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Conserved domains on  [gi|119604486|gb|EAW84080|]
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DNA (cytosine-5-)-methyltransferase 1, isoform CRA_a [Homo sapiens]

Protein Classification

DNA (cytosine-5)-methyltransferase 1( domain architecture ID 10534294)

DNA (cytosine-5)-methyltransferase 1 preferentially methylates CpG residues in hemimethylated DNA and associates with DNA replication sites in S phase, maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication. It is responsible for maintaining methylation patterns established in development.

Gene Symbol:  DNMT1
Gene Ontology:  GO:0003886|GO:0003677|GO:0009008|GO:0008327|GO:0010424
PubMed:  11005794|35410490|21507353

Graphical summary

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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) ...
 1027-1163 2.23e-90

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: 289.01  E-value: 2.23e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1027 DEDLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNKFYRPENTHKSTPASYHADINLLYW 1106
Cdd:cd04711     1 DEDLYPEYYRKSSDYIKGSNLDAPEPFRIGRIKEIFCAKRSNGKPNESDIKLRINKFYRPENTHKGFKATYHADINMLYW 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119604486 1107 SDEEAVVDFKAVQGRCTVEYGEDLPECVQVYSMGGPNRFYFLEAYNAKSKSFEDPPN 1163
Cdd:cd04711    81 SDEEATVDFSAVQGRCTVEYGEDLPESVQEYSGGGPDRFYFLEAYNAKTKSFEDPPN 137
BAH_Dnmt1_I cd04760
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 816-939 2.07e-72

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: 237.36  E-value: 2.07e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  816 AETLEVGDCVSVIPDDSSKPLYLARVTALWEDSSNGQMFHAHWFCAGTDTVLGATSDPLELFLVDECEDMQLSYIHSKVK 895
Cdd:cd04760     1 GEELEAGDCVSVKPDDPTKPLYIARVTYMWKDSIGGKMFHAHWFCRGSDTVLGETSDPLELFLVDECEDMALSSIHGKVN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 119604486  896 VIYKAPSENWAMEGGMDPESLLEGDDGKTYFYQLWYDQDYARFE 939
Cdd:cd04760    81 VIYKAPSENWSMEGGMDEEDEIFEDDGKTFFYQKWYDPECARFE 124
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
1199-1655 2.82e-61

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


:

Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 211.59  E-value: 2.82e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1199 PKLRTLDVFSGCGGLSEGFHQAGIsDTLWAIEMWDPAAQAFRLNNPGSTVFTEDcnilLKLVMAGETtnsrgqrlpqKGD 1278
Cdd:COG0270     2 KKLTVIDLFAGAGGLSLGFEKAGF-EVVFAVEIDPDACETYRANFPEAKVIEGD----IRDIDPEEL----------IPD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1279 VEMLCGGPPCQGFSGMNRfnSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTF 1358
Cdd:COG0270    67 VDLLIGGPPCQPFSVAGK--RKGLEDPRGTLFFEFIRIVEELRPKAFVLENVPGLLSSDKGKTFEEILKELEELGYRVDY 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1359 GVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLPE 1438
Cdd:COG0270   145 KVLNAADYGVPQNRERVFIVGFRKDLDLFEFPEPTH----------------------------LKPYVTVGDALEDLPD 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1439 vrngasaleisyngepqswfqrqlrgaqyqpilrDHICKdmsalvaarmrhiplapgsdwrdlpnievrlsdgtmarklr 1518
Cdd:COG0270   197 ----------------------------------AHEAR----------------------------------------- 201

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1519 ythhdrkngrsssgalrgvcscveagkacdpaarqfntlipwclphtgnrhnhwaglygrlewdgFFSTTVTNpePMGKQ 1598
Cdd:COG0270   202 -----------------------------------------------------------------YLSETITA--GYGGG 214

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119604486 1599 GRVLHPEQHRVVSVRECARSQGFPDTYRLFGNILDKHRQVGNAVPPPLAKAIGLEIK 1655
Cdd:COG0270   215 GRFLHPGEPRRLTVREAARLQGFPDDFKFPGSKTQAYRQIGNAVPPPLAEAIAKAIL 271
DNMT1-RFD pfam12047
Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a ...
 461-596 2.66e-55

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: 189.09  E-value: 2.66e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486   461 YEALPQHKLTCFSVYCKHGHLCPIDTGLIEKNIELFFSGSAKPIYDDDPSLEG-GVNGKN----LGPINEWWITGFDGGE 535
Cdd:pfam12047    1 EEDRPQRKLTDFELYDKDGHLCPFDVLLIEKNVDIFISGIVKPIDEDEPSLDGkGIEDKGmqikLGPIKEWTISGFDGGE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119604486   536 KALIGFSTSFAEYILMDPSPEYAPIFGLMQEKIYISKIVVEFLQSN--SDSTYEDLINKIETT 596
Cdd:pfam12047   81 KALIWLSTEFAWYKLLKPSAEYAPIYELVYEKARLSVEVVEFLQRSpgSELSYEDLINRVLTS 143
DMAP_binding pfam06464
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
 78-167 3.28e-27

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


:

