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Conserved domains on  [gi|159163271|pdb|1WEE|A]
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Chain A, PHD finger family protein

Protein Classification

PHD finger domain-containing protein( domain architecture ID 366290)

PHD (plant homeodomain) finger domain-containing protein

Gene Ontology:  GO:0008270|GO:0005515
PubMed:  16297627|21514168

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PHD_SF super family cl22851
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
18-63 3.40e-21

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) finger typically characterized as Cys4HisCys3, and a non-canonical extended PHD finger, characterized as Cys2HisCys5HisCys2His. Variations include the RAG2 PHD finger characterized by Cys3His2Cys2His and the PHD finger 5 found in nuclear receptor-binding SET domain-containing proteins characterized by Cys4HisCys2His. The PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. Single or multiple copies of PHD fingers have been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors. The PHD finger domain SF is structurally similar to the RING and FYVE_like superfamilies.


The actual alignment was detected with superfamily member cd15556:

Pssm-ID: 473978 [Multi-domain]  Cd Length: 46  Bit Score: 77.42  E-value: 3.40e-21
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*.
1WEE_A      18 DCKCGTKDDDGERMLACDGCGVWHHTRCIGINNADALPSKFLCFRC 63
Cdd:cd15556  1 DCSCGTRDDDGERMIACDVCEVWQHTRCVGIADNEEPPDHFLCRRC 46
 
Name Accession Description Interval E-value
PHD_MMD1_like cd15556
PHD finger found in Arabidopsis thaliana PHD finger protein MALE MEIOCYTE DEATH 1 (MMD1), PHD ...
18-63 3.40e-21

PHD finger found in Arabidopsis thaliana PHD finger protein MALE MEIOCYTE DEATH 1 (MMD1), PHD finger protein MALE STERILITY 1 (MS1), and similar proteins; MMD1 is a plant homeodomain (PHD) finger protein expressed in male meiocytes. It is encoded by the gene DUET, which is required for male meiotic chromosome organization and progression. MMD1 has been implicated in the regulation of gene expression during meiosis. The mmd1 mutation triggers cell death in male meiocytes. MS1 is a nuclear transcriptional activator that is important for tapetal development and pollen wall biosynthesis. It contains a Leu zipper-like domain and a PHD finger motif, both of which are essential for its function.


Pssm-ID: 277031 [Multi-domain]  Cd Length: 46  Bit Score: 77.42  E-value: 3.40e-21
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*.
1WEE_A      18 DCKCGTKDDDGERMLACDGCGVWHHTRCIGINNADALPSKFLCFRC 63
Cdd:cd15556  1 DCSCGTRDDDGERMIACDVCEVWQHTRCVGIADNEEPPDHFLCRRC 46
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
19-65 2.39e-06

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains. Several PHD fingers have been identified as binding modules of methylated histone H3.


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 40.17  E-value: 2.39e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
1WEE_A        19 CKCGTKDDDGERMLACDGCGVWHHTRCIGI--NNADALPSKFLCFRCIE 65
Cdd:pfam00628  2 CAVCGKSDDGGELVQCDGCDDWFHLACLGPplDPAEIPSGEWLCPECKP 50
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
19-63 1.39e-04

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 35.65  E-value: 1.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
1WEE_A         19 CKCGTKDDDGErMLACDGCGVWHHTRCIGINNADALP-SKFLCFRC 63
Cdd:smart00249  3 SVCGKPDDGGE-LLQCDGCDRWYHQTCLGPPLLEEEPdGKWYCPKC 47
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
22-64 2.25e-03

PHD zinc finger-containing protein [General function prediction only];


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 34.57  E-value: 2.25e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
1WEE_A       22 GTKDDDGERMLACDGCGVWHHTRCIGINNadaLPS-KFLCFRCI 64
Cdd:COG5141 201 STHNENSNAIVFCDGCEICVHQSCYGIQF---LPEgFWLCRKCI 241
 
Name Accession Description Interval E-value
PHD_MMD1_like cd15556
PHD finger found in Arabidopsis thaliana PHD finger protein MALE MEIOCYTE DEATH 1 (MMD1), PHD ...
18-63 3.40e-21

PHD finger found in Arabidopsis thaliana PHD finger protein MALE MEIOCYTE DEATH 1 (MMD1), PHD finger protein MALE STERILITY 1 (MS1), and similar proteins; MMD1 is a plant homeodomain (PHD) finger protein expressed in male meiocytes. It is encoded by the gene DUET, which is required for male meiotic chromosome organization and progression. MMD1 has been implicated in the regulation of gene expression during meiosis. The mmd1 mutation triggers cell death in male meiocytes. MS1 is a nuclear transcriptional activator that is important for tapetal development and pollen wall biosynthesis. It contains a Leu zipper-like domain and a PHD finger motif, both of which are essential for its function.


Pssm-ID: 277031 [Multi-domain]  Cd Length: 46  Bit Score: 77.42  E-value: 3.40e-21
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*.
1WEE_A      18 DCKCGTKDDDGERMLACDGCGVWHHTRCIGINNADALPSKFLCFRC 63
Cdd:cd15556  1 DCSCGTRDDDGERMIACDVCEVWQHTRCVGIADNEEPPDHFLCRRC 46
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
19-65 2.39e-06

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains. Several PHD fingers have been identified as binding modules of methylated histone H3.


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 40.17  E-value: 2.39e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
1WEE_A        19 CKCGTKDDDGERMLACDGCGVWHHTRCIGI--NNADALPSKFLCFRCIE 65
Cdd:pfam00628  2 CAVCGKSDDGGELVQCDGCDDWFHLACLGPplDPAEIPSGEWLCPECKP 50
PHD_MLL5 cd15550
PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that ...
19-63 5.19e-06

PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. It contains a single plant homeodomain (PHD) finger followed by a catalytic SET domain. MLL5 can be recruited to E2F1-responsive promoters to stimulate H3K4 trimethylation and transcriptional activation by binding to the cell cycle regulator host cell factor (HCF-1), thereby facilitating the cell cycle G1 to S phase transition. It is also involved in mitotic fidelity and genomic integrity by modulating the stability of the chromosomal passenger complex (CPC) via the interaction with Borealin. Moreover, MLL5 is a component of a complex associated with retinoic acid receptor that requires GlcN Acylation of its SET domain in order to activate its histone lysine methyltransferase activity. It also participates in the camptothecin (CPT)-induced p53 activation. Furthermore, MLL5 indirectly regulates H3K4 methylation, represses cyclin A2 (CycA) expression, and promotes myogenic differentiation.


Pssm-ID: 277025 [Multi-domain]  Cd Length: 44  Bit Score: 38.84  E-value: 5.19e-06
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*
1WEE_A      19 CKCGTKDDDGeRMLACDGCGVWHHTRCIGInNADALPSKFLCFRC 63
Cdd:cd15550  2 CICGFEHDDG-FMICCDKCSVWQHGDCMGI-DRENIPDSYLCEQC 44
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
19-63 1.78e-05

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) finger typically characterized as Cys4HisCys3, and a non-canonical extended PHD finger, characterized as Cys2HisCys5HisCys2His. Variations include the RAG2 PHD finger characterized by Cys3His2Cys2His and the PHD finger 5 found in nuclear receptor-binding SET domain-containing proteins characterized by Cys4HisCys2His. The PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. Single or multiple copies of PHD fingers have been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors. The PHD finger domain SF is structurally similar to the RING and FYVE_like superfamilies.


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 37.68  E-value: 1.78e-05
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*.
1WEE_A      19 CKCGTKDDDGERMLACDGCGVWHHTRCIGINNADALPS-KFLCFRC 63
Cdd:cd15489  3 IVCGKGGDLGGELLQCDGCGKWFHADCLGPPLSSFVPNgKWICPVC 48
PHD_SPP1 cd16039
PHD finger found in Set1 complex component SPP1; Set1C component SPP1, also called COMPASS ...
24-63 2.16e-05

PHD finger found in Set1 complex component SPP1; Set1C component SPP1, also called COMPASS component Spp1, or Complex proteins associated with set1 protein Spp1, or Suppressor of PRP protein 1, is a component of the COMPASS complex that links histone methylation to initiation of meiotic recombination. It induces double-strand break (DSB) formation by tethering to recombinationally cold regions. SPP1 interacts with H3K4me3 and Mer2, a protein required for DSB formation, to promote recruitment of potential meiotic DSB sites to the chromosomal axis. SPP1 contains a PHD finger, a zinc binding motif.


