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Conserved domains on  [gi|1884086654|ref|NP_001372945|]
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zinc finger CW-type PWWP domain protein 1 isoform 4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PWWP_ZCWPW1 cd20145
PWWP domain found in zinc finger CW-type PWWP domain protein 1 (ZCWPW1) and similar proteins; ...
311-426 1.52e-55

PWWP domain found in zinc finger CW-type PWWP domain protein 1 (ZCWPW1) and similar proteins; ZCWPW1 is a histone H3K4me3 reader. It is associated with late-onset Alzheimer's disease (LOAD). In addition to the PWWP domain, ZCWPW1 contains a zinc finger CW (zf-CW) domain that is a histone modification reader for the histone H3 tail with trimethylated K4. The PWWP domain specifically recognizes DNA and histone methylated lysines.


:

Pssm-ID: 438973  Cd Length: 115  Bit Score: 184.29  E-value: 1.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884086654 311 VAYASYIPGSIIWAKQYGYPWWPGMIESDPDLGEYFLFTSHlDSLPSKYHVTFFGETVSRAWIPVNMLKNFQELSLELSV 390
Cdd:cd20145     1 LIYTKYTPGSLVWAKMPGYPWWPAMVEDDPDTEEFFWLDEE-SDIPTKYHVTFFDKPVSRAWVRASSIKPFTDNSNEPNL 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1884086654 391 MKKRRNDCSQKLGVALMMAQEAEQISIQERVNLFGF 426
Cdd:cd20145    80 TKKKGKKYKKRLNEAVEMAREALKLSIKERLKKFGF 115
zf-CW pfam07496
CW-type Zinc Finger; This domain appears to be a zinc finger. The alignment shows four ...
256-302 1.15e-16

CW-type Zinc Finger; This domain appears to be a zinc finger. The alignment shows four conserved cysteine residues and a conserved tryptophan. It was first identified by, and is predicted to be a "highly specialized mononuclear four-cysteine zinc finger...that plays a role in DNA binding and/or promoting protein-protein interactions in complicated eukaryotic processes including...chromatin methylation status and early embryonic development." Weak homology to pfam00628 further evidences these predictions (personal obs: C Yeats). Twelve different CW-domain-containing protein subfamilies are described, with different subfamilies being characteriztic of vertebrates, higher plants and other animals in which these domain is found.


:

Pssm-ID: 462181  Cd Length: 46  Bit Score: 73.88  E-value: 1.15e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1884086654 256 VWVQCSfpNCGKWRRLCGNIDPSVLPDNWSCDQNTDVQYNRCDIPEE 302
Cdd:pfam07496   1 YWVQCD--SCLKWRRLPTEIDPYELPEPWYCSMNPDPKYNSCDAPEE 45
 
Name Accession Description Interval E-value
PWWP_ZCWPW1 cd20145
PWWP domain found in zinc finger CW-type PWWP domain protein 1 (ZCWPW1) and similar proteins; ...
311-426 1.52e-55

PWWP domain found in zinc finger CW-type PWWP domain protein 1 (ZCWPW1) and similar proteins; ZCWPW1 is a histone H3K4me3 reader. It is associated with late-onset Alzheimer's disease (LOAD). In addition to the PWWP domain, ZCWPW1 contains a zinc finger CW (zf-CW) domain that is a histone modification reader for the histone H3 tail with trimethylated K4. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438973  Cd Length: 115  Bit Score: 184.29  E-value: 1.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884086654 311 VAYASYIPGSIIWAKQYGYPWWPGMIESDPDLGEYFLFTSHlDSLPSKYHVTFFGETVSRAWIPVNMLKNFQELSLELSV 390
Cdd:cd20145     1 LIYTKYTPGSLVWAKMPGYPWWPAMVEDDPDTEEFFWLDEE-SDIPTKYHVTFFDKPVSRAWVRASSIKPFTDNSNEPNL 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1884086654 391 MKKRRNDCSQKLGVALMMAQEAEQISIQERVNLFGF 426
Cdd:cd20145    80 TKKKGKKYKKRLNEAVEMAREALKLSIKERLKKFGF 115
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
319-414 3.12e-20

