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Conserved domains on  [gi|755528341|ref|XP_011240695|]
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DNA (cytosine-5)-methyltransferase 1 isoform X2 [Mus musculus]

Protein Classification

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) ...
 858-993 3.97e-80

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: 259.74  E-value: 3.97e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  858 NETLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIHCGKK-KGKVNEADIKLRLYKFYRPENTHRSYNGSYHTDINMLYW 936
Cdd:cd04711     1 DEDLYPEYYRKSSDYIKGSNLDAPEPFRIGRIKEIFCAKRsNGKPNESDIKLRINKFYRPENTHKGFKATYHADINMLYW 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755528341  937 SDEEAVVNFSDVQGRCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKNFEDPPN 993
Cdd:cd04711    81 SDEEATVDFSAVQGRCTVEYGEDLPESVQEYSGGGPDRFYFLEAYNAKTKSFEDPPN 137
BAH_Dnmt1_I cd04760
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 647-770 2.95e-64

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


:

Pssm-ID: 240107  Cd Length: 124  Bit Score: 213.86  E-value: 2.95e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  647 EMLEVGDCVSVIPDDSSKPLYLARVTALWEDKNGQMMFHAHWFCAGTDTVLGATSDPLELFLVGECENMQLSYIHSKVKV 726
Cdd:cd04760     2 EELEAGDCVSVKPDDPTKPLYIARVTYMWKDSIGGKMFHAHWFCRGSDTVLGETSDPLELFLVDECEDMALSSIHGKVNV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 755528341  727 IYKAPSENWAMEGGTDPEtTLPGAEDGKTYFFQLWYNQEYARFE 770
Cdd:cd04760    82 IYKAPSENWSMEGGMDEE-DEIFEDDGKTFFYQKWYDPECARFE 124
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
1029-1487 5.93e-64

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


:

Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 218.91  E-value: 5.93e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1029 PKLRTLDVFSGCGGLSEGFHQAGIsETLWAIEMWDPAAQAFRLNNPGTTVFTEDcnvlLKLVMAGEVtnslgqrlpqKGD 1108
Cdd:COG0270     2 KKLTVIDLFAGAGGLSLGFEKAGF-EVVFAVEIDPDACETYRANFPEAKVIEGD----IRDIDPEEL----------IPD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1109 VEMLCGGPPCQGFSGMNRfnSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSYRRSMVLKLTLRCLVRMGYQCTF 1188
Cdd:COG0270    67 VDLLIGGPPCQPFSVAGK--RKGLEDPRGTLFFEFIRIVEELRPKAFVLENVPGLLSSDKGKTFEEILKELEELGYRVDY 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1189 GVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLPE 1268
Cdd:COG0270   145 KVLNAADYGVPQNRERVFIVGFRKDLDLFEFPEPTH----------------------------LKPYVTVGDALEDLPD 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1269 iqngasnseipyngeplswfqrqlrgshyqpilrDHICKDMSPLVAARmrhiplfpgsdwrdlpniqvrlgdgviahklq 1348
Cdd:COG0270   197 ----------------------------------AHEARYLSETITAG-------------------------------- 210

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1349 ytfhdvkngysstgalrgvcscaegkacdpesrqfstlipwclphtgnrhnhwaglygrlewdgffsttvtnpepMGKQG 1428
Cdd:COG0270   211 ---------------------------------------------------------------------------YGGGG 215

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755528341 1429 RVLHPEQHRVVSVRECARSQGFPDSYRFFGNILDRHRQVGNAVPPPLAKAIGLEIKLCL 1487
Cdd:COG0270   216 RFLHPGEPRRLTVREAARLQGFPDDFKFPGSKTQAYRQIGNAVPPPLAEAIAKAILKAL 274
DNMT1-RFD pfam12047
Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a ...
 294-429 3.15e-52

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: 180.23  E-value: 3.15e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341   294 YEDSPMHRFTSFSVYCSRGHLCPVDTGLIEKNVELYFSGCAKAIHDENPSMEG-GINGKN----LGPINQWWLSGFDGGE 368
Cdd:pfam12047    1 EEDRPQRKLTDFELYDKDGHLCPFDVLLIEKNVDIFISGIVKPIDEDEPSLDGkGIEDKGmqikLGPIKEWTISGFDGGE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755528341   369 KVLIGFSTAFAEYILMEPSKEYEPIFGLMQEKIYISKIVVEFLQNNP--DAVYEDLINKIETT 429
Cdd:pfam12047   81 KALIWLSTEFAWYKLLKPSAEYAPIYELVYEKARLSVEVVEFLQRSPgsELSYEDLINRVLTS 143
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 537-583 1.55e-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: 83.17  E-value: 1.55e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 755528341   537 ENAMKRRRCGVCEVCQQPE-CGKCKACKDMVKFGGTGRSKQACLKRRC 583
Cdd:pfam02008    1 RNRRKRRRCGVCEGCQRPEdCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
PHA03169 super family cl27451
hypothetical protein; Provisional
 68-198 8.19e-03

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PHA03169:

Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.34  E-value: 8.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341   68 KEESEEGNSAESAAEERDQDKKRRVVDTESGAAAAVEKLEEVTAGTQLGPEEPCEQEDDNRSlrRHTRELSLRRKSKEDP 147
Cdd:PHA03169   97 SESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPS--PNQQPSSFLQPSHEDS 174