Pssm-ID: 277186  Cd Length: 46  Bit Score: 37.46  E-value: 2.16e-05
                       10        20        30        40
               ....*....|....*....|....*....|....*....|.
1WEE_A      24 KDDDGERMLACDGCGVWHHTRCIGINNAD-ALPSKFLCFRC 63
Cdd:cd16039  6 KPDDGRWMIACDGCDEWYHFTCVNIPEADvELVDSFFCPPC 46
PHD_Bye1p_SIZ1_like cd15570
PHD domain found in Saccharomyces cerevisiae bypass of ESS1 protein 1 (Bye1p), the E3 Sumo ...
19-63 6.17e-05

PHD domain found in Saccharomyces cerevisiae bypass of ESS1 protein 1 (Bye1p), the E3 Sumo Ligase SIZ1, and similar proteins; Yeast Bye1p is a nuclear transcription factor with a domain resembling the central domain in the transcription elongation factor TFIIS and plays an inhibitory role during transcription elongation. It functions as a multicopy suppressor of Ess1, a peptidyl-prolyl cis-trans isomerase involved in proline isomerization of the C-terminal domain (CTD) of RNA polymerase II (Pol II). Bye1p contains an N-terminal plant homeodomain (PHD) finger, a central Pol II-binding TFIIS-like domain (TLD) domain, and a C-terminal Spen paralogue and orthologue C-terminal (SPOC) domain. The PHD domain binds to a histone H3 tail peptide containing trimethylated lysine 4 (H3K4me3). The TLD domain is responsible for the association with chromatin. Plant SIZ1 protein is a SUMO (small ubiquitin-related modifier) E3 ligase that facilitates conjugation of SUMO to substrate target proteins (sumoylation) and belongs to the protein inhibitor of activated STAT (PIAS) protein family. It negatively regulates abscisic acid (ABA) signaling, which is dependent on the bZIP transcripton factor ABI5. It also modulates plant growth and plays a role in drought stress response likely through the regulation of gene expression. SIZ1 functions as a floral repressor that not only represses the salicylic acid (SA)-dependent pathway, but also promotes FLOWERING LOCUS C (FLC) expression by repressing FLOWERING LOCUS D (FLD) activity through sumoylation. SIZ1 contains a PHD finger, which specifically binds methylated histone H3 at lysine 4 and arginine 2.


Pssm-ID: 277045  Cd Length: 50  Bit Score: 36.28  E-value: 6.17e-05
                       10        20        30        40        50
               ....*....|....*....|....*....|....*....|....*....|
1WEE_A      19 CKCGTKDDDGErMLACDGCGVWHHTRCIGINNADA-----LPSKFLCFRC 63
Cdd:cd15570  2 CPCGSSMEDGS-MIQCEGCKTWQHMDCVLIPDKPAdglpeLPSKFYCELC 50
PHD_Hop1p_like cd15558
PHD finger found in Schizosaccharomyces pombe meiosis-specific protein hop1 (Hop1p) and ...
19-63 1.08e-04

PHD finger found in Schizosaccharomyces pombe meiosis-specific protein hop1 (Hop1p) and similar proteins; Fission yeast Hop1p, also termed linear element-associated protein hop1, is an S. pombe homolog of the synaptonemal complex (SC)-associated protein Hop1 in Saccharomyces cerevisiae. In contrast to S. cerevisiae, S. pombe forms thin threads, known as linear elements (LinEs), in meiotic nuclei, instead of a canonical synaptonemal complex. LinEs contain Rec10 protein and are evolutionary relics of SC axial elements. Fission yeast Hop1p is a linear element (LinE)-associated protein. It also associates with Rec10, which plays a role in recruiting the recombination machinery to chromatin. Hop1p contains an N-terminal HORMA (for Hop1p, Rev7p, and MAD2) domain and a C-terminal plant homeodomain (PHD) finger.


Pssm-ID: 277033  Cd Length: 47  Bit Score: 35.88  E-value: 1.08e-04
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*..
1WEE_A      19 CKCGTKDDDGErMLACDGCGVWHHTRCIGINNAD--ALPSKFLCFRC 63
Cdd:cd15558  2 CECGDWGEDGA-MIQCAFCDTWQHLLCYGFESAKdpRIPDIHVCYRC 47
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
19-63 1.39e-04

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 35.65  E-value: 1.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
1WEE_A         19 CKCGTKDDDGErMLACDGCGVWHHTRCIGINNADALP-SKFLCFRC 63
Cdd:smart00249  3 SVCGKPDDGGE-LLQCDGCDRWYHQTCLGPPLLEEEPdGKWYCPKC 47
PHD2_3_BPTF cd15560
PHD finger 2 and 3 found in bromodomain and PHD finger-containing transcription factor (BPTF); ...
19-63 1.87e-04

PHD finger 2 and 3 found in bromodomain and PHD finger-containing transcription factor (BPTF); BPTF, also termed nucleosome-remodeling factor subunit BPTF, or fetal Alz-50 clone 1 protein (FAC1), or fetal Alzheimer antigen, functions as a transcriptional regulator that exhibits altered expression and subcellular localization during neuronal development and neurodegenerative diseases such as Alzheimer's disease. It interacts with the human orthologue of the Kelch-like Ech-associated protein (Keap1). Its function and subcellular localization can be regulated by Keap1. Moreover, BPTF is a novel DNA-binding protein that recognizes the DNA sequence CACAACAC and represses transcription through this site in a phosphorylation-dependent manner. Furthermore, BPTF interacts with the Myc-associated zinc finger protein (ZF87/MAZ) and alters its transcriptional activity, which has been implicated in gene regulation in neurodegeneration. Some family members contain two or three plant homeodomain (PHD) fingers, which may be involved in complex formation with histone H3 trimethylated at K4 (H3K4me3). This family corresponds to the second and third PHD fingers.


Pssm-ID: 277035  Cd Length: 47  Bit Score: 35.01  E-value: 1.87e-04
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*.
1WEE_A      19 CKCGTKDDDGERMLACDGCGVWHHTRCIGINNADA-LPSKFLCFRC 63
Cdd:cd15560  2 CICRTPYDESQFYIGCDRCQDWFHGRCVGILQSEAeKIDEYVCPQC 47
PHD_PHF20_like cd15549
PHD finger found in PHD finger protein 20 (PHF20) and PHD finger protein 20-like protein 1 ...
19-63 1.12e-03

PHD finger found in PHD finger protein 20 (PHF20) and PHD finger protein 20-like protein 1 (P20L1); PHF20, also termed Glioma-expressed antigen 2, or hepatocellular carcinoma-associated antigen 58, or novel zinc finger protein, or transcription factor TZP (referring to Tudor and zinc finger domain containing protein), is a regulator of NF-kappaB activation by disrupting recruitment of PP2A to p65. It also functions as a transcription factor that binds Akt and plays a role in Akt cell survival/growth signaling. Moreover, it transcriptionally regulates p53. The phosphorylation of PHF20 on Ser291 mediated by protein kinase B (PKB) is essential in tumorigenesis via the regulation of p53 mediated signaling. P20L1 is an active malignant brain tumor (MBT) domain-containing protein that binds to monomethylated lysine 142 on DNA (Cytosine-5) Methyltransferase 1 (DNMT1) (DNMT1K142me1) and colocalizes at the perinucleolar space in a SET7-dependent manner. Its MBT domain reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 proteasomal degradation. Both PHF20 and PHF20L1 contain an N-terminal MBT domain, two Tudor domains, a plant homeodomain (PHD) finger and the putative DNA-binding domains, AT hook and Cys2His2-type zinc finger.


Pssm-ID: 277024  Cd Length: 45  Bit Score: 33.22  E-value: 1.12e-03
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*
1WEE_A      19 CKCGTKDDDGeRMLACDGCGVWHHTRCIGINNADALPSKFLCFRC 63
Cdd:cd15549  2 CICGVNEENG-LMIQCELCLCWQHGVCMGIEEEESVPERYVCYVC 45
PHD3_Lid2p_like cd15520
PHD finger 3 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar ...
18-63 1.69e-03

PHD finger 3 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar proteins; Lid2p is a trimethyl H3K4 (H3K4me3) demethylase responsible for H3K4 hypomethylation in heterochromatin. It interacts with the histone lysine-9 methyltransferase, Clr4, through the Dos1/Clr8-Rik1 complex, and mediates H3K9 methylation and small RNA production. It also acts cooperatively with the histone modification enzymes Set1 and Lsd1, and plays an essential role in cross-talk between H3K4 and H3K9 methylation in euchromatin. Lid2p contains a JmjC domain, three PHD fingers and a JmjN domain. The family corresponds to the third PHD finger.


Pssm-ID: 276995  Cd Length: 47  Bit Score: 32.57  E-value: 1.69e-03
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*..
1WEE_A      18 DCKCGTKDDDGERMLACDGCGVWHHTRCIGINNADA-LPSKFLCFRC 63
Cdd:cd15520  1 RCGCGEGFNIADRMIFCDRCERTVHLDCVGLSDRIVdSPSEFFCPEC 47
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
22-64 2.25e-03

PHD zinc finger-containing protein [General function prediction only];


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 34.57  E-value: 2.25e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
1WEE_A       22 GTKDDDGERMLACDGCGVWHHTRCIGINNadaLPS-KFLCFRCI 64
Cdd:COG5141 201 STHNENSNAIVFCDGCEICVHQSCYGIQF---LPEgFWLCRKCI 241
PHD_ash2p_like cd15583
PHD finger found in Schizosaccharomyces pombe Set1 complex component ash2 (spAsh2p) and ...
18-63 4.32e-03

PHD finger found in Schizosaccharomyces pombe Set1 complex component ash2 (spAsh2p) and similar proteins; spAsh2p, also termed Set1C component ash2, or COMPASS component ash2, or complex proteins associated with set1 protein ash2, or Lid2 complex component ash2, or Lid2C component ash2, is orthologous to Drosophila melanogaster Ash2 protein. Both spAsh2p and D. melanogaster Ash2 contain a plant homeodomain (PHD) finger and a SPRY domain. In contrast, its counterpart in Saccharomyces cerevisiae, Bre2p, has no PHD finger and is not included in this family. spAsh2p shows histone H3 Lys4 (H3K4) methyltransferase activity through its PHD finger. It also interacts with Lid2p in S. pombe. Human Ash2L contains an atypical PHD finger that lacks part of the Cys4HisCys3 signature characteristic of PHD fingers, it binds to only one zinc ion through the second half of the motif and does not have histone tail binding activity.


Pssm-ID: 277058  Cd Length: 50  Bit Score: 31.55  E-value: 4.32e-03
                       10        20        30        40        50
               ....*....|....*....|....*....|....*....|....*....|
1WEE_A      18 DCKCGTKDDDGERMLACDGCGVWHHTRCIGINNADALP----SKFLCFRC 63
Cdd:cd15583  1 YCYCGKDRNLGEVELQCSICLKWFHAKCVSIDNGSCLPfmtnYQFVCKRC 50
PHD_BAZ1A cd15627
PHD finger found in bromodomain adjacent to zinc finger domain protein 1A (BAZ1A); BAZ1A, also ...
19-46 5.09e-03

PHD finger found in bromodomain adjacent to zinc finger domain protein 1A (BAZ1A); BAZ1A, also termed ATP-dependent chromatin-remodeling protein, or ATP-utilizing chromatin assembly and remodeling factor 1 (ACF1), or CHRAC subunit ACF1, or Williams syndrome transcription factor-related chromatin-remodeling factor 180 (WCRF180), or WALp1, is a subunit of the conserved imitation switch (ISWI)-family ATP-dependent chromatin assembly and remodeling factor (ACF)/chromatin accessibility complex (CHRAC) chromatin remodeling complex, which is required for DNA replication through heterochromatin. It alters the remodeling properties of the ATPase motor protein sucrose nonfermenting-2 homolog (SNF2H). Moreover, BAZ1A and its complexes play important roles in DNA double-strand break (DSB) repair. It is essential for averting improper gene expression during spermatogenesis. It also regulates transcriptional repression of vitamin D3 receptor-regulated genes. BAZ1A contains a WAC motif, a DDT domain, BAZ 1 and BAZ 2 motifs, a WAKZ (WSTF/Acf1/KIAA0314/ZK783.4) motif, a plant homeodomain (PHD) finger, and a bromodomain.


Pssm-ID: 277097 [Multi-domain]  Cd Length: 46  Bit Score: 31.59  E-value: 5.09e-03
                       10        20
               ....*....|....*....|....*...
1WEE_A      19 CKCGTKDDDGERMLACDGCGVWHHTRCI 46
Cdd:cd15627  2 CRICRRKGDAEKMLLCDGCDRGHHMYCL 29
PHD_PHF20L1 cd15633
PHD finger found in PHD finger protein 20-like protein 1 (P20L1); P20L1 is an active malignant ...
19-63 9.20e-03

PHD finger found in PHD finger protein 20-like protein 1 (P20L1); P20L1 is an active malignant brain tumor (MBT) domain-containing protein that binds to monomethylated lysine 142 on DNA (Cytosine-5) Methyltransferase 1 (DNMT1) (DNMT1K142me1) and colocalizes at the perinucleolar space in a SET7-dependent manner. Its MBT domain reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 proteasomal degradation. In addition to the MBT domain, PHF20L1 also contains two Tudor domains, a plant homeodomain (PHD) finger and the putative DNA-binding domains, AT hook and Cys2His2-type zinc finger.


Pssm-ID: 277103  Cd Length: 46  Bit Score: 30.76  E-value: 9.20e-03
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*
1WEE_A      19 CKCGTKDDDGeRMLACDGCGVWHHTRCIGINNaDALPSKFLCFRC 63
Cdd:cd15633  2 CICEMDEENG-FMIQCEECLCWQHSVCMGLLE-ESIPEQYICYIC 44
 
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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