLSLAKSLL-QHDAQVEILSVDNNGCFLGDIYVNhDTNFALKLLSQGLAWCQGYASQS 602
Cdd:pfam00565   5 VGIDAPETAKPN-TPVQPFGKEAKEFLKKLVlGKKVVVLEFDKDKYGRTLGYVYLN-GKNINEELVKEGLAWVYKAYPPN 82
                          90       100
                  ....*....|....*....|....
gi 19075617   603 NVQYSQYHDTEAAAKEQKVGMWHD 626
Cdd:pfam00565  83 FKHYDELLAAEEEAKKKKKGLWSD 106
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
327-467 7.54e-17

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 78.95  E-value: 7.54e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617 327 DYSAVVSRVISTDTLEVRKDNGVEcRIQLSSIRHP--RPSNEKEAPYQLEAREFLRKKIIGKRVQVSLDFIRPGQNDLPA 404
Cdd:COG1525  23 TLTAGVVRVIDGDTLRVRDDGKGE-RVRLAGIDAPelGQPCGPEQPCGEEARQALRALLAGKTVTLEPDEGRDRYGRLLA 101
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19075617 405 InnCTVklsDGTNVALMVVKSGYATVIRYrmdsVDRSPIYDFLIEAEKAAQEGRKGMWSGKKP 467
Cdd:COG1525 102 Y--VYV---DGRDLNEELVREGLAWAYRR----YSPDKYADRYLAAEAEARAARRGLWSDAFP 155
SNc cd00175
Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and ...
14-140 3.75e-15

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: 72.69  E-value: 3.75e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617  14 SGDSFNILIKDNAkkitEKQFSLAYVECPRFRR------EGDEPFAFEAQEFSRRLVVGRPASVSTLYVIPtSKREYGRI 87
Cdd:cd00175   4 DGDTIRVRLPPGP----LITVRLSGIDAPETARpnkgksETDEPFGEEAKEFLKKLLLGKKVQVEVDSKDR-YGRTLGTV 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 19075617  88 RTSEF-DLAESLLREGLAKLRPEATRNEGTSEnsyfvSLEEAQDHAQQYKLGIW 140
Cdd:cd00175  79 YLNGGeNIAEELVKEGLARVYRYYPDDSEYYD-----ELLEAEEAAKKARKGLW 127
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
352-463 5.26e-14

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


Pssm-ID: 395448  Cd Length: 106  Bit Score: 68.89  E-value: 5.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617   352 RIQLSSIRHPRPS--NEKEAPYQLEAREFLRKKIIGKRVQVSLDFIRPGQNDLPAInnctvkLSDGTNVALMVVKSGYAT 429
Cdd:pfam00565   1 RVRLVGIDAPETAkpNTPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYGRTLGYV------YLNGKNINEELVKEGLAW 74
                          90       100       110
                  ....*....|....*....|....*....|....
gi 19075617   430 VIRYRMDsvdRSPIYDFLIEAEKAAQEGRKGMWS 463
Cdd:pfam00565  75 VYKAYPP---NFKHYDELLAAEEEAKKKKKGLWS 105
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
524-636 3.07e-12

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 65.47  E-value: 3.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617 524 AGIRTPRTARNDQeKGEPFAEESLSLAKSLLQhDAQVEILSV---DNNGCFLGDIYVNhDTNFALKLLSQGLAW-CQGYA 599
Cdd:COG1525  51 AGIDAPELGQPCG-PEQPCGEEARQALRALLA-GKTVTLEPDegrDRYGRLLAYVYVD-GRDLNEELVREGLAWaYRRYS 127
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 19075617 600 SQSNVQysQYHDTEAAAKEQKVGMWHD--YVPPEKKAAS 636
Cdd:COG1525 128 PDKYAD--RYLAAEAEARAARRGLWSDafPVPPEWRRRK 164
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
197-312 2.55e-11

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


Pssm-ID: 395448  Cd Length: 106  Bit Score: 61.18  E-value: 2.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617   197 TISLAGVRCPRStftatspEQTSSEQEPCGDEAKQFVVTRLLQRNVVIELLDLAPNGvSFLGNVLHPAGNIATFLLSSGL 276
Cdd:pfam00565   1 RVRLVGIDAPET-------AKPNTPVQPFGKEAKEFLKKLVLGKKVVVLEFDKDKYG-RTLGYVYLNGKNINEELVKEGL 72
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 19075617   277 GRVADNHISAlgPETMQSLRTIERKAKISRLGIWKN 312
Cdd:pfam00565  73 AWVYKAYPPN--FKHYDELLAAEEEAKKKKKGLWSD 106
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
15-146 3.29e-11

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 62.39  E-value: 3.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617  15 GDSFNILIKDNAKKITekqfsLAYVECP--RFRREGDEPFAFEAQEFSRRLVVGRpasvsTLYVIPTSKR-EYGR----I 87
Cdd:COG1525  34 GDTLRVRDDGKGERVR-----LAGIDAPelGQPCGPEQPCGEEARQALRALLAGK-----TVTLEPDEGRdRYGRllayV 103
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19075617  88 RTSEFDLAESLLREGLAKLRPEATRNEgtsensYFVSLEEAQDHAQQYKLGIWGPSDDV 146
Cdd:COG1525 104 YVDGRDLNEELVREGLAWAYRRYSPDK------YADRYLAAEAEARAARRGLWSDAFPV 156
YncB COG1525
Endonuclease YncB, thermonuclease family [Replication, recombination and repair];
163-310 3.28e-10

