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Conserved domains on  [gi|767918849|ref|XP_011509774|]
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methyl-CpG-binding domain protein 5 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PWWP_MBD5 cd20141
PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is ...
1616-1712 6.57e-54

PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is a methyl-CpG-binding protein that binds to heterochromatin. It does not interact with either methylated or unmethylated DNA. MBD5 acts as a transcriptional regulator responsible for 2q23.1 deletion syndrome. It belongs to the MBD family proteins, which play central roles in transcriptional regulation and development. The PWWP domain specifically recognizes DNA and histone methylated lysines.


:

Pssm-ID: 438969  Cd Length: 92  Bit Score: 182.90  E-value: 6.57e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918849 1616 FNVGDLVWGQIKGLTSWPGKLVREDDVHNScqqspEEGKVWVMWFGLHTFTQVEPEKLKTLTEGLEAYSRVRKRNRKSGK 1695
Cdd:cd20141     1 FNVGDLVWGQIRGFPSWPGKLVSENDVGKT-----NEGKVWVSWFGDHSFGQVEPDKLKTLSEGLEAHHRARKRTRKGRK 75
                          90
                  ....*....|....*..
gi 767918849 1696 LNNHLEAAIHEAMSELD 1712
Cdd:cd20141    76 LNNHLEAAIQEAMSELD 92
MBD super family cl00110
MeCP2, MBD1, MBD2, MBD3, MBD4, CLLD8-like, and BAZ2A-like proteins constitute a family of ...
21-79 2.03e-04

MeCP2, MBD1, MBD2, MBD3, MBD4, CLLD8-like, and BAZ2A-like proteins constitute a family of proteins that share the methyl-CpG-binding domain (MBD). The MBD consists of about 70 residues and is defined as the minimal region required for binding to methylated DNA by a methyl-CpG-binding protein which binds specifically to methylated DNA. The MBD can recognize a single symmetrically methylated CpG either as naked DNA or within chromatin. MeCP2, MBD1 and MBD2 (and likely MBD3) form complexes with histone deacetylase and are involved in histone deacetylase-dependent repression of transcription. MBD4 is an endonuclease that forms a complex with the DNA mismatch-repair protein MLH1. The MBDs present in putative chromatin remodelling subunit, BAZ2A, and putative histone methyltransferase, CLLD8, represent two phylogenetically distinct groups within the MBD protein family.


The actual alignment was detected with superfamily member smart00391:

Pssm-ID: 469618  Cd Length: 77  Bit Score: 41.59  E-value: 2.03e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767918849     21 VPVGWQRRVDQ---------NGVLYVSPSGSLLSCLEQVKTYLLTDGTCKCGLECplilpkvFNFDPG 79
Cdd:smart00391    8 LPCGWRRETKQrksgrsagkFDVYYISPCGKKLRSKSELARYLHKNGDLSLDLEC-------FDFNAT 68
 
Name Accession Description Interval E-value
PWWP_MBD5 cd20141
PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is ...
1616-1712 6.57e-54

PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is a methyl-CpG-binding protein that binds to heterochromatin. It does not interact with either methylated or unmethylated DNA. MBD5 acts as a transcriptional regulator responsible for 2q23.1 deletion syndrome. It belongs to the MBD family proteins, which play central roles in transcriptional regulation and development. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438969  Cd Length: 92  Bit Score: 182.90  E-value: 6.57e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918849 1616 FNVGDLVWGQIKGLTSWPGKLVREDDVHNScqqspEEGKVWVMWFGLHTFTQVEPEKLKTLTEGLEAYSRVRKRNRKSGK 1695
Cdd:cd20141     1 FNVGDLVWGQIRGFPSWPGKLVSENDVGKT-----NEGKVWVSWFGDHSFGQVEPDKLKTLSEGLEAHHRARKRTRKGRK 75
                          90
                  ....*....|....*..
gi 767918849 1696 LNNHLEAAIHEAMSELD 1712
Cdd:cd20141    76 LNNHLEAAIQEAMSELD 92
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
1619-1712 8.94e-16

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyzes all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organizing higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression.