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: 85.56  E-value: 3.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884086654 319 GSIIWAKQYGYPWWPGMIESDPDLGEYFLftsHLDSLPSKYHVTFFGeTVSRAWIPVNMLKNFQELSLELSVMKKRRNDC 398
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVVDPEELPENVL---KPKKKDGEYLVRFFG-DSEFAWVKPKDLKPFDEGDEFEYLKKKKKKKK 76
                          90
                  ....*....|....*.
gi 1884086654 399 SQKLGVALMMAQEAEQ 414
Cdd:pfam00855  77 KKAFKKALEEAEEALK 92
zf-CW pfam07496
CW-type Zinc Finger; This domain appears to be a zinc finger. The alignment shows four ...
256-302 1.15e-16

CW-type Zinc Finger; This domain appears to be a zinc finger. The alignment shows four conserved cysteine residues and a conserved tryptophan. It was first identified by, and is predicted to be a "highly specialized mononuclear four-cysteine zinc finger...that plays a role in DNA binding and/or promoting protein-protein interactions in complicated eukaryotic processes including...chromatin methylation status and early embryonic development." Weak homology to pfam00628 further evidences these predictions (personal obs: C Yeats). Twelve different CW-domain-containing protein subfamilies are described, with different subfamilies being characteriztic of vertebrates, higher plants and other animals in which these domain is found.


Pssm-ID: 462181  Cd Length: 46  Bit Score: 73.88  E-value: 1.15e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1884086654 256 VWVQCSfpNCGKWRRLCGNIDPSVLPDNWSCDQNTDVQYNRCDIPEE 302
Cdd:pfam07496   1 YWVQCD--SCLKWRRLPTEIDPYELPEPWYCSMNPDPKYNSCDAPEE 45
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
318-379 1.30e-08

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 51.58  E-value: 1.30e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1884086654  318 PGSIIWAKQYGYPWWPGMIESDPDLGEYFLFTSHLDSLpskYHVTFFG--ETvsrAWIPVNMLK 379
Cdd:smart00293   3 PGDLVWAKMKGFPWWPALVISPKMTPDNIMKRKSDENL---YPVLFFGdkDT---AWIPSSKLF 60
 
Name Accession Description Interval E-value
PWWP_ZCWPW1 cd20145
PWWP domain found in zinc finger CW-type PWWP domain protein 1 (ZCWPW1) and similar proteins; ...
311-426 1.52e-55

PWWP domain found in zinc finger CW-type PWWP domain protein 1 (ZCWPW1) and similar proteins; ZCWPW1 is a histone H3K4me3 reader. It is associated with late-onset Alzheimer's disease (LOAD). In addition to the PWWP domain, ZCWPW1 contains a zinc finger CW (zf-CW) domain that is a histone modification reader for the histone H3 tail with trimethylated K4. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438973  Cd Length: 115  Bit Score: 184.29  E-value: 1.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884086654 311 VAYASYIPGSIIWAKQYGYPWWPGMIESDPDLGEYFLFTSHlDSLPSKYHVTFFGETVSRAWIPVNMLKNFQELSLELSV 390
Cdd:cd20145     1 LIYTKYTPGSLVWAKMPGYPWWPAMVEDDPDTEEFFWLDEE-SDIPTKYHVTFFDKPVSRAWVRASSIKPFTDNSNEPNL 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1884086654 391 MKKRRNDCSQKLGVALMMAQEAEQISIQERVNLFGF 426
Cdd:cd20145    80 TKKKGKKYKKRLNEAVEMAREALKLSIKERLKKFGF 115
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
319-414 3.12e-20

