NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|214010196|ref|NP_445806|]
View 

DNA (cytosine-5)-methyltransferase 1 [Rattus norvegicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
BAH_Dnmt1_II cd04711
BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5) ...
 969-1105 1.32e-83

BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5)-methyltransferases from Bilateria, Dnmt1 and similar proteins. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the genome. These effects include transcriptional repression via inhibition of transcription factor binding, the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting, and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


:

Pssm-ID: 240062  Cd Length: 137  Bit Score: 269.75  E-value: 1.32e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  969 NENLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIHCGKKKGGKVNEADIKIRLYKFYRPENTHKSIQATYHADINLLYW 1048
Cdd:cd04711     1 DEDLYPEYYRKSSDYIKGSNLDAPEPFRIGRIKEIFCAKRSNGKPNESDIKLRINKFYRPENTHKGFKATYHADINMLYW 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 214010196 1049 SDEEAVVDFSDVQGRCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKSFEDPPN 1105
Cdd:cd04711    81 SDEEATVDFSAVQGRCTVEYGEDLPESVQEYSGGGPDRFYFLEAYNAKTKSFEDPPN 137
BAH_Dnmt1_I cd04760
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 759-881 9.79e-64

BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5)-methyltransferases from Bilateria, Dnmt1 and similar proteins. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the genome. These effects include transcriptional repression via inhibition of transcription factor binding, the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting, and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


:

Pssm-ID: 240107  Cd Length: 124  Bit Score: 212.32  E-value: 9.79e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  759 ETLEVGDCVSVIPDDPSKPLYLARVTALWEDKN-GQMFHAHWFCAGTDTVLGATSDPLELFLVGECENMQLSYIHSKVKV 837
Cdd:cd04760     2 EELEAGDCVSVKPDDPTKPLYIARVTYMWKDSIgGKMFHAHWFCRGSDTVLGETSDPLELFLVDECEDMALSSIHGKVNV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 214010196  838 IYRGPSPNWAMEGGMDPEaMLPGAEDGKTYFYQFWYSQDYARFE 881
Cdd:cd04760    82 IYKAPSENWSMEGGMDEE-DEIFEDDGKTFFYQKWYDPECARFE 124
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
1141-1599 7.52e-63

DNA-cytosine methylase [Replication, recombination and repair];


:

Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 215.83  E-value: 7.52e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1141 PKLRTLDVFSGCGGLTEGFHQAGIsETLWAIEMWEPAAQAFRLNNPGTTVFTEDcnvlLKLVMAGEVtnslgqrlpqKGD 1220
Cdd:COG0270     2 KKLTVIDLFAGAGGLSLGFEKAGF-EVVFAVEIDPDACETYRANFPEAKVIEGD----IRDIDPEEL----------IPD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1221 VEMLCGGPPCQGFSGMNRfnSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFRRSMVLKLTLRCLVRMGYQCTF 1300
Cdd:COG0270    67 VDLLIGGPPCQPFSVAGK--RKGLEDPRGTLFFEFIRIVEELRPKAFVLENVPGLLSSDKGKTFEEILKELEELGYRVDY 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1301 GVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLPE 1380
Cdd:COG0270   145 KVLNAADYGVPQNRERVFIVGFRKDLDLFEFPEPTH----------------------------LKPYVTVGDALEDLPD 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1381 iqngasapeisyngepqswfqrqlrgshyqpilrDHICKdmsalvaarmrhiplspgsdwrdlpniqvrlrdgvitnklr 1460
Cdd:COG0270   197 ----------------------------------AHEAR----------------------------------------- 201

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1461 ytfhdtkngcsstgalrgvcscaegktcdpasrqfntlipwclphtgnrhnhwaglygrlewdgFFSTTVTNpePMGKQG 1540
Cdd:COG0270   202 ----------------------------------------------------------------YLSETITA--GYGGGG 215

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 214010196 1541 RVLHPEQHRVVSVRECARSQGFPDTYRLFGNILDRHRQVGNAVPPPLAKAIGLEIKLCL 1599
Cdd:COG0270   216 RFLHPGEPRRLTVREAARLQGFPDDFKFPGSKTQAYRQIGNAVPPPLAEAIAKAILKAL 274
DNMT1-RFD pfam12047
Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a ...
 405-540 1.74e-51

Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a cytosine specific DNA methyltransferase enzyme. It functions non-catalytically to target the protein towards replication foci. This allows the DNMT1 protein to methylate the correct residues. This domain targets DMAP1 and HDAC2 to the replication foci during the S phase of mitosis. They are thought to have some importance in conversion of critical histone lysine moieties.


:

Pssm-ID: 463444  Cd Length: 143  Bit Score: 177.92  E-value: 1.74e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196   405 YDSSPMHKFTFFSVYCSRGHLCPVDTGLIEKNVELYFSGVAKAIHEENPSVEG-GVNGKN----LGPINQWWISGFDGGE 479
Cdd:pfam12047    1 EEDRPQRKLTDFELYDKDGHLCPFDVLLIEKNVDIFISGIVKPIDEDEPSLDGkGIEDKGmqikLGPIKEWTISGFDGGE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 214010196   480 KALIGFSTAFAEYFLMEPSPEYAPIFGLMQEKIYISKIVVEFLQSNP--DAVYEDLINKIETT 540
Cdd:pfam12047   81 KALIWLSTEFAWYKLLKPSAEYAPIYELVYEKARLSVEVVEFLQRSPgsELSYEDLINRVLTS 143
DMAP_binding pfam06464
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
 16-106 5.35e-24

DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.


:

Pssm-ID: 368923 [Multi-domain]  Cd Length: 104  Bit Score: 97.88  E-value: 5.35e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196    16 PAGSLPDHVRRRLKDLERDG----LTEKECVKEKLNLLHEFL---------QTEIKSQLCDLETKLHKEELSEEGYLAKV 82
Cdd:pfam06464    1 NPPSLPDDVRERLSELDLDLsegdITEKGYEKKKLKLLRKFLlhpetptklSAEAQNQLASLETKLRDEELSEEVYLEKV 80

                           90       100
                   ....*....|....*....|....
gi 214010196    83 KTLLNKDLCLENGTLSLTQKANGC 106
Cdd:pfam06464   81 KALLAKELERENGLNAPTKEQSGL 104
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 649-695 6.07e-19

CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases.