Pssm-ID: 368923 [Multi-domain]  Cd Length: 104  Bit Score: 107.12  E-value: 3.28e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486    78 PAISLPDDVRRRLKDLERDS----LTEKECVKEKLNLLHEFL---------QTEIKNQLCDLETKLRKEELSEEGYLAKV 144
Cdd:pfam06464    1 NPPSLPDDVRERLSELDLDLsegdITEKGYEKKKLKLLRKFLlhpetptklSAEAQNQLASLETKLRDEELSEEVYLEKV 80

                           90       100
                   ....*....|....*....|...
gi 119604486   145 KSLLNKDLSLENGAHAYNREVNG 167
Cdd:pfam06464   81 KALLAKELERENGLNAPTKEQSG 103
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 707-753 5.22e-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: 82.02  E-value: 5.22e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 119604486   707 ENAFKRRRCGVCEVCQQPE-CGKCKACKDMVKFGGSGRSKQACQERRC 753
Cdd:pfam02008    1 RNRRKRRRCGVCEGCQRPEdCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
 
Name Accession Description Interval E-value
BAH_Dnmt1_II cd04711
BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5) ...
 1027-1163 2.23e-90

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: 289.01  E-value: 2.23e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1027 DEDLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNKFYRPENTHKSTPASYHADINLLYW 1106
Cdd:cd04711     1 DEDLYPEYYRKSSDYIKGSNLDAPEPFRIGRIKEIFCAKRSNGKPNESDIKLRINKFYRPENTHKGFKATYHADINMLYW 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119604486 1107 SDEEAVVDFKAVQGRCTVEYGEDLPECVQVYSMGGPNRFYFLEAYNAKSKSFEDPPN 1163
Cdd:cd04711    81 SDEEATVDFSAVQGRCTVEYGEDLPESVQEYSGGGPDRFYFLEAYNAKTKSFEDPPN 137
BAH_Dnmt1_I cd04760
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 816-939 2.07e-72

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: 237.36  E-value: 2.07e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  816 AETLEVGDCVSVIPDDSSKPLYLARVTALWEDSSNGQMFHAHWFCAGTDTVLGATSDPLELFLVDECEDMQLSYIHSKVK 895
Cdd:cd04760     1 GEELEAGDCVSVKPDDPTKPLYIARVTYMWKDSIGGKMFHAHWFCRGSDTVLGETSDPLELFLVDECEDMALSSIHGKVN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 119604486  896 VIYKAPSENWAMEGGMDPESLLEGDDGKTYFYQLWYDQDYARFE 939
Cdd:cd04760    81 VIYKAPSENWSMEGGMDEEDEIFEDDGKTFFYQKWYDPECARFE 124
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
1199-1655 2.82e-61

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


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 211.59  E-value: 2.82e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1199 PKLRTLDVFSGCGGLSEGFHQAGIsDTLWAIEMWDPAAQAFRLNNPGSTVFTEDcnilLKLVMAGETtnsrgqrlpqKGD 1278
Cdd:COG0270     2 KKLTVIDLFAGAGGLSLGFEKAGF-EVVFAVEIDPDACETYRANFPEAKVIEGD----IRDIDPEEL----------IPD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1279 VEMLCGGPPCQGFSGMNRfnSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTF 1358
Cdd:COG0270    67 VDLLIGGPPCQPFSVAGK--RKGLEDPRGTLFFEFIRIVEELRPKAFVLENVPGLLSSDKGKTFEEILKELEELGYRVDY 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1359 GVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLPE 1438
Cdd:COG0270   145 KVLNAADYGVPQNRERVFIVGFRKDLDLFEFPEPTH----------------------------LKPYVTVGDALEDLPD 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1439 vrngasaleisyngepqswfqrqlrgaqyqpilrDHICKdmsalvaarmrhiplapgsdwrdlpnievrlsdgtmarklr 1518
Cdd:COG0270   197 ----------------------------------AHEAR----------------------------------------- 201

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1519 ythhdrkngrsssgalrgvcscveagkacdpaarqfntlipwclphtgnrhnhwaglygrlewdgFFSTTVTNpePMGKQ 1598
Cdd:COG0270   202 -----------------------------------------------------------------YLSETITA--GYGGG 214

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119604486 1599 GRVLHPEQHRVVSVRECARSQGFPDTYRLFGNILDKHRQVGNAVPPPLAKAIGLEIK 1655
Cdd:COG0270   215 GRFLHPGEPRRLTVREAARLQGFPDDFKFPGSKTQAYRQIGNAVPPPLAEAIAKAIL 271
DNMT1-RFD pfam12047
Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a ...
 461-596 2.66e-55

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: 189.09  E-value: 2.66e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486   461 YEALPQHKLTCFSVYCKHGHLCPIDTGLIEKNIELFFSGSAKPIYDDDPSLEG-GVNGKN----LGPINEWWITGFDGGE 535
Cdd:pfam12047    1 EEDRPQRKLTDFELYDKDGHLCPFDVLLIEKNVDIFISGIVKPIDEDEPSLDGkGIEDKGmqikLGPIKEWTISGFDGGE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119604486   536 KALIGFSTSFAEYILMDPSPEYAPIFGLMQEKIYISKIVVEFLQSN--SDSTYEDLINKIETT 596
Cdd:pfam12047   81 KALIWLSTEFAWYKLLKPSAEYAPIYELVYEKARLSVEVVEFLQRSpgSELSYEDLINRVLTS 143
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
1201-1655 1.12e-38