Pssm-ID: 459964 [Multi-domain]  Cd Length: 92  Bit Score: 74.38  E-value: 8.94e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918849  1619 GDLVWGQIKGLTSWPGKLVREDDVHNSC-QQSPEEGKVWVMWFGLHTFTQVEPEKLKTLTEGLEAYSRVRKRNRKSGKln 1697
Cdd:pfam00855    1 GDLVWAKLKGYPWWPARVVDPEELPENVlKPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEFEYLKKKKKKKKKK-- 78
                           90
                   ....*....|....*
gi 767918849  1698 nHLEAAIHEAMSELD 1712
Cdd:pfam00855   79 -AFKKALEEAEEALK 92
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
1616-1677 5.31e-09

domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 53.89  E-value: 5.31e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767918849   1616 FNVGDLVWGQIKGLTSWPGKLV-REDDVHNSCQQSPEEGKVWVMWFGLHTFTQVEPEKLKTLT 1677
Cdd:smart00293    1 FKPGDLVWAKMKGFPWWPALVIsPKMTPDNIMKRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
MBD smart00391
Methyl-CpG binding domain; Methyl-CpG binding domain, also known as the TAM (TTF-IIP5, ARBP, ...
21-79 2.03e-04

Methyl-CpG binding domain; Methyl-CpG binding domain, also known as the TAM (TTF-IIP5, ARBP, MeCP1) domain


Pssm-ID: 128673  Cd Length: 77  Bit Score: 41.59  E-value: 2.03e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767918849     21 VPVGWQRRVDQ---------NGVLYVSPSGSLLSCLEQVKTYLLTDGTCKCGLECplilpkvFNFDPG 79
Cdd:smart00391    8 LPCGWRRETKQrksgrsagkFDVYYISPCGKKLRSKSELARYLHKNGDLSLDLEC-------FDFNAT 68
 
Name Accession Description Interval E-value
PWWP_MBD5 cd20141
PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is ...
1616-1712 6.57e-54

PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is a methyl-CpG-binding protein that binds to heterochromatin. It does not interact with either methylated or unmethylated DNA. MBD5 acts as a transcriptional regulator responsible for 2q23.1 deletion syndrome. It belongs to the MBD family proteins, which play central roles in transcriptional regulation and development. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438969  Cd Length: 92  Bit Score: 182.90  E-value: 6.57e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918849 1616 FNVGDLVWGQIKGLTSWPGKLVREDDVHNScqqspEEGKVWVMWFGLHTFTQVEPEKLKTLTEGLEAYSRVRKRNRKSGK 1695
Cdd:cd20141     1 FNVGDLVWGQIRGFPSWPGKLVSENDVGKT-----NEGKVWVSWFGDHSFGQVEPDKLKTLSEGLEAHHRARKRTRKGRK 75
                          90
                  ....*....|....*..
gi 767918849 1696 LNNHLEAAIHEAMSELD 1712
Cdd:cd20141    76 LNNHLEAAIQEAMSELD 92
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
1619-1710 2.01e-17

PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids and is composed of a five-stranded antiparallel beta-barrel followed by a helical region. It is found in numerous proteins that are involved in cell division, growth, and differentiation. Most PWWP-domain proteins seem to be nuclear, often DNA-binding, proteins that function as transcription factors regulating a variety of developmental processes. PWWP domains specifically recognize DNA and histone methylated lysines at the level of the nucleosome. Based on the fact that other regions of PWWP-domain proteins are responsible for nuclear localization and DNA-binding, is likely that the PWWP domain acts as a site for protein-protein binding interactions, influencing chromatin remodeling and thereby regulating transcriptional processes. Some PWWP-domain proteins have been linked to cancer or other diseases; some are known to function as growth factors.