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: 85.56  E-value: 3.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884086654 319 GSIIWAKQYGYPWWPGMIESDPDLGEYFLftsHLDSLPSKYHVTFFGeTVSRAWIPVNMLKNFQELSLELSVMKKRRNDC 398
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVVDPEELPENVL---KPKKKDGEYLVRFFG-DSEFAWVKPKDLKPFDEGDEFEYLKKKKKKKK 76
                          90
                  ....*....|....*.
gi 1884086654 399 SQKLGVALMMAQEAEQ 414
Cdd:pfam00855  77 KKAFKKALEEAEEALK 92
PWWP_ZCWPW2 cd20146
PWWP domain found in zinc finger CW-type PWWP domain protein 2 (ZCWPW2) and similar proteins; ...
313-420 3.29e-19

PWWP domain found in zinc finger CW-type PWWP domain protein 2 (ZCWPW2) and similar proteins; ZCWPW2 is a histone H3K4me3 reader. In addition to the PWWP domain, ZCWPW2 contains a zinc finger CW (zf-CW) domain that is a histone modification reader for the histone H3 tail with trimethylated K4. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438974  Cd Length: 113  Bit Score: 83.50  E-value: 3.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884086654 313 YASYIPGSIIWAKQYGYPWWPGMIESDPDLGEYFLFTShlDSLPSKYHVTFFGETVSRAWIPVNMLKNFQELSLELSVMK 392
Cdd:cd20146     6 YSQLPLGSLVWAKMTGYPRWPAILTPDPICGEYVDYDE--DGEVEKYHVEFLGKPHSHAWISAKSVEPYNSNTKTPKCKT 83
                          90       100
                  ....*....|....*....|....*...
gi 1884086654 393 KRRNDCSQKLGVALMMAQEAEQISIQER 420
Cdd:cd20146    84 KKSKKRKKSYESALEEAERLLKLTCEER 111
PWWP_NSD_rpt1 cd20144
first PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
318-419 6.78e-18

first PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein family consists of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1 that are critical in maintaining the chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising in suppressing cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and play nonredundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, through mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (C5HCH). This model corresponds to the first PWWP domain. This family also includes Drosophila melanogaster maternal-effect sterile 4 (dMes4) that may act as a histone-lysine N-methyltransferase required for wing morphogenesis. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438972  Cd Length: 114  Bit Score: 79.67  E-value: 6.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884086654 318 PGSIIWAKQYGYPWWPGMIESDPDLGEYFLFTSHLDSLPSKYHVTFFGETVSRAWIPVNML------KNFQELSLELSVM 391
Cdd:cd20144     1 VGDLVWAKVSGHPWWPCMVTYDPESGLYTKIKGSGGRTYRQYHVQFFGDNGERGWVSEKSLmpfegkEKFEELVKELKKK 80
                          90       100
                  ....*....|....*....|....*...
gi 1884086654 392 KKRRNDCSQKLGVALMMAQEAEQISIQE 419
Cdd:cd20144    81 AKKKSKKAKLEKKVKPSRRKKWEIAVEE 108
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
319-412 1.04e-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: 78.31  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884086654 319 GSIIWAKQYGYPWWPGMIESDPDLGEYFLFTSHldslPSKYHVTFFGETvSRAWIPVNMLKNFQELSLELSVMKKRRNdc 398
Cdd:cd05162     1 GDLVWAKLKGYPWWPARVVDPEELPEEVGKKKK----KGGVLVQFFGDN-DYAWVKSKNIKPFEEGFKKEFKKKKKKS-- 73
                          90
                  ....*....|....
gi 1884086654 399 sQKLGVALMMAQEA 412
Cdd:cd05162    74 -KKFKKAVEEAEEA 86
zf-CW pfam07496
CW-type Zinc Finger; This domain appears to be a zinc finger. The alignment shows four ...
256-302 1.15e-16

CW-type Zinc Finger; This domain appears to be a zinc finger. The alignment shows four conserved cysteine residues and a conserved tryptophan. It was first identified by, and is predicted to be a "highly specialized mononuclear four-cysteine zinc finger...that plays a role in DNA binding and/or promoting protein-protein interactions in complicated eukaryotic processes including...chromatin methylation status and early embryonic development." Weak homology to pfam00628 further evidences these predictions (personal obs: C Yeats). Twelve different CW-domain-containing protein subfamilies are described, with different subfamilies being characteriztic of vertebrates, higher plants and other animals in which these domain is found.