:

Pssm-ID: 366873  Cd Length: 48  Bit Score: 81.63  E-value: 6.07e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 214010196   649 ENTMKRRRCGVCEVCQQPE-CGKCKACKDMVKFGGTGRSKQACLKRRC 695
Cdd:pfam02008    1 RNRRKRRRCGVCEGCQRPEdCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
PRK12678 super family cl36163
transcription termination factor Rho; Provisional
 109-327 7.08e-06

transcription termination factor Rho; Provisional


The actual alignment was detected with superfamily member PRK12678:

Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 50.67  E-value: 7.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  109 NGSRPTWKAEMADSNRSPRSRPKPRGPRRSKSDSETMIEASSSSVATRRTTRQTTITSHFKGPAKRKPKEDSEKGnanes 188
Cdd:PRK12678   60 GGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERG----- 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  189 AAEERDQDKKRRVAGTESRASRAGESVEKPERVRPGtqlcQEEQGEQEDDRRPRRQTRELASRRKSREDPDREARPGTHL 268
Cdd:PRK12678  135 EAARRGAARKAGEGGEQPATEARADAAERTEEEERD----ERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRRE 210

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 214010196  269 DVDDDDEKDKRSSRPRSQPRDLATKRRPKEEVEQITPEPPEGKDEDEREEKRRKTTRKK 327
Cdd:PRK12678  211 QGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDR 269
 
Name Accession Description Interval E-value
BAH_Dnmt1_II cd04711
BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5) ...
 969-1105 1.32e-83

BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5)-methyltransferases from Bilateria, Dnmt1 and similar proteins. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the genome. These effects include transcriptional repression via inhibition of transcription factor binding, the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting, and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240062  Cd Length: 137  Bit Score: 269.75  E-value: 1.32e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  969 NENLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIHCGKKKGGKVNEADIKIRLYKFYRPENTHKSIQATYHADINLLYW 1048
Cdd:cd04711     1 DEDLYPEYYRKSSDYIKGSNLDAPEPFRIGRIKEIFCAKRSNGKPNESDIKLRINKFYRPENTHKGFKATYHADINMLYW 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 214010196 1049 SDEEAVVDFSDVQGRCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKSFEDPPN 1105
Cdd:cd04711    81 SDEEATVDFSAVQGRCTVEYGEDLPESVQEYSGGGPDRFYFLEAYNAKTKSFEDPPN 137
BAH_Dnmt1_I cd04760
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 759-881 9.79e-64

BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5)-methyltransferases from Bilateria, Dnmt1 and similar proteins. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the genome. These effects include transcriptional repression via inhibition of transcription factor binding, the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting, and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240107  Cd Length: 124  Bit Score: 212.32  E-value: 9.79e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  759 ETLEVGDCVSVIPDDPSKPLYLARVTALWEDKN-GQMFHAHWFCAGTDTVLGATSDPLELFLVGECENMQLSYIHSKVKV 837
Cdd:cd04760     2 EELEAGDCVSVKPDDPTKPLYIARVTYMWKDSIgGKMFHAHWFCRGSDTVLGETSDPLELFLVDECEDMALSSIHGKVNV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 214010196  838 IYRGPSPNWAMEGGMDPEaMLPGAEDGKTYFYQFWYSQDYARFE 881
Cdd:cd04760    82 IYKAPSENWSMEGGMDEE-DEIFEDDGKTFFYQKWYDPECARFE 124
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
1141-1599 7.52e-63

DNA-cytosine methylase [Replication, recombination and repair];


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 215.83  E-value: 7.52e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1141 PKLRTLDVFSGCGGLTEGFHQAGIsETLWAIEMWEPAAQAFRLNNPGTTVFTEDcnvlLKLVMAGEVtnslgqrlpqKGD 1220
Cdd:COG0270     2 KKLTVIDLFAGAGGLSLGFEKAGF-EVVFAVEIDPDACETYRANFPEAKVIEGD----IRDIDPEEL----------IPD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1221 VEMLCGGPPCQGFSGMNRfnSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFRRSMVLKLTLRCLVRMGYQCTF 1300
Cdd:COG0270    67 VDLLIGGPPCQPFSVAGK--RKGLEDPRGTLFFEFIRIVEELRPKAFVLENVPGLLSSDKGKTFEEILKELEELGYRVDY 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1301 GVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLPE 1380
Cdd:COG0270   145 KVLNAADYGVPQNRERVFIVGFRKDLDLFEFPEPTH----------------------------LKPYVTVGDALEDLPD 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1381 iqngasapeisyngepqswfqrqlrgshyqpilrDHICKdmsalvaarmrhiplspgsdwrdlpniqvrlrdgvitnklr 1460
Cdd:COG0270   197 ----------------------------------AHEAR----------------------------------------- 201

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1461 ytfhdtkngcsstgalrgvcscaegktcdpasrqfntlipwclphtgnrhnhwaglygrlewdgFFSTTVTNpePMGKQG 1540
Cdd:COG0270   202 ----------------------------------------------------------------YLSETITA--GYGGGG 215

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 214010196 1541 RVLHPEQHRVVSVRECARSQGFPDTYRLFGNILDRHRQVGNAVPPPLAKAIGLEIKLCL 1599
Cdd:COG0270   216 RFLHPGEPRRLTVREAARLQGFPDDFKFPGSKTQAYRQIGNAVPPPLAEAIAKAILKAL 274
DNMT1-RFD pfam12047
Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a ...
 405-540 1.74e-51

Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a cytosine specific DNA methyltransferase enzyme. It functions non-catalytically to target the protein towards replication foci. This allows the DNMT1 protein to methylate the correct residues. This domain targets DMAP1 and HDAC2 to the replication foci during the S phase of mitosis. They are thought to have some importance in conversion of critical histone lysine moieties.


Pssm-ID: 463444  Cd Length: 143  Bit Score: 177.92  E-value: 1.74e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196   405 YDSSPMHKFTFFSVYCSRGHLCPVDTGLIEKNVELYFSGVAKAIHEENPSVEG-GVNGKN----LGPINQWWISGFDGGE 479
Cdd:pfam12047    1 EEDRPQRKLTDFELYDKDGHLCPFDVLLIEKNVDIFISGIVKPIDEDEPSLDGkGIEDKGmqikLGPIKEWTISGFDGGE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 214010196   480 KALIGFSTAFAEYFLMEPSPEYAPIFGLMQEKIYISKIVVEFLQSNP--DAVYEDLINKIETT 540
Cdd:pfam12047   81 KALIWLSTEFAWYKLLKPSAEYAPIYELVYEKARLSVEVVEFLQRSPgsELSYEDLINRVLTS 143
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
1143-1596 5.31e-40

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 151.70  E-value: 5.31e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1143 LRTLDVFSGCGGLTEGFHQAGIsETLWAIEMWEPAAQAFRLNNPgTTVFtedcnvllklvmaGEVTNSLGQRLPqkgDVE 1222
Cdd:pfam00145    1 FKFIDLFAGIGGFRLGLEQAGF-ECVAANEIDKSAAKTYEANFP-KVPI-------------GDITLIDIKDIP---DID 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1223 MLCGGPPCQGFS--GMNRFNSRTYskfkNSLVVSFLSYCDYYRPRFFLLENVRNFVSFRRSMVLKLTLRCLVRMGYQCTF 1300
Cdd:pfam00145   63 ILTGGFPCQDFSiaGKQKGFEDTR----GTLFFEIIRIIKEKKPKAFLLENVKGLLSHDNGNTLNVILETLEELGYHVSW 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1301 GVLQAGQYGVAQTRRRAIILAAAPG-EKLPLFPEPlhvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLP 1379
Cdd:pfam00145  139 KVLNASDYGVPQNRERVFIVGIRKDlNLNVLVPVP------------------------------EFDFPKPKDLTGTIR 188