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 147.84  E-value: 1.12e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1201 LRTLDVFSGCGGLSEGFHQAGIsDTLWAIEMWDPAAQAFRLNNPgSTVFtedcnillklvmaGETTNSRGQRLPqkgDVE 1280
Cdd:pfam00145    1 FKFIDLFAGIGGFRLGLEQAGF-ECVAANEIDKSAAKTYEANFP-KVPI-------------GDITLIDIKDIP---DID 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1281 MLCGGPPCQGFS--GMNRFNSRTYskfkNSLVVSFLSYCDYYRPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTF 1358
Cdd:pfam00145   63 ILTGGFPCQDFSiaGKQKGFEDTR----GTLFFEIIRIIKEKKPKAFLLENVKGLLSHDNGNTLNVILETLEELGYHVSW 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1359 GVLQAGQYGVAQTRRRAIILAAAPG-EKLPLFPEPlhvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLP 1437
Cdd:pfam00145  139 KVLNASDYGVPQNRERVFIVGIRKDlNLNVLVPVP------------------------------EFDFPKPKDLTGTIR 188

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1438 EVRNGASALEISYNGEpqswfqrqlrgaqyqpilrDHICKDMSalvaaRMRHIPLAPGSDWRDLPNIEvRLSDGTMARKL 1517
Cdd:pfam00145  189 DLLEEPSLDENKYNLS-------------------DKFVENHE-----RRKPTTKAPGGGYPTYLLRN-RIDKVEEGKGP 243

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1518 RYTHhdRKNGRsssgalrgvcscveagkacdpaarqfntlipWCLPHTGnrhnhwaglygrlewdgffsttvtnpePMGK 1597
Cdd:pfam00145  244 SFTY--RKSGR-------------------------------PEAPKTG---------------------------ILGK 263

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1598 QGR--VLHPEQHRVVSVRECARSQGFPDTYRLFGNILDKHRQVGNAVPPPLAKAIGLEIK 1655
Cdd:pfam00145  264 NGErfRGHPKNIRRLTPRECARLQGFPDDFIFPGSKTQLYKQIGNAVPVPVAEAIAKAIK 323
BAH smart00439
Bromo adjacent homology domain;
1040-1162 2.18e-35

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 131.26  E-value: 2.18e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486   1040 DYIKGSNLDAPEPYRIGRIKEIFCPKKsngrpNETDIKIRVNKFYRPENTHKStpASYHADINLLYWSDEEAVVDFKAVQ 1119
Cdd:smart00439    6 DFVLVEPDDADEPYYIGRIEEIFETKK-----NSESKMVRVRWFYRPEETVLE--KAALFDKNEVFLSDEYDTVPLSDII 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 119604486   1120 GRCTVEYGEDLPECVQVYSMGGPNRFYFLEAYNAKSKSFEDPP 1162
Cdd:smart00439   79 GKCNVLYKSDYPGLRPEGSIGEPDVFFCESAYDPEKGSFKKLP 121
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 1033-1162 5.10e-32

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: 121.65  E-value: 5.10e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1033 EHYRKySDYIKGSNLDAPEPYRIGRIKEIFCPKKSNgrpnetDIKIRVNKFYRPENTHKSTPASYHADinLLYWSDEEAV 1112
Cdd:pfam01426    1 ETYSV-GDFVLVEPDDADEPYYVARIEELFEDTKNG------KKMVRVQWFYRPEETVHRAGKAFNKD--ELFLSDEEDD 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 119604486  1113 VDFKAVQGRCTVEYGEDLPECvQVYSMGGPNRFYFLEAYNAKSKSFEDPP 1162
Cdd:pfam01426   72 VPLSAIIGKCSVLHKSDLESL-DPYKIKEPDDFFCELLYDPKTKSFKKLP 120
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
 1201-1655 1.29e-31

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: 125.81  E-value: 1.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1201 LRTLDVFSGCGGLSEGFHQAGiSDTLWAIEMWDPAAQAFRLNNPgstvftedcnillKLVMAGETTNSRGQRLPqkGDVE 1280
Cdd:cd00315     1 LRVIDLFAGIGGFRLGLEKAG-FEIVAANEIDKSAAETYEANFP-------------NKLIEGDITKIDEKDFI--PDID 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1281 MLCGGPPCQGFS--GMNRFNSRTYSKfknslvvSFLSYCDY---YRPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQ 1355
Cdd:cd00315    65 LLTGGFPCQPFSiaGKRKGFEDTRGT-------LFFEIIRIlkeKKPKYFLLENVKGLLTHDNGNTLKVILNTLEELGYN 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1356 CTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFapracqlsvvvDDKKFVSNITRLSSGPFRTITVrdtmsd 1435
Cdd:cd00315   138 VYWKLLNASDYGVPQNRERVFIIGIRKDLILNFFSPFPKPS-----------EKKKTLKDILRIRDPDEPSPTL------ 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1436 lpevrngasaleisyngepqswfqrqlrgaqyqpilrdhickdmsalvaarmrhiplapgsdwrdlpnievrlsdgtmar 1515
Cdd:cd00315       --------------------------------------------------------------------------------

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1516 klrythhdrkngrsssgalrgvcscveagkacdpaarqfntlipwclphTGNRHNHWAGLYgrlewdgffsttvtnpepM 1595
Cdd:cd00315   201 -------------------------------------------------TASYGKGTGSVH------------------P 213

