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Conserved domains on  [gi|12963557|ref|NP_075667|]
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DNA methyltransferase 1-associated protein 1 [Mus musculus]

Protein Classification

DNA methyltransferase 1-associated protein 1( domain architecture ID 11242173)

DNA methyltransferase 1-associated protein 1 (DMAP1) is involved in transcription repression and activation

CATH:  1.20.58.1880
Gene Symbol:  DMAP1
Gene Ontology:  GO:0003714|GO:0003677|GO:0006281|GO:0006355|GO:0003700
PubMed:  19845771|8882580
SCOP:  4000317

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DMAP1 pfam05499
DNA methyltransferase 1-associated protein 1 (DMAP1); DNA methylation can contribute to ...
 243-400 3.64e-102

DNA methyltransferase 1-associated protein 1 (DMAP1); DNA methylation can contribute to transcriptional silencing through several transcriptionally repressive complexes, which include methyl-CpG binding domain proteins (MBDs) and histone deacetylases (HDACs). The chief enzyme that maintains mammalian DNA methylation, DNMT1, can also establish a repressive transcription complex. The non-catalytic amino terminus of DNMT1 binds to HDAC2 and DMAP1 (for DNMT1 associated protein), and can mediate transcriptional repression. DMAP1 has intrinsic transcription repressive activity, and binds to the transcriptional co-repressor TSG101. DMAP1 is targeted to replication foci through interaction with the far N terminus of DNMT1 throughout S phase, whereas HDAC2 joins DNMT1 and DMAP1 only during late S phase, providing a platform for how histones may become deacetylated in heterochromatin following replication.


:

Pssm-ID: 398903  Cd Length: 163  Bit Score: 301.90  E-value: 3.64e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963557   243 EEEYLLQELRKIEARKKEREKRSQDLQKLITAADTTAEQRRTERKAPKKKLPQKKEAEKPAVPE---TAGIKFPDFKSAG 319
Cdd:pfam05499   1 EEEMLLQELRKIEARKKEREKKTQDLQKLITAADSQAEARRSERKSTKKKLPQQRSKESSVSPEpvlTAGIKFPDFKSSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963557   320 VTLRSQRMKLPSSVGQKKIKALEQMLLELGVELSPTPTEELVHMFNELRSDLVLLYELKQACANCEYELQMLRHRHEALA 399
Cdd:pfam05499  81 VSLRSQRMKLPASVGQKKTKAIEQLLEELKIDLNPMPTEEICQHFNELRSDIVLLYELKQALANCEFELQSLRHQYEALA 160


                  .
gi 12963557   400 R 400
Cdd:pfam05499 161 P 161
SANT_DAMP1_like pfam16282
SANT/Myb-like domain of DAMP1; This domain, approximately 90 residues, is mainly found in DNA ...
 124-203 3.91e-48

SANT/Myb-like domain of DAMP1; This domain, approximately 90 residues, is mainly found in DNA methyltransferase 1-associated protein 1 (DAMP1) that plays an important role in development and maintenace of genome integrity in various mammalia species. It mainly consists of tandem repeats of three alpha-helices that are arranged in a helix-turn-helix motif and shows a structual similarity with SANT domain and Myb DNA-binding domain, indicating it contains a putative DNA binding site.


:

Pssm-ID: 465084  Cd Length: 80  Bit Score: 159.94  E-value: 3.91e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963557   124 YPFARFNKTVQVPVYSEQEYQLYLHDDAWTKAETDHLFDLSRRFDLRFVVIHDRYDHQQFKKRSVEDLKERYYHICAKLA 203
Cdd:pfam16282   1 YPFAKFNKKVDIPTYTDEEYERHLKDDDWTKEETDYLFDLCRRYDLRFIVIADRYDFPPGKKRSVEDLKERYYSVCRKLL 80
 
Name Accession Description Interval E-value
DMAP1 pfam05499
DNA methyltransferase 1-associated protein 1 (DMAP1); DNA methylation can contribute to ...
 243-400 3.64e-102

DNA methyltransferase 1-associated protein 1 (DMAP1); DNA methylation can contribute to transcriptional silencing through several transcriptionally repressive complexes, which include methyl-CpG binding domain proteins (MBDs) and histone deacetylases (HDACs). The chief enzyme that maintains mammalian DNA methylation, DNMT1, can also establish a repressive transcription complex. The non-catalytic amino terminus of DNMT1 binds to HDAC2 and DMAP1 (for DNMT1 associated protein), and can mediate transcriptional repression. DMAP1 has intrinsic transcription repressive activity, and binds to the transcriptional co-repressor TSG101. DMAP1 is targeted to replication foci through interaction with the far N terminus of DNMT1 throughout S phase, whereas HDAC2 joins DNMT1 and DMAP1 only during late S phase, providing a platform for how histones may become deacetylated in heterochromatin following replication.


Pssm-ID: 398903  Cd Length: 163  Bit Score: 301.90  E-value: 3.64e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963557   243 EEEYLLQELRKIEARKKEREKRSQDLQKLITAADTTAEQRRTERKAPKKKLPQKKEAEKPAVPE---TAGIKFPDFKSAG 319
Cdd:pfam05499   1 EEEMLLQELRKIEARKKEREKKTQDLQKLITAADSQAEARRSERKSTKKKLPQQRSKESSVSPEpvlTAGIKFPDFKSSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963557   320 VTLRSQRMKLPSSVGQKKIKALEQMLLELGVELSPTPTEELVHMFNELRSDLVLLYELKQACANCEYELQMLRHRHEALA 399
Cdd:pfam05499  81 VSLRSQRMKLPASVGQKKTKAIEQLLEELKIDLNPMPTEEICQHFNELRSDIVLLYELKQALANCEFELQSLRHQYEALA 160


                  .
gi 12963557   400 R 400
Cdd:pfam05499 161 P 161
SANT_DAMP1_like pfam16282
SANT/Myb-like domain of DAMP1; This domain, approximately 90 residues, is mainly found in DNA ...
 124-203 3.91e-48

SANT/Myb-like domain of DAMP1; This domain, approximately 90 residues, is mainly found in DNA methyltransferase 1-associated protein 1 (DAMP1) that plays an important role in development and maintenace of genome integrity in various mammalia species. It mainly consists of tandem repeats of three alpha-helices that are arranged in a helix-turn-helix motif and shows a structual similarity with SANT domain and Myb DNA-binding domain, indicating it contains a putative DNA binding site.


Pssm-ID: 465084  Cd Length: 80  Bit Score: 159.94  E-value: 3.91e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963557   124 YPFARFNKTVQVPVYSEQEYQLYLHDDAWTKAETDHLFDLSRRFDLRFVVIHDRYDHQQFKKRSVEDLKERYYHICAKLA 203
Cdd:pfam16282   1 YPFAKFNKKVDIPTYTDEEYERHLKDDDWTKEETDYLFDLCRRYDLRFIVIADRYDFPPGKKRSVEDLKERYYSVCRKLL 80
SANT_DMAP1_like cd11658
SANT/myb-like domain of Human Dna Methyltransferase 1 Associated Protein 1-like; These ...
 152-199 4.44e-20

SANT/myb-like domain of Human Dna Methyltransferase 1 Associated Protein 1-like; These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.


Pssm-ID: 212556  Cd Length: 46  Bit Score: 83.23  E-value: 4.44e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 12963557 152 WTKAETDHLFDLSRRFDLRFVVIHDRYDHQqfKKRSVEDLKERYYHIC 199
Cdd:cd11658   1 WTKEETDYLFDLVKRFDLRWNVILDRYPFQ--KGRSVEDLKEKYYHLC 46
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 224-301 3.27e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 3.27e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12963557 224 RRRKEQLERLYNRTPEQVAEEEYLLQELRKIEARKKEREKRSQDLQKLITAADTTAEQRRTERKAPKKKLPQKKEAEK 301
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
 
Name Accession Description Interval E-value
DMAP1 pfam05499
DNA methyltransferase 1-associated protein 1 (DMAP1); DNA methylation can contribute to ...
 243-400 3.64e-102