Pssm-ID: 438958 [Multi-domain]  Cd Length: 86  Bit Score: 78.69  E-value: 2.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918849 1619 GDLVWGQIKGLTSWPGKLVREDDVHNSCQQSPEEGKVWVMWFGLHTFTQVEPEKLKTLTEGLEAYSRVRKRNRKSgklnn 1698
Cdd:cd05162     1 GDLVWAKLKGYPWWPARVVDPEELPEEVGKKKKKGGVLVQFFGDNDYAWVKSKNIKPFEEGFKKEFKKKKKKSKK----- 75
                          90
                  ....*....|..
gi 767918849 1699 hLEAAIHEAMSE 1710
Cdd:cd05162    76 -FKKAVEEAEEA 86
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
1619-1712 8.94e-16

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyzes all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organizing higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression.


Pssm-ID: 459964 [Multi-domain]  Cd Length: 92  Bit Score: 74.38  E-value: 8.94e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918849  1619 GDLVWGQIKGLTSWPGKLVREDDVHNSC-QQSPEEGKVWVMWFGLHTFTQVEPEKLKTLTEGLEAYSRVRKRNRKSGKln 1697
Cdd:pfam00855    1 GDLVWAKLKGYPWWPARVVDPEELPENVlKPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEFEYLKKKKKKKKKK-- 78
                           90
                   ....*....|....*
gi 767918849  1698 nHLEAAIHEAMSELD 1712
Cdd:pfam00855   79 -AFKKALEEAEEALK 92
PWWP_DNMT3 cd05835
PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family ...
1617-1711 1.10e-15

PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family includes DNMT3A and DNMT3B, which are required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNMT3A, also called DNA methyltransferase HsaIIIA, DNA MTase HsaIIIA, or M.HsaIIIA, modifies DNA in a non-processive manner and also methylates non-CpG sites. It may preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. DNMT3A is recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. DNMT3B, also called DNA methyltransferase HsaIIIB, DNA MTase HsaIIIB, or M.HsaIIIB, may preferentially methylate nucleosomal DNA within the nucleosome core region. DNMT3B may function as a transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. Members of this family contains a PWWP domain that is responsible for establishing DNA methylation patterns during embryogenesis and gametogenesis. In tumorigenesis, DNA methylation by DNMT3B is known to play a role in the inactivation of tumor suppressor genes. In addition, a point mutation in the PWWP domain of DNMT3B has been identified in patients with ICF (immunodeficiency, centromeric instability, and facial anomalie) syndrome , a rare autosomal recessive disorder characterized by hypomethylation of classical satellite DNA.


Pssm-ID: 438960 [Multi-domain]  Cd Length: 89  Bit Score: 73.83  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918849 1617 NVGDLVWGQIKGLTSWPGKLVReddvHNSCQQSPE-EGKVWVMWFGLHTFTQVEPEKLKTLTEGLEAYSRVRKRNRKsgk 1695
Cdd:cd05835     1 KIGDLVWAKLKGSPWWPGIVVS----HKDCGQKPPaEGSVWVFWFGDHKVSEVPLDKILPFAEFFNKFYISKNSSKL--- 73
                          90
                  ....*....|....*.
gi 767918849 1696 lnnhLEAAIHEAMSEL 1711
Cdd:cd05835    74 ----YKKAVYEALKEA 85
PWWP_DNMT3A cd20154
PWWP domain found in DNA (cytosine-5)-methyltransferase 3A (DNMT3A); DNMT3A, also called DNA ...
1614-1683 9.36e-10

PWWP domain found in DNA (cytosine-5)-methyltransferase 3A (DNMT3A); DNMT3A, also called DNA methyltransferase HsaIIIA, DNA MTase HsaIIIA, or M.HsaIIIA, is required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. It modifies DNA in a non-processive manner and also methylates non-CpG sites. It may preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. DNMT3A is recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. It contains a PWWP domain that binds methylated histone.


Pssm-ID: 438982  Cd Length: 134  Bit Score: 58.44  E-value: 9.36e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918849 1614 RTFNVGDLVWGQIKGLTSWPGKLVREDDVHNScqqSPEEGKVWVMWFGLHTFTQVEPEKLKTLTEGLEAY 1683
Cdd:cd20154     4 RGFGIGELVWGKLRGFSWWPGRIVSWWMTGRS---RAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFSSAF 70
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
1616-1677 5.31e-09

domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 53.89  E-value: 5.31e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767918849   1616 FNVGDLVWGQIKGLTSWPGKLV-REDDVHNSCQQSPEEGKVWVMWFGLHTFTQVEPEKLKTLT 1677
Cdd:smart00293    1 FKPGDLVWAKMKGFPWWPALVIsPKMTPDNIMKRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
1616-1688 8.29e-09

PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called 3-hydroxyisobutyrate dehydrogenase-like protein, cytokine-like nuclear factor N-PAC, nuclear protein NP60, or nuclear protein of 60 kDa, is a putative oxidoreductase that is recruited on chromatin and promotes KDM1B demethylase activity. It recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3). GLYR1 enhances the activity of MAP2K4 and MAP2K6 kinases to phosphorylate p38-alpha. In addition to the PWWP domain, GLYR1 also contains an AT-hook and a C-terminal NAD-binding domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438961 [Multi-domain]  Cd Length: 86  Bit Score: 54.15  E-value: 8.29e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767918849 1616 FNVGDLVWGQIKGLTSWPGKLVREDDvhNSCQQSPEEGKVWVMWFGLHTFTQVEPEKLKTLTEGLEAYSRVRK 1688
Cdd:cd05836     1 FKIGDLVWAKMKGFPPWPGKIVNPPP--DLKKPPRKKKMHCVYFFGSENYAWIEDENIKPYEEFKEEMLKSKK 71
PWWP_DNMT3B cd20155
PWWP domain found in DNA (cytosine-5)-methyltransferase 3B (DNMT3B); DNMT3B, also called DNA ...
1618-1677 4.12e-07

PWWP domain found in DNA (cytosine-5)-methyltransferase 3B (DNMT3B); DNMT3B, also called DNA methyltransferase HsaIIIB, DNA MTase HsaIIIB, or M.HsaIIIB, is required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. It may preferentially methylate nucleosomal DNA within the nucleosome core region. DNMT3B may function as a transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. In tumorigenesis, DNA methylation by DNMT3B is known to play a role in the inactivation of tumor suppressor genes. In addition, a point mutation in the PWWP domain of DNMT3B has been identified in patients with ICF (immunodeficiency, centromeric instability, and facial anomalies) syndrome, a rare autosomal recessive disorder characterized by hypomethylation of classical satellite DNA.


Pssm-ID: 438983  Cd Length: 117  Bit Score: 50.25  E-value: 4.12e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918849 1618 VGDLVWGQIKGLTSWPGKLVredDVHNSCQQSPEEGKVWVMWFGLHTFTQVEPEKLKTLT 1677
Cdd:cd20155     2 IGELVWGKIKGFSWWPAMVV---SWRATGKRQASSGMRWLQWFGDGKFSEVSADKLVSLT 58
PWWP_AtATX1-like cd20142
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
1617-1691 9.14e-06

PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like proteins ATX1, ATX2, and similar proteins; This family includes A. thaliana ATX1 and ATX2, which are sister paralogs originating from a segmental chromosomal duplication. They are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1, also called protein SET domain group 27, or trithorax-homolog protein 1 (TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1 regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2, also called protein SET domain group 30, or trithorax-homolog protein 2 (TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). Both ATX1 and ATX2 are multi-domain containing proteins that consist of an N-terminal PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438970 [Multi-domain]  Cd Length: 97  Bit Score: 45.81  E-value: 9.14e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767918849 1617 NVGDLVWGQIKGLTSWPGKLVRED---DVHNSCQQSPEEGKVWVMWFGLHTFTQVEPEKLKTLTEGLEA-YSRVRKRNR 1691
Cdd:cd20142     1 SPGDVVWAKVKGYPMWPALVIDEEhaeRCGLEANRPGKKGTVPVQFFGTYEVARLNPKKVVGFSKGLDLkYHSKCKAPV 79
PWWP_PWWP2 cd20140
PWWP domain found in the PWWP domain-containing protein 2 (PWWP2) family; The PWWP2 family ...
1614-1711 2.21e-05

PWWP domain found in the PWWP domain-containing protein 2 (PWWP2) family; The PWWP2 family includes PWWP2A and its paralog PWWP2B. PWWP2A is a H2A.Z-specific chromatin binding protein which may play an important role in the neural crest stem cell migration and differentiation during early development. It is also required for proper mitosis progression. PWWP2A and PWWP2B form a stable complex with NuRD subunits MTA1/2/3:HDAC1/2:RBBP4/7, but not with MBD2/3, p66alpha/beta, and CHD3/4. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438968  Cd Length: 92  Bit Score: 44.56  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918849 1614 RTFNVGDLVWGQIKGLTSWPGKLvreddVHNSCQQSPEEGKVW----VMWFGLHTFTQVEPEKLKTLtegLEAY-SRVRK 1688
Cdd:cd20140     2 RTLRVGDIVWGKIHGFPWWPGRI-----LSITVSRDDNGELSTqeahVSWFGSSTTSYMPCSQLYPF---LEDFkLRYNK 73
                          90       100
                  ....*....|....*....|...
gi 767918849 1689 RNRKSGKlnnhleAAIHEAMSEL 1711
Cdd:cd20140    74 KKRGPYK------EAVRQALEAA 90
PWWP_PWWP2B cd20153
PWWP domain found in PWWP domain-containing protein 2B (PWWP2B); PWWP2B is a paralog of PWWP2A, ...
1614-1712 2.56e-05

PWWP domain found in PWWP domain-containing protein 2B (PWWP2B); PWWP2B is a paralog of PWWP2A, a H2A.Z-specific chromatin binding protein which may play an important role in the neural crest stem cell migration and differentiation during early development. PWWP2A and PWWP2B form a stable complex with NuRD subunits MTA1/2/3:HDAC1/2:RBBP4/7, but not with MBD2/3, p66alpha/beta, and CHD3/4. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438981  Cd Length: 116  Bit Score: 45.33  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918849 1614 RTFNVGDLVWGQIKGLTSWPGKLV-----REDDVHNSCQQSPeegkvwVMWFGLHTFTQVEPEKLKTLTEgleaYSRVRK 1688
Cdd:cd20153    12 RTVSVGDIVWGKIHGFPWWPARVLsislsQKEDGEPSWQEAK------VSWFGSPTTSLLSVSKLSPFSE----FFKLRF 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 767918849 1689 RNRKSG----------KLNNHLEAAIHEAMSELD 1712
Cdd:cd20153    82 NRKKKGmyrkaiteaaKAAEHLTPEIRELLTQFE 115
MBD smart00391
Methyl-CpG binding domain; Methyl-CpG binding domain, also known as the TAM (TTF-IIP5, ARBP, ...
21-79 2.03e-04

Methyl-CpG binding domain; Methyl-CpG binding domain, also known as the TAM (TTF-IIP5, ARBP, MeCP1) domain


Pssm-ID: 128673  Cd Length: 77  Bit Score: 41.59  E-value: 2.03e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767918849     21 VPVGWQRRVDQ---------NGVLYVSPSGSLLSCLEQVKTYLLTDGTCKCGLECplilpkvFNFDPG 79
Cdd:smart00391    8 LPCGWRRETKQrksgrsagkFDVYYISPCGKKLRSKSELARYLHKNGDLSLDLEC-------FDFNAT 68
PWWP_HULK cd20147
PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family ...
1619-1695 9.31e-04

PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family includes HUA2-like proteins 1-3 (HULK1-3), which are probable transcription factors that act with partial redundancy with each other. They may play diverse and essential roles in the control of plant development, physiology and flowering time. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438975 [Multi-domain]  Cd Length: 92  Bit Score: 40.17  E-value: 9.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767918849 1619 GDLVWGQIKGLTSWPGKLVREDDVhnscQQSPEEGKVWVMWFGLHTFTQVEPEKLKTLTEGLEAYSRVRKRNRKSGK 1695
Cdd:cd20147     1 GDLVLAKVKGFPAWPAQVSEPEDW----GSAPDPKKVFVHFFGTQQIGFCNPGELSEFTEEIKQSLLARTLKKKKGS 73
PWWP_HRP cd05834
PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The ...
1616-1691 3.22e-03

PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The HRP family includes hepatoma-derived growth factor (HDGF), and HDGF-related proteins (HRPs). HDGF, also called high mobility group protein 1-like 2 (HMG-1L2), is a heparin-binding protein that acts as a transcriptional repressor with mitogenic activity for fibroblasts. It is a prognostic factor in several types of cancer. HDGFL1 is also called PWWP domain-containing protein 1 (PWWP1). Its biological function remains unclear. HDGFL2, also called HDGF-related protein 2 (HRP-2), or hepatoma-derived growth factor 2 (HDGF-2), is involved in cellular growth control, through the regulation of cyclin D1 expression. HDGFL3, also called HDGF-related protein 3 (HRP-3), enhances DNA synthesis and may play a role in cell proliferation. The family also includes PC4 and SFRS1-interacting protein (PSIP) and similar proteins. PSIP, also called CLL-associated antigen KW-7, dense fine speckles 70 kDa protein (DFS 70), lens epithelium-derived growth factor (LEDGF), or transcriptional coactivator p75/p52, acts as a transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Members of the HRP family contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438959 [Multi-domain]  Cd Length: 82  Bit Score: 38.30  E-value: 3.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767918849 1616 FNVGDLVWGQIKGLTSWPGKLvreDDVHNscQQSPEEGKVWVMWFGLHTFTQVEPEKLKTLTEGLEAYSRVRKRNR 1691
Cdd:cd05834     1 FKPGDLVFAKVKGYPPWPARI---DEIPE--GAKIPKNKYPVFFYGTHETAFLKPKDLFPYEENKEKYGKPRKRKG 71
PWWP_AtATX3-like cd20143
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
1619-1713 6.14e-03

PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like protein ATX3, ATX4, ATX5, and similar proteins; The family includes A. thaliana ATX3 (also called protein SET domain group 14, or trithorax-homolog protein 3), ATX4 (also called protein SET domain group 16, or trithorax-homolog protein 4) and ATX5 (also called protein SET domain group 29, or trithorax-homolog protein 5), which belong to the histone-lysine methyltransferase family. They show distinct phylogenetic origins from the family of ATX1 and ATX2. They are multi-domain containing protein that consists of an N-terminal PWWP domain, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438971 [Multi-domain]  Cd Length: 100  Bit Score: 38.12  E-value: 6.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918849 1619 GDLVWGQIKGLTSWPGKLVREDDVHNSCQQSPEEGKVWVMWFGL---HTFTQVEPEKLKTLTEGLEAYSR-VRKRNRKSG 1694
Cdd:cd20143     3 GDLVWAKVGTHPFWPARVVEPAEQAEEVRRRCVPGSLCVYFFGPggsRDYGWVRRSMIFPFTDDLARFQTqKIKNKKRPQ 82
                          90
                  ....*....|....*....
gi 767918849 1695 KLNNHLEAAIhEAMSELDK 1713
Cdd:cd20143    83 EFQEALEEAK-LADAGFEE 100
 
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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