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119604486 1596 GKQGRVLHPEQHRVVSVRECARSQGFPDTYRLFG-NILDKHRQVGNAVPPPLAKAIGLEIK 1655
Cdd:cd00315   214 TAPDMIGKESNIRRLTPRECARLQGFPDDFEFPGkSVTQAYRQIGNSVPVPVAEAIAKAIK 274
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
 1205-1654 2.88e-30

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: 123.21  E-value: 2.88e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1205 DVFSGCGGLSEGFHQAGIsDTLWAIEmWDPAAQA-FRLNnpgstvFTEDCNIllklvmaGETTNSRGQRLPqkgDVEMLC 1283
Cdd:TIGR00675    3 DLFAGIGGIRLGFEQAGF-KCVFASE-IDKYAQKtYEAN------FGNKVPF-------GDITKISPSDIP---DFDILL 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1284 GGPPCQGFSgMNRFNsRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTFGVLQA 1363
Cdd:TIGR00675   65 GGFPCQPFS-IAGKR-KGFEDTRGTLFFEIVRILKEKKPKFFLLENVKGLVSHDKGRTFKVIIETLEELGYKVYYKVLNA 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1364 GQYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlsSGPFRTITVRDtmsdlpevrnga 1443
Cdd:TIGR00675  143 KDFGVPQNRERIYIVGFRDFDDKLNFEFPKP--------------------------IYVAKKKRIGD------------ 184

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1444 sALEISYNGEPqswfqrqlrgaqyQPILRDHICKDMSALvaarmrhiplapgsdwrdlpnievrlsdgtmarklrythhd 1523
Cdd:TIGR00675  185 -LLDLSVDLEE-------------KYYLSEEKKNGLLLL----------------------------------------- 209

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1524 RKNGRSSSGALrgvcscveagkacdpaaRQFNTLipwclphtgNRHNHWAGLYGRLEWDGFFSTTVTNPEPMGKQGR-VL 1602
Cdd:TIGR00675  210 LENMRKKEGTG-----------------EQIGSF---------YNRESKSSIIRTLSARGYTFVKGGKSVLIVPHKStVV 263

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 119604486  1603 HPEQHRVVSVRECARSQGFPDTYRLFGNILDKHRQVGNAVPPPLAKAIGLEI 1654
Cdd:TIGR00675  264 HPGRIRRLTPRECARLQGFPDDFKFPVSDSQLYKQAGNAVVVPVIEAIAKQI 315
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 817-942 2.96e-29

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: 113.56  E-value: 2.96e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486   817 ETLEVGDCVSVIPDDSSKPLYLARVTALWEDSSNG-QMFHAHWFCAGTDTV--LGATSDPLELFLVDECEDMQLSYIHSK 893
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGkKMVRVQWFYRPEETVhrAGKAFNKDELFLSDEEDDVPLSAIIGK 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 119604486   894 VKVIYKAPSENWAMEggmdpesllEGDDGKTYFYQLWYDQDYARFESPP 942
Cdd:pfam01426   81 CSVLHKSDLESLDPY---------KIKEPDDFFCELLYDPKTKSFKKLP 120
BAH smart00439
Bromo adjacent homology domain;
818-942 5.69e-29

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 112.77  E-value: 5.69e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486    818 TLEVGDCVSVIPDDSSKPLYLARVTALWEDSSNGQ--MFHAHWFCAGTDTVLGAT--SDPLELFLVDECEDMQLSYIHSK 893
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSEskMVRVRWFYRPEETVLEKAalFDKNEVFLSDEYDTVPLSDIIGK 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 119604486    894 VKVIYKAPSENWAMEGGMDPEsllegddgKTYFYQLWYDQDYARFESPP 942
Cdd:smart00439   81 CNVLYKSDYPGLRPEGSIGEP--------DVFFCESAYDPEKGSFKKLP 121
DMAP_binding pfam06464
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
 78-167 3.28e-27

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


Pssm-ID: 368923 [Multi-domain]  Cd Length: 104  Bit Score: 107.12  E-value: 3.28e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486    78 PAISLPDDVRRRLKDLERDS----LTEKECVKEKLNLLHEFL---------QTEIKNQLCDLETKLRKEELSEEGYLAKV 144
Cdd:pfam06464    1 NPPSLPDDVRERLSELDLDLsegdITEKGYEKKKLKLLRKFLlhpetptklSAEAQNQLASLETKLRDEELSEEVYLEKV 80

                           90       100
                   ....*....|....*....|...
gi 119604486   145 KSLLNKDLSLENGAHAYNREVNG 167
Cdd:pfam06464   81 KALLAKELERENGLNAPTKEQSG 103
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 707-753 5.22e-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: 82.02  E-value: 5.22e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 119604486   707 ENAFKRRRCGVCEVCQQPE-CGKCKACKDMVKFGGSGRSKQACQERRC 753
Cdd:pfam02008    1 RNRRKRRRCGVCEGCQRPEdCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
 
Name Accession Description Interval E-value
BAH_Dnmt1_II cd04711
BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5) ...
 1027-1163 2.23e-90