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1380 EIQNGASAPEISYNGEpqswfqrqlrgshyqpilrDHICKDMSalvaaRMRHIPLSPGSDWRDLpNIQVRLRDGVITNKL 1459
Cdd:pfam00145  189 DLLEEPSLDENKYNLS-------------------DKFVENHE-----RRKPTTKAPGGGYPTY-LLRNRIDKVEEGKGP 243

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1460 RYTFHDtkngcsstgalrgvcscaegktcdpasrqfntlipwclphtgnrhnhwaglYGRLEwdgffsttVTNPEPMGKQ 1539
Cdd:pfam00145  244 SFTYRK---------------------------------------------------SGRPE--------APKTGILGKN 264

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 214010196  1540 GR--VLHPEQHRVVSVRECARSQGFPDTYRLFGNILDRHRQVGNAVPPPLAKAIGLEIK 1596
Cdd:pfam00145  265 GErfRGHPKNIRRLTPRECARLQGFPDDFIFPGSKTQLYKQIGNAVPVPVAEAIAKAIK 323
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
 1143-1596 1.12e-33

Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many aspects of biology. Cytosine-specific DNA methylases are found both in prokaryotes and eukaryotes. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the mammalian genome. These effects include transcriptional repression via inhibition of transcription factor binding or the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability.


Pssm-ID: 238192 [Multi-domain]  Cd Length: 275  Bit Score: 131.59  E-value: 1.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1143 LRTLDVFSGCGGLTEGFHQAGiSETLWAIEMWEPAAQAFRLNNPGTTVFtedcnvllklvmaGEVTNSLGQRLPqkGDVE 1222
Cdd:cd00315     1 LRVIDLFAGIGGFRLGLEKAG-FEIVAANEIDKSAAETYEANFPNKLIE-------------GDITKIDEKDFI--PDID 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1223 MLCGGPPCQGFS--GMNRFNSRTYSKfknslvvSFLSYCDY---YRPRFFLLENVRNFVSFRRSMVLKLTLRCLVRMGYQ 1297
Cdd:cd00315    65 LLTGGFPCQPFSiaGKRKGFEDTRGT-------LFFEIIRIlkeKKPKYFLLENVKGLLTHDNGNTLKVILNTLEELGYN 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1298 CTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFapracqlsvvvDDKKFVSNITRLSSGPFRTITVrdtmsd 1377
Cdd:cd00315   138 VYWKLLNASDYGVPQNRERVFIIGIRKDLILNFFSPFPKPS-----------EKKKTLKDILRIRDPDEPSPTL------ 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1378 lpeiqngasapeisyngepqswfqrqlrgshyqpilrdhickdmsalvaarmrhiplspgsdwrdlpniqvrlrdgvitn 1457
Cdd:cd00315       --------------------------------------------------------------------------------

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1458 klrytfhdtkngcsstgalrgvcscaegktcdpasrqfntlipwclphTGNRHNHWAGLYgrlewdgffsttvtnpepMG 1537
Cdd:cd00315   201 ------------------------------------------------TASYGKGTGSVH------------------PT 214

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1538 KQGRVLHPEQHRVVSVRECARSQGFPDTYRLFG-NILDRHRQVGNAVPPPLAKAIGLEIK 1596
Cdd:cd00315   215 APDMIGKESNIRRLTPRECARLQGFPDDFEFPGkSVTQAYRQIGNSVPVPVAEAIAKAIK 274
BAH smart00439
Bromo adjacent homology domain;
982-1104 2.05e-33

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 125.48  E-value: 2.05e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196    982 DYIKGSNLDAPEPYRIGRIKEIHCGKKkggkvNEADIKIRLYKFYRPENTHKSiqATYHADINLLYWSDEEAVVDFSDVQ 1061
Cdd:smart00439    6 DFVLVEPDDADEPYYIGRIEEIFETKK-----NSESKMVRVRWFYRPEETVLE--KAALFDKNEVFLSDEYDTVPLSDII 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 214010196   1062 GRCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKSFEDPP 1104
Cdd:smart00439   79 GKCNVLYKSDYPGLRPEGSIGEPDVFFCESAYDPEKGSFKKLP 121
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 975-1104 3.22e-30

BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.


Pssm-ID: 460207  Cd Length: 120  Bit Score: 116.25  E-value: 3.22e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196   975 EHYRKySDYIKGSNLDAPEPYRIGRIKEIHCGKKKGgkvneaDIKIRLYKFYRPENTHKSIQATYHADinLLYWSDEEAV 1054
Cdd:pfam01426    1 ETYSV-GDFVLVEPDDADEPYYVARIEELFEDTKNG------KKMVRVQWFYRPEETVHRAGKAFNKD--ELFLSDEEDD 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 214010196  1055 VDFSDVQGRCTVEYGEDLLESIQDYSqGGPDRFYFLEAYNSKTKSFEDPP 1104
Cdd:pfam01426   72 VPLSAIIGKCSVLHKSDLESLDPYKI-KEPDDFFCELLYDPKTKSFKKLP 120
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
 1147-1595 1.40e-29

DNA-methyltransferase (dcm); All proteins in this family for which functions are known are DNA-cytosine methyltransferases. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273211 [Multi-domain]  Cd Length: 315  Bit Score: 120.89  E-value: 1.40e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1147 DVFSGCGGLTEGFHQAGIsETLWAIEMWEPAAQAFRLNNPGTTVFtedcnvllklvmaGEVTNSLGQRLPqkgDVEMLCG 1226
Cdd:TIGR00675    3 DLFAGIGGIRLGFEQAGF-KCVFASEIDKYAQKTYEANFGNKVPF-------------GDITKISPSDIP---DFDILLG 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1227 GPPCQGFSgMNRFNsRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFRRSMVLKLTLRCLVRMGYQCTFGVLQAG 1306
Cdd:TIGR00675   66 GFPCQPFS-IAGKR-KGFEDTRGTLFFEIVRILKEKKPKFFLLENVKGLVSHDKGRTFKVIIETLEELGYKVYYKVLNAK 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1307 QYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlsSGPFRTITVRDtmsdlpeiqngas 1386
Cdd:TIGR00675  144 DFGVPQNRERIYIVGFRDFDDKLNFEFPKP--------------------------IYVAKKKRIGD------------- 184

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1387 APEISYNGEPqswfqrqlrgshyQPILRDHICKDMSaLVAARMRHIPLSpGSDWRDLpniqvrlrdgvitnklrytfhdt 1466
Cdd:TIGR00675  185 LLDLSVDLEE-------------KYYLSEEKKNGLL-LLLENMRKKEGT-GEQIGSF----------------------- 226

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1467 kngcsstgalrgvcscaegKTCDPASRQFNTLipwclphTGNRHNHWAGlygrlewdgffstTVTNPEPMGKQGRVlHPE 1546
Cdd:TIGR00675  227 -------------------YNRESKSSIIRTL-------SARGYTFVKG-------------GKSVLIVPHKSTVV-HPG 266