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


Pssm-ID: 441134 [Multi-domain]  Cd Length: 164  Bit Score: 59.69  E-value: 3.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617 163 AHKGKKLNGIVETIRNGDQVRVRLflspkQHQLVTISLAGVRCPRSTftatspeQTSSEQEPCGDEAKQFVVTRLLQRNV 242
Cdd:COG1525  18 AAAAATLTAGVVRVIDGDTLRVRD-----DGKGERVRLAGIDAPELG-------QPCGPEQPCGEEARQALRALLAGKTV 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19075617 243 VIELLD--------LApngVSFLGNVlhpagNIATFLLSSGLGRVADNHisaLGPETMQSLRTIERKAKISRLGIW 310
Cdd:COG1525  86 TLEPDEgrdrygrlLA---YVYVDGR-----DLNEELVREGLAWAYRRY---SPDKYADRYLAAEAEARAARRGLW 150
Tudor_AtTudor1-like cd20443
Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor ...
662-770 3.99e-10

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: 58.25  E-value: 3.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617 662 GKFSFQIIGTGI-----QQLETL-MSDLGSLKKSFKPSEkinvGMNVAAISALDNAMYRGRVLRCDRENQAA-----DVL 730
Cdd:cd20443   2 GRFYVQVVSDQRlssiqQQLEGLsLKDKANPPGGFNPKK----GELVLAQFSADNSWNRAMVVNAPRQGTQSpkdeyEVF 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 19075617 731 LYDYGSVEQIPFKNISSLPDTYTKLKPQAQLARLSYVQLP 770
Cdd:cd20443  78 YIDYGNQETVPLSALRPLDPSVSSAPGLAQLCSLAHIKVP 117
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
675-753 2.94e-09

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: 54.61  E-value: 2.94e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617 675 QLETLMSDLGS-------LKKSFKPSEkinvGMNVAAISALDNAMYRGRVLRCDRENQAaDVLLYDYGSVEQIPFKNISS 747
Cdd:cd20433   4 QLEKLMEKLRFeiasnppLPGSYTPRK----GDLCAAKFVEDGEWYRAKVEKVEGDKKV-HVLYIDYGNREVLPSTRLAA 78

                ....*.
gi 19075617 748 LPDTYT 753
Cdd:cd20433  79 LPPAFS 84
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
698-748 3.63e-08

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: 50.21  E-value: 3.63e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 19075617 698 VGMNVAAISALDNAMYRGRVLRCDRENQaADVLLYDYGSVEQIPFKNISSL 748
Cdd:cd20379   1 VGDLCAAKYEEDGKWYRARVLEVLSNDK-VEVFFVDYGNTETVPLSDLRPL 50
SNase pfam00565
Staphylococcal nuclease homolog; Present in all three domains of cellular life. Four copies in ...
34-140 1.97e-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: 50.01  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617    34 FSLAYVECPRFRREGD--EPFAFEAQEFSRRLVVGRpasvsTLYVIPTSKREYGR----IRTSEFDLAESLLREGLAKLR 107
Cdd:pfam00565   2 VRLVGIDAPETAKPNTpvQPFGKEAKEFLKKLVLGK-----KVVVLEFDKDKYGRtlgyVYLNGKNINEELVKEGLAWVY 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 19075617   108 PEATRNEGTSEnsyfvSLEEAQDHAQQYKLGIW 140
Cdd:pfam00565  77 KAYPPNFKHYD-----ELLAAEEEAKKKKKGLW 104
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
695-749 4.64e-07

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: 47.27  E-value: 4.64e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 19075617    695 KINVGMNVAAISaLDNAMYRGRVLRCDRENQaADVLLYDYGSVEQIPFKNISSLP 749
Cdd:smart00333   2 TFKVGDKVAARW-EDGEWYRARIVKVDGEQL-YEVFFIDYGNEEVVPPSDLRQLP 54
Tudor_TDRD2 cd20412
Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, ...
675-759 2.36e-05

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: 43.82  E-value: 2.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075617 675 QLETL---MSDLGSLKKSFKPSEKINVGMNVAAISALDNAMYRGRVLRCdRENQAADVLLYDYGSVEQIPFKNISSLPDT 751
Cdd:cd20412   5 QLDKLvqeMTQYYESEENRHTLLTVQVGDIVAAPFRHDGSWYRARVLGF-LENGNLDLYFVDYGDSGYVPLEDLRALRSD 83

                ....*...
gi 19075617 752 YTKLKPQA 759
Cdd:cd20412  84 FLSLPFQA 91
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
713-774 7.09e-03

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: 36.30  E-value: 7.09e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19075617 713 YRGRVLRCDRENQAADVLLYDYGSVEQIPFKNISSLPDTYTKLKPQAqlARLSYVQLPPPSS 774
Cdd:cd20423  20 CRALIDNVYEPVEMVEVTYVDYGNKELVSLKNLRSISEEFLKLKAQA--FRCSLYNLIQPSG 79
 
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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