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755528341  148 DREARPETHLDEDEDGkkdkrssrprsqprDPAAKRRPKEAEPEQVAPETP 198
Cdd:PHA03169  175 PEEPEPPTSEPEPDSP--------------GPPQSETPTSSPPPQSPPDEP 211
 
Name Accession Description Interval E-value
BAH_Dnmt1_II cd04711
BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5) ...
 858-993 3.97e-80

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: 259.74  E-value: 3.97e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  858 NETLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIHCGKK-KGKVNEADIKLRLYKFYRPENTHRSYNGSYHTDINMLYW 936
Cdd:cd04711     1 DEDLYPEYYRKSSDYIKGSNLDAPEPFRIGRIKEIFCAKRsNGKPNESDIKLRINKFYRPENTHKGFKATYHADINMLYW 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755528341  937 SDEEAVVNFSDVQGRCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKNFEDPPN 993
Cdd:cd04711    81 SDEEATVDFSAVQGRCTVEYGEDLPESVQEYSGGGPDRFYFLEAYNAKTKSFEDPPN 137
BAH_Dnmt1_I cd04760
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 647-770 2.95e-64

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


Pssm-ID: 240107  Cd Length: 124  Bit Score: 213.86  E-value: 2.95e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  647 EMLEVGDCVSVIPDDSSKPLYLARVTALWEDKNGQMMFHAHWFCAGTDTVLGATSDPLELFLVGECENMQLSYIHSKVKV 726
Cdd:cd04760     2 EELEAGDCVSVKPDDPTKPLYIARVTYMWKDSIGGKMFHAHWFCRGSDTVLGETSDPLELFLVDECEDMALSSIHGKVNV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 755528341  727 IYKAPSENWAMEGGTDPEtTLPGAEDGKTYFFQLWYNQEYARFE 770
Cdd:cd04760    82 IYKAPSENWSMEGGMDEE-DEIFEDDGKTFFYQKWYDPECARFE 124
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
1029-1487 5.93e-64

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


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 218.91  E-value: 5.93e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1029 PKLRTLDVFSGCGGLSEGFHQAGIsETLWAIEMWDPAAQAFRLNNPGTTVFTEDcnvlLKLVMAGEVtnslgqrlpqKGD 1108
Cdd:COG0270     2 KKLTVIDLFAGAGGLSLGFEKAGF-EVVFAVEIDPDACETYRANFPEAKVIEGD----IRDIDPEEL----------IPD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1109 VEMLCGGPPCQGFSGMNRfnSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSYRRSMVLKLTLRCLVRMGYQCTF 1188
Cdd:COG0270    67 VDLLIGGPPCQPFSVAGK--RKGLEDPRGTLFFEFIRIVEELRPKAFVLENVPGLLSSDKGKTFEEILKELEELGYRVDY 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1189 GVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLPE 1268
Cdd:COG0270   145 KVLNAADYGVPQNRERVFIVGFRKDLDLFEFPEPTH----------------------------LKPYVTVGDALEDLPD 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1269 iqngasnseipyngeplswfqrqlrgshyqpilrDHICKDMSPLVAARmrhiplfpgsdwrdlpniqvrlgdgviahklq 1348
Cdd:COG0270   197 ----------------------------------AHEARYLSETITAG-------------------------------- 210

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1349 ytfhdvkngysstgalrgvcscaegkacdpesrqfstlipwclphtgnrhnhwaglygrlewdgffsttvtnpepMGKQG 1428
Cdd:COG0270   211 ---------------------------------------------------------------------------YGGGG 215

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755528341 1429 RVLHPEQHRVVSVRECARSQGFPDSYRFFGNILDRHRQVGNAVPPPLAKAIGLEIKLCL 1487
Cdd:COG0270   216 RFLHPGEPRRLTVREAARLQGFPDDFKFPGSKTQAYRQIGNAVPPPLAEAIAKAILKAL 274
DNMT1-RFD pfam12047
Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a ...
 294-429 3.15e-52

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: 180.23  E-value: 3.15e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341   294 YEDSPMHRFTSFSVYCSRGHLCPVDTGLIEKNVELYFSGCAKAIHDENPSMEG-GINGKN----LGPINQWWLSGFDGGE 368
Cdd:pfam12047    1 EEDRPQRKLTDFELYDKDGHLCPFDVLLIEKNVDIFISGIVKPIDEDEPSLDGkGIEDKGmqikLGPIKEWTISGFDGGE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755528341   369 KVLIGFSTAFAEYILMEPSKEYEPIFGLMQEKIYISKIVVEFLQNNP--DAVYEDLINKIETT 429
Cdd:pfam12047   81 KALIWLSTEFAWYKLLKPSAEYAPIYELVYEKARLSVEVVEFLQRSPgsELSYEDLINRVLTS 143
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
1031-1484 1.56e-39

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 150.16  E-value: 1.56e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1031 LRTLDVFSGCGGLSEGFHQAGIsETLWAIEMWDPAAQAFRLNNPgTTVFtedcnvllklvmaGEVTNSLGQRLPqkgDVE 1110
Cdd:pfam00145    1 FKFIDLFAGIGGFRLGLEQAGF-ECVAANEIDKSAAKTYEANFP-KVPI-------------GDITLIDIKDIP---DID 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1111 MLCGGPPCQGFS--GMNRFNSRTYskfkNSLVVSFLSYCDYYRPRFFLLENVRNFVSYRRSMVLKLTLRCLVRMGYQCTF 1188
Cdd:pfam00145   63 ILTGGFPCQDFSiaGKQKGFEDTR----GTLFFEIIRIIKEKKPKAFLLENVKGLLSHDNGNTLNVILETLEELGYHVSW 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1189 GVLQAGQYGVAQTRRRAIILAAAPG-EKLPLFPEPlhvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLP 1267
Cdd:pfam00145  139 KVLNASDYGVPQNRERVFIVGIRKDlNLNVLVPVP------------------------------EFDFPKPKDLTGTIR 188

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1268 EIQNGASNSEIPYNGEplswfqrqlrgshyqpilrDHICKDMSplvaaRMRHIPLFPGSDWRDlpniqvrlgdgviahkl 1347
Cdd:pfam00145  189 DLLEEPSLDENKYNLS-------------------DKFVENHE-----RRKPTTKAPGGGYPT----------------- 227

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1348 QYTFHDVKNGYSStgalrgvcscaegkacdpesrqfstlipwclphtgnrhNHWAGLYGRlewDGFFSTTVTnpEPMGKQ 1427
Cdd:pfam00145  228 YLLRNRIDKVEEG--------------------------------------KGPSFTYRK---SGRPEAPKT--GILGKN 264

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 755528341  1428 GR--VLHPEQHRVVSVRECARSQGFPDSYRFFGNILDRHRQVGNAVPPPLAKAIGLEIK 1484
Cdd:pfam00145  265 GErfRGHPKNIRRLTPRECARLQGFPDDFIFPGSKTQLYKQIGNAVPVPVAEAIAKAIK 323
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
 1031-1484 2.42e-35

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: 136.60  E-value: 2.42e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1031 LRTLDVFSGCGGLSEGFHQAGiSETLWAIEMWDPAAQAFRLNNPGTTVFtedcnvllklvmaGEVTNSLGQRLPqkGDVE 1110
Cdd:cd00315     1 LRVIDLFAGIGGFRLGLEKAG-FEIVAANEIDKSAAETYEANFPNKLIE-------------GDITKIDEKDFI--PDID 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1111 MLCGGPPCQGFS--GMNRFNSRTYSKfknslvvSFLSYCDY---YRPRFFLLENVRNFVSYRRSMVLKLTLRCLVRMGYQ 1185
Cdd:cd00315    65 LLTGGFPCQPFSiaGKRKGFEDTRGT-------LFFEIIRIlkeKKPKYFLLENVKGLLTHDNGNTLKVILNTLEELGYN 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1186 CTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFapracqlsvvvDDKKFVSNITRLSSGPFRTITVRdtmsd 1265
Cdd:cd00315   138 VYWKLLNASDYGVPQNRERVFIIGIRKDLILNFFSPFPKPS-----------EKKKTLKDILRIRDPDEPSPTLT----- 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1266 lpeiqngASNseipyngeplswfqrqlrgshyqpilrdhickdmsplvaarmrhiplfpgsdwrdlpniqvrlgdgviaH 1345
Cdd:cd00315   202 -------ASY---------------------------------------------------------------------G 205

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1346 KLQYTFHDVKNGYSstgalrgvcscaegkacdpesrqfstlipwclphtgnrhnhwaglygrlewdgffsttvtnpepmg 1425
Cdd:cd00315   206 KGTGSVHPTAPDMI------------------------------------------------------------------ 219

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1426 kqgrvLHPEQHRVVSVRECARSQGFPDSYRFFG-NILDRHRQVGNAVPPPLAKAIGLEIK 1484
Cdd:cd00315   220 -----GKESNIRRLTPRECARLQGFPDDFEFPGkSVTQAYRQIGNSVPVPVAEAIAKAIK 274
BAH smart00439
Bromo adjacent homology domain;
871-992 1.03e-32

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 123.56  E-value: 1.03e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341    871 DYIKGSNLDAPEPYRIGRIKEIHCGKKkgkvNEADIKLRLYKFYRPENTHRSYNgsYHTDINMLYWSDEEAVVNFSDVQG 950
Cdd:smart00439    6 DFVLVEPDDADEPYYIGRIEEIFETKK----NSESKMVRVRWFYRPEETVLEKA--ALFDKNEVFLSDEYDTVPLSDIIG 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 755528341    951 RCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKNFEDPP 992
Cdd:smart00439   80 KCNVLYKSDYPGLRPEGSIGEPDVFFCESAYDPEKGSFKKLP 121
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
 1035-1483 1.25e-32