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 214010196  1547 QHRVVSVRECARSQGFPDTYRLFGNILDRHRQVGNAVPPPLAKAIGLEI 1595
Cdd:TIGR00675  267 RIRRLTPRECARLQGFPDDFKFPVSDSQLYKQAGNAVVVPVIEAIAKQI 315
BAH smart00439
Bromo adjacent homology domain;
760-884 4.27e-26

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 104.68  E-value: 4.27e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196    760 TLEVGDCVSVIPDDPSKPLYLARVTALWEDKNGQ---MFHAHWFCAGTDTVLGAT--SDPLELFLVGECENMQLSYIHSK 834
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSeskMVRVRWFYRPEETVLEKAalFDKNEVFLSDEYDTVPLSDIIGK 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 214010196    835 VKVIYRGPSPNWAMEGGMDPEamlpgaedgKTYFYQFWYSQDYARFESPP 884
Cdd:smart00439   81 CNVLYKSDYPGLRPEGSIGEP---------DVFFCESAYDPEKGSFKKLP 121
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 759-884 5.18e-26

BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.


Pssm-ID: 460207  Cd Length: 120  Bit Score: 104.31  E-value: 5.18e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196   759 ETLEVGDCVSVIPDDPSKPLYLARVTALWEDKNG--QMFHAHWFCAGTDTV--LGATSDPLELFLVGECENMQLSYIHSK 834
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNgkKMVRVQWFYRPEETVhrAGKAFNKDELFLSDEEDDVPLSAIIGK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 214010196   835 VKVIYRGPSPNWAMEGGMDPeamlpgaedgKTYFYQFWYSQDYARFESPP 884
Cdd:pfam01426   81 CSVLHKSDLESLDPYKIKEP----------DDFFCELLYDPKTKSFKKLP 120
DMAP_binding pfam06464
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
 16-106 5.35e-24

DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.


Pssm-ID: 368923 [Multi-domain]  Cd Length: 104  Bit Score: 97.88  E-value: 5.35e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196    16 PAGSLPDHVRRRLKDLERDG----LTEKECVKEKLNLLHEFL---------QTEIKSQLCDLETKLHKEELSEEGYLAKV 82
Cdd:pfam06464    1 NPPSLPDDVRERLSELDLDLsegdITEKGYEKKKLKLLRKFLlhpetptklSAEAQNQLASLETKLRDEELSEEVYLEKV 80

                           90       100
                   ....*....|....*....|....
gi 214010196    83 KTLLNKDLCLENGTLSLTQKANGC 106
Cdd:pfam06464   81 KALLAKELERENGLNAPTKEQSGL 104
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 649-695 6.07e-19

CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases.


Pssm-ID: 366873  Cd Length: 48  Bit Score: 81.63  E-value: 6.07e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 214010196   649 ENTMKRRRCGVCEVCQQPE-CGKCKACKDMVKFGGTGRSKQACLKRRC 695
Cdd:pfam02008    1 RNRRKRRRCGVCEGCQRPEdCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 109-327 7.08e-06

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 50.67  E-value: 7.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  109 NGSRPTWKAEMADSNRSPRSRPKPRGPRRSKSDSETMIEASSSSVATRRTTRQTTITSHFKGPAKRKPKEDSEKGnanes 188
Cdd:PRK12678   60 GGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERG----- 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  189 AAEERDQDKKRRVAGTESRASRAGESVEKPERVRPGtqlcQEEQGEQEDDRRPRRQTRELASRRKSREDPDREARPGTHL 268
Cdd:PRK12678  135 EAARRGAARKAGEGGEQPATEARADAAERTEEEERD----ERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRRE 210

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 214010196  269 DVDDDDEKDKRSSRPRSQPRDLATKRRPKEEVEQITPEPPEGKDEDEREEKRRKTTRKK 327
Cdd:PRK12678  211 QGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDR 269
Caldesmon pfam02029
Caldesmon;
173-353 4.87e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.39  E-value: 4.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196   173 KRKPKEDSEKGNANESAAEERDQDKKrrvagTESRASRAGESVEKPERvRPGTQlcqEEQG--EQEDDRRPRRQTR--EL 248
Cdd:pfam02029   12 RRRAREERRRQKEEEEPSGQVTESVE-----PNEHNSYEEDSELKPSG-QGGLD---EEEAflDRTAKREERRQKRlqEA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196   249 ASRRKSREDPDREARPGTHLDVDDDDEKDKRSSRPRSQPRDL-------ATKRRPKEEVEQITP-EPPEGKDEDEREEKR 320
Cdd:pfam02029   83 LERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRlgrykeeETEIREKEYQENKWStEVRQAEEEGEEEEDK 162

                          170       180       190
                   ....*....|....*....|....*....|...
gi 214010196   321 RKTTRKKPEPLSIPVQSRVERKASQGKASAIPK 353
Cdd:pfam02029  163 SEEAEEVPTENFAKEEVKDEKIKKEKKVKYESK 195
 
Name Accession Description Interval E-value
BAH_Dnmt1_II cd04711
BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5) ...
 969-1105 1.32e-83

BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5)-methyltransferases from Bilateria, Dnmt1 and similar proteins. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the genome. These effects include transcriptional repression via inhibition of transcription factor binding, the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting, and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240062  Cd Length: 137  Bit Score: 269.75  E-value: 1.32e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  969 NENLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIHCGKKKGGKVNEADIKIRLYKFYRPENTHKSIQATYHADINLLYW 1048
Cdd:cd04711     1 DEDLYPEYYRKSSDYIKGSNLDAPEPFRIGRIKEIFCAKRSNGKPNESDIKLRINKFYRPENTHKGFKATYHADINMLYW 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 214010196 1049 SDEEAVVDFSDVQGRCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKSFEDPPN 1105
Cdd:cd04711    81 SDEEATVDFSAVQGRCTVEYGEDLPESVQEYSGGGPDRFYFLEAYNAKTKSFEDPPN 137
BAH_Dnmt1_I cd04760
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 759-881 9.79e-64

BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5)-methyltransferases from Bilateria, Dnmt1 and similar proteins. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the genome. These effects include transcriptional repression via inhibition of transcription factor binding, the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting, and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240107  Cd Length: 124  Bit Score: 212.32  E-value: 9.79e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  759 ETLEVGDCVSVIPDDPSKPLYLARVTALWEDKN-GQMFHAHWFCAGTDTVLGATSDPLELFLVGECENMQLSYIHSKVKV 837
Cdd:cd04760     2 EELEAGDCVSVKPDDPTKPLYIARVTYMWKDSIgGKMFHAHWFCRGSDTVLGETSDPLELFLVDECEDMALSSIHGKVNV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 214010196  838 IYRGPSPNWAMEGGMDPEaMLPGAEDGKTYFYQFWYSQDYARFE 881
Cdd:cd04760    82 IYKAPSENWSMEGGMDEE-DEIFEDDGKTFFYQKWYDPECARFE 124
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
1141-1599 7.52e-63

DNA-cytosine methylase [Replication, recombination and repair];


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 215.83  E-value: 7.52e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1141 PKLRTLDVFSGCGGLTEGFHQAGIsETLWAIEMWEPAAQAFRLNNPGTTVFTEDcnvlLKLVMAGEVtnslgqrlpqKGD 1220
Cdd:COG0270     2 KKLTVIDLFAGAGGLSLGFEKAGF-EVVFAVEIDPDACETYRANFPEAKVIEGD----IRDIDPEEL----------IPD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1221 VEMLCGGPPCQGFSGMNRfnSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFRRSMVLKLTLRCLVRMGYQCTF 1300
Cdd:COG0270    67 VDLLIGGPPCQPFSVAGK--RKGLEDPRGTLFFEFIRIVEELRPKAFVLENVPGLLSSDKGKTFEEILKELEELGYRVDY 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1301 GVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLPE 1380
Cdd:COG0270   145 KVLNAADYGVPQNRERVFIVGFRKDLDLFEFPEPTH----------------------------LKPYVTVGDALEDLPD 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1381 iqngasapeisyngepqswfqrqlrgshyqpilrDHICKdmsalvaarmrhiplspgsdwrdlpniqvrlrdgvitnklr 1460
Cdd:COG0270   197 ----------------------------------AHEAR----------------------------------------- 201

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1461 ytfhdtkngcsstgalrgvcscaegktcdpasrqfntlipwclphtgnrhnhwaglygrlewdgFFSTTVTNpePMGKQG 1540
Cdd:COG0270   202 ----------------------------------------------------------------YLSETITA--GYGGGG 215

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 214010196 1541 RVLHPEQHRVVSVRECARSQGFPDTYRLFGNILDRHRQVGNAVPPPLAKAIGLEIKLCL 1599
Cdd:COG0270   216 RFLHPGEPRRLTVREAARLQGFPDDFKFPGSKTQAYRQIGNAVPPPLAEAIAKAILKAL 274
DNMT1-RFD pfam12047
Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a ...
 405-540 1.74e-51

Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a cytosine specific DNA methyltransferase enzyme. It functions non-catalytically to target the protein towards replication foci. This allows the DNMT1 protein to methylate the correct residues. This domain targets DMAP1 and HDAC2 to the replication foci during the S phase of mitosis. They are thought to have some importance in conversion of critical histone lysine moieties.


Pssm-ID: 463444  Cd Length: 143  Bit Score: 177.92  E-value: 1.74e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196   405 YDSSPMHKFTFFSVYCSRGHLCPVDTGLIEKNVELYFSGVAKAIHEENPSVEG-GVNGKN----LGPINQWWISGFDGGE 479
Cdd:pfam12047    1 EEDRPQRKLTDFELYDKDGHLCPFDVLLIEKNVDIFISGIVKPIDEDEPSLDGkGIEDKGmqikLGPIKEWTISGFDGGE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 214010196   480 KALIGFSTAFAEYFLMEPSPEYAPIFGLMQEKIYISKIVVEFLQSNP--DAVYEDLINKIETT 540
Cdd:pfam12047   81 KALIWLSTEFAWYKLLKPSAEYAPIYELVYEKARLSVEVVEFLQRSPgsELSYEDLINRVLTS 143
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
1143-1596 5.31e-40

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 151.70  E-value: 5.31e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1143 LRTLDVFSGCGGLTEGFHQAGIsETLWAIEMWEPAAQAFRLNNPgTTVFtedcnvllklvmaGEVTNSLGQRLPqkgDVE 1222
Cdd:pfam00145    1 FKFIDLFAGIGGFRLGLEQAGF-ECVAANEIDKSAAKTYEANFP-KVPI-------------GDITLIDIKDIP---DID 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1223 MLCGGPPCQGFS--GMNRFNSRTYskfkNSLVVSFLSYCDYYRPRFFLLENVRNFVSFRRSMVLKLTLRCLVRMGYQCTF 1300
Cdd:pfam00145   63 ILTGGFPCQDFSiaGKQKGFEDTR----GTLFFEIIRIIKEKKPKAFLLENVKGLLSHDNGNTLNVILETLEELGYHVSW 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1301 GVLQAGQYGVAQTRRRAIILAAAPG-EKLPLFPEPlhvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLP 1379
Cdd:pfam00145  139 KVLNASDYGVPQNRERVFIVGIRKDlNLNVLVPVP------------------------------EFDFPKPKDLTGTIR 188

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1380 EIQNGASAPEISYNGEpqswfqrqlrgshyqpilrDHICKDMSalvaaRMRHIPLSPGSDWRDLpNIQVRLRDGVITNKL 1459
Cdd:pfam00145  189 DLLEEPSLDENKYNLS-------------------DKFVENHE-----RRKPTTKAPGGGYPTY-LLRNRIDKVEEGKGP 243

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1460 RYTFHDtkngcsstgalrgvcscaegktcdpasrqfntlipwclphtgnrhnhwaglYGRLEwdgffsttVTNPEPMGKQ 1539
Cdd:pfam00145  244 SFTYRK---------------------------------------------------SGRPE--------APKTGILGKN 264

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 214010196  1540 GR--VLHPEQHRVVSVRECARSQGFPDTYRLFGNILDRHRQVGNAVPPPLAKAIGLEIK 1596
Cdd:pfam00145  265 GErfRGHPKNIRRLTPRECARLQGFPDDFIFPGSKTQLYKQIGNAVPVPVAEAIAKAIK 323
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
 1143-1596 1.12e-33

Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many aspects of biology. Cytosine-specific DNA methylases are found both in prokaryotes and eukaryotes. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the mammalian genome. These effects include transcriptional repression via inhibition of transcription factor binding or the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability.


Pssm-ID: 238192 [Multi-domain]  Cd Length: 275  Bit Score: 131.59  E-value: 1.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1143 LRTLDVFSGCGGLTEGFHQAGiSETLWAIEMWEPAAQAFRLNNPGTTVFtedcnvllklvmaGEVTNSLGQRLPqkGDVE 1222
Cdd:cd00315     1 LRVIDLFAGIGGFRLGLEKAG-FEIVAANEIDKSAAETYEANFPNKLIE-------------GDITKIDEKDFI--PDID 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1223 MLCGGPPCQGFS--GMNRFNSRTYSKfknslvvSFLSYCDY---YRPRFFLLENVRNFVSFRRSMVLKLTLRCLVRMGYQ 1297
Cdd:cd00315    65 LLTGGFPCQPFSiaGKRKGFEDTRGT-------LFFEIIRIlkeKKPKYFLLENVKGLLTHDNGNTLKVILNTLEELGYN 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1298 CTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFapracqlsvvvDDKKFVSNITRLSSGPFRTITVrdtmsd 1377
Cdd:cd00315   138 VYWKLLNASDYGVPQNRERVFIIGIRKDLILNFFSPFPKPS-----------EKKKTLKDILRIRDPDEPSPTL------ 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1378 lpeiqngasapeisyngepqswfqrqlrgshyqpilrdhickdmsalvaarmrhiplspgsdwrdlpniqvrlrdgvitn 1457
Cdd:cd00315       --------------------------------------------------------------------------------

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1458 klrytfhdtkngcsstgalrgvcscaegktcdpasrqfntlipwclphTGNRHNHWAGLYgrlewdgffsttvtnpepMG 1537
Cdd:cd00315   201 ------------------------------------------------TASYGKGTGSVH------------------PT 214

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1538 KQGRVLHPEQHRVVSVRECARSQGFPDTYRLFG-NILDRHRQVGNAVPPPLAKAIGLEIK 1596
Cdd:cd00315   215 APDMIGKESNIRRLTPRECARLQGFPDDFEFPGkSVTQAYRQIGNSVPVPVAEAIAKAIK 274
BAH smart00439
Bromo adjacent homology domain;
982-1104 2.05e-33

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 125.48  E-value: 2.05e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196    982 DYIKGSNLDAPEPYRIGRIKEIHCGKKkggkvNEADIKIRLYKFYRPENTHKSiqATYHADINLLYWSDEEAVVDFSDVQ 1061
Cdd:smart00439    6 DFVLVEPDDADEPYYIGRIEEIFETKK-----NSESKMVRVRWFYRPEETVLE--KAALFDKNEVFLSDEYDTVPLSDII 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 214010196   1062 GRCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKSFEDPP 1104
Cdd:smart00439   79 GKCNVLYKSDYPGLRPEGSIGEPDVFFCESAYDPEKGSFKKLP 121
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 975-1104 3.22e-30

BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.


Pssm-ID: 460207  Cd Length: 120  Bit Score: 116.25  E-value: 3.22e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196   975 EHYRKySDYIKGSNLDAPEPYRIGRIKEIHCGKKKGgkvneaDIKIRLYKFYRPENTHKSIQATYHADinLLYWSDEEAV 1054
Cdd:pfam01426    1 ETYSV-GDFVLVEPDDADEPYYVARIEELFEDTKNG------KKMVRVQWFYRPEETVHRAGKAFNKD--ELFLSDEEDD 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 214010196  1055 VDFSDVQGRCTVEYGEDLLESIQDYSqGGPDRFYFLEAYNSKTKSFEDPP 1104
Cdd:pfam01426   72 VPLSAIIGKCSVLHKSDLESLDPYKI-KEPDDFFCELLYDPKTKSFKKLP 120
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
 1147-1595 1.40e-29

DNA-methyltransferase (dcm); All proteins in this family for which functions are known are DNA-cytosine methyltransferases. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273211 [Multi-domain]  Cd Length: 315  Bit Score: 120.89  E-value: 1.40e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1147 DVFSGCGGLTEGFHQAGIsETLWAIEMWEPAAQAFRLNNPGTTVFtedcnvllklvmaGEVTNSLGQRLPqkgDVEMLCG 1226
Cdd:TIGR00675    3 DLFAGIGGIRLGFEQAGF-KCVFASEIDKYAQKTYEANFGNKVPF-------------GDITKISPSDIP---DFDILLG 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1227 GPPCQGFSgMNRFNsRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFRRSMVLKLTLRCLVRMGYQCTFGVLQAG 1306
Cdd:TIGR00675   66 GFPCQPFS-IAGKR-KGFEDTRGTLFFEIVRILKEKKPKFFLLENVKGLVSHDKGRTFKVIIETLEELGYKVYYKVLNAK 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1307 QYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlsSGPFRTITVRDtmsdlpeiqngas 1386
Cdd:TIGR00675  144 DFGVPQNRERIYIVGFRDFDDKLNFEFPKP--------------------------IYVAKKKRIGD------------- 184

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1387 APEISYNGEPqswfqrqlrgshyQPILRDHICKDMSaLVAARMRHIPLSpGSDWRDLpniqvrlrdgvitnklrytfhdt 1466
Cdd:TIGR00675  185 LLDLSVDLEE-------------KYYLSEEKKNGLL-LLLENMRKKEGT-GEQIGSF----------------------- 226

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  1467 kngcsstgalrgvcscaegKTCDPASRQFNTLipwclphTGNRHNHWAGlygrlewdgffstTVTNPEPMGKQGRVlHPE 1546
Cdd:TIGR00675  227 -------------------YNRESKSSIIRTL-------SARGYTFVKG-------------GKSVLIVPHKSTVV-HPG 266

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 214010196  1547 QHRVVSVRECARSQGFPDTYRLFGNILDRHRQVGNAVPPPLAKAIGLEI 1595
Cdd:TIGR00675  267 RIRRLTPRECARLQGFPDDFKFPVSDSQLYKQAGNAVVVPVIEAIAKQI 315
BAH smart00439
Bromo adjacent homology domain;
760-884 4.27e-26

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 104.68  E-value: 4.27e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196    760 TLEVGDCVSVIPDDPSKPLYLARVTALWEDKNGQ---MFHAHWFCAGTDTVLGAT--SDPLELFLVGECENMQLSYIHSK 834
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSeskMVRVRWFYRPEETVLEKAalFDKNEVFLSDEYDTVPLSDIIGK 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 214010196    835 VKVIYRGPSPNWAMEGGMDPEamlpgaedgKTYFYQFWYSQDYARFESPP 884
Cdd:smart00439   81 CNVLYKSDYPGLRPEGSIGEP---------DVFFCESAYDPEKGSFKKLP 121
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 759-884 5.18e-26

BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.


Pssm-ID: 460207  Cd Length: 120  Bit Score: 104.31  E-value: 5.18e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196   759 ETLEVGDCVSVIPDDPSKPLYLARVTALWEDKNG--QMFHAHWFCAGTDTV--LGATSDPLELFLVGECENMQLSYIHSK 834
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNgkKMVRVQWFYRPEETVhrAGKAFNKDELFLSDEEDDVPLSAIIGK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 214010196   835 VKVIYRGPSPNWAMEGGMDPeamlpgaedgKTYFYQFWYSQDYARFESPP 884
Cdd:pfam01426   81 CSVLHKSDLESLDPYKIKEP----------DDFFCELLYDPKTKSFKKLP 120
DMAP_binding pfam06464
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
 16-106 5.35e-24

DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.


Pssm-ID: 368923 [Multi-domain]  Cd Length: 104  Bit Score: 97.88  E-value: 5.35e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196    16 PAGSLPDHVRRRLKDLERDG----LTEKECVKEKLNLLHEFL---------QTEIKSQLCDLETKLHKEELSEEGYLAKV 82
Cdd:pfam06464    1 NPPSLPDDVRERLSELDLDLsegdITEKGYEKKKLKLLRKFLlhpetptklSAEAQNQLASLETKLRDEELSEEVYLEKV 80

                           90       100
                   ....*....|....*....|....
gi 214010196    83 KTLLNKDLCLENGTLSLTQKANGC 106
Cdd:pfam06464   81 KALLAKELERENGLNAPTKEQSGL 104
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 649-695 6.07e-19

CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases.


Pssm-ID: 366873  Cd Length: 48  Bit Score: 81.63  E-value: 6.07e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 214010196   649 ENTMKRRRCGVCEVCQQPE-CGKCKACKDMVKFGGTGRSKQACLKRRC 695
Cdd:pfam02008    1 RNRRKRRRCGVCEGCQRPEdCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 973-1100 1.64e-18

BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). BAH domains have first been described as domains found in the polybromo protein and Yeast Rsc1/Rsc2 (Remodeling of the Structure of Chromatin). They also occur in mammalian DNA methyltransferases and the MTA1 subunits of histone deacetylase complexes. A BAH domain is also found in Yeast Sir3p and in the origin receptor complex protein 1 (Orc1p), where it was found to interact with the N-terminal lobe of the silence information regulator 1 protein (Sir1p), confirming the initial hypothesis that BAH plays a role in protein-protein interactions.


Pssm-ID: 239835 [Multi-domain]  Cd Length: 123  Bit Score: 82.82  E-value: 1.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  973 YPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIHCGKkkggkvnEADIKIRLYKFYRPENTHKSiqATYHADINLLYWSDEE 1052
Cdd:cd04370     1 GITYEVGDSVYVEPDDSIKSDPPYIARIEELWEDT-------NGSKQVKVRWFYRPEETPKG--LSPFALRRELFLSDHL 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 214010196 1053 AVVDFSDVQGRCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKSF 1100
Cdd:cd04370    72 DEIPVESIIGKCKVLFVSEFEGLKQRPNKIDTDDFFCRLAYDPTTKEF 119
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 758-882 2.13e-17

BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). BAH domains have first been described as domains found in the polybromo protein and Yeast Rsc1/Rsc2 (Remodeling of the Structure of Chromatin). They also occur in mammalian DNA methyltransferases and the MTA1 subunits of histone deacetylase complexes. A BAH domain is also found in Yeast Sir3p and in the origin receptor complex protein 1 (Orc1p), where it was found to interact with the N-terminal lobe of the silence information regulator 1 protein (Sir1p), confirming the initial hypothesis that BAH plays a role in protein-protein interactions.


Pssm-ID: 239835 [Multi-domain]  Cd Length: 123  Bit Score: 79.74  E-value: 2.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  758 EETLEVGDCVSVIPDD--PSKPLYLARVTALWEDKNG-QMFHAHWFCAGTDTVLGATS--DPLELFLVGECENMQLSYIH 832
Cdd:cd04370     1 GITYEVGDSVYVEPDDsiKSDPPYIARIEELWEDTNGsKQVKVRWFYRPEETPKGLSPfaLRRELFLSDHLDEIPVESII 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 214010196  833 SKVKVIYrgPSPNWameggmdPEAMLPGAEDGKTYFYQFWYSQDYARFES 882
Cdd:cd04370    81 GKCKVLF--VSEFE-------GLKQRPNKIDTDDFFCRLAYDPTTKEFKA 121
BAH_plantDCM_II cd04708
BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5) ...
 931-1155 1.59e-14

BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5)-methyltransferases (DCM) from plants. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the genome. These effects include transcriptional repression via inhibition of transcription factor binding, the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting, and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240059  Cd Length: 202  Bit Score: 74.03  E-value: 1.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  931 TKNGVVYRLGDSVYLPPEAFTfnikmaspmkrskrdpvnenlypEHYRKYSDYIKGSNLDAPePYRIGRIKEIHCGKK-K 1009
Cdd:cd04708     2 VYDGVTYSVGDFLYVSPDAFA-----------------------EEERERATFKAGRNVGLK-AFVVCQVLEIVVEKEsK 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196 1010 GGKVNEADIKIRlyKFYRPENThkSIQATYHADINLLYWSDEEAVVDFSDVQGRCTVEYGEDLLESiQDYSQGGPdRFYF 1089
Cdd:cd04708    58 QADVASTQVKVR--RFYRPEDV--SPEKAYASDIREVYYSEDTLTVPVEAVEGKCEVRKKSDLPDS-DAPVIFEH-VFFC 131

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 214010196 1090 LEAYNSKTKSFEDPPNHARSPGNKGKGKGKGKGK-----GKPQVSEPKEPEAAIKLPKLRTLDVFSGCGGL 1155
Cdd:cd04708   132 ELLYDPAKGSLKQLPPNIKEEAYSTGASDSALRKrkgkgKGDSESDSEAPVKAPKENRLATLDIFAGCGGL 202
BAH_fungalPHD cd04710
BAH, or Bromo Adjacent Homology domain, as present in fungal proteins containing PHD domains. ...
 974-1102 2.53e-08

BAH, or Bromo Adjacent Homology domain, as present in fungal proteins containing PHD domains. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240061  Cd Length: 135  Bit Score: 54.30  E-value: 2.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  974 PEHYRKySDYIKGSNLDAPEPYRIGRIKEI----HCGKKKGGKVNEA-DIKIRLYKFYRPenthKSIQATYHADINLLYW 1048
Cdd:cd04710     9 GELLKV-NDHIYMSSEPPGEPYYIGRIMEFvpkhEFPSGIHARVFPAsYFQVRLNWYYRP----RDISRRVVADSRLLYA 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 214010196 1049 SDEEAVVDFSDVQGRCTVEYgEDLLESIQDYSQgGPDRFYFLEAYNSKTKSFED 1102
Cdd:cd04710    84 SMHSDICPIGSVRGKCTVRH-RDQIPDLEEYKK-RPNHFYFDQLFDRYILRYYD 135
BAH_DCM_I cd04712
BAH, or Bromo Adjacent Homology domain, as present in DNA (Cytosine-5)-methyltransferases (DCM) ...
 756-839 1.62e-06

BAH, or Bromo Adjacent Homology domain, as present in DNA (Cytosine-5)-methyltransferases (DCM) 1. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the genome. These effects include transcriptional repression via inhibition of transcription factor binding, the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting, and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240063  Cd Length: 130  Bit Score: 48.94  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  756 IDEETLEVGDCVSVIPDDPSKPLYLA----------RVTALWEDKNG-QMFHAHWFCAGTDTVLGATSDPLELFLVGECE 824
Cdd:cd04712     1 IHGLTIRVGDVVSVERDDADSTTKWNddhrwlplvqFVEYMKKGSDGsKMFHGRWLYRGCDTVLGNYANERELFLTNECT 80

                          90
                  ....*....|....*
gi 214010196  825 NMQLSYIHSKVKVIY 839
Cdd:cd04712    81 CLELDLLSTEIKGVH 95
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 109-327 7.08e-06

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 50.67  E-value: 7.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  109 NGSRPTWKAEMADSNRSPRSRPKPRGPRRSKSDSETMIEASSSSVATRRTTRQTTITSHFKGPAKRKPKEDSEKGnanes 188
Cdd:PRK12678   60 GGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERG----- 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  189 AAEERDQDKKRRVAGTESRASRAGESVEKPERVRPGtqlcQEEQGEQEDDRRPRRQTRELASRRKSREDPDREARPGTHL 268
Cdd:PRK12678  135 EAARRGAARKAGEGGEQPATEARADAAERTEEEERD----ERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRRE 210

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 214010196  269 DVDDDDEKDKRSSRPRSQPRDLATKRRPKEEVEQITPEPPEGKDEDEREEKRRKTTRKK 327
Cdd:PRK12678  211 QGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDR 269
rne PRK10811
ribonuclease E; Reviewed
 168-357 2.23e-05

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 49.27  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  168 FKGPAKRKPKEDSEKGNANEsaaEERDQDkkRRVAGTESRASRAGESVEKPERVRpgtqlcqEEQGEQ-EDDRRPRRQTR 246
Cdd:PRK10811  580 FSGGEETKPQEQPAPKAEAK---PERQQD--RRKPRQNNRRDRNERRDTRDNRTR-------REGRENrEENRRNRRQAQ 647

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  247 ElasrrksREDPDREARPGTHLDVDDDDEKDKRSSRPRSQPRDLATKRRPKEEVEQITPEPPEGKDEDEREEKRRKTTRK 326
Cdd:PRK10811  648 Q-------QTAETRESQQAEVTEKARTQDEQQQAPRRERQRRRNDEKRQAQQEAKALNVEEQSVQETEQEERVQQVQPRR 720

                         170       180       190
                  ....*....|....*....|....*....|...
gi 214010196  327 KPEPLS--IPVQSRVERKASQGKASAIPKLNPP 357
Cdd:PRK10811  721 KQRQLNqkVRIEQSVAEEAVAPVVEETVAAEPV 753
PTZ00121 PTZ00121
MAEBL; Provisional
 172-350 2.75e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  172 AKRKPKEDSEKGNANESAAEERDQDKKRRV----AGTESRAS---RAGESVEKPERVRPGTQLCQEEQGEQEDDRRPRRQ 244
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAKKAEEAKKAdeakKAEEAKKAdeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE 1574

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  245 TRELASRRKSREDPDREARPGTHLDVDDDDEKDK-RSSRPRSQPRDLATKRRPKEEVEQitpePPEGKDEDEREEKRRKT 323
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaEEAKKAEEAKIKAEELKKAEEEKK----KVEQLKKKEAEEKKKAE 1650

                         170       180
                  ....*....|....*....|....*..
gi 214010196  324 TRKKPEPLSIPVQSRVERKASQGKASA 350
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKA 1677
BAH_polybromo cd04717
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human ...
 761-800 2.94e-05

BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human polybromo protein (BAF180) is a component of the SWI/SNF chromatin-remodeling complex PBAF. It is thought that polybromo participates in transcriptional regulation. Saccharomyces cerevisiae RSC1 and RSC2 are part of the 15-subunit nucleosome remodeling RSC complex. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240068  Cd Length: 121  Bit Score: 44.88  E-value: 2.94e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 214010196  761 LEVGDCVSVIPDDPSKPLYLARVTALWEDKNGQ-MFHAHWF 800
Cdd:cd04717     4 YRVGDCVYVANPEDPSKPIIFRIERLWKDEDGEkFFFGCWF 44
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 758-800 6.04e-05

BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. BAHCC1 stands for BAH domain and coiled-coil containing 1. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240065  Cd Length: 121  Bit Score: 44.31  E-value: 6.04e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 214010196  758 EETLEVGDCVSVIPDDPSKPLYLARVTALWEDKNGQM-FHAHWF 800
Cdd:cd04714     1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMvVRVKWY 44
PTZ00121 PTZ00121
MAEBL; Provisional
 169-329 1.11e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  169 KGPAKRKPKEDSEKGNANESAAEERDQDKKRRVAGTESRASRAGESVEKPERvRPGTQLCQEEQGEQEDDRRPRRQTREL 248
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE-ENKIKAAEEAKKAEEDKKKAEEAKKAE 1684

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  249 ASRRKSREDPDREARpgthldvddDDEKDKRSSRPRSQPRDLATKRRPKEEVEQITPEppEGKDEDEREEKRRKTTRKKP 328
Cdd:PTZ00121 1685 EDEKKAAEALKKEAE---------EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE--EAKKEAEEDKKKAEEAKKDE 1753


                  .
gi 214010196  329 E 329
Cdd:PTZ00121 1754 E 1754
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 107-321 3.70e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 45.28  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  107 PANGSRPTWKAEMADSNRSPRSRPKPRGPRRSKSDSETMIEASSSSVATRRTTRQTTITSHfkgPAKRKPKEDSEKGNAN 186
Cdd:PRK12678   75 AAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGE---AARRGAARKAGEGGEQ 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  187 ESAAEERDQDKKRRVAGTESRASRAGESVEKPERVRPGTQLCQEEQ--GEQEDDRRPRRQTRElASRRKSREDPDREARP 264
Cdd:PRK12678  152 PATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGrdGDDRDRRDRREQGDR-REERGRRDGGDRRGRR 230

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 214010196  265 GthldvddddekdkRSSRPRSQPRDLATKRRPKEEVEQITPEPPEGKDEDEREEKRR 321
Cdd:PRK12678  231 R-------------RRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGR 274
Caldesmon pfam02029
Caldesmon;
173-353 4.87e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.39  E-value: 4.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196   173 KRKPKEDSEKGNANESAAEERDQDKKrrvagTESRASRAGESVEKPERvRPGTQlcqEEQG--EQEDDRRPRRQTR--EL 248
Cdd:pfam02029   12 RRRAREERRRQKEEEEPSGQVTESVE-----PNEHNSYEEDSELKPSG-QGGLD---EEEAflDRTAKREERRQKRlqEA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196   249 ASRRKSREDPDREARPGTHLDVDDDDEKDKRSSRPRSQPRDL-------ATKRRPKEEVEQITP-EPPEGKDEDEREEKR 320
Cdd:pfam02029   83 LERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRlgrykeeETEIREKEYQENKWStEVRQAEEEGEEEEDK 162

                          170       180       190
                   ....*....|....*....|....*....|...
gi 214010196   321 RKTTRKKPEPLSIPVQSRVERKASQGKASAIPK 353
Cdd:pfam02029  163 SEEAEEVPTENFAKEEVKDEKIKKEKKVKYESK 195
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 100-263 5.61e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 41.43  E-value: 5.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  100 TQKANGCPANGSRPTWKAEMADSNRSPRSRPKPRGPRRSKSDSETMIEASSSSVATRRTTRQTTITSHFKGPAKRKPKED 179
Cdd:PRK12678   76 AARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATE 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010196  180 SEKGNANESAAEERDQDKKRRVAGTESRASRAGESVEKPERVRPGTQLCQE---EQGEQEDDR--RPRRQTRELASRRKS 254
Cdd:PRK12678  156 ARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRdrrEQGDRREERgrRDGGDRRGRRRRRDR 235


                  ....*....
gi 214010196  255 REDPDREAR 263
Cdd:PRK12678  236 RDARGDDNR 244
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH