NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15239810|ref|NP_199727|]
View 

methyltransferase 1 [Arabidopsis thaliana]

Protein Classification

DNA (cytosine-5)-methyltransferase 1; DNA cytosine methyltransferase( domain architecture ID 10572340)

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.| DNA cytosine methyltransferase is a class I SAM-dependent methyltransferase that catalyzes specific methylation on cytosine on both strands and protects the DNA from cleavage

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_plantDCM_II cd04708
BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5) ...
904-1105 1.94e-102

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: 325.57  E-value: 1.94e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810  904 FFINGIEYSVEDFVYVNPDSIGGlKEGSKTSFKSGRNIGLRAYVVCQLLEIVPKESRK-ADLGSFDVKVRRFYRPEDVSA 982
Cdd:cd04708    1 FVYDGVTYSVGDFLYVSPDAFAE-EERERATFKAGRNVGLKAFVVCQVLEIVVEKESKqADVASTQVKVRRFYRPEDVSP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810  983 EKAYASDIQELYFSQDTVVLPPGALEGKCEVRKKSDMPLSREYPISDHIFFCDLFFDTSKGSLKQLPANMKP-KFSTIKD 1061
Cdd:cd04708   80 EKAYASDIREVYYSEDTLTVPVEAVEGKCEVRKKSDLPDSDAPVIFEHVFFCELLYDPAKGSLKQLPPNIKEeAYSTGAS 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15239810 1062 DTLLRKKKGKGVEsEIESEIVKPVEPPKEIRLATLDIFAGCGGL 1105
Cdd:cd04708  160 DSALRKRKGKGKG-DSESDSEAPVKAPKENRLATLDIFAGCGGL 202
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
1092-1524 2.25e-67

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


:

Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 228.92  E-value: 2.25e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1092 RLATLDIFAGCGGLSHGLKKAGVsDAKWAIEYEEPAGQAFKQNHPESTVFVdncnvilraimekgGDqddcVSTTEANEL 1171
Cdd:COG0270    3 KLTVIDLFAGAGGLSLGFEKAGF-EVVFAVEIDPDACETYRANFPEAKVIE--------------GD----IRDIDPEEL 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1172 aaklteeqkstlplPGQVDFINGGPPCQGFSGMNR---FNQSSWSkvqceMILAFLSFADYFRPRYFLLENVRTFVSFNK 1248
Cdd:COG0270   64 --------------IPDVDLLIGGPPCQPFSVAGKrkgLEDPRGT-----LFFEFIRIVEELRPKAFVLENVPGLLSSDK 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1249 GQTFQLTLASLLEMGYQVRFGILEAGAYGVSQSRKRAFIWAAAPEEVLPEWPEPMHvfgvpklkislsqglhyaavrsta 1328
Cdd:COG0270  125 GKTFEEILKELEELGYRVDYKVLNAADYGVPQNRERVFIVGFRKDLDLFEFPEPTH------------------------ 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1329 lgaPFRPITVRDTIGDLPSvengdsrtnkeykevavswfqkeirgntialtDHICKAMNElnlirckliptrpgadwhdl 1408
Cdd:COG0270  181 ---LKPYVTVGDALEDLPD--------------------------------AHEARYLSE-------------------- 205
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1409 pkrkvTLsdgrveemipfclpnTAErhngwkglygrldwqgnfptsvtdpqpMGKVGMCFHPEQHRILTVRECARSQGFP 1488
Cdd:COG0270  206 -----TI---------------TAG---------------------------YGGGGRFLHPGEPRRLTVREAARLQGFP 238
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 15239810 1489 DSYEFAGNINHKHRQIGNAVPPPLAFALGRKLKEAL 1524
Cdd:COG0270  239 DDFKFPGSKTQAYRQIGNAVPPPLAEAIAKAILKAL 274
DNMT1-RFD pfam12047
Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a ...
78-214 8.19e-46

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: 161.74  E-value: 8.19e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810     78 VEDRPTRRLNDFVLFDSDGVPQPLEMLEIH---DIFVSGAILPSDVCTDKEKEKGVRCTS----FGRVEHWSISGYEDGS 150
Cdd:pfam12047    1 EEDRPQRKLTDFELYDKDGHLCPFDVLLIEknvDIFISGIVKPIDEDEPSLDGKGIEDKGmqikLGPIKEWTISGFDGGE 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15239810    151 -PVIWISTELADYDCRKPAASYRKVYDYFYEKARASVAVYKKLSKSSGgdPDIGLEELLAAVVRS 214
Cdd:pfam12047   81 kALIWLSTEFAWYKLLKPSAEYAPIYELVYEKARLSVEVVEFLQRSPG--SELSYEDLINRVLTS 143
BAH_DCM_I cd04712
BAH, or Bromo Adjacent Homology domain, as present in DNA (Cytosine-5)-methyltransferases (DCM) ...
732-869 6.63e-42

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: 149.86  E-value: 6.63e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810  732 VGGEMVAVGGAVTLEVDDPD----------EMPAIYFVEYMFESTDHCKMLHGRFLQRGSMTVLGNAANERELFLTNECM 801
Cdd:cd04712    1 IHGLTIRVGDVVSVERDDADsttkwnddhrWLPLVQFVEYMKKGSDGSKMFHGRWLYRGCDTVLGNYANERELFLTNECT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239810  802 TTQLK----DIKGVASFEIRSRPWGhqyrkknitadkldwaralerkvKDLPTEYYCKSLYSPERGGFFSLP 869
Cdd:cd04712   81 CLELDllstEIKGVHKVDWSGTPWG-----------------------KGLPEFFVRQSYYWPERGAFTSLK 129
DNMT1-RFD pfam12047
Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a ...
386-535 3.69e-30

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: 117.06  E-value: 3.69e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810    386 EHLPHRMLHNWALYNSDLRFISLELLPMKQCDDIdvniFGSGVVTDdngswISLNDPDSGSQSHDPDGMCIFLSQIKEWM 465
Cdd:pfam12047    2 EDRPQRKLTDFELYDKDGHLCPFDVLLIEKNVDI----FISGIVKP-----IDEDEPSLDGKGIEDKGMQIKLGPIKEWT 72
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15239810    466 IEFGSD-DIISISIRTDVAWYRLGKPSKLYAPWWKPVLKTARVGISILTFLRVESRvARLSFADVTKRLSG 535
Cdd:pfam12047   73 ISGFDGgEKALIWLSTEFAWYKLLKPSAEYAPIYELVYEKARLSVEVVEFLQRSPG-SELSYEDLINRVLT 142
 
Name Accession Description Interval E-value
BAH_plantDCM_II cd04708
BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5) ...
904-1105 1.94e-102

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: 325.57  E-value: 1.94e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810  904 FFINGIEYSVEDFVYVNPDSIGGlKEGSKTSFKSGRNIGLRAYVVCQLLEIVPKESRK-ADLGSFDVKVRRFYRPEDVSA 982
Cdd:cd04708    1 FVYDGVTYSVGDFLYVSPDAFAE-EERERATFKAGRNVGLKAFVVCQVLEIVVEKESKqADVASTQVKVRRFYRPEDVSP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810  983 EKAYASDIQELYFSQDTVVLPPGALEGKCEVRKKSDMPLSREYPISDHIFFCDLFFDTSKGSLKQLPANMKP-KFSTIKD 1061
Cdd:cd04708   80 EKAYASDIREVYYSEDTLTVPVEAVEGKCEVRKKSDLPDSDAPVIFEHVFFCELLYDPAKGSLKQLPPNIKEeAYSTGAS 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15239810 1062 DTLLRKKKGKGVEsEIESEIVKPVEPPKEIRLATLDIFAGCGGL 1105
Cdd:cd04708  160 DSALRKRKGKGKG-DSESDSEAPVKAPKENRLATLDIFAGCGGL 202
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
1092-1524 2.25e-67

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


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 228.92  E-value: 2.25e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1092 RLATLDIFAGCGGLSHGLKKAGVsDAKWAIEYEEPAGQAFKQNHPESTVFVdncnvilraimekgGDqddcVSTTEANEL 1171
Cdd:COG0270    3 KLTVIDLFAGAGGLSLGFEKAGF-EVVFAVEIDPDACETYRANFPEAKVIE--------------GD----IRDIDPEEL 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1172 aaklteeqkstlplPGQVDFINGGPPCQGFSGMNR---FNQSSWSkvqceMILAFLSFADYFRPRYFLLENVRTFVSFNK 1248
Cdd:COG0270   64 --------------IPDVDLLIGGPPCQPFSVAGKrkgLEDPRGT-----LFFEFIRIVEELRPKAFVLENVPGLLSSDK 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1249 GQTFQLTLASLLEMGYQVRFGILEAGAYGVSQSRKRAFIWAAAPEEVLPEWPEPMHvfgvpklkislsqglhyaavrsta 1328
Cdd:COG0270  125 GKTFEEILKELEELGYRVDYKVLNAADYGVPQNRERVFIVGFRKDLDLFEFPEPTH------------------------ 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1329 lgaPFRPITVRDTIGDLPSvengdsrtnkeykevavswfqkeirgntialtDHICKAMNElnlirckliptrpgadwhdl 1408
Cdd:COG0270  181 ---LKPYVTVGDALEDLPD--------------------------------AHEARYLSE-------------------- 205
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1409 pkrkvTLsdgrveemipfclpnTAErhngwkglygrldwqgnfptsvtdpqpMGKVGMCFHPEQHRILTVRECARSQGFP 1488
Cdd:COG0270  206 -----TI---------------TAG---------------------------YGGGGRFLHPGEPRRLTVREAARLQGFP 238
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 15239810 1489 DSYEFAGNINHKHRQIGNAVPPPLAFALGRKLKEAL 1524
Cdd:COG0270  239 DDFKFPGSKTQAYRQIGNAVPPPLAEAIAKAILKAL 274
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
1093-1522 1.50e-49

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 179.43  E-value: 1.50e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1093 LATLDIFAGCGGLSHGLKKAGVSDAkWAIEYEEPAGQAFKQNHPEsTVFVDncnvilraimekggdqddcvstteanela 1172
Cdd:pfam00145    1 FKFIDLFAGIGGFRLGLEQAGFECV-AANEIDKSAAKTYEANFPK-VPIGD----------------------------- 49
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1173 akLTEEQKSTLPlpgQVDFINGGPPCQGFS------GMNRFNQSSWSKVqCEMILAFlsfadyfRPRYFLLENVRTFVSF 1246
Cdd:pfam00145   50 --ITLIDIKDIP---DIDILTGGFPCQDFSiagkqkGFEDTRGTLFFEI-IRIIKEK-------KPKAFLLENVKGLLSH 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1247 NKGQTFQLTLASLLEMGYQVRFGILEAGAYGVSQSRKRAFIWAA---APEEVLPEWPEpmhvFGVPKlkislsqglhyaa 1323
Cdd:pfam00145  117 DNGNTLNVILETLEELGYHVSWKVLNASDYGVPQNRERVFIVGIrkdLNLNVLVPVPE----FDFPK------------- 179
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1324 vrstalgapfrPITVRDTIGDLPsvENGDSRTNKEYkevavswfqkeirgntiaLTDHICkamneLNLIRcklIPTRPGA 1403
Cdd:pfam00145  180 -----------PKDLTGTIRDLL--EEPSLDENKYN------------------LSDKFV-----ENHER---RKPTTKA 220
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1404 DWHDLPKrkvTLSDGRVEEMIPFclpntaerhNGWKGLYGRLDWQGNFPTSVTDPQPMGKVGmcfHPEQHRILTVRECAR 1483
Cdd:pfam00145  221 PGGGYPT---YLLRNRIDKVEEG---------KGPSFTYRKSGRPEAPKTGILGKNGERFRG---HPKNIRRLTPRECAR 285
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 15239810   1484 SQGFPDSYEFAGNINHKHRQIGNAVPPPLAFALGRKLKE 1522
Cdd:pfam00145  286 LQGFPDDFIFPGSKTQLYKQIGNAVPVPVAEAIAKAIKK 324
DNMT1-RFD pfam12047
Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a ...
78-214 8.19e-46

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: 161.74  E-value: 8.19e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810     78 VEDRPTRRLNDFVLFDSDGVPQPLEMLEIH---DIFVSGAILPSDVCTDKEKEKGVRCTS----FGRVEHWSISGYEDGS 150
Cdd:pfam12047    1 EEDRPQRKLTDFELYDKDGHLCPFDVLLIEknvDIFISGIVKPIDEDEPSLDGKGIEDKGmqikLGPIKEWTISGFDGGE 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15239810    151 -PVIWISTELADYDCRKPAASYRKVYDYFYEKARASVAVYKKLSKSSGgdPDIGLEELLAAVVRS 214
Cdd:pfam12047   81 kALIWLSTEFAWYKLLKPSAEYAPIYELVYEKARLSVEVVEFLQRSPG--SELSYEDLINRVLTS 143
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
1093-1522 5.02e-44

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: 161.63  E-value: 5.02e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1093 LATLDIFAGCGGLSHGLKKAGvSDAKWAIEYEEPAGQAFKQNHPESTVFvdncnvilraimekgGDqddcvstteanela 1172
Cdd:cd00315    1 LRVIDLFAGIGGFRLGLEKAG-FEIVAANEIDKSAAETYEANFPNKLIE---------------GD-------------- 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1173 akLTEEQKSTLPlpGQVDFINGGPPCQGFS---GMNRFNQSSWSkvqcemilAFLSFADY---FRPRYFLLENVRTFVSF 1246
Cdd:cd00315   51 --ITKIDEKDFI--PDIDLLTGGFPCQPFSiagKRKGFEDTRGT--------LFFEIIRIlkeKKPKYFLLENVKGLLTH 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1247 NKGQTFQLTLASLLEMGYQVRFGILEAGAYGVSQSRKRAFIWAA-APEEVLPEWPEPMhvfgVPKLKislsqglhyaavr 1325
Cdd:cd00315  119 DNGNTLKVILNTLEELGYNVYWKLLNASDYGVPQNRERVFIIGIrKDLILNFFSPFPK----PSEKK------------- 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1326 stalgapfrpITVRDTIGdlpsvengdsrtnkeykevavsWFQKEIRGNTIaltdhickamnelnlirckliptrpgadw 1405
Cdd:cd00315  182 ----------KTLKDILR----------------------IRDPDEPSPTL----------------------------- 200
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1406 hdlpkrkvtlsdgrveemipfclpnTAERHNGWkglyGRLDWQGNFptsvtdpqpmgkvgMCFHPEQHRILTVRECARSQ 1485
Cdd:cd00315  201 -------------------------TASYGKGT----GSVHPTAPD--------------MIGKESNIRRLTPRECARLQ 237
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 15239810 1486 GFPDSYEFAG-NINHKHRQIGNAVPPPLAFALGRKLKE 1522
Cdd:cd00315  238 GFPDDFEFPGkSVTQAYRQIGNSVPVPVAEAIAKAIKE 275
BAH_DCM_I cd04712
BAH, or Bromo Adjacent Homology domain, as present in DNA (Cytosine-5)-methyltransferases (DCM) ...
732-869 6.63e-42

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: 149.86  E-value: 6.63e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810  732 VGGEMVAVGGAVTLEVDDPD----------EMPAIYFVEYMFESTDHCKMLHGRFLQRGSMTVLGNAANERELFLTNECM 801
Cdd:cd04712    1 IHGLTIRVGDVVSVERDDADsttkwnddhrWLPLVQFVEYMKKGSDGSKMFHGRWLYRGCDTVLGNYANERELFLTNECT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239810  802 TTQLK----DIKGVASFEIRSRPWGhqyrkknitadkldwaralerkvKDLPTEYYCKSLYSPERGGFFSLP 869
Cdd:cd04712   81 CLELDllstEIKGVHKVDWSGTPWG-----------------------KGLPEFFVRQSYYWPERGAFTSLK 129
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
1097-1520 2.62e-36

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: 140.54  E-value: 2.62e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1097 DIFAGCGGLSHGLKKAGVsDAKWAIEYEEPAGQAFKQNHPESTVFVDncnvilraimekggdqddcvstteanelaakLT 1176
Cdd:TIGR00675    3 DLFAGIGGIRLGFEQAGF-KCVFASEIDKYAQKTYEANFGNKVPFGD-------------------------------IT 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1177 EEQKSTLPlpgQVDFINGGPPCQGFS---GMNRFNQSSWSkvqcemilAFLSFADYFR---PRYFLLENVRTFVSFNKGQ 1250
Cdd:TIGR00675   51 KISPSDIP---DFDILLGGFPCQPFSiagKRKGFEDTRGT--------LFFEIVRILKekkPKFFLLENVKGLVSHDKGR 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1251 TFQLTLASLLEMGYQVRFGILEAGAYGVSQSRKRAFIWAAAPEEVLPEWPEPMHVFgvpklkislsqglhyaavrstalg 1330
Cdd:TIGR00675  120 TFKVIIETLEELGYKVYYKVLNAKDFGVPQNRERIYIVGFRDFDDKLNFEFPKPIY------------------------ 175
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1331 apfrpITVRDTIGDLPSVENGDSrtNKEYkevavswfqkeirgntiaLTDHICKAMNELnlirckliptrpgadwhdlpK 1410
Cdd:TIGR00675  176 -----VAKKKRIGDLLDLSVDLE--EKYY------------------LSEEKKNGLLLL--------------------L 210
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1411 RKVTLSDGRVEEMIPFclpntaERHNGWKGLYGRLDWQGNFPTSVTDPQPMGKVG-MCFHPEQHRILTVRECARSQGFPD 1489
Cdd:TIGR00675  211 ENMRKKEGTGEQIGSF------YNRESKSSIIRTLSARGYTFVKGGKSVLIVPHKsTVVHPGRIRRLTPRECARLQGFPD 284
                          410       420       430
                   ....*....|....*....|....*....|.
gi 15239810   1490 SYEFAGNINHKHRQIGNAVPPPLAFALGRKL 1520
Cdd:TIGR00675  285 DFKFPVSDSQLYKQAGNAVVVPVIEAIAKQI 315
BAH smart00439
Bromo adjacent homology domain;
910-1049 2.42e-30

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 116.62  E-value: 2.42e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810     910 EYSVEDFVYVNPDSigglkegsktsfksgrniGLRAYVVCQLLEIVPKESRKadlGSFDVKVRRFYRPEDVSAEKAYASD 989
Cdd:smart00439    1 TISVGDFVLVEPDD------------------ADEPYYIGRIEEIFETKKNS---ESKMVRVRWFYRPEETVLEKAALFD 59
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239810     990 IQELYFSQDTVVLPPGALEGKCEVRKKSDMPLSREYPIS--DHIFFCDLFFDTSKGSLKQLP 1049
Cdd:smart00439   60 KNEVFLSDEYDTVPLSDIIGKCNVLYKSDYPGLRPEGSIgePDVFFCESAYDPEKGSFKKLP 121
DNMT1-RFD pfam12047
Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a ...
386-535 3.69e-30

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: 117.06  E-value: 3.69e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810    386 EHLPHRMLHNWALYNSDLRFISLELLPMKQCDDIdvniFGSGVVTDdngswISLNDPDSGSQSHDPDGMCIFLSQIKEWM 465
Cdd:pfam12047    2 EDRPQRKLTDFELYDKDGHLCPFDVLLIEKNVDI----FISGIVKP-----IDEDEPSLDGKGIEDKGMQIKLGPIKEWT 72
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15239810    466 IEFGSD-DIISISIRTDVAWYRLGKPSKLYAPWWKPVLKTARVGISILTFLRVESRvARLSFADVTKRLSG 535
Cdd:pfam12047   73 ISGFDGgEKALIWLSTEFAWYKLLKPSAEYAPIYELVYEKARLSVEVVEFLQRSPG-SELSYEDLINRVLT 142
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
735-869 3.94e-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: 113.17  E-value: 3.94e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810    735 EMVAVGGAVTLEVDDPDEMPAIYFVEYMFESTDHC-KMLHGRFLQRGSMTV--LGNAANERELFLTNECMTTQLKDIKGV 811
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGkKMVRVQWFYRPEETVhrAGKAFNKDELFLSDEEDDVPLSAIIGK 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 15239810    812 ASFEIRSRPWGHQYRKknitadkldwaralerkvKDLPTEYYCKSLYSPERGGFFSLP 869
Cdd:pfam01426   81 CSVLHKSDLESLDPYK------------------IKEPDDFFCELLYDPKTKSFKKLP 120
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
909-1049 1.21e-27

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: 108.93  E-value: 1.21e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810    909 IEYSVEDFVYVNPDSIGglkegsktsfksgrniglRAYVVCQLLEIvpKESRKAdlGSFDVKVRRFYRPEDVSAEKAYAS 988
Cdd:pfam01426    1 ETYSVGDFVLVEPDDAD------------------EPYYVARIEEL--FEDTKN--GKKMVRVQWFYRPEETVHRAGKAF 58
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239810    989 DIQELYFSQDTVVLPPGALEGKCEVRKKSDMPLSREYPIS-DHIFFCDLFFDTSKGSLKQLP 1049
Cdd:pfam01426   59 NKDELFLSDEEDDVPLSAIIGKCSVLHKSDLESLDPYKIKePDDFFCELLYDPKTKSFKKLP 120
BAH smart00439
Bromo adjacent homology domain;
736-869 5.05e-27

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 106.99  E-value: 5.05e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810     736 MVAVGGAVTLEVDDPDEMPAIYFVEYMFESTD--HCKMLHGRFLQRGSMTVLGNAA--NERELFLTNECMTTQLKDIKGV 811
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKnsESKMVRVRWFYRPEETVLEKAAlfDKNEVFLSDEYDTVPLSDIIGK 80
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 15239810     812 ASFEIRSRPWGHQYRKKNItadkldwaralerkvkdLPTEYYCKSLYSPERGGFFSLP 869
Cdd:smart00439   81 CNVLYKSDYPGLRPEGSIG-----------------EPDVFFCESAYDPEKGSFKKLP 121
PRK10458 PRK10458
DNA cytosine methylase; Provisional
1096-1266 5.55e-05

DNA cytosine methylase; Provisional


Pssm-ID: 236696 [Multi-domain]  Cd Length: 467  Bit Score: 47.37  E-value: 5.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810  1096 LDIFAGCGGLSHGLKKAG---VSDAKWAIEyeepAGQAFKQNH---PESTVFvdncNVILRAIMEKGgdqDDCVSTTEAn 1169
Cdd:PRK10458   92 IDLFAGIGGIRRGFEAIGgqcVFTSEWNKH----AVRTYKANWycdPATHRF----NEDIRDITLSH---KEGVSDEEA- 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810  1170 elAAKLTEEqkstlpLPgQVDFINGGPPCQGFS--GMNRFNqsSWSKV---QCEM--ILAF--LSFADYFRPRYFLLENV 1240
Cdd:PRK10458  160 --AEHIRQH------IP-DHDVLLAGFPCQPFSlaGVSKKN--SLGRAhgfECETqgTLFFdvARIIDAKRPAIFVLENV 228
                         170       180
                  ....*....|....*....|....*.
gi 15239810  1241 RTFVSFNKGQTFQLTLASLLEMGYQV 1266
Cdd:PRK10458  229 KNLKSHDKGKTFRIIMQTLDELGYDV 254
 
Name Accession Description Interval E-value
BAH_plantDCM_II cd04708
BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5) ...
904-1105 1.94e-102

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: 325.57  E-value: 1.94e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810  904 FFINGIEYSVEDFVYVNPDSIGGlKEGSKTSFKSGRNIGLRAYVVCQLLEIVPKESRK-ADLGSFDVKVRRFYRPEDVSA 982
Cdd:cd04708    1 FVYDGVTYSVGDFLYVSPDAFAE-EERERATFKAGRNVGLKAFVVCQVLEIVVEKESKqADVASTQVKVRRFYRPEDVSP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810  983 EKAYASDIQELYFSQDTVVLPPGALEGKCEVRKKSDMPLSREYPISDHIFFCDLFFDTSKGSLKQLPANMKP-KFSTIKD 1061
Cdd:cd04708   80 EKAYASDIREVYYSEDTLTVPVEAVEGKCEVRKKSDLPDSDAPVIFEHVFFCELLYDPAKGSLKQLPPNIKEeAYSTGAS 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15239810 1062 DTLLRKKKGKGVEsEIESEIVKPVEPPKEIRLATLDIFAGCGGL 1105
Cdd:cd04708  160 DSALRKRKGKGKG-DSESDSEAPVKAPKENRLATLDIFAGCGGL 202
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
1092-1524 2.25e-67

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


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 228.92  E-value: 2.25e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1092 RLATLDIFAGCGGLSHGLKKAGVsDAKWAIEYEEPAGQAFKQNHPESTVFVdncnvilraimekgGDqddcVSTTEANEL 1171
Cdd:COG0270    3 KLTVIDLFAGAGGLSLGFEKAGF-EVVFAVEIDPDACETYRANFPEAKVIE--------------GD----IRDIDPEEL 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1172 aaklteeqkstlplPGQVDFINGGPPCQGFSGMNR---FNQSSWSkvqceMILAFLSFADYFRPRYFLLENVRTFVSFNK 1248
Cdd:COG0270   64 --------------IPDVDLLIGGPPCQPFSVAGKrkgLEDPRGT-----LFFEFIRIVEELRPKAFVLENVPGLLSSDK 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1249 GQTFQLTLASLLEMGYQVRFGILEAGAYGVSQSRKRAFIWAAAPEEVLPEWPEPMHvfgvpklkislsqglhyaavrsta 1328
Cdd:COG0270  125 GKTFEEILKELEELGYRVDYKVLNAADYGVPQNRERVFIVGFRKDLDLFEFPEPTH------------------------ 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1329 lgaPFRPITVRDTIGDLPSvengdsrtnkeykevavswfqkeirgntialtDHICKAMNElnlirckliptrpgadwhdl 1408
Cdd:COG0270  181 ---LKPYVTVGDALEDLPD--------------------------------AHEARYLSE-------------------- 205
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1409 pkrkvTLsdgrveemipfclpnTAErhngwkglygrldwqgnfptsvtdpqpMGKVGMCFHPEQHRILTVRECARSQGFP 1488
Cdd:COG0270  206 -----TI---------------TAG---------------------------YGGGGRFLHPGEPRRLTVREAARLQGFP 238
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 15239810 1489 DSYEFAGNINHKHRQIGNAVPPPLAFALGRKLKEAL 1524
Cdd:COG0270  239 DDFKFPGSKTQAYRQIGNAVPPPLAEAIAKAILKAL 274
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
1093-1522 1.50e-49

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 179.43  E-value: 1.50e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1093 LATLDIFAGCGGLSHGLKKAGVSDAkWAIEYEEPAGQAFKQNHPEsTVFVDncnvilraimekggdqddcvstteanela 1172
Cdd:pfam00145    1 FKFIDLFAGIGGFRLGLEQAGFECV-AANEIDKSAAKTYEANFPK-VPIGD----------------------------- 49
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1173 akLTEEQKSTLPlpgQVDFINGGPPCQGFS------GMNRFNQSSWSKVqCEMILAFlsfadyfRPRYFLLENVRTFVSF 1246
Cdd:pfam00145   50 --ITLIDIKDIP---DIDILTGGFPCQDFSiagkqkGFEDTRGTLFFEI-IRIIKEK-------KPKAFLLENVKGLLSH 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1247 NKGQTFQLTLASLLEMGYQVRFGILEAGAYGVSQSRKRAFIWAA---APEEVLPEWPEpmhvFGVPKlkislsqglhyaa 1323
Cdd:pfam00145  117 DNGNTLNVILETLEELGYHVSWKVLNASDYGVPQNRERVFIVGIrkdLNLNVLVPVPE----FDFPK------------- 179
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1324 vrstalgapfrPITVRDTIGDLPsvENGDSRTNKEYkevavswfqkeirgntiaLTDHICkamneLNLIRcklIPTRPGA 1403
Cdd:pfam00145  180 -----------PKDLTGTIRDLL--EEPSLDENKYN------------------LSDKFV-----ENHER---RKPTTKA 220
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1404 DWHDLPKrkvTLSDGRVEEMIPFclpntaerhNGWKGLYGRLDWQGNFPTSVTDPQPMGKVGmcfHPEQHRILTVRECAR 1483
Cdd:pfam00145  221 PGGGYPT---YLLRNRIDKVEEG---------KGPSFTYRKSGRPEAPKTGILGKNGERFRG---HPKNIRRLTPRECAR 285
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 15239810   1484 SQGFPDSYEFAGNINHKHRQIGNAVPPPLAFALGRKLKE 1522
Cdd:pfam00145  286 LQGFPDDFIFPGSKTQLYKQIGNAVPVPVAEAIAKAIKK 324
DNMT1-RFD pfam12047
Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a ...
78-214 8.19e-46

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: 161.74  E-value: 8.19e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810     78 VEDRPTRRLNDFVLFDSDGVPQPLEMLEIH---DIFVSGAILPSDVCTDKEKEKGVRCTS----FGRVEHWSISGYEDGS 150
Cdd:pfam12047    1 EEDRPQRKLTDFELYDKDGHLCPFDVLLIEknvDIFISGIVKPIDEDEPSLDGKGIEDKGmqikLGPIKEWTISGFDGGE 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15239810    151 -PVIWISTELADYDCRKPAASYRKVYDYFYEKARASVAVYKKLSKSSGgdPDIGLEELLAAVVRS 214
Cdd:pfam12047   81 kALIWLSTEFAWYKLLKPSAEYAPIYELVYEKARLSVEVVEFLQRSPG--SELSYEDLINRVLTS 143
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
1093-1522 5.02e-44

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: 161.63  E-value: 5.02e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1093 LATLDIFAGCGGLSHGLKKAGvSDAKWAIEYEEPAGQAFKQNHPESTVFvdncnvilraimekgGDqddcvstteanela 1172
Cdd:cd00315    1 LRVIDLFAGIGGFRLGLEKAG-FEIVAANEIDKSAAETYEANFPNKLIE---------------GD-------------- 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1173 akLTEEQKSTLPlpGQVDFINGGPPCQGFS---GMNRFNQSSWSkvqcemilAFLSFADY---FRPRYFLLENVRTFVSF 1246
Cdd:cd00315   51 --ITKIDEKDFI--PDIDLLTGGFPCQPFSiagKRKGFEDTRGT--------LFFEIIRIlkeKKPKYFLLENVKGLLTH 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1247 NKGQTFQLTLASLLEMGYQVRFGILEAGAYGVSQSRKRAFIWAA-APEEVLPEWPEPMhvfgVPKLKislsqglhyaavr 1325
Cdd:cd00315  119 DNGNTLKVILNTLEELGYNVYWKLLNASDYGVPQNRERVFIIGIrKDLILNFFSPFPK----PSEKK------------- 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1326 stalgapfrpITVRDTIGdlpsvengdsrtnkeykevavsWFQKEIRGNTIaltdhickamnelnlirckliptrpgadw 1405
Cdd:cd00315  182 ----------KTLKDILR----------------------IRDPDEPSPTL----------------------------- 200
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810 1406 hdlpkrkvtlsdgrveemipfclpnTAERHNGWkglyGRLDWQGNFptsvtdpqpmgkvgMCFHPEQHRILTVRECARSQ 1485
Cdd:cd00315  201 -------------------------TASYGKGT----GSVHPTAPD--------------MIGKESNIRRLTPRECARLQ 237
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 15239810 1486 GFPDSYEFAG-NINHKHRQIGNAVPPPLAFALGRKLKE 1522
Cdd:cd00315  238 GFPDDFEFPGkSVTQAYRQIGNSVPVPVAEAIAKAIKE 275
BAH_DCM_I cd04712
BAH, or Bromo Adjacent Homology domain, as present in DNA (Cytosine-5)-methyltransferases (DCM) ...
732-869 6.63e-42

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: 149.86  E-value: 6.63e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810  732 VGGEMVAVGGAVTLEVDDPD----------EMPAIYFVEYMFESTDHCKMLHGRFLQRGSMTVLGNAANERELFLTNECM 801
Cdd:cd04712    1 IHGLTIRVGDVVSVERDDADsttkwnddhrWLPLVQFVEYMKKGSDGSKMFHGRWLYRGCDTVLGNYANERELFLTNECT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239810  802 TTQLK----DIKGVASFEIRSRPWGhqyrkknitadkldwaralerkvKDLPTEYYCKSLYSPERGGFFSLP 869
Cdd:cd04712   81 CLELDllstEIKGVHKVDWSGTPWG-----------------------KGLPEFFVRQSYYWPERGAFTSLK 129
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
1097-1520 2.62e-36

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: 140.54  E-value: 2.62e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1097 DIFAGCGGLSHGLKKAGVsDAKWAIEYEEPAGQAFKQNHPESTVFVDncnvilraimekggdqddcvstteanelaakLT 1176
Cdd:TIGR00675    3 DLFAGIGGIRLGFEQAGF-KCVFASEIDKYAQKTYEANFGNKVPFGD-------------------------------IT 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1177 EEQKSTLPlpgQVDFINGGPPCQGFS---GMNRFNQSSWSkvqcemilAFLSFADYFR---PRYFLLENVRTFVSFNKGQ 1250
Cdd:TIGR00675   51 KISPSDIP---DFDILLGGFPCQPFSiagKRKGFEDTRGT--------LFFEIVRILKekkPKFFLLENVKGLVSHDKGR 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1251 TFQLTLASLLEMGYQVRFGILEAGAYGVSQSRKRAFIWAAAPEEVLPEWPEPMHVFgvpklkislsqglhyaavrstalg 1330
Cdd:TIGR00675  120 TFKVIIETLEELGYKVYYKVLNAKDFGVPQNRERIYIVGFRDFDDKLNFEFPKPIY------------------------ 175
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1331 apfrpITVRDTIGDLPSVENGDSrtNKEYkevavswfqkeirgntiaLTDHICKAMNELnlirckliptrpgadwhdlpK 1410
Cdd:TIGR00675  176 -----VAKKKRIGDLLDLSVDLE--EKYY------------------LSEEKKNGLLLL--------------------L 210
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810   1411 RKVTLSDGRVEEMIPFclpntaERHNGWKGLYGRLDWQGNFPTSVTDPQPMGKVG-MCFHPEQHRILTVRECARSQGFPD 1489
Cdd:TIGR00675  211 ENMRKKEGTGEQIGSF------YNRESKSSIIRTLSARGYTFVKGGKSVLIVPHKsTVVHPGRIRRLTPRECARLQGFPD 284
                          410       420       430
                   ....*....|....*....|....*....|.
gi 15239810   1490 SYEFAGNINHKHRQIGNAVPPPLAFALGRKL 1520
Cdd:TIGR00675  285 DFKFPVSDSQLYKQAGNAVVVPVIEAIAKQI 315
BAH smart00439
Bromo adjacent homology domain;
910-1049 2.42e-30

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 116.62  E-value: 2.42e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810     910 EYSVEDFVYVNPDSigglkegsktsfksgrniGLRAYVVCQLLEIVPKESRKadlGSFDVKVRRFYRPEDVSAEKAYASD 989
Cdd:smart00439    1 TISVGDFVLVEPDD------------------ADEPYYIGRIEEIFETKKNS---ESKMVRVRWFYRPEETVLEKAALFD 59
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239810     990 IQELYFSQDTVVLPPGALEGKCEVRKKSDMPLSREYPIS--DHIFFCDLFFDTSKGSLKQLP 1049
Cdd:smart00439   60 KNEVFLSDEYDTVPLSDIIGKCNVLYKSDYPGLRPEGSIgePDVFFCESAYDPEKGSFKKLP 121
DNMT1-RFD pfam12047
Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a ...
386-535 3.69e-30

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: 117.06  E-value: 3.69e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810    386 EHLPHRMLHNWALYNSDLRFISLELLPMKQCDDIdvniFGSGVVTDdngswISLNDPDSGSQSHDPDGMCIFLSQIKEWM 465
Cdd:pfam12047    2 EDRPQRKLTDFELYDKDGHLCPFDVLLIEKNVDI----FISGIVKP-----IDEDEPSLDGKGIEDKGMQIKLGPIKEWT 72
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15239810    466 IEFGSD-DIISISIRTDVAWYRLGKPSKLYAPWWKPVLKTARVGISILTFLRVESRvARLSFADVTKRLSG 535
Cdd:pfam12047   73 ISGFDGgEKALIWLSTEFAWYKLLKPSAEYAPIYELVYEKARLSVEVVEFLQRSPG-SELSYEDLINRVLT 142
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
735-869 3.94e-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: 113.17  E-value: 3.94e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810    735 EMVAVGGAVTLEVDDPDEMPAIYFVEYMFESTDHC-KMLHGRFLQRGSMTV--LGNAANERELFLTNECMTTQLKDIKGV 811
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGkKMVRVQWFYRPEETVhrAGKAFNKDELFLSDEEDDVPLSAIIGK 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 15239810    812 ASFEIRSRPWGHQYRKknitadkldwaralerkvKDLPTEYYCKSLYSPERGGFFSLP 869
Cdd:pfam01426   81 CSVLHKSDLESLDPYK------------------IKEPDDFFCELLYDPKTKSFKKLP 120
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
909-1049 1.21e-27

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: 108.93  E-value: 1.21e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810    909 IEYSVEDFVYVNPDSIGglkegsktsfksgrniglRAYVVCQLLEIvpKESRKAdlGSFDVKVRRFYRPEDVSAEKAYAS 988
Cdd:pfam01426    1 ETYSVGDFVLVEPDDAD------------------EPYYVARIEEL--FEDTKN--GKKMVRVQWFYRPEETVHRAGKAF 58
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239810    989 DIQELYFSQDTVVLPPGALEGKCEVRKKSDMPLSREYPIS-DHIFFCDLFFDTSKGSLKQLP 1049
Cdd:pfam01426   59 NKDELFLSDEEDDVPLSAIIGKCSVLHKSDLESLDPYKIKePDDFFCELLYDPKTKSFKKLP 120
BAH smart00439
Bromo adjacent homology domain;
736-869 5.05e-27

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 106.99  E-value: 5.05e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810     736 MVAVGGAVTLEVDDPDEMPAIYFVEYMFESTD--HCKMLHGRFLQRGSMTVLGNAA--NERELFLTNECMTTQLKDIKGV 811
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKnsESKMVRVRWFYRPEETVLEKAAlfDKNEVFLSDEYDTVPLSDIIGK 80
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 15239810     812 ASFEIRSRPWGHQYRKKNItadkldwaralerkvkdLPTEYYCKSLYSPERGGFFSLP 869
Cdd:smart00439   81 CNVLYKSDYPGLRPEGSIG-----------------EPDVFFCESAYDPEKGSFKKLP 121
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
908-1048 4.04e-20

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: 87.45  E-value: 4.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810  908 GIEYSVEDFVYVNPDSIGGLKEgsktsfksgrniglraYVVCQLLEIvpkesRKADLGSFDVKVRRFYRPEDVSAEKAYA 987
Cdd:cd04370    1 GITYEVGDSVYVEPDDSIKSDP----------------PYIARIEEL-----WEDTNGSKQVKVRWFYRPEETPKGLSPF 59
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15239810  988 SDIQELYFSQDTVVLPPGALEGKCEVR--KKSDMPLSREYPISDHIFFCDLFFDTSKGSLKQL 1048
Cdd:cd04370   60 ALRRELFLSDHLDEIPVESIIGKCKVLfvSEFEGLKQRPNKIDTDDFFCRLAYDPTTKEFKAL 122
BAH_Dnmt1_I cd04760
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
734-810 4.79e-11

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: 61.71  E-value: 4.79e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15239810  734 GEMVAVGGAVTLEVDDPDEMPAIYFVEYMFESTDHCKMLHGRFLQRGSMTVLGNAANERELFLTNECMTTQLKDIKG 810
Cdd:cd04760    1 GEELEAGDCVSVKPDDPTKPLYIARVTYMWKDSIGGKMFHAHWFCRGSDTVLGETSDPLELFLVDECEDMALSSIHG 77
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
734-865 1.02e-10

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: 60.48  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810  734 GEMVAVGGAVTLEVDDPD--EMPAIYFVEYMFESTDHCKMLHGRFLQRGSMTVLGNA--ANERELFLTNECMTTQLKDIK 809
Cdd:cd04370    1 GITYEVGDSVYVEPDDSIksDPPYIARIEELWEDTNGSKQVKVRWFYRPEETPKGLSpfALRRELFLSDHLDEIPVESII 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15239810  810 GVASFEIRSRPWGHQYRKKnitadkldwaralerkvKDLPTEYYCKSLYSPERGGF 865
Cdd:cd04370   81 GKCKVLFVSEFEGLKQRPN-----------------KIDTDDFFCRLAYDPTTKEF 119
BAH_fungalPHD cd04710
BAH, or Bromo Adjacent Homology domain, as present in fungal proteins containing PHD domains. ...
907-1039 6.44e-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: 53.14  E-value: 6.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810  907 NGIEYSVEDFVYVNPDSIGglkegsktsfksgrniglRAYVVCQLLEIVPKES-------RKADLGSFDVKVRRFYRPED 979
Cdd:cd04710    8 NGELLKVNDHIYMSSEPPG------------------EPYYIGRIMEFVPKHEfpsgihaRVFPASYFQVRLNWYYRPRD 69
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810  980 VSaeKAYASDIQELYFSQDTVVLPPGALEGKCEVRKKSDMPLSREYPISDHIFFCDLFFD 1039
Cdd:cd04710   70 IS--RRVVADSRLLYASMHSDICPIGSVRGKCTVRHRDQIPDLEEYKKRPNHFYFDQLFD 127
PRK10458 PRK10458
DNA cytosine methylase; Provisional
1096-1266 5.55e-05

DNA cytosine methylase; Provisional


Pssm-ID: 236696 [Multi-domain]  Cd Length: 467  Bit Score: 47.37  E-value: 5.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810  1096 LDIFAGCGGLSHGLKKAG---VSDAKWAIEyeepAGQAFKQNH---PESTVFvdncNVILRAIMEKGgdqDDCVSTTEAn 1169
Cdd:PRK10458   92 IDLFAGIGGIRRGFEAIGgqcVFTSEWNKH----AVRTYKANWycdPATHRF----NEDIRDITLSH---KEGVSDEEA- 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239810  1170 elAAKLTEEqkstlpLPgQVDFINGGPPCQGFS--GMNRFNqsSWSKV---QCEM--ILAF--LSFADYFRPRYFLLENV 1240
Cdd:PRK10458  160 --AEHIRQH------IP-DHDVLLAGFPCQPFSlaGVSKKN--SLGRAhgfECETqgTLFFdvARIIDAKRPAIFVLENV 228
                         170       180
                  ....*....|....*....|....*.
gi 15239810  1241 RTFVSFNKGQTFQLTLASLLEMGYQV 1266
Cdd:PRK10458  229 KNLKSHDKGKTFRIIMQTLDELGYDV 254
BAH_Dnmt1_II cd04711
BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5) ...
968-1022 1.68e-03

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: 40.17  E-value: 1.68e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15239810  968 DVKVR--RFYRPEDVSA--EKAYASDIQELYFSQDTVVLPPGALEGKCEVRKKSDMPLS 1022
Cdd:cd04711   49 DIKLRinKFYRPENTHKgfKATYHADINMLYWSDEEATVDFSAVQGRCTVEYGEDLPES 107
 
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