Pssm-ID: 462181  Cd Length: 46  Bit Score: 73.88  E-value: 1.15e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1884086654 256 VWVQCSfpNCGKWRRLCGNIDPSVLPDNWSCDQNTDVQYNRCDIPEE 302
Cdd:pfam07496   1 YWVQCD--SCLKWRRLPTEIDPYELPEPWYCSMNPDPKYNSCDAPEE 45
PWWP_MSH6 cd05837
PWWP domain found in DNA mismatch repair protein MSH6 and similar proteins; MSH6, also called ...
318-423 3.34e-16

PWWP domain found in DNA mismatch repair protein MSH6 and similar proteins; MSH6, also called G/T mismatch-binding protein (GTBP or GTMBP), MutS protein homolog 6, or MutS-alpha 160 kDa subunit (p160), is a mismatch repair protein homologous to bacterial MutS. It is a component of the post-replicative DNA mismatch repair system (MMR). It heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, it forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Mutations in MSH6 have been linked to increased cancer susceptibility, particularly in hereditary nonpolyposis colorectal cancer in humans. MSH6 contains a PWWP domain, but its role in MSH6 remains unclear. MSH6 orthologs found in Saccharomyces cerevisiae, Caenorhabditis elegans, and Arabidopsis thaliana lack the PWWP domain. PWWP domains typically recognize DNA and histone methylated lysines.


Pssm-ID: 438962  Cd Length: 103  Bit Score: 74.63  E-value: 3.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884086654 318 PGSIIWAKQYGYPWWPGMIESDPDLGEYFLFTShldslPSKYHVTFFGETVSRAWIPVNMLKNFQELSLELSVMK--KRR 395
Cdd:cd05837     3 PGDLVWAKLEGYPWWPSLVCNHPTTGFHKKFGK-----KGEVHVQFFDDPPSRAWVKAKNVKPFTGSDDKEFQKGgmFFS 77
                          90       100
                  ....*....|....*....|....*...
gi 1884086654 396 NDCSQKLGVAlmMAQEAEQISIQERVNL 423
Cdd:cd05837    78 KDPKWKKAVK--EADKALKLSVEERLKL 103
PWWP_NSD2_rpt1 cd20162
first PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins; ...
316-426 3.58e-12

first PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins; NSD2, also called histone-lysine N-methyltransferase NSD2, multiple myeloma SET domain-containing protein (MMSET), or protein trithorax-5 Wolf-Hirschhorn syndrome candidate 1 protein (WHSC1), is overexpressed frequently in the t(4;14) translocation in 15% to 20% of multiple myeloma. It plays important roles in cancer cell proliferation, survival, and tumor growth, through mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. It also enhances androgen receptor (AR)-mediated transcription. The principal chromatin-regulatory activity of NSD2 is dimethylation of histone H3 at lysine 36 (H3K36me2). NSD2 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, a high mobility group (HMG) box, five PHD (plant-homeodomain) zinc finger motifs, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD domains mediate chromatin interaction and recognition of histone marks. This model corresponds to the first PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438990  Cd Length: 128  Bit Score: 63.78  E-value: 3.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884086654 316 YIPGSIIWAKQYGYPWWPGMIESDPDLGEYFLFTSHLDSLpSKYHVTFFGETVSRAWI------PVNMLKNFQEL---SL 386
Cdd:cd20162     1 YNVGDLVWSKVSGYPWWPCMVSADPLLHSHTKLKGQKKSA-RQYHVQFFGDAPERAWIfekslvPFEGEGQFEQLcqeSA 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1884086654 387 ELSVMKKRRND----CSQKL----GVALMMAQEAEQISIQERVNLFGF 426
Cdd:cd20162    80 KQAPTKAEKIKllkpISGKLraqwDMGIVQAEEAASMTVEERKAKFTF 127
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
318-379 1.30e-08