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: 289.01  E-value: 2.23e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1027 DEDLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNKFYRPENTHKSTPASYHADINLLYW 1106
Cdd:cd04711     1 DEDLYPEYYRKSSDYIKGSNLDAPEPFRIGRIKEIFCAKRSNGKPNESDIKLRINKFYRPENTHKGFKATYHADINMLYW 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119604486 1107 SDEEAVVDFKAVQGRCTVEYGEDLPECVQVYSMGGPNRFYFLEAYNAKSKSFEDPPN 1163
Cdd:cd04711    81 SDEEATVDFSAVQGRCTVEYGEDLPESVQEYSGGGPDRFYFLEAYNAKTKSFEDPPN 137
BAH_Dnmt1_I cd04760
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 816-939 2.07e-72

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: 237.36  E-value: 2.07e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  816 AETLEVGDCVSVIPDDSSKPLYLARVTALWEDSSNGQMFHAHWFCAGTDTVLGATSDPLELFLVDECEDMQLSYIHSKVK 895
Cdd:cd04760     1 GEELEAGDCVSVKPDDPTKPLYIARVTYMWKDSIGGKMFHAHWFCRGSDTVLGETSDPLELFLVDECEDMALSSIHGKVN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 119604486  896 VIYKAPSENWAMEGGMDPESLLEGDDGKTYFYQLWYDQDYARFE 939
Cdd:cd04760    81 VIYKAPSENWSMEGGMDEEDEIFEDDGKTFFYQKWYDPECARFE 124
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
1199-1655 2.82e-61

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


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 211.59  E-value: 2.82e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1199 PKLRTLDVFSGCGGLSEGFHQAGIsDTLWAIEMWDPAAQAFRLNNPGSTVFTEDcnilLKLVMAGETtnsrgqrlpqKGD 1278
Cdd:COG0270     2 KKLTVIDLFAGAGGLSLGFEKAGF-EVVFAVEIDPDACETYRANFPEAKVIEGD----IRDIDPEEL----------IPD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1279 VEMLCGGPPCQGFSGMNRfnSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTF 1358
Cdd:COG0270    67 VDLLIGGPPCQPFSVAGK--RKGLEDPRGTLFFEFIRIVEELRPKAFVLENVPGLLSSDKGKTFEEILKELEELGYRVDY 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1359 GVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLPE 1438
Cdd:COG0270   145 KVLNAADYGVPQNRERVFIVGFRKDLDLFEFPEPTH----------------------------LKPYVTVGDALEDLPD 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1439 vrngasaleisyngepqswfqrqlrgaqyqpilrDHICKdmsalvaarmrhiplapgsdwrdlpnievrlsdgtmarklr 1518
Cdd:COG0270   197 ----------------------------------AHEAR----------------------------------------- 201

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1519 ythhdrkngrsssgalrgvcscveagkacdpaarqfntlipwclphtgnrhnhwaglygrlewdgFFSTTVTNpePMGKQ 1598
Cdd:COG0270   202 -----------------------------------------------------------------YLSETITA--GYGGG 214

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119604486 1599 GRVLHPEQHRVVSVRECARSQGFPDTYRLFGNILDKHRQVGNAVPPPLAKAIGLEIK 1655
Cdd:COG0270   215 GRFLHPGEPRRLTVREAARLQGFPDDFKFPGSKTQAYRQIGNAVPPPLAEAIAKAIL 271
DNMT1-RFD pfam12047
Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a ...
 461-596 2.66e-55

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: 189.09  E-value: 2.66e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486   461 YEALPQHKLTCFSVYCKHGHLCPIDTGLIEKNIELFFSGSAKPIYDDDPSLEG-GVNGKN----LGPINEWWITGFDGGE 535
Cdd:pfam12047    1 EEDRPQRKLTDFELYDKDGHLCPFDVLLIEKNVDIFISGIVKPIDEDEPSLDGkGIEDKGmqikLGPIKEWTISGFDGGE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119604486   536 KALIGFSTSFAEYILMDPSPEYAPIFGLMQEKIYISKIVVEFLQSN--SDSTYEDLINKIETT 596
Cdd:pfam12047   81 KALIWLSTEFAWYKLLKPSAEYAPIYELVYEKARLSVEVVEFLQRSpgSELSYEDLINRVLTS 143
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
1201-1655 1.12e-38

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 147.84  E-value: 1.12e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1201 LRTLDVFSGCGGLSEGFHQAGIsDTLWAIEMWDPAAQAFRLNNPgSTVFtedcnillklvmaGETTNSRGQRLPqkgDVE 1280
Cdd:pfam00145    1 FKFIDLFAGIGGFRLGLEQAGF-ECVAANEIDKSAAKTYEANFP-KVPI-------------GDITLIDIKDIP---DID 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1281 MLCGGPPCQGFS--GMNRFNSRTYskfkNSLVVSFLSYCDYYRPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTF 1358
Cdd:pfam00145   63 ILTGGFPCQDFSiaGKQKGFEDTR----GTLFFEIIRIIKEKKPKAFLLENVKGLLSHDNGNTLNVILETLEELGYHVSW 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1359 GVLQAGQYGVAQTRRRAIILAAAPG-EKLPLFPEPlhvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLP 1437
Cdd:pfam00145  139 KVLNASDYGVPQNRERVFIVGIRKDlNLNVLVPVP------------------------------EFDFPKPKDLTGTIR 188

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1438 EVRNGASALEISYNGEpqswfqrqlrgaqyqpilrDHICKDMSalvaaRMRHIPLAPGSDWRDLPNIEvRLSDGTMARKL 1517
Cdd:pfam00145  189 DLLEEPSLDENKYNLS-------------------DKFVENHE-----RRKPTTKAPGGGYPTYLLRN-RIDKVEEGKGP 243

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1518 RYTHhdRKNGRsssgalrgvcscveagkacdpaarqfntlipWCLPHTGnrhnhwaglygrlewdgffsttvtnpePMGK 1597
Cdd:pfam00145  244 SFTY--RKSGR-------------------------------PEAPKTG---------------------------ILGK 263

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1598 QGR--VLHPEQHRVVSVRECARSQGFPDTYRLFGNILDKHRQVGNAVPPPLAKAIGLEIK 1655
Cdd:pfam00145  264 NGErfRGHPKNIRRLTPRECARLQGFPDDFIFPGSKTQLYKQIGNAVPVPVAEAIAKAIK 323
BAH smart00439
Bromo adjacent homology domain;
1040-1162 2.18e-35

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 131.26  E-value: 2.18e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486   1040 DYIKGSNLDAPEPYRIGRIKEIFCPKKsngrpNETDIKIRVNKFYRPENTHKStpASYHADINLLYWSDEEAVVDFKAVQ 1119
Cdd:smart00439    6 DFVLVEPDDADEPYYIGRIEEIFETKK-----NSESKMVRVRWFYRPEETVLE--KAALFDKNEVFLSDEYDTVPLSDII 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 119604486   1120 GRCTVEYGEDLPECVQVYSMGGPNRFYFLEAYNAKSKSFEDPP 1162
Cdd:smart00439   79 GKCNVLYKSDYPGLRPEGSIGEPDVFFCESAYDPEKGSFKKLP 121
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 1033-1162 5.10e-32

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: 121.65  E-value: 5.10e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1033 EHYRKySDYIKGSNLDAPEPYRIGRIKEIFCPKKSNgrpnetDIKIRVNKFYRPENTHKSTPASYHADinLLYWSDEEAV 1112
Cdd:pfam01426    1 ETYSV-GDFVLVEPDDADEPYYVARIEELFEDTKNG------KKMVRVQWFYRPEETVHRAGKAFNKD--ELFLSDEEDD 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 119604486  1113 VDFKAVQGRCTVEYGEDLPECvQVYSMGGPNRFYFLEAYNAKSKSFEDPP 1162
Cdd:pfam01426   72 VPLSAIIGKCSVLHKSDLESL-DPYKIKEPDDFFCELLYDPKTKSFKKLP 120
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
 1201-1655 1.29e-31

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: 125.81  E-value: 1.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1201 LRTLDVFSGCGGLSEGFHQAGiSDTLWAIEMWDPAAQAFRLNNPgstvftedcnillKLVMAGETTNSRGQRLPqkGDVE 1280
Cdd:cd00315     1 LRVIDLFAGIGGFRLGLEKAG-FEIVAANEIDKSAAETYEANFP-------------NKLIEGDITKIDEKDFI--PDID 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1281 MLCGGPPCQGFS--GMNRFNSRTYSKfknslvvSFLSYCDY---YRPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQ 1355
Cdd:cd00315    65 LLTGGFPCQPFSiaGKRKGFEDTRGT-------LFFEIIRIlkeKKPKYFLLENVKGLLTHDNGNTLKVILNTLEELGYN 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1356 CTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFapracqlsvvvDDKKFVSNITRLSSGPFRTITVrdtmsd 1435
Cdd:cd00315   138 VYWKLLNASDYGVPQNRERVFIIGIRKDLILNFFSPFPKPS-----------EKKKTLKDILRIRDPDEPSPTL------ 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1436 lpevrngasaleisyngepqswfqrqlrgaqyqpilrdhickdmsalvaarmrhiplapgsdwrdlpnievrlsdgtmar 1515
Cdd:cd00315       --------------------------------------------------------------------------------

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1516 klrythhdrkngrsssgalrgvcscveagkacdpaarqfntlipwclphTGNRHNHWAGLYgrlewdgffsttvtnpepM 1595
Cdd:cd00315   201 -------------------------------------------------TASYGKGTGSVH------------------P 213

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119604486 1596 GKQGRVLHPEQHRVVSVRECARSQGFPDTYRLFG-NILDKHRQVGNAVPPPLAKAIGLEIK 1655
Cdd:cd00315   214 TAPDMIGKESNIRRLTPRECARLQGFPDDFEFPGkSVTQAYRQIGNSVPVPVAEAIAKAIK 274
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
 1205-1654 2.88e-30

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: 123.21  E-value: 2.88e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1205 DVFSGCGGLSEGFHQAGIsDTLWAIEmWDPAAQA-FRLNnpgstvFTEDCNIllklvmaGETTNSRGQRLPqkgDVEMLC 1283
Cdd:TIGR00675    3 DLFAGIGGIRLGFEQAGF-KCVFASE-IDKYAQKtYEAN------FGNKVPF-------GDITKISPSDIP---DFDILL 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1284 GGPPCQGFSgMNRFNsRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTFGVLQA 1363
Cdd:TIGR00675   65 GGFPCQPFS-IAGKR-KGFEDTRGTLFFEIVRILKEKKPKFFLLENVKGLVSHDKGRTFKVIIETLEELGYKVYYKVLNA 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1364 GQYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlsSGPFRTITVRDtmsdlpevrnga 1443
Cdd:TIGR00675  143 KDFGVPQNRERIYIVGFRDFDDKLNFEFPKP--------------------------IYVAKKKRIGD------------ 184

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1444 sALEISYNGEPqswfqrqlrgaqyQPILRDHICKDMSALvaarmrhiplapgsdwrdlpnievrlsdgtmarklrythhd 1523
Cdd:TIGR00675  185 -LLDLSVDLEE-------------KYYLSEEKKNGLLLL----------------------------------------- 209

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  1524 RKNGRSSSGALrgvcscveagkacdpaaRQFNTLipwclphtgNRHNHWAGLYGRLEWDGFFSTTVTNPEPMGKQGR-VL 1602
Cdd:TIGR00675  210 LENMRKKEGTG-----------------EQIGSF---------YNRESKSSIIRTLSARGYTFVKGGKSVLIVPHKStVV 263

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 119604486  1603 HPEQHRVVSVRECARSQGFPDTYRLFGNILDKHRQVGNAVPPPLAKAIGLEI 1654
Cdd:TIGR00675  264 HPGRIRRLTPRECARLQGFPDDFKFPVSDSQLYKQAGNAVVVPVIEAIAKQI 315
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 817-942 2.96e-29

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: 113.56  E-value: 2.96e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486   817 ETLEVGDCVSVIPDDSSKPLYLARVTALWEDSSNG-QMFHAHWFCAGTDTV--LGATSDPLELFLVDECEDMQLSYIHSK 893
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGkKMVRVQWFYRPEETVhrAGKAFNKDELFLSDEEDDVPLSAIIGK 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 119604486   894 VKVIYKAPSENWAMEggmdpesllEGDDGKTYFYQLWYDQDYARFESPP 942
Cdd:pfam01426   81 CSVLHKSDLESLDPY---------KIKEPDDFFCELLYDPKTKSFKKLP 120
BAH smart00439
Bromo adjacent homology domain;
818-942 5.69e-29

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 112.77  E-value: 5.69e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486    818 TLEVGDCVSVIPDDSSKPLYLARVTALWEDSSNGQ--MFHAHWFCAGTDTVLGAT--SDPLELFLVDECEDMQLSYIHSK 893
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSEskMVRVRWFYRPEETVLEKAalFDKNEVFLSDEYDTVPLSDIIGK 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 119604486    894 VKVIYKAPSENWAMEGGMDPEsllegddgKTYFYQLWYDQDYARFESPP 942
Cdd:smart00439   81 CNVLYKSDYPGLRPEGSIGEP--------DVFFCESAYDPEKGSFKKLP 121
DMAP_binding pfam06464
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
 78-167 3.28e-27

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


Pssm-ID: 368923 [Multi-domain]  Cd Length: 104  Bit Score: 107.12  E-value: 3.28e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486    78 PAISLPDDVRRRLKDLERDS----LTEKECVKEKLNLLHEFL---------QTEIKNQLCDLETKLRKEELSEEGYLAKV 144
Cdd:pfam06464    1 NPPSLPDDVRERLSELDLDLsegdITEKGYEKKKLKLLRKFLlhpetptklSAEAQNQLASLETKLRDEELSEEVYLEKV 80

                           90       100
                   ....*....|....*....|...
gi 119604486   145 KSLLNKDLSLENGAHAYNREVNG 167
Cdd:pfam06464   81 KALLAKELERENGLNAPTKEQSG 103
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 816-940 4.35e-23

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: 96.31  E-value: 4.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  816 AETLEVGDCVSVIPDDS--SKPLYLARVTALWEDSSNGQMFHAHWFCAGTDTVLGATS--DPLELFLVDECEDMQLSYIH 891
Cdd:cd04370     1 GITYEVGDSVYVEPDDSikSDPPYIARIEELWEDTNGSKQVKVRWFYRPEETPKGLSPfaLRRELFLSDHLDEIPVESII 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 119604486  892 SKVKVIYKAPSENWAMEGGMdpesllegDDGKTYFYQLWYDQDYARFES 940
Cdd:cd04370    81 GKCKVLFVSEFEGLKQRPNK--------IDTDDFFCRLAYDPTTKEFKA 121
BAH_plantDCM_II cd04708
BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5) ...
 989-1213 2.94e-19

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: 87.90  E-value: 2.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  989 TKNGILYRVGDGVYLPPEAFTfniklsspvkrprkepvdedlypEHYRKYSDYIKGSNLDAPePYRIGRIKEIFcPKKSN 1068
Cdd:cd04708     2 VYDGVTYSVGDFLYVSPDAFA-----------------------EEERERATFKAGRNVGLK-AFVVCQVLEIV-VEKES 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1069 GRPNETDIKIRVNKFYRPENThkSTPASYHADINLLYWSDEEAVVDFKAVQGRCTVEYGEDLPECvQVYSMGGPNrFYFL 1148
Cdd:cd04708    57 KQADVASTQVKVRRFYRPEDV--SPEKAYASDIREVYYSEDTLTVPVEAVEGKCEVRKKSDLPDS-DAPVIFEHV-FFCE 132

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1149 EAYNAKSKSFEDPPNHARSPGNKGKGKGKGKGKPKSQACEPSEPEIEIKL--PK---LRTLDVFSGCGGL 1213
Cdd:cd04708   133 LLYDPAKGSLKQLPPNIKEEAYSTGASDSALRKRKGKGKGDSESDSEAPVkaPKenrLATLDIFAGCGGL 202
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 1031-1158 5.02e-19

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: 84.37  E-value: 5.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1031 YPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNgrpnetdIKIRVNKFYRPENTHKStpASYHADINLLYWSDEE 1110
Cdd:cd04370     1 GITYEVGDSVYVEPDDSIKSDPPYIARIEELWEDTNGS-------KQVKVRWFYRPEETPKG--LSPFALRRELFLSDHL 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 119604486 1111 AVVDFKAVQGRCTVEYGEDLPECVQVYSMGGPNRFYFLEAYNAKSKSF 1158
Cdd:cd04370    72 DEIPVESIIGKCKVLFVSEFEGLKQRPNKIDTDDFFCRLAYDPTTKEF 119
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 707-753 5.22e-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: 82.02  E-value: 5.22e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 119604486   707 ENAFKRRRCGVCEVCQQPE-CGKCKACKDMVKFGGSGRSKQACQERRC 753
Cdd:pfam02008    1 RNRRKRRRCGVCEGCQRPEdCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
BAH_DCM_I cd04712
BAH, or Bromo Adjacent Homology domain, as present in DNA (Cytosine-5)-methyltransferases (DCM) ...
 814-943 8.50e-09

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: 55.49  E-value: 8.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  814 IDAETLEVGDCVSVIPDDSSKPLYLA----------RVTALWEDSSNGQMFHAHWFCAGTDTVLGATSDPLELFLVDECE 883
Cdd:cd04712     1 IHGLTIRVGDVVSVERDDADSTTKWNddhrwlplvqFVEYMKKGSDGSKMFHGRWLYRGCDTVLGNYANERELFLTNECT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  884 DMQLSYIHSKVKVIYKAPsenWamegGMDPESlleGDDGKTYFYQLWYDQDYARFESPPK 943
Cdd:cd04712    81 CLELDLLSTEIKGVHKVD---W----SGTPWG---KGLPEFFVRQSYYWPERGAFTSLKR 130
BAH_fungalPHD cd04710
BAH, or Bromo Adjacent Homology domain, as present in fungal proteins containing PHD domains. ...
 1032-1160 2.20e-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: 2.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486 1032 PEHYRKySDYIKGSNLDAPEPYRIGRIKEiFCPKKSN-------GRPNETDiKIRVNKFYRPENTHKSTPAsyhaDINLL 1104
Cdd:cd04710     9 GELLKV-NDHIYMSSEPPGEPYYIGRIME-FVPKHEFpsgiharVFPASYF-QVRLNWYYRPRDISRRVVA----DSRLL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119604486 1105 YWSDEEAVVDFKAVQGRCTVEYG---EDLPECVQvysmgGPNRFYFLEAYNAKSKSFED 1160
Cdd:cd04710    82 YASMHSDICPIGSVRGKCTVRHRdqiPDLEEYKK-----RPNHFYFDQLFDRYILRYYD 135
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 817-859 7.39e-06

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: 46.63  E-value: 7.39e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 119604486  817 ETLEVGDCVSVIPDDSSKPLYLARVTALWEDSSNGQMFHAHWF 859
Cdd:cd04714     2 EIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWY 44
BAH_polybromo cd04717
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human ...
 819-859 2.43e-04

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: 42.57  E-value: 2.43e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 119604486  819 LEVGDCVSVIPDDSSKPLYLARVTALWEDSSNGQMFHAHWF 859
Cdd:cd04717     4 YRVGDCVYVANPEDPSKPIIFRIERLWKDEDGEKFFFGCWF 44
BAH_plantDCM_I cd04716
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 818-940 2.88e-04

BAH, or Bromo Adjacent Homology domain, first 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: 240067  Cd Length: 122  Bit Score: 42.43  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  818 TLEVGDCVSViPDDSSKPLYLARVTALWEDSSNGQMFHAHWFCAGTDTVLGATS---DPLELFLVDECEDMQLSYIHSKV 894
Cdd:cd04716     3 TYNLGDDAYV-QGGEGEEPFICKITEFFEGTDGKTYFTAQWFYRAEDTVIERQAtnhDKKRVFYSEIKNDNPLDCLISKV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 119604486  895 KVIYKAPSENWAMEggmdpESLLEGDDgktYFYQLWYDQDYARFES 940
Cdd:cd04716    82 KILQVPPNVGTKRK-----KPNSEKCD---YYYDMEYCVPYSTFQT 119
BAH_plant_1 cd04721
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 813-890 7.67e-03

BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. 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: 240072  Cd Length: 130  Bit Score: 38.19  E-value: 7.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119604486  813 CIDAETLEVGDCVSVIPDDSSKplYLARVTALWEDSSNGQMFHAHWFcAGTDTVLGATSD----PLELFLVDECEDMQLS 888
Cdd:cd04721     2 CRNGVTISVHDFVYVLSEEEDR--YVAYIEDLYEDKKGSKMVKVRWF-HTTDEVGAALSPdsvnPREIFLSPNLQVISVE 78


                  ..
gi 119604486  889 YI 890
Cdd:cd04721    79 CI 80
 
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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