DNA methyltransferase 1-associated protein 1 (DMAP1); DNA methylation can contribute to transcriptional silencing through several transcriptionally repressive complexes, which include methyl-CpG binding domain proteins (MBDs) and histone deacetylases (HDACs). The chief enzyme that maintains mammalian DNA methylation, DNMT1, can also establish a repressive transcription complex. The non-catalytic amino terminus of DNMT1 binds to HDAC2 and DMAP1 (for DNMT1 associated protein), and can mediate transcriptional repression. DMAP1 has intrinsic transcription repressive activity, and binds to the transcriptional co-repressor TSG101. DMAP1 is targeted to replication foci through interaction with the far N terminus of DNMT1 throughout S phase, whereas HDAC2 joins DNMT1 and DMAP1 only during late S phase, providing a platform for how histones may become deacetylated in heterochromatin following replication.


Pssm-ID: 398903  Cd Length: 163  Bit Score: 301.90  E-value: 3.64e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963557   243 EEEYLLQELRKIEARKKEREKRSQDLQKLITAADTTAEQRRTERKAPKKKLPQKKEAEKPAVPE---TAGIKFPDFKSAG 319
Cdd:pfam05499   1 EEEMLLQELRKIEARKKEREKKTQDLQKLITAADSQAEARRSERKSTKKKLPQQRSKESSVSPEpvlTAGIKFPDFKSSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963557   320 VTLRSQRMKLPSSVGQKKIKALEQMLLELGVELSPTPTEELVHMFNELRSDLVLLYELKQACANCEYELQMLRHRHEALA 399
Cdd:pfam05499  81 VSLRSQRMKLPASVGQKKTKAIEQLLEELKIDLNPMPTEEICQHFNELRSDIVLLYELKQALANCEFELQSLRHQYEALA 160


                  .
gi 12963557   400 R 400
Cdd:pfam05499 161 P 161
SANT_DAMP1_like pfam16282
SANT/Myb-like domain of DAMP1; This domain, approximately 90 residues, is mainly found in DNA ...
 124-203 3.91e-48

SANT/Myb-like domain of DAMP1; This domain, approximately 90 residues, is mainly found in DNA methyltransferase 1-associated protein 1 (DAMP1) that plays an important role in development and maintenace of genome integrity in various mammalia species. It mainly consists of tandem repeats of three alpha-helices that are arranged in a helix-turn-helix motif and shows a structual similarity with SANT domain and Myb DNA-binding domain, indicating it contains a putative DNA binding site.


Pssm-ID: 465084  Cd Length: 80  Bit Score: 159.94  E-value: 3.91e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963557   124 YPFARFNKTVQVPVYSEQEYQLYLHDDAWTKAETDHLFDLSRRFDLRFVVIHDRYDHQQFKKRSVEDLKERYYHICAKLA 203
Cdd:pfam16282   1 YPFAKFNKKVDIPTYTDEEYERHLKDDDWTKEETDYLFDLCRRYDLRFIVIADRYDFPPGKKRSVEDLKERYYSVCRKLL 80
SANT_DMAP1_like cd11658
SANT/myb-like domain of Human Dna Methyltransferase 1 Associated Protein 1-like; These ...
 152-199 4.44e-20

SANT/myb-like domain of Human Dna Methyltransferase 1 Associated Protein 1-like; These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.


Pssm-ID: 212556  Cd Length: 46  Bit Score: 83.23  E-value: 4.44e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 12963557 152 WTKAETDHLFDLSRRFDLRFVVIHDRYDHQqfKKRSVEDLKERYYHIC 199
Cdd:cd11658   1 WTKEETDYLFDLVKRFDLRWNVILDRYPFQ--KGRSVEDLKEKYYHLC 46
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 224-301 3.27e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 3.27e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12963557 224 RRRKEQLERLYNRTPEQVAEEEYLLQELRKIEARKKEREKRSQDLQKLITAADTTAEQRRTERKAPKKKLPQKKEAEK 301
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 223-300 9.24e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 36.94  E-value: 9.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12963557   223 ERRRKEQLERLYNRTPEQVAEEEYLLQElrkIEARKKEREKRSQDLQKLITAADTTAEQRRTERKAPKKKLPQKKEAE 300
Cdd:pfam05672  33 ERLEKEEEERLRKEELRRRAEEERARRE---EEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAE 107
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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