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 51.58  E-value: 1.30e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1884086654  318 PGSIIWAKQYGYPWWPGMIESDPDLGEYFLFTSHLDSLpskYHVTFFG--ETvsrAWIPVNMLK 379
Cdd:smart00293   3 PGDLVWAKMKGFPWWPALVISPKMTPDNIMKRKSDENL---YPVLFFGdkDT---AWIPSSKLF 60
PWWP_NSD3_rpt1 cd20163
first PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar proteins; ...
319-426 2.16e-08

first PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar proteins; NSD3, also called histone-lysine N-methyltransferase NSD3, protein whistle, WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, or Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1-like protein 1, or WHSC1L1), is a lysine methyltransferase encoded by gene NSD3, which is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD3 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, five plant-homeodomain (PHD) zinc finger motifs, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD domains are involved in protein-protein interactions. This model corresponds to the first PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438991  Cd Length: 130  Bit Score: 53.01  E-value: 2.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884086654 319 GSIIWAKQYGYPWWPGMIESDPDLGEYflftSHLDSLPSK-YHVTFFGETVSRAWI------PVNMLKNFQELSLE---- 387
Cdd:cd20163     4 GDLVWSKVGTYPWWPCMVSSDPQLEVH----TKINTRGAReYHVQFFSSQPERAWVhekrvrEYKGHKQYEELLAEatkq 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1884086654 388 -------LSVMKKRRNDCSQKLGVALMMAQEAEQISIQERVNLFGF 426
Cdd:cd20163    80 asnhsekQKIRKPRPQRERAQWDIGIAHAEKALKMTREERIEQYTF 125
PWWP_PWWP2 cd20140
PWWP domain found in the PWWP domain-containing protein 2 (PWWP2) family; The PWWP2 family ...
319-395 1.02e-07

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: 49.95  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884086654 319 GSIIWAKQYGYPWWPGMI----ESDPDLGEyflftshldSLPSKYHVTFFGeTVSRAWIPVNMLKNFQElSLELSVMKKR 394
Cdd:cd20140     7 GDIVWGKIHGFPWWPGRIlsitVSRDDNGE---------LSTQEAHVSWFG-SSTTSYMPCSQLYPFLE-DFKLRYNKKK 75

                  .
gi 1884086654 395 R 395
Cdd:cd20140    76 R 76
PWWP_NSD1_rpt1 cd20161
first PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and ...
316-374 3.84e-07

first PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and similar proteins; NSD1, also called H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, androgen receptor coactivator 267 kDa protein, androgen receptor-associated protein of 267 kDa, H3-K36-HMTase H4-K20-HMTase, Lysine N-methyltransferase 3B (KMT3B), or NR-binding SET domain-containing protein, is a lysine methyltransferase that preferentially methylates H3 on Lysine36 (H3-K36) and H4 on Lysine20 (H4-K20), which is primarily associated with active transcription. It plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. It can alter transcription by interacting with the protein NSD1-interacting zinc finger protein 1 (NIZP1). It also mitigates caspase-1 activation by listeriolysin o (LLO) in macrophages, and requires functional LLO for the regulation of IL-1beta secretion. Moreover, NSD1 regulates RNA polymerase II (RNAP II) recruitment to bone morphogenetic protein 4 (BMP4). NSD1 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD domains are involved in protein-protein interactions. The model corresponds to the first PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438989  Cd Length: 116  Bit Score: 49.01  E-value: 3.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1884086654 316 YIPGSIIWAKQYGYPWWPGMIESDPDLGEYFLFTSHLDSLPSKYHVTFFGETVSRAWIP 374
Cdd:cd20161     4 YEVGDLVWAKFSRRPWWPCRICADPLLDTHSKMKVPSRRPCRQYYVETLGELTEKAWVA 62
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
316-393 1.26e-06

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: 46.83  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884086654 316 YIPGSIIWAKQYGYPWWPGMIeSDPDLgeyflftsHLDSLPSK---YHVTFFGeTVSRAWIPVNMLKNFQELSLELSVMK 392
Cdd:cd05836     1 FKIGDLVWAKMKGFPPWPGKI-VNPPP--------DLKKPPRKkkmHCVYFFG-SENYAWIEDENIKPYEEFKEEMLKSK 70

                  .
gi 1884086654 393 K 393
Cdd:cd05836    71 K 71
PWWP_HRP cd05834
PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The ...
316-365 1.78e-06

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: 46.01  E-value: 1.78e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1884086654 316 YIPGSIIWAKQYGYPWWPGMIESDPDLGEyflftshldSLPSKYHVTFFG 365
Cdd:cd05834     1 FKPGDLVFAKVKGYPPWPARIDEIPEGAK---------IPKNKYPVFFYG 41
PWWP_DNMT3 cd05835
PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family ...
318-395 5.14e-06

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: 44.94  E-value: 5.14e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1884086654 318 PGSIIWAKQYGYPWWPGMIESDPDLGEYflftshlDSLPSKYHVTFFGE-TVSRawIPVNMLKNFQELSLELSVMKKRR 395
Cdd:cd05835     2 IGDLVWAKLKGSPWWPGIVVSHKDCGQK-------PPAEGSVWVFWFGDhKVSE--VPLDKILPFAEFFNKFYISKNSS 71
PWWP_BS69 cd20159
PWWP domain found in protein BS69 and similar proteins; Protein BS69, also called zinc finger ...
321-393 7.64e-06

PWWP domain found in protein BS69 and similar proteins; Protein BS69, also called zinc finger MYND domain-containing protein 11 (ZMYND11 or ZMY11), is a ubiquitously expressed nuclear protein acting as a transcriptional co-repressor in association with various transcription factors. It was originally identified as an adenovirus 5 E1A-binding protein that inhibits E1A transactivation, as well as c-Myb transcription. It also mediates repression, at least in part, through interaction with the co-repressor N-CoR. Moreover, it interacts with Toll-interleukin 1 receptor domain (TIR)-containing adaptor molecule-1 (TICAM-1, also named TRIF) to facilitate NF-kappaB activation and type I IFN induction. It associates with PIAS1, a SUMO E3 enzyme, and Ubc9, a SUMO E2 enzyme, and plays an inhibitory role in muscle and neuronal differentiation. Moreover, BS69 regulates Epstein-Barr virus (EBV) latent membrane protein 1 (LMP1)/C-terminal activation region 2 (CTAR2)-mediated NF-kappaB activation by interfering with the complex formation between TNFR-associated death domain protein (TRADD) and LMP1/CTAR2. It also cooperates with tumor necrosis factor receptor (TNFR)-associated factor 3 (TRAF3) in the regulation of EBV-derived LMP1/CTAR1-induced NF-kappaB activation. Furthermore, BS69 is involved in the p53-p21Cip1-mediated senescence pathway. BS69 contains a plant homeodomain (PHD) finger, a bromodomain, a proline-tryptophan-tryptophan-proline (PWWP) domain, and a MYeloid translocation protein 8, Nervy and DEAF-1 (MYND) domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438987  Cd Length: 85  Bit Score: 44.51  E-value: 7.64e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1884086654 321 IIWAKQYGYPWWPG--MIESDpdlgeyflftshldslpSKYHVTFFGETVSRAWIPVNMLKNFqELSLELSVMKK 393
Cdd:cd20159     9 LVWAKQKGFPYWPAkvIQKED-----------------NQYDVRFFGGHHQRAWIPKENIKPI-TTSPKQLKVKR 65
PWWP_BRPF cd05839
PWWP domain found in the bromodomain and PHD finger-containing (BRPF) protein family; The BRPF ...
318-396 2.61e-05

PWWP domain found in the bromodomain and PHD finger-containing (BRPF) protein family; The BRPF family of proteins includes BRPF1, BRD1/BRPF2, and BRPF3. They are scaffold proteins that form monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complexes with other regulatory subunits, such as inhibitor of growth 5 (ING5) and Esa1-associated factor 6 ortholog (EAF6). BRPF proteins have multiple domains, including a plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, C2HC5HC2H, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. The PHD finger binds to lysine 4 of histone H3 (K4H3), the bromodomain interacts with acetylated lysines on N-terminal tails of histones and other proteins, and the PWWP domain shows histone-binding and chromatin association properties.


Pssm-ID: 438964  Cd Length: 106  Bit Score: 43.41  E-value: 2.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884086654 318 PGSIIWAKQYGYPWWPGMI--ESDPDLGEYF----LFTSHLDSLPSKYH-VTFFGETVSRAWIPVN---MLKNFQELSLE 387
Cdd:cd05839     3 PGDLVWAKCRGYPWYPAEIvdPKDPKEGNGVpipvPPDRVLKKSNEKLYlVLFFDAKRTWGWLPRNklrPLGVDEELDKL 82

                  ....*....
gi 1884086654 388 LSVMKKRRN 396
Cdd:cd05839    83 KLSEAKKSK 91
PWWP_PRKCBP1 cd20160
PWWP domain found in protein kinase C-binding protein 1 (PRKCBP1) and similar proteins; ...
317-397 7.30e-05

PWWP domain found in protein kinase C-binding protein 1 (PRKCBP1) and similar proteins; PRKCBP1, also called cutaneous T-cell lymphoma-associated antigen se14-3 (CTCL-associated antigen se14-3), Rack7, or zinc finger MYND domain-containing protein 8 (ZMYND8), is a novel receptor for activated C-kinase (RACK)-like protein that may play an important role in the activation and regulation of PKC-beta I, and the PKC signaling cascade. It also has been identified as a formin homology-2-domain containing protein 1 (FHOD1)-binding protein that may be involved in FHOD1-regulated actin polymerization and transcription. Moreover, PRKCBP1 may function as a REST co-repressor 2 (RCOR2) interacting factor. They form a RCOR2/ZMYND8 complex which might be involved in the regulation of neural differentiation. PRKCBP1 contains a plant homeodomain (PHD) finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438988  Cd Length: 91  Bit Score: 41.78  E-value: 7.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884086654 317 IPGSIIWAKQYGYPWWPG--MIESDPDLgeyflftshldslpskyHVTFFGETvSRAWIPVnmlKNFQELSLELSV-MKK 393
Cdd:cd20160     5 KPHLLVWAKLKGFPFWPAkaLRVNNGQV-----------------DVRFFGAH-DRAWVPV---KDCYLYSKEPPTsVKK 63

                  ....
gi 1884086654 394 RRND 397
Cdd:cd20160    64 KKSG 67
PWWP_AtATX3-like cd20143
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
319-414 1.02e-04

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: 41.59  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884086654 319 GSIIWAKQYGYPWWPGMIESDPDLGEYflftSHLDSLPSKYHVTFFGETVSR--AWIPVNMLKNFQElSLELSVMKKRRN 396
Cdd:cd20143     3 GDLVWAKVGTHPFWPARVVEPAEQAEE----VRRRCVPGSLCVYFFGPGGSRdyGWVRRSMIFPFTD-DLARFQTQKIKN 77
                          90
                  ....*....|....*....
gi 1884086654 397 DCSQK-LGVALMMAQEAEQ 414
Cdd:cd20143    78 KKRPQeFQEALEEAKLADA 96
PWWP_HDGF cd20148
PWWP domain found in Hepatoma-derived growth factor (HDGF); HDGF, also called high mobility ...
316-395 2.25e-04

PWWP domain found in Hepatoma-derived growth factor (HDGF); 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 contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438976 [Multi-domain]  Cd Length: 87  Bit Score: 40.39  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884086654 316 YIPGSIIWAKQYGYPWWPGMIESDPDlgeyflftSHLDSLPSKYHVTFFGeTVSRAWIPVNMLKNFQELSLELSVMKKRR 395
Cdd:cd20148     1 YKCGDLVFAKMKGYPHWPARIDEMPE--------AAVKSTANKYQVFFFG-THETAFLGPKDLFPYEESKEKFGKPNKRK 71
PWWP_BS69-like cd05841
PWWP domain found in protein BS69, protein kinase C-binding protein 1 (PRKCBP1) and similar ...
321-376 2.81e-04

PWWP domain found in protein BS69, protein kinase C-binding protein 1 (PRKCBP1) and similar proteins; Protein BS69, also called zinc finger MYND domain-containing protein 11 (ZMYND11 or ZMY11), is a ubiquitously expressed nuclear protein acting as a transcriptional co-repressor in association with various transcription factors. It was originally identified as an adenovirus 5 E1A-binding protein that inhibits E1A transactivation, as well as c-Myb transcription. BS69 is a multi-domain protein, containing bromo, plant homeodomain (PHD), proline-tryptophan-tryptophan-proline (PWWP), and MYeloid translocation protein 8, Nervy and DEAF-1 (MYND) domains. The specific role of the PWWP domain within BS69 is not clearly identified, but BS69 functions in chromatin remodeling, consistent with other PWWP-containing proteins. PRKCBP1, also called cutaneous T-cell lymphoma-associated antigen se14-3 (CTCL-associated antigen se14-3), Rack7, or zinc finger MYND domain-containing protein 8 (ZMYND8), is a novel receptor for activated C-kinase (RACK)-like protein that may play an important role in the activation and regulation of PKC-beta I, and the PKC signaling cascade. It also has been identified as a formin homology-2-domain containing protein 1 (FHOD1)-binding protein that may be involved in FHOD1-regulated actin polymerization and transcription. Moreover, PRKCBP1 may function as a REST co-repressor 2 (RCOR2) interacting factor. They form a RCOR2/ZMYND8 complex which might be involved in the regulation of neural differentiation. PRKCBP1 contains a PHD finger, a bromodomain, and a PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438966  Cd Length: 89  Bit Score: 40.07  E-value: 2.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1884086654 321 IIWAKQYGYPWWPG--MIESDpdlgeyflftSHLDslpskyhVTFFGeTVSRAWIPVN 376
Cdd:cd05841     9 LVWVKLDGFPFWPAkvMGTKD----------GQVD-------VRFFG-DYDRAWLPSK 48
PWWP_HULK cd20147
PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family ...
319-395 2.13e-03

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: 37.85  E-value: 2.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1884086654 319 GSIIWAKQYGYPWWPGMIESDPDLGEYflftshldSLPSKYHVTFFGeTVSRAWIPVNMLKNFQELSLELSVMKKRR 395
Cdd:cd20147     1 GDLVLAKVKGFPAWPAQVSEPEDWGSA--------PDPKKVFVHFFG-TQQIGFCNPGELSEFTEEIKQSLLARTLK 68
PWWP_PWWP2A cd20152
PWWP domain found in PWWP domain-containing protein 2A (PWWP2A); PWWP2A is a H2A.Z-specific ...
319-336 2.26e-03

PWWP domain found in PWWP domain-containing protein 2A (PWWP2A); 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 its paralog 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: 438980  Cd Length: 122  Bit Score: 38.45  E-value: 2.26e-03
                          10
                  ....*....|....*...
gi 1884086654 319 GSIIWAKQYGYPWWPGMI 336
Cdd:cd20152    23 GDIVWAKIYGFPWWPARI 40
PWWP_ScIOC4-like cd05840
PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar ...
319-379 2.75e-03

PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar proteins; ScIOC4 functions as a component of the ISW1B complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW1B complex acts within coding regions to control the amount of RNA polymerase II released into productive elongation and to coordinate elongation with termination and pre-mRNA processing. The family also includes Schizosaccharomyces pombe PWWP domain-containing proteins 1 and 2 (SpPDP1 and SpPDP2). SpPDP1 associates with Set9 to regulate its chromatin localization and methyltransferase activity towards H4K20. Members of this family contain a PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438965  Cd Length: 94  Bit Score: 37.28  E-value: 2.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1884086654 319 GSIIWAKQYGYPWWPGMIESDPDLGEYFLFTSHL--DSLPSKYHVTFFGETvSRAWIPVNMLK 379
Cdd:cd05840     1 GDLVLAKVKGYPPWPAMVLPEELLPKNVLKAKKRkpKