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Conserved domains on  [gi|313661499|ref|NP_001186362|]
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DNA (cytosine-5)-methyltransferase 1 isoform 4 [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) ...
 851-986 4.05e-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: 4.05e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  851 NETLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIHCGKK-KGKVNEADIKLRLYKFYRPENTHRSYNGSYHTDINMLYW 929
Cdd:cd04711     1 DEDLYPEYYRKSSDYIKGSNLDAPEPFRIGRIKEIFCAKRsNGKPNESDIKLRINKFYRPENTHKGFKATYHADINMLYW 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 313661499  930 SDEEAVVNFSDVQGRCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKNFEDPPN 986
Cdd:cd04711    81 SDEEATVDFSAVQGRCTVEYGEDLPESVQEYSGGGPDRFYFLEAYNAKTKSFEDPPN 137
BAH_Dnmt1_I cd04760
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 640-763 2.69e-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: 2.69e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  640 EMLEVGDCVSVIPDDSSKPLYLARVTALWEDKNGQMMFHAHWFCAGTDTVLGATSDPLELFLVGECENMQLSYIHSKVKV 719
Cdd:cd04760     2 EELEAGDCVSVKPDDPTKPLYIARVTYMWKDSIGGKMFHAHWFCRGSDTVLGETSDPLELFLVDECEDMALSSIHGKVNV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 313661499  720 IYKAPSENWAMEGGTDPEtTLPGAEDGKTYFFQLWYNQEYARFE 763
Cdd:cd04760    82 IYKAPSENWSMEGGMDEE-DEIFEDDGKTFFYQKWYDPECARFE 124
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
1022-1480 5.90e-64

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


:

Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 218.91  E-value: 5.90e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1022 PKLRTLDVFSGCGGLSEGFHQAGIsETLWAIEMWDPAAQAFRLNNPGTTVFTEDcnvlLKLVMAGEVtnslgqrlpqKGD 1101
Cdd:COG0270     2 KKLTVIDLFAGAGGLSLGFEKAGF-EVVFAVEIDPDACETYRANFPEAKVIEGD----IRDIDPEEL----------IPD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1102 VEMLCGGPPCQGFSGMNRfnSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSYRRSMVLKLTLRCLVRMGYQCTF 1181
Cdd:COG0270    67 VDLLIGGPPCQPFSVAGK--RKGLEDPRGTLFFEFIRIVEELRPKAFVLENVPGLLSSDKGKTFEEILKELEELGYRVDY 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1182 GVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLPE 1261
Cdd:COG0270   145 KVLNAADYGVPQNRERVFIVGFRKDLDLFEFPEPTH----------------------------LKPYVTVGDALEDLPD 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1262 iqngasnseipyngeplswfqrqlrgshyqpilrDHICKDMSPLVAARmrhiplfpgsdwrdlpniqvrlgdgviahklq 1341
Cdd:COG0270   197 ----------------------------------AHEARYLSETITAG-------------------------------- 210

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1342 ytfhdvkngysstgalrgvcscaegkacdpesrqfstlipwclphtgnrhnhwaglygrlewdgffsttvtnpepMGKQG 1421
Cdd:COG0270   211 ---------------------------------------------------------------------------YGGGG 215

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 313661499 1422 RVLHPEQHRVVSVRECARSQGFPDSYRFFGNILDRHRQVGNAVPPPLAKAIGLEIKLCL 1480
Cdd:COG0270   216 RFLHPGEPRRLTVREAARLQGFPDDFKFPGSKTQAYRQIGNAVPPPLAEAIAKAILKAL 274
DNMT1-RFD pfam12047
Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a ...
 287-422 3.62e-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: 179.84  E-value: 3.62e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499   287 YEDSPMHRFTSFSVYCSRGHLCPVDTGLIEKNVELYFSGCAKAIHDENPSMEG-GINGKN----LGPINQWWLSGFDGGE 361
Cdd:pfam12047    1 EEDRPQRKLTDFELYDKDGHLCPFDVLLIEKNVDIFISGIVKPIDEDEPSLDGkGIEDKGmqikLGPIKEWTISGFDGGE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313661499   362 KVLIGFSTAFAEYILMEPSKEYEPIFGLMQEKIYISKIVVEFLQNNP--DAVYEDLINKIETT 422
Cdd:pfam12047   81 KALIWLSTEFAWYKLLKPSAEYAPIYELVYEKARLSVEVVEFLQRSPgsELSYEDLINRVLTS 143
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 530-576 1.18e-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: 83.56  E-value: 1.18e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 313661499   530 ENAMKRRRCGVCEVCQQPE-CGKCKACKDMVKFGGTGRSKQACLKRRC 576
Cdd:pfam02008    1 RNRRKRRRCGVCEGCQRPEdCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
PHA03169 super family cl27451
hypothetical protein; Provisional
 61-191 8.43e-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: 8.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499   61 KEESEEGNSAESAAEERDQDKKRRVVDTESGAAAAVEKLEEVTAGTQLGPEEPCEQEDDNRSlrRHTRELSLRRKSKEDP 140
Cdd:PHA03169   97 SESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPS--PNQQPSSFLQPSHEDS 174

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 313661499  141 DREARPETHLDEDEDGkkdkrssrprsqprDPAAKRRPKEAEPEQVAPETP 191
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) ...
 851-986 4.05e-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: 4.05e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  851 NETLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIHCGKK-KGKVNEADIKLRLYKFYRPENTHRSYNGSYHTDINMLYW 929
Cdd:cd04711     1 DEDLYPEYYRKSSDYIKGSNLDAPEPFRIGRIKEIFCAKRsNGKPNESDIKLRINKFYRPENTHKGFKATYHADINMLYW 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 313661499  930 SDEEAVVNFSDVQGRCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKNFEDPPN 986
Cdd:cd04711    81 SDEEATVDFSAVQGRCTVEYGEDLPESVQEYSGGGPDRFYFLEAYNAKTKSFEDPPN 137
BAH_Dnmt1_I cd04760
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 640-763 2.69e-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: 2.69e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  640 EMLEVGDCVSVIPDDSSKPLYLARVTALWEDKNGQMMFHAHWFCAGTDTVLGATSDPLELFLVGECENMQLSYIHSKVKV 719
Cdd:cd04760     2 EELEAGDCVSVKPDDPTKPLYIARVTYMWKDSIGGKMFHAHWFCRGSDTVLGETSDPLELFLVDECEDMALSSIHGKVNV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 313661499  720 IYKAPSENWAMEGGTDPEtTLPGAEDGKTYFFQLWYNQEYARFE 763
Cdd:cd04760    82 IYKAPSENWSMEGGMDEE-DEIFEDDGKTFFYQKWYDPECARFE 124
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
1022-1480 5.90e-64

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


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 218.91  E-value: 5.90e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1022 PKLRTLDVFSGCGGLSEGFHQAGIsETLWAIEMWDPAAQAFRLNNPGTTVFTEDcnvlLKLVMAGEVtnslgqrlpqKGD 1101
Cdd:COG0270     2 KKLTVIDLFAGAGGLSLGFEKAGF-EVVFAVEIDPDACETYRANFPEAKVIEGD----IRDIDPEEL----------IPD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1102 VEMLCGGPPCQGFSGMNRfnSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSYRRSMVLKLTLRCLVRMGYQCTF 1181
Cdd:COG0270    67 VDLLIGGPPCQPFSVAGK--RKGLEDPRGTLFFEFIRIVEELRPKAFVLENVPGLLSSDKGKTFEEILKELEELGYRVDY 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1182 GVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLPE 1261
Cdd:COG0270   145 KVLNAADYGVPQNRERVFIVGFRKDLDLFEFPEPTH----------------------------LKPYVTVGDALEDLPD 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1262 iqngasnseipyngeplswfqrqlrgshyqpilrDHICKDMSPLVAARmrhiplfpgsdwrdlpniqvrlgdgviahklq 1341
Cdd:COG0270   197 ----------------------------------AHEARYLSETITAG-------------------------------- 210

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1342 ytfhdvkngysstgalrgvcscaegkacdpesrqfstlipwclphtgnrhnhwaglygrlewdgffsttvtnpepMGKQG 1421
Cdd:COG0270   211 ---------------------------------------------------------------------------YGGGG 215

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 313661499 1422 RVLHPEQHRVVSVRECARSQGFPDSYRFFGNILDRHRQVGNAVPPPLAKAIGLEIKLCL 1480
Cdd:COG0270   216 RFLHPGEPRRLTVREAARLQGFPDDFKFPGSKTQAYRQIGNAVPPPLAEAIAKAILKAL 274
DNMT1-RFD pfam12047
Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a ...
 287-422 3.62e-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: 179.84  E-value: 3.62e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499   287 YEDSPMHRFTSFSVYCSRGHLCPVDTGLIEKNVELYFSGCAKAIHDENPSMEG-GINGKN----LGPINQWWLSGFDGGE 361
Cdd:pfam12047    1 EEDRPQRKLTDFELYDKDGHLCPFDVLLIEKNVDIFISGIVKPIDEDEPSLDGkGIEDKGmqikLGPIKEWTISGFDGGE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313661499   362 KVLIGFSTAFAEYILMEPSKEYEPIFGLMQEKIYISKIVVEFLQNNP--DAVYEDLINKIETT 422
Cdd:pfam12047   81 KALIWLSTEFAWYKLLKPSAEYAPIYELVYEKARLSVEVVEFLQRSPgsELSYEDLINRVLTS 143
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
1024-1477 1.71e-39

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 150.16  E-value: 1.71e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1024 LRTLDVFSGCGGLSEGFHQAGIsETLWAIEMWDPAAQAFRLNNPgTTVFtedcnvllklvmaGEVTNSLGQRLPqkgDVE 1103
Cdd:pfam00145    1 FKFIDLFAGIGGFRLGLEQAGF-ECVAANEIDKSAAKTYEANFP-KVPI-------------GDITLIDIKDIP---DID 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1104 MLCGGPPCQGFS--GMNRFNSRTYskfkNSLVVSFLSYCDYYRPRFFLLENVRNFVSYRRSMVLKLTLRCLVRMGYQCTF 1181
Cdd:pfam00145   63 ILTGGFPCQDFSiaGKQKGFEDTR----GTLFFEIIRIIKEKKPKAFLLENVKGLLSHDNGNTLNVILETLEELGYHVSW 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1182 GVLQAGQYGVAQTRRRAIILAAAPG-EKLPLFPEPlhvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLP 1260
Cdd:pfam00145  139 KVLNASDYGVPQNRERVFIVGIRKDlNLNVLVPVP------------------------------EFDFPKPKDLTGTIR 188

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1261 EIQNGASNSEIPYNGEplswfqrqlrgshyqpilrDHICKDMSplvaaRMRHIPLFPGSDWRDlpniqvrlgdgviahkl 1340
Cdd:pfam00145  189 DLLEEPSLDENKYNLS-------------------DKFVENHE-----RRKPTTKAPGGGYPT----------------- 227

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1341 QYTFHDVKNGYSStgalrgvcscaegkacdpesrqfstlipwclphtgnrhNHWAGLYGRlewDGFFSTTVTnpEPMGKQ 1420
Cdd:pfam00145  228 YLLRNRIDKVEEG--------------------------------------KGPSFTYRK---SGRPEAPKT--GILGKN 264

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 313661499  1421 GR--VLHPEQHRVVSVRECARSQGFPDSYRFFGNILDRHRQVGNAVPPPLAKAIGLEIK 1477
Cdd:pfam00145  265 GErfRGHPKNIRRLTPRECARLQGFPDDFIFPGSKTQLYKQIGNAVPVPVAEAIAKAIK 323
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
 1024-1477 2.41e-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: 2.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1024 LRTLDVFSGCGGLSEGFHQAGiSETLWAIEMWDPAAQAFRLNNPGTTVFtedcnvllklvmaGEVTNSLGQRLPqkGDVE 1103
Cdd:cd00315     1 LRVIDLFAGIGGFRLGLEKAG-FEIVAANEIDKSAAETYEANFPNKLIE-------------GDITKIDEKDFI--PDID 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1104 MLCGGPPCQGFS--GMNRFNSRTYSKfknslvvSFLSYCDY---YRPRFFLLENVRNFVSYRRSMVLKLTLRCLVRMGYQ 1178
Cdd:cd00315    65 LLTGGFPCQPFSiaGKRKGFEDTRGT-------LFFEIIRIlkeKKPKYFLLENVKGLLTHDNGNTLKVILNTLEELGYN 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1179 CTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFapracqlsvvvDDKKFVSNITRLSSGPFRTITVRdtmsd 1258
Cdd:cd00315   138 VYWKLLNASDYGVPQNRERVFIIGIRKDLILNFFSPFPKPS-----------EKKKTLKDILRIRDPDEPSPTLT----- 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1259 lpeiqngASNseipyngeplswfqrqlrgshyqpilrdhickdmsplvaarmrhiplfpgsdwrdlpniqvrlgdgviaH 1338
Cdd:cd00315   202 -------ASY---------------------------------------------------------------------G 205

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1339 KLQYTFHDVKNGYSstgalrgvcscaegkacdpesrqfstlipwclphtgnrhnhwaglygrlewdgffsttvtnpepmg 1418
Cdd:cd00315   206 KGTGSVHPTAPDMI------------------------------------------------------------------ 219

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1419 kqgrvLHPEQHRVVSVRECARSQGFPDSYRFFG-NILDRHRQVGNAVPPPLAKAIGLEIK 1477
Cdd:cd00315   220 -----GKESNIRRLTPRECARLQGFPDDFEFPGkSVTQAYRQIGNSVPVPVAEAIAKAIK 274
BAH smart00439
Bromo adjacent homology domain;
864-985 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 313661499    864 DYIKGSNLDAPEPYRIGRIKEIHCGKKkgkvNEADIKLRLYKFYRPENTHRSYNgsYHTDINMLYWSDEEAVVNFSDVQG 943
Cdd:smart00439    6 DFVLVEPDDADEPYYIGRIEEIFETKK----NSESKMVRVRWFYRPEETVLEKA--ALFDKNEVFLSDEYDTVPLSDIIG 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 313661499    944 RCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKNFEDPP 985
Cdd:smart00439   80 KCNVLYKSDYPGLRPEGSIGEPDVFFCESAYDPEKGSFKKLP 121
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
 1028-1476 1.33e-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: 1.33e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1028 DVFSGCGGLSEGFHQAGIsETLWAIEmWDPAAQA-FRLNNPGTTVFtedcnvllklvmaGEVTNSLGQRLPqkgDVEMLC 1106
Cdd:TIGR00675    3 DLFAGIGGIRLGFEQAGF-KCVFASE-IDKYAQKtYEANFGNKVPF-------------GDITKISPSDIP---DFDILL 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1107 GGPPCQGFSgMNRFNsRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSYRRSMVLKLTLRCLVRMGYQCTFGVLQA 1186
Cdd:TIGR00675   65 GGFPCQPFS-IAGKR-KGFEDTRGTLFFEIVRILKEKKPKFFLLENVKGLVSHDKGRTFKVIIETLEELGYKVYYKVLNA 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1187 GQYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlsSGPFRTITVRDTMSDLPEIQNGA 1266
Cdd:TIGR00675  143 KDFGVPQNRERIYIVGFRDFDDKLNFEFPKP--------------------------IYVAKKKRIGDLLDLSVDLEEKY 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1267 SNSEIPYNGEplswfqrqlrgshyqpilrdhickdmsPLVAARMRHIPLFpGSDWRdlpNIQVRLGDGVIAHKLqytfhd 1346
Cdd:TIGR00675  197 YLSEEKKNGL---------------------------LLLLENMRKKEGT-GEQIG---SFYNRESKSSIIRTL------ 239

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1347 vkngysstgalrgvcscaegkacdpesrqfstlipwclphTGNRHNHWAGlygrlewdgffstTVTNPEPMGKQGRVlHP 1426
Cdd:TIGR00675  240 ----------------------------------------SARGYTFVKG-------------GKSVLIVPHKSTVV-HP 265

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 313661499  1427 EQHRVVSVRECARSQGFPDSYRFFGNILDRHRQVGNAVPPPLAKAIGLEI 1476
Cdd:TIGR00675  266 GRIRRLTPRECARLQGFPDDFKFPVSDSQLYKQAGNAVVVPVIEAIAKQI 315
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 852-985 5.34e-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: 5.34e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499   852 ETLYPEHYRKYSDYikgsnlDAPEPYRIGRIKEIHCGKKKGKvneadIKLRLYKFYRPENTHRSYNGSYHTDinMLYWSD 931
Cdd:pfam01426    1 ETYSVGDFVLVEPD------DADEPYYVARIEELFEDTKNGK-----KMVRVQWFYRPEETVHRAGKAFNKD--ELFLSD 67

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 313661499   932 EEAVVNFSDVQGRCTVEYGEDLLESIQDYSqGGPDRFYFLEAYNSKTKNFEDPP 985
Cdd:pfam01426   68 EEDDVPLSAIIGKCSVLHKSDLESLDPYKI-KEPDDFFCELLYDPKTKSFKKLP 120
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 640-766 5.44e-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: 5.44e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499   640 EMLEVGDCVSVIPDDSSKPLYLARVTALWED-KNGQMMFHAHWFCAGTDTV--LGATSDPLELFLVGECENMQLSYIHSK 716
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDtKNGKKMVRVQWFYRPEETVhrAGKAFNKDELFLSDEEDDVPLSAIIGK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 313661499   717 VKVIYKAPSENWAMEGGTDPettlpgaedgKTYFFQLWYNQEYARFESPP 766
Cdd:pfam01426   81 CSVLHKSDLESLDPYKIKEP----------DDFFCELLYDPKTKSFKKLP 120
BAH smart00439
Bromo adjacent homology domain;
641-766 2.33e-26

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 105.07  E-value: 2.33e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499    641 MLEVGDCVSVIPDDSSKPLYLARVTALWEDKNG--QMMFHAHWFCAGTDTVLGAT--SDPLELFLVGECENMQLSYIHSK 716
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNseSKMVRVRWFYRPEETVLEKAalFDKNEVFLSDEYDTVPLSDIIGK 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 313661499    717 VKVIYKAPSENWAMEGGTDPETtlpgaedgkTYFFQLWYNQEYARFESPP 766
Cdd:smart00439   81 CNVLYKSDYPGLRPEGSIGEPD---------VFFCESAYDPEKGSFKKLP 121
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 530-576 1.18e-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: 83.56  E-value: 1.18e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 313661499   530 ENAMKRRRCGVCEVCQQPE-CGKCKACKDMVKFGGTGRSKQACLKRRC 576
Cdd:pfam02008    1 RNRRKRRRCGVCEGCQRPEdCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
PHA03169 PHA03169
hypothetical protein; Provisional
 61-191 8.43e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.34  E-value: 8.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499   61 KEESEEGNSAESAAEERDQDKKRRVVDTESGAAAAVEKLEEVTAGTQLGPEEPCEQEDDNRSlrRHTRELSLRRKSKEDP 140
Cdd:PHA03169   97 SESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPS--PNQQPSSFLQPSHEDS 174

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 313661499  141 DREARPETHLDEDEDGkkdkrssrprsqprDPAAKRRPKEAEPEQVAPETP 191
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) ...
 851-986 4.05e-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: 4.05e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  851 NETLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIHCGKK-KGKVNEADIKLRLYKFYRPENTHRSYNGSYHTDINMLYW 929
Cdd:cd04711     1 DEDLYPEYYRKSSDYIKGSNLDAPEPFRIGRIKEIFCAKRsNGKPNESDIKLRINKFYRPENTHKGFKATYHADINMLYW 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 313661499  930 SDEEAVVNFSDVQGRCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKNFEDPPN 986
Cdd:cd04711    81 SDEEATVDFSAVQGRCTVEYGEDLPESVQEYSGGGPDRFYFLEAYNAKTKSFEDPPN 137
BAH_Dnmt1_I cd04760
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 640-763 2.69e-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: 2.69e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  640 EMLEVGDCVSVIPDDSSKPLYLARVTALWEDKNGQMMFHAHWFCAGTDTVLGATSDPLELFLVGECENMQLSYIHSKVKV 719
Cdd:cd04760     2 EELEAGDCVSVKPDDPTKPLYIARVTYMWKDSIGGKMFHAHWFCRGSDTVLGETSDPLELFLVDECEDMALSSIHGKVNV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 313661499  720 IYKAPSENWAMEGGTDPEtTLPGAEDGKTYFFQLWYNQEYARFE 763
Cdd:cd04760    82 IYKAPSENWSMEGGMDEE-DEIFEDDGKTFFYQKWYDPECARFE 124
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
1022-1480 5.90e-64

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


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 218.91  E-value: 5.90e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1022 PKLRTLDVFSGCGGLSEGFHQAGIsETLWAIEMWDPAAQAFRLNNPGTTVFTEDcnvlLKLVMAGEVtnslgqrlpqKGD 1101
Cdd:COG0270     2 KKLTVIDLFAGAGGLSLGFEKAGF-EVVFAVEIDPDACETYRANFPEAKVIEGD----IRDIDPEEL----------IPD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1102 VEMLCGGPPCQGFSGMNRfnSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSYRRSMVLKLTLRCLVRMGYQCTF 1181
Cdd:COG0270    67 VDLLIGGPPCQPFSVAGK--RKGLEDPRGTLFFEFIRIVEELRPKAFVLENVPGLLSSDKGKTFEEILKELEELGYRVDY 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1182 GVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLPE 1261
Cdd:COG0270   145 KVLNAADYGVPQNRERVFIVGFRKDLDLFEFPEPTH----------------------------LKPYVTVGDALEDLPD 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1262 iqngasnseipyngeplswfqrqlrgshyqpilrDHICKDMSPLVAARmrhiplfpgsdwrdlpniqvrlgdgviahklq 1341
Cdd:COG0270   197 ----------------------------------AHEARYLSETITAG-------------------------------- 210

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1342 ytfhdvkngysstgalrgvcscaegkacdpesrqfstlipwclphtgnrhnhwaglygrlewdgffsttvtnpepMGKQG 1421
Cdd:COG0270   211 ---------------------------------------------------------------------------YGGGG 215

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 313661499 1422 RVLHPEQHRVVSVRECARSQGFPDSYRFFGNILDRHRQVGNAVPPPLAKAIGLEIKLCL 1480
Cdd:COG0270   216 RFLHPGEPRRLTVREAARLQGFPDDFKFPGSKTQAYRQIGNAVPPPLAEAIAKAILKAL 274
DNMT1-RFD pfam12047
Cytosine specific DNA methyltransferase replication foci domain; This domain is part of a ...
 287-422 3.62e-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: 179.84  E-value: 3.62e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499   287 YEDSPMHRFTSFSVYCSRGHLCPVDTGLIEKNVELYFSGCAKAIHDENPSMEG-GINGKN----LGPINQWWLSGFDGGE 361
Cdd:pfam12047    1 EEDRPQRKLTDFELYDKDGHLCPFDVLLIEKNVDIFISGIVKPIDEDEPSLDGkGIEDKGmqikLGPIKEWTISGFDGGE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313661499   362 KVLIGFSTAFAEYILMEPSKEYEPIFGLMQEKIYISKIVVEFLQNNP--DAVYEDLINKIETT 422
Cdd:pfam12047   81 KALIWLSTEFAWYKLLKPSAEYAPIYELVYEKARLSVEVVEFLQRSPgsELSYEDLINRVLTS 143
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
1024-1477 1.71e-39

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 150.16  E-value: 1.71e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1024 LRTLDVFSGCGGLSEGFHQAGIsETLWAIEMWDPAAQAFRLNNPgTTVFtedcnvllklvmaGEVTNSLGQRLPqkgDVE 1103
Cdd:pfam00145    1 FKFIDLFAGIGGFRLGLEQAGF-ECVAANEIDKSAAKTYEANFP-KVPI-------------GDITLIDIKDIP---DID 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1104 MLCGGPPCQGFS--GMNRFNSRTYskfkNSLVVSFLSYCDYYRPRFFLLENVRNFVSYRRSMVLKLTLRCLVRMGYQCTF 1181
Cdd:pfam00145   63 ILTGGFPCQDFSiaGKQKGFEDTR----GTLFFEIIRIIKEKKPKAFLLENVKGLLSHDNGNTLNVILETLEELGYHVSW 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1182 GVLQAGQYGVAQTRRRAIILAAAPG-EKLPLFPEPlhvfapracqlsvvvddkkfvsnitrlssgPFRTITVRDTMSDLP 1260
Cdd:pfam00145  139 KVLNASDYGVPQNRERVFIVGIRKDlNLNVLVPVP------------------------------EFDFPKPKDLTGTIR 188

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1261 EIQNGASNSEIPYNGEplswfqrqlrgshyqpilrDHICKDMSplvaaRMRHIPLFPGSDWRDlpniqvrlgdgviahkl 1340
Cdd:pfam00145  189 DLLEEPSLDENKYNLS-------------------DKFVENHE-----RRKPTTKAPGGGYPT----------------- 227

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1341 QYTFHDVKNGYSStgalrgvcscaegkacdpesrqfstlipwclphtgnrhNHWAGLYGRlewDGFFSTTVTnpEPMGKQ 1420
Cdd:pfam00145  228 YLLRNRIDKVEEG--------------------------------------KGPSFTYRK---SGRPEAPKT--GILGKN 264

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 313661499  1421 GR--VLHPEQHRVVSVRECARSQGFPDSYRFFGNILDRHRQVGNAVPPPLAKAIGLEIK 1477
Cdd:pfam00145  265 GErfRGHPKNIRRLTPRECARLQGFPDDFIFPGSKTQLYKQIGNAVPVPVAEAIAKAIK 323
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
 1024-1477 2.41e-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: 2.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1024 LRTLDVFSGCGGLSEGFHQAGiSETLWAIEMWDPAAQAFRLNNPGTTVFtedcnvllklvmaGEVTNSLGQRLPqkGDVE 1103
Cdd:cd00315     1 LRVIDLFAGIGGFRLGLEKAG-FEIVAANEIDKSAAETYEANFPNKLIE-------------GDITKIDEKDFI--PDID 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1104 MLCGGPPCQGFS--GMNRFNSRTYSKfknslvvSFLSYCDY---YRPRFFLLENVRNFVSYRRSMVLKLTLRCLVRMGYQ 1178
Cdd:cd00315    65 LLTGGFPCQPFSiaGKRKGFEDTRGT-------LFFEIIRIlkeKKPKYFLLENVKGLLTHDNGNTLKVILNTLEELGYN 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1179 CTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFapracqlsvvvDDKKFVSNITRLSSGPFRTITVRdtmsd 1258
Cdd:cd00315   138 VYWKLLNASDYGVPQNRERVFIIGIRKDLILNFFSPFPKPS-----------EKKKTLKDILRIRDPDEPSPTLT----- 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1259 lpeiqngASNseipyngeplswfqrqlrgshyqpilrdhickdmsplvaarmrhiplfpgsdwrdlpniqvrlgdgviaH 1338
Cdd:cd00315   202 -------ASY---------------------------------------------------------------------G 205

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1339 KLQYTFHDVKNGYSstgalrgvcscaegkacdpesrqfstlipwclphtgnrhnhwaglygrlewdgffsttvtnpepmg 1418
Cdd:cd00315   206 KGTGSVHPTAPDMI------------------------------------------------------------------ 219

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499 1419 kqgrvLHPEQHRVVSVRECARSQGFPDSYRFFG-NILDRHRQVGNAVPPPLAKAIGLEIK 1477
Cdd:cd00315   220 -----GKESNIRRLTPRECARLQGFPDDFEFPGkSVTQAYRQIGNSVPVPVAEAIAKAIK 274
BAH smart00439
Bromo adjacent homology domain;
864-985 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 313661499    864 DYIKGSNLDAPEPYRIGRIKEIHCGKKkgkvNEADIKLRLYKFYRPENTHRSYNgsYHTDINMLYWSDEEAVVNFSDVQG 943
Cdd:smart00439    6 DFVLVEPDDADEPYYIGRIEEIFETKK----NSESKMVRVRWFYRPEETVLEKA--ALFDKNEVFLSDEYDTVPLSDIIG 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 313661499    944 RCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKNFEDPP 985
Cdd:smart00439   80 KCNVLYKSDYPGLRPEGSIGEPDVFFCESAYDPEKGSFKKLP 121
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
 1028-1476 1.33e-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: 1.33e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1028 DVFSGCGGLSEGFHQAGIsETLWAIEmWDPAAQA-FRLNNPGTTVFtedcnvllklvmaGEVTNSLGQRLPqkgDVEMLC 1106
Cdd:TIGR00675    3 DLFAGIGGIRLGFEQAGF-KCVFASE-IDKYAQKtYEANFGNKVPF-------------GDITKISPSDIP---DFDILL 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1107 GGPPCQGFSgMNRFNsRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSYRRSMVLKLTLRCLVRMGYQCTFGVLQA 1186
Cdd:TIGR00675   65 GGFPCQPFS-IAGKR-KGFEDTRGTLFFEIVRILKEKKPKFFLLENVKGLVSHDKGRTFKVIIETLEELGYKVYYKVLNA 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1187 GQYGVAQTRRRAIILAAAPGEKLPLFPEPLHvfapracqlsvvvddkkfvsnitrlsSGPFRTITVRDTMSDLPEIQNGA 1266
Cdd:TIGR00675  143 KDFGVPQNRERIYIVGFRDFDDKLNFEFPKP--------------------------IYVAKKKRIGDLLDLSVDLEEKY 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1267 SNSEIPYNGEplswfqrqlrgshyqpilrdhickdmsPLVAARMRHIPLFpGSDWRdlpNIQVRLGDGVIAHKLqytfhd 1346
Cdd:TIGR00675  197 YLSEEKKNGL---------------------------LLLLENMRKKEGT-GEQIG---SFYNRESKSSIIRTL------ 239

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  1347 vkngysstgalrgvcscaegkacdpesrqfstlipwclphTGNRHNHWAGlygrlewdgffstTVTNPEPMGKQGRVlHP 1426
Cdd:TIGR00675  240 ----------------------------------------SARGYTFVKG-------------GKSVLIVPHKSTVV-HP 265

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 313661499  1427 EQHRVVSVRECARSQGFPDSYRFFGNILDRHRQVGNAVPPPLAKAIGLEI 1476
Cdd:TIGR00675  266 GRIRRLTPRECARLQGFPDDFKFPVSDSQLYKQAGNAVVVPVIEAIAKQI 315
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 852-985 5.34e-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: 5.34e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499   852 ETLYPEHYRKYSDYikgsnlDAPEPYRIGRIKEIHCGKKKGKvneadIKLRLYKFYRPENTHRSYNGSYHTDinMLYWSD 931
Cdd:pfam01426    1 ETYSVGDFVLVEPD------DADEPYYVARIEELFEDTKNGK-----KMVRVQWFYRPEETVHRAGKAFNKD--ELFLSD 67

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 313661499   932 EEAVVNFSDVQGRCTVEYGEDLLESIQDYSqGGPDRFYFLEAYNSKTKNFEDPP 985
Cdd:pfam01426   68 EEDDVPLSAIIGKCSVLHKSDLESLDPYKI-KEPDDFFCELLYDPKTKSFKKLP 120
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 640-766 5.44e-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: 5.44e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499   640 EMLEVGDCVSVIPDDSSKPLYLARVTALWED-KNGQMMFHAHWFCAGTDTV--LGATSDPLELFLVGECENMQLSYIHSK 716
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDtKNGKKMVRVQWFYRPEETVhrAGKAFNKDELFLSDEEDDVPLSAIIGK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 313661499   717 VKVIYKAPSENWAMEGGTDPettlpgaedgKTYFFQLWYNQEYARFESPP 766
Cdd:pfam01426   81 CSVLHKSDLESLDPYKIKEP----------DDFFCELLYDPKTKSFKKLP 120
BAH smart00439
Bromo adjacent homology domain;
641-766 2.33e-26

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 105.07  E-value: 2.33e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499    641 MLEVGDCVSVIPDDSSKPLYLARVTALWEDKNG--QMMFHAHWFCAGTDTVLGAT--SDPLELFLVGECENMQLSYIHSK 716
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNseSKMVRVRWFYRPEETVLEKAalFDKNEVFLSDEYDTVPLSDIIGK 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 313661499    717 VKVIYKAPSENWAMEGGTDPETtlpgaedgkTYFFQLWYNQEYARFESPP 766
Cdd:smart00439   81 CNVLYKSDYPGLRPEGSIGEPD---------VFFCESAYDPEKGSFKKLP 121
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 639-764 2.69e-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: 2.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  639 EEMLEVGDCVSVIPDDS--SKPLYLARVTALWEDKNGQMMFHAHWFCAGTDTVLGATS--DPLELFLVGECENMQLSYIH 714
Cdd:cd04370     1 GITYEVGDSVYVEPDDSikSDPPYIARIEELWEDTNGSKQVKVRWFYRPEETPKGLSPfaLRRELFLSDHLDEIPVESII 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 313661499  715 SKVKVIYKAPSENWAMeggtdpettLPGAEDGKTYFFQLWYNQEYARFES 764
Cdd:cd04370    81 GKCKVLFVSEFEGLKQ---------RPNKIDTDDFFCRLAYDPTTKEFKA 121
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 530-576 1.18e-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: 83.56  E-value: 1.18e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 313661499   530 ENAMKRRRCGVCEVCQQPE-CGKCKACKDMVKFGGTGRSKQACLKRRC 576
Cdd:pfam02008    1 RNRRKRRRCGVCEGCQRPEdCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 855-981 1.35e-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: 1.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  855 YPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIHCGKkkgkvnEADIKLRLYKFYRPENTHRSYngSYHTDINMLYWSDEEA 934
Cdd:cd04370     1 GITYEVGDSVYVEPDDSIKSDPPYIARIEELWEDT------NGSKQVKVRWFYRPEETPKGL--SPFALRRELFLSDHLD 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 313661499  935 VVNFSDVQGRCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKNF 981
Cdd:cd04370    73 EIPVESIIGKCKVLFVSEFEGLKQRPNKIDTDDFFCRLAYDPTTKEF 119
BAH_plantDCM_II cd04708
BAH, or Bromo Adjacent Homology domain, second copy present in DNA (Cytosine-5) ...
 813-1036 1.21e-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: 68.26  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  813 TKNGVVYRLGDSVYLPPEAFTfnikvaspvkrpkkdpvnetlypEHYRKYSDYIKGSNLDAPePYRIGRIKEIHCGK--K 890
Cdd:cd04708     2 VYDGVTYSVGDFLYVSPDAFA-----------------------EEERERATFKAGRNVGLK-AFVVCQVLEIVVEKesK 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  891 KGKVNEADIKLRlyKFYRPENThrSYNGSYHTDINMLYWSDEEAVVNFSDVQGRCTVEYGEDLLESiQDYSQGGPdRFYF 970
Cdd:cd04708    58 QADVASTQVKVR--RFYRPEDV--SPEKAYASDIREVYYSEDTLTVPVEAVEGKCEVRKKSDLPDS-DAPVIFEH-VFFC 131