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: 129.75  E-value: 1.25e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1035 DVFSGCGGLSEGFHQAGIsETLWAIEmWDPAAQA-FRLNNPGTTVFtedcnvllklvmaGEVTNSLGQRLPqkgDVEMLC 1113
Cdd:TIGR00675    3 DLFAGIGGIRLGFEQAGF-KCVFASE-IDKYAQKtYEANFGNKVPF-------------GDITKISPSDIP---DFDILL 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1114 GGPPCQGFSgMNRFNsRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSYRRSMVLKLTLRCLVRMGYQCTFGVLQA 1193
Cdd:TIGR00675   65 GGFPCQPFS-IAGKR-KGFEDTRGTLFFEIVRILKEKKPKFFLLENVKGLVSHDKGRTFKVIIETLEELGYKVYYKVLNA 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1194 GQYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlsSGPFRTITVRDTMSDLPEIQNGA 1273
Cdd:TIGR00675  143 KDFGVPQNRERIYIVGFRDFDDKLNFEFPKP--------------------------IYVAKKKRIGDLLDLSVDLEEKY 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1274 SNSEIPYNGEplswfqrqlrgshyqpilrdhickdmsPLVAARMRHIPLFpGSDWRdlpNIQVRLGDGVIAHKLqytfhd 1353
Cdd:TIGR00675  197 YLSEEKKNGL---------------------------LLLLENMRKKEGT-GEQIG---SFYNRESKSSIIRTL------ 239

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1354 vkngysstgalrgvcscaegkacdpesrqfstlipwclphTGNRHNHWAGlygrlewdgffstTVTNPEPMGKQGRVlHP 1433
Cdd:TIGR00675  240 ----------------------------------------SARGYTFVKG-------------GKSVLIVPHKSTVV-HP 265

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 755528341  1434 EQHRVVSVRECARSQGFPDSYRFFGNILDRHRQVGNAVPPPLAKAIGLEI 1483
Cdd:TIGR00675  266 GRIRRLTPRECARLQGFPDDFKFPVSDSQLYKQAGNAVVVPVIEAIAKQI 315
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 859-992 5.27e-31

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: 118.56  E-value: 5.27e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341   859 ETLYPEHYRKYSDYikgsnlDAPEPYRIGRIKEIHCGKKKGKvneadIKLRLYKFYRPENTHRSYNGSYHTDinMLYWSD 938
Cdd:pfam01426    1 ETYSVGDFVLVEPD------DADEPYYVARIEELFEDTKNGK-----KMVRVQWFYRPEETVHRAGKAFNKD--ELFLSD 67

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 755528341   939 EEAVVNFSDVQGRCTVEYGEDLLESIQDYSqGGPDRFYFLEAYNSKTKNFEDPP 992
Cdd:pfam01426   68 EEDDVPLSAIIGKCSVLHKSDLESLDPYKI-KEPDDFFCELLYDPKTKSFKKLP 120
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 647-773 5.52e-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: 107.01  E-value: 5.52e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341   647 EMLEVGDCVSVIPDDSSKPLYLARVTALWED-KNGQMMFHAHWFCAGTDTV--LGATSDPLELFLVGECENMQLSYIHSK 723
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDtKNGKKMVRVQWFYRPEETVhrAGKAFNKDELFLSDEEDDVPLSAIIGK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 755528341   724 VKVIYKAPSENWAMEGGTDPettlpgaedgKTYFFQLWYNQEYARFESPP 773
Cdd:pfam01426   81 CSVLHKSDLESLDPYKIKEP----------DDFFCELLYDPKTKSFKKLP 120
BAH smart00439
Bromo adjacent homology domain;
648-773 2.35e-26

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 105.07  E-value: 2.35e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341    648 MLEVGDCVSVIPDDSSKPLYLARVTALWEDKNG--QMMFHAHWFCAGTDTVLGAT--SDPLELFLVGECENMQLSYIHSK 723
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNseSKMVRVRWFYRPEETVLEKAalFDKNEVFLSDEYDTVPLSDIIGK 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 755528341    724 VKVIYKAPSENWAMEGGTDPETtlpgaedgkTYFFQLWYNQEYARFESPP 773
Cdd:smart00439   81 CNVLYKSDYPGLRPEGSIGEPD---------VFFCESAYDPEKGSFKKLP 121
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 537-583 1.55e-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: 83.17  E-value: 1.55e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 755528341   537 ENAMKRRRCGVCEVCQQPE-CGKCKACKDMVKFGGTGRSKQACLKRRC 583
Cdd:pfam02008    1 RNRRKRRRCGVCEGCQRPEdCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
PHA03169 PHA03169
hypothetical protein; Provisional
 68-198 8.19e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.34  E-value: 8.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341   68 KEESEEGNSAESAAEERDQDKKRRVVDTESGAAAAVEKLEEVTAGTQLGPEEPCEQEDDNRSlrRHTRELSLRRKSKEDP 147
Cdd:PHA03169   97 SESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPS--PNQQPSSFLQPSHEDS 174

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755528341  148 DREARPETHLDEDEDGkkdkrssrprsqprDPAAKRRPKEAEPEQVAPETP 198
Cdd:PHA03169  175 PEEPEPPTSEPEPDSP--------------GPPQSETPTSSPPPQSPPDEP 211
 
Name Accession Description Interval E-value
BAH_Dnmt1_II cd04711
BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5) ...
 858-993 3.97e-80

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: 259.74  E-value: 3.97e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  858 NETLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIHCGKK-KGKVNEADIKLRLYKFYRPENTHRSYNGSYHTDINMLYW 936
Cdd:cd04711     1 DEDLYPEYYRKSSDYIKGSNLDAPEPFRIGRIKEIFCAKRsNGKPNESDIKLRINKFYRPENTHKGFKATYHADINMLYW 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755528341  937 SDEEAVVNFSDVQGRCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKNFEDPPN 993
Cdd:cd04711    81 SDEEATVDFSAVQGRCTVEYGEDLPESVQEYSGGGPDRFYFLEAYNAKTKSFEDPPN 137
BAH_Dnmt1_I cd04760
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 647-770 2.95e-64

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


Pssm-ID: 240107  Cd Length: 124  Bit Score: 213.86  E-value: 2.95e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  647 EMLEVGDCVSVIPDDSSKPLYLARVTALWEDKNGQMMFHAHWFCAGTDTVLGATSDPLELFLVGECENMQLSYIHSKVKV 726
Cdd:cd04760     2 EELEAGDCVSVKPDDPTKPLYIARVTYMWKDSIGGKMFHAHWFCRGSDTVLGETSDPLELFLVDECEDMALSSIHGKVNV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 755528341  727 IYKAPSENWAMEGGTDPEtTLPGAEDGKTYFFQLWYNQEYARFE 770
Cdd:cd04760    82 IYKAPSENWSMEGGMDEE-DEIFEDDGKTFFYQKWYDPECARFE 124
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
1029-1487 5.93e-64

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


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 218.91  E-value: 5.93e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1029 PKLRTLDVFSGCGGLSEGFHQAGIsETLWAIEMWDPAAQAFRLNNPGTTVFTEDcnvlLKLVMAGEVtnslgqrlpqKGD 1108
Cdd:COG0270     2 KKLTVIDLFAGAGGLSLGFEKAGF-EVVFAVEIDPDACETYRANFPEAKVIEGD----IRDIDPEEL----------IPD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1109 VEMLCGGPPCQGFSGMNRfnSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSYRRSMVLKLTLRCLVRMGYQCTF 1188
Cdd:COG0270    67 VDLLIGGPPCQPFSVAGK--RKGLEDPRGTLFFEFIRIVEELRPKAFVLENVPGLLSSDKGKTFEEILKELEELGYRVDY 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1189 GVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLPE 1268
Cdd:COG0270   145 KVLNAADYGVPQNRERVFIVGFRKDLDLFEFPEPTH----------------------------LKPYVTVGDALEDLPD 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1269 iqngasnseipyngeplswfqrqlrgshyqpilrDHICKDMSPLVAARmrhiplfpgsdwrdlpniqvrlgdgviahklq 1348
Cdd:COG0270   197 ----------------------------------AHEARYLSETITAG-------------------------------- 210

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1349 ytfhdvkngysstgalrgvcscaegkacdpesrqfstlipwclphtgnrhnhwaglygrlewdgffsttvtnpepMGKQG 1428
Cdd:COG0270   211 ---------------------------------------------------------------------------YGGGG 215

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755528341 1429 RVLHPEQHRVVSVRECARSQGFPDSYRFFGNILDRHRQVGNAVPPPLAKAIGLEIKLCL 1487
Cdd:COG0270   216 RFLHPGEPRRLTVREAARLQGFPDDFKFPGSKTQAYRQIGNAVPPPLAEAIAKAILKAL 274
DNMT1-RFD pfam12047
Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a ...
 294-429 3.15e-52

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: 180.23  E-value: 3.15e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341   294 YEDSPMHRFTSFSVYCSRGHLCPVDTGLIEKNVELYFSGCAKAIHDENPSMEG-GINGKN----LGPINQWWLSGFDGGE 368
Cdd:pfam12047    1 EEDRPQRKLTDFELYDKDGHLCPFDVLLIEKNVDIFISGIVKPIDEDEPSLDGkGIEDKGmqikLGPIKEWTISGFDGGE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755528341   369 KVLIGFSTAFAEYILMEPSKEYEPIFGLMQEKIYISKIVVEFLQNNP--DAVYEDLINKIETT 429
Cdd:pfam12047   81 KALIWLSTEFAWYKLLKPSAEYAPIYELVYEKARLSVEVVEFLQRSPgsELSYEDLINRVLTS 143
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
1031-1484 1.56e-39

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 150.16  E-value: 1.56e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1031 LRTLDVFSGCGGLSEGFHQAGIsETLWAIEMWDPAAQAFRLNNPgTTVFtedcnvllklvmaGEVTNSLGQRLPqkgDVE 1110
Cdd:pfam00145    1 FKFIDLFAGIGGFRLGLEQAGF-ECVAANEIDKSAAKTYEANFP-KVPI-------------GDITLIDIKDIP---DID 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1111 MLCGGPPCQGFS--GMNRFNSRTYskfkNSLVVSFLSYCDYYRPRFFLLENVRNFVSYRRSMVLKLTLRCLVRMGYQCTF 1188
Cdd:pfam00145   63 ILTGGFPCQDFSiaGKQKGFEDTR----GTLFFEIIRIIKEKKPKAFLLENVKGLLSHDNGNTLNVILETLEELGYHVSW 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1189 GVLQAGQYGVAQTRRRAIILAAAPG-EKLPLFPEPlhvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLP 1267
Cdd:pfam00145  139 KVLNASDYGVPQNRERVFIVGIRKDlNLNVLVPVP------------------------------EFDFPKPKDLTGTIR 188

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1268 EIQNGASNSEIPYNGEplswfqrqlrgshyqpilrDHICKDMSplvaaRMRHIPLFPGSDWRDlpniqvrlgdgviahkl 1347
Cdd:pfam00145  189 DLLEEPSLDENKYNLS-------------------DKFVENHE-----RRKPTTKAPGGGYPT----------------- 227

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1348 QYTFHDVKNGYSStgalrgvcscaegkacdpesrqfstlipwclphtgnrhNHWAGLYGRlewDGFFSTTVTnpEPMGKQ 1427
Cdd:pfam00145  228 YLLRNRIDKVEEG--------------------------------------KGPSFTYRK---SGRPEAPKT--GILGKN 264

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 755528341  1428 GR--VLHPEQHRVVSVRECARSQGFPDSYRFFGNILDRHRQVGNAVPPPLAKAIGLEIK 1484
Cdd:pfam00145  265 GErfRGHPKNIRRLTPRECARLQGFPDDFIFPGSKTQLYKQIGNAVPVPVAEAIAKAIK 323
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
 1031-1484 2.42e-35

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: 136.60  E-value: 2.42e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1031 LRTLDVFSGCGGLSEGFHQAGiSETLWAIEMWDPAAQAFRLNNPGTTVFtedcnvllklvmaGEVTNSLGQRLPqkGDVE 1110
Cdd:cd00315     1 LRVIDLFAGIGGFRLGLEKAG-FEIVAANEIDKSAAETYEANFPNKLIE-------------GDITKIDEKDFI--PDID 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1111 MLCGGPPCQGFS--GMNRFNSRTYSKfknslvvSFLSYCDY---YRPRFFLLENVRNFVSYRRSMVLKLTLRCLVRMGYQ 1185
Cdd:cd00315    65 LLTGGFPCQPFSiaGKRKGFEDTRGT-------LFFEIIRIlkeKKPKYFLLENVKGLLTHDNGNTLKVILNTLEELGYN 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1186 CTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFapracqlsvvvDDKKFVSNITRLSSGPFRTITVRdtmsd 1265
Cdd:cd00315   138 VYWKLLNASDYGVPQNRERVFIIGIRKDLILNFFSPFPKPS-----------EKKKTLKDILRIRDPDEPSPTLT----- 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1266 lpeiqngASNseipyngeplswfqrqlrgshyqpilrdhickdmsplvaarmrhiplfpgsdwrdlpniqvrlgdgviaH 1345
Cdd:cd00315   202 -------ASY---------------------------------------------------------------------G 205

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1346 KLQYTFHDVKNGYSstgalrgvcscaegkacdpesrqfstlipwclphtgnrhnhwaglygrlewdgffsttvtnpepmg 1425
Cdd:cd00315   206 KGTGSVHPTAPDMI------------------------------------------------------------------ 219

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341 1426 kqgrvLHPEQHRVVSVRECARSQGFPDSYRFFG-NILDRHRQVGNAVPPPLAKAIGLEIK 1484
Cdd:cd00315   220 -----GKESNIRRLTPRECARLQGFPDDFEFPGkSVTQAYRQIGNSVPVPVAEAIAKAIK 274
BAH smart00439
Bromo adjacent homology domain;
871-992 1.03e-32

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 123.56  E-value: 1.03e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341    871 DYIKGSNLDAPEPYRIGRIKEIHCGKKkgkvNEADIKLRLYKFYRPENTHRSYNgsYHTDINMLYWSDEEAVVNFSDVQG 950
Cdd:smart00439    6 DFVLVEPDDADEPYYIGRIEEIFETKK----NSESKMVRVRWFYRPEETVLEKA--ALFDKNEVFLSDEYDTVPLSDIIG 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 755528341    951 RCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKNFEDPP 992
Cdd:smart00439   80 KCNVLYKSDYPGLRPEGSIGEPDVFFCESAYDPEKGSFKKLP 121
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
 1035-1483 1.25e-32

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: 129.75  E-value: 1.25e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1035 DVFSGCGGLSEGFHQAGIsETLWAIEmWDPAAQA-FRLNNPGTTVFtedcnvllklvmaGEVTNSLGQRLPqkgDVEMLC 1113
Cdd:TIGR00675    3 DLFAGIGGIRLGFEQAGF-KCVFASE-IDKYAQKtYEANFGNKVPF-------------GDITKISPSDIP---DFDILL 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1114 GGPPCQGFSgMNRFNsRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSYRRSMVLKLTLRCLVRMGYQCTFGVLQA 1193
Cdd:TIGR00675   65 GGFPCQPFS-IAGKR-KGFEDTRGTLFFEIVRILKEKKPKFFLLENVKGLVSHDKGRTFKVIIETLEELGYKVYYKVLNA 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1194 GQYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlsSGPFRTITVRDTMSDLPEIQNGA 1273
Cdd:TIGR00675  143 KDFGVPQNRERIYIVGFRDFDDKLNFEFPKP--------------------------IYVAKKKRIGDLLDLSVDLEEKY 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1274 SNSEIPYNGEplswfqrqlrgshyqpilrdhickdmsPLVAARMRHIPLFpGSDWRdlpNIQVRLGDGVIAHKLqytfhd 1353
Cdd:TIGR00675  197 YLSEEKKNGL---------------------------LLLLENMRKKEGT-GEQIG---SFYNRESKSSIIRTL------ 239

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  1354 vkngysstgalrgvcscaegkacdpesrqfstlipwclphTGNRHNHWAGlygrlewdgffstTVTNPEPMGKQGRVlHP 1433
Cdd:TIGR00675  240 ----------------------------------------SARGYTFVKG-------------GKSVLIVPHKSTVV-HP 265

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 755528341  1434 EQHRVVSVRECARSQGFPDSYRFFGNILDRHRQVGNAVPPPLAKAIGLEI 1483
Cdd:TIGR00675  266 GRIRRLTPRECARLQGFPDDFKFPVSDSQLYKQAGNAVVVPVIEAIAKQI 315
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 859-992 5.27e-31

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: 118.56  E-value: 5.27e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341   859 ETLYPEHYRKYSDYikgsnlDAPEPYRIGRIKEIHCGKKKGKvneadIKLRLYKFYRPENTHRSYNGSYHTDinMLYWSD 938
Cdd:pfam01426    1 ETYSVGDFVLVEPD------DADEPYYVARIEELFEDTKNGK-----KMVRVQWFYRPEETVHRAGKAFNKD--ELFLSD 67

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 755528341   939 EEAVVNFSDVQGRCTVEYGEDLLESIQDYSqGGPDRFYFLEAYNSKTKNFEDPP 992
Cdd:pfam01426   68 EEDDVPLSAIIGKCSVLHKSDLESLDPYKI-KEPDDFFCELLYDPKTKSFKKLP 120
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 647-773 5.52e-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: 107.01  E-value: 5.52e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341   647 EMLEVGDCVSVIPDDSSKPLYLARVTALWED-KNGQMMFHAHWFCAGTDTV--LGATSDPLELFLVGECENMQLSYIHSK 723
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDtKNGKKMVRVQWFYRPEETVhrAGKAFNKDELFLSDEEDDVPLSAIIGK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 755528341   724 VKVIYKAPSENWAMEGGTDPettlpgaedgKTYFFQLWYNQEYARFESPP 773
Cdd:pfam01426   81 CSVLHKSDLESLDPYKIKEP----------DDFFCELLYDPKTKSFKKLP 120
BAH smart00439
Bromo adjacent homology domain;
648-773 2.35e-26

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 105.07  E-value: 2.35e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341    648 MLEVGDCVSVIPDDSSKPLYLARVTALWEDKNG--QMMFHAHWFCAGTDTVLGAT--SDPLELFLVGECENMQLSYIHSK 723
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNseSKMVRVRWFYRPEETVLEKAalFDKNEVFLSDEYDTVPLSDIIGK 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 755528341    724 VKVIYKAPSENWAMEGGTDPETtlpgaedgkTYFFQLWYNQEYARFESPP 773
Cdd:smart00439   81 CNVLYKSDYPGLRPEGSIGEPD---------VFFCESAYDPEKGSFKKLP 121
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 646-771 2.60e-21

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: 90.91  E-value: 2.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  646 EEMLEVGDCVSVIPDDS--SKPLYLARVTALWEDKNGQMMFHAHWFCAGTDTVLGATS--DPLELFLVGECENMQLSYIH 721
Cdd:cd04370     1 GITYEVGDSVYVEPDDSikSDPPYIARIEELWEDTNGSKQVKVRWFYRPEETPKGLSPfaLRRELFLSDHLDEIPVESII 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 755528341  722 SKVKVIYKAPSENWAMeggtdpettLPGAEDGKTYFFQLWYNQEYARFES 771
Cdd:cd04370    81 GKCKVLFVSEFEGLKQ---------RPNKIDTDDFFCRLAYDPTTKEFKA 121
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 537-583 1.55e-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: 83.17  E-value: 1.55e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 755528341   537 ENAMKRRRCGVCEVCQQPE-CGKCKACKDMVKFGGTGRSKQACLKRRC 583
Cdd:pfam02008    1 RNRRKRRRCGVCEGCQRPEdCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 862-988 1.33e-17

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


Pssm-ID: 239835 [Multi-domain]  Cd Length: 123  Bit Score: 80.13  E-value: 1.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  862 YPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIHCGKkkgkvnEADIKLRLYKFYRPENTHRSYngSYHTDINMLYWSDEEA 941
Cdd:cd04370     1 GITYEVGDSVYVEPDDSIKSDPPYIARIEELWEDT------NGSKQVKVRWFYRPEETPKGL--SPFALRRELFLSDHLD 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 755528341  942 VVNFSDVQGRCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKNF 988
Cdd:cd04370    73 EIPVESIIGKCKVLFVSEFEGLKQRPNKIDTDDFFCRLAYDPTTKEF 119
BAH_plantDCM_II cd04708
BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5) ...
 820-1043 1.17e-12

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: 68.64  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  820 TKNGVVYRLGDSVYLPPEAFTfnikvaspvkrpkkdpvnetlypEHYRKYSDYIKGSNLDAPePYRIGRIKEIHCGK--K 897
Cdd:cd04708     2 VYDGVTYSVGDFLYVSPDAFA-----------------------EEERERATFKAGRNVGLK-AFVVCQVLEIVVEKesK 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  898 KGKVNEADIKLRlyKFYRPENThrSYNGSYHTDINMLYWSDEEAVVNFSDVQGRCTVEYGEDLLESiQDYSQGGPdRFYF 977
Cdd:cd04708    58 QADVASTQVKVR--RFYRPEDV--SPEKAYASDIREVYYSEDTLTVPVEAVEGKCEVRKKSDLPDS-DAPVIFEH-VFFC 131

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755528341  978 LEAYNSKTKNFEDPPNHARSPGNKGKGKGKGKGK-----GKHQVSEPKEPEAAIKLPKLRTLDVFSGCGGL 1043
Cdd:cd04708   132 ELLYDPAKGSLKQLPPNIKEEAYSTGASDSALRKrkgkgKGDSESDSEAPVKAPKENRLATLDIFAGCGGL 202
BAH_DCM_I cd04712
BAH, or Bromo Adjacent Homology domain, as present in DNA (Cytosine-5)-methyltransferases (DCM) ...
 644-774 5.68e-08

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: 53.18  E-value: 5.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  644 IDEEMLEVGDCVSVIPDDSSKPLYLA----------RVTALWEDKNGQMMFHAHWFCAGTDTVLGATSDPLELFLVGECE 713
Cdd:cd04712     1 IHGLTIRVGDVVSVERDDADSTTKWNddhrwlplvqFVEYMKKGSDGSKMFHGRWLYRGCDTVLGNYANERELFLTNECT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755528341  714 NMQLSYIHSKVKVIYKAPsenWAM--EGGTDPEttlpgaedgkTYFFQLWYNQEYARFESPPK 774
Cdd:cd04712    81 CLELDLLSTEIKGVHKVD---WSGtpWGKGLPE----------FFVRQSYYWPERGAFTSLKR 130
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 646-689 2.82e-07

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: 50.86  E-value: 2.82e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 755528341  646 EEMLEVGDCVSVIPDDSSKPLYLARVTALWEDKNGQMMFHAHWF 689
Cdd:cd04714     1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWY 44
BAH_fungalPHD cd04710
BAH, or Bromo Adjacent Homology domain, as present in fungal proteins containing PHD domains. ...
 863-990 4.75e-07

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: 50.45  E-value: 4.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  863 PEHYRKySDYIKGSNLDAPEPYRIGRI------KEIHCGKKKGKVNEADIKLRLYKFYRPENTHRSYNgsyhTDINMLYW 936
Cdd:cd04710     9 GELLKV-NDHIYMSSEPPGEPYYIGRImefvpkHEFPSGIHARVFPASYFQVRLNWYYRPRDISRRVV----ADSRLLYA 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 755528341  937 SDEEAVVNFSDVQGRCTVEYgEDLLESIQDYSQgGPDRFYFLEAYNSKTKNFED 990
Cdd:cd04710    84 SMHSDICPIGSVRGKCTVRH-RDQIPDLEEYKK-RPNHFYFDQLFDRYILRYYD 135
BAH_polybromo cd04717
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human ...
 648-689 6.58e-06

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: 46.81  E-value: 6.58e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 755528341  648 MLEVGDCVSVIPDDSSKPLYLARVTALWEDKNGQMMFHAHWF 689
Cdd:cd04717     3 QYRVGDCVYVANPEDPSKPIIFRIERLWKDEDGEKFFFGCWF 44
BAH_plant_1 cd04721
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 651-708 3.47e-04

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: 42.05  E-value: 3.47e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755528341  651 VGDCVSVIPDDSSKplYLARVTALWEDKNGQMMFHAHWFcAGTDTVLGATSD----PLELFL 708
Cdd:cd04721    10 VHDFVYVLSEEEDR--YVAYIEDLYEDKKGSKMVKVRWF-HTTDEVGAALSPdsvnPREIFL 68
BAH_plantDCM_I cd04716
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 650-771 6.97e-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: 40.89  E-value: 6.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341  650 EVGDCVSViPDDSSKPLYLARVTALWEDKNGQMMFHAHWFCAGTDTVLGATS---DPLELFLVGECENMQLSYIHSKVKV 726
Cdd:cd04716     5 NLGDDAYV-QGGEGEEPFICKITEFFEGTDGKTYFTAQWFYRAEDTVIERQAtnhDKKRVFYSEIKNDNPLDCLISKVKI 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 755528341  727 IYKAPSENwameggtdPETTLPGAEDGKtYFFQLWYNQEYARFES 771
Cdd:cd04716    84 LQVPPNVG--------TKRKKPNSEKCD-YYYDMEYCVPYSTFQT 119
PHA03169 PHA03169
hypothetical protein; Provisional
 68-198 8.19e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.34  E-value: 8.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528341   68 KEESEEGNSAESAAEERDQDKKRRVVDTESGAAAAVEKLEEVTAGTQLGPEEPCEQEDDNRSlrRHTRELSLRRKSKEDP 147
Cdd:PHA03169   97 SESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPS--PNQQPSSFLQPSHEDS 174

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755528341  148 DREARPETHLDEDEDGkkdkrssrprsqprDPAAKRRPKEAEPEQVAPETP 198
Cdd:PHA03169  175 PEEPEPPTSEPEPDSP--------------GPPQSETPTSSPPPQSPPDEP 211
 
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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