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313661499  971 LEAYNSKTKNFEDPPNHARSPGNKGKGKGKGKGK-----GKHQVSEPKEPEAAIKLPKLRTLDVFSGCGGL 1036
Cdd:cd04708   132 ELLYDPAKGSLKQLPPNIKEEAYSTGASDSALRKrkgkgKGDSESDSEAPVKAPKENRLATLDIFAGCGGL 202
BAH_DCM_I cd04712
BAH, or Bromo Adjacent Homology domain, as present in DNA (Cytosine-5)-methyltransferases (DCM) ...
 637-767 5.49e-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: 5.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  637 IDEEMLEVGDCVSVIPDDSSKPLYLA----------RVTALWEDKNGQMMFHAHWFCAGTDTVLGATSDPLELFLVGECE 706
Cdd:cd04712     1 IHGLTIRVGDVVSVERDDADSTTKWNddhrwlplvqFVEYMKKGSDGSKMFHGRWLYRGCDTVLGNYANERELFLTNECT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313661499  707 NMQLSYIHSKVKVIYKAPsenWAM--EGGTDPEttlpgaedgkTYFFQLWYNQEYARFESPPK 767
Cdd:cd04712    81 CLELDLLSTEIKGVHKVD---WSGtpWGKGLPE----------FFVRQSYYWPERGAFTSLKR 130
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 639-682 2.78e-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: 2.78e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 313661499  639 EEMLEVGDCVSVIPDDSSKPLYLARVTALWEDKNGQMMFHAHWF 682
Cdd:cd04714     1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWY 44
BAH_fungalPHD cd04710
BAH, or Bromo Adjacent Homology domain, as present in fungal proteins containing PHD domains. ...
 856-983 4.77e-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: 4.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  856 PEHYRKySDYIKGSNLDAPEPYRIGRI------KEIHCGKKKGKVNEADIKLRLYKFYRPENTHRSYNgsyhTDINMLYW 929
Cdd:cd04710     9 GELLKV-NDHIYMSSEPPGEPYYIGRImefvpkHEFPSGIHARVFPASYFQVRLNWYYRPRDISRRVV----ADSRLLYA 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 313661499  930 SDEEAVVNFSDVQGRCTVEYgEDLLESIQDYSQgGPDRFYFLEAYNSKTKNFED 983
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 ...
 641-682 6.68e-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: 6.68e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 313661499  641 MLEVGDCVSVIPDDSSKPLYLARVTALWEDKNGQMMFHAHWF 682
Cdd:cd04717     3 QYRVGDCVYVANPEDPSKPIIFRIERLWKDEDGEKFFFGCWF 44
BAH_plant_1 cd04721
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 644-701 3.45e-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: 3.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 313661499  644 VGDCVSVIPDDSSKplYLARVTALWEDKNGQMMFHAHWFcAGTDTVLGATSD----PLELFL 701
Cdd:cd04721    10 VHDFVYVLSEEEDR--YVAYIEDLYEDKKGSKMVKVRWF-HTTDEVGAALSPdsvnPREIFL 68
BAH_plantDCM_I cd04716
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 643-764 6.94e-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: 6.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499  643 EVGDCVSViPDDSSKPLYLARVTALWEDKNGQMMFHAHWFCAGTDTVLGATS---DPLELFLVGECENMQLSYIHSKVKV 719
Cdd:cd04716     5 NLGDDAYV-QGGEGEEPFICKITEFFEGTDGKTYFTAQWFYRAEDTVIERQAtnhDKKRVFYSEIKNDNPLDCLISKVKI 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 313661499  720 IYKAPSENwameggtdPETTLPGAEDGKtYFFQLWYNQEYARFES 764
Cdd:cd04716    84 LQVPPNVG--------TKRKKPNSEKCD-YYYDMEYCVPYSTFQT 119
PHA03169 PHA03169
hypothetical protein; Provisional
 61-191 8.43e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.34  E-value: 8.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499   61 KEESEEGNSAESAAEERDQDKKRRVVDTESGAAAAVEKLEEVTAGTQLGPEEPCEQEDDNRSlrRHTRELSLRRKSKEDP 140
Cdd:PHA03169   97 SESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPS--PNQQPSSFLQPSHEDS 174

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 313661499  141 DREARPETHLDEDEDGkkdkrssrprsqprDPAAKRRPKEAEPEQVAPETP 191
Cdd:PHA03169  175 PEEPEPPTSEPEPDSP--------------GPPQSETPTSSPPPQSPPDEP 211
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 2-177 9.43e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 40.66  E-value: 9.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499    2 ADSNRSPRSRPKPRGPRRSKSDSDTLSVETSPSSVATRRTTRQTTITAHFTKGPTKRKPKEESEEGNSAESAAEERDQDK 81
Cdd:PRK12678   67 AATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAG 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313661499   82 KRRVVDTESGAAAAVEKLEEVTAGTQLGPEEPCEQEDDNRSLRRHTRELslRRKSKEDPDREARPETHLDEDEDGKKDKR 161
Cdd:PRK12678  147 EGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREE--RGRDGDDRDRRDRREQGDRREERGRRDGG 224

                         170
                  ....*....|....*.
gi 313661499  162 SSRPRSQPRDPAAKRR 177
Cdd:PRK12678  225 DRRGRRRRRDRRDARG 240
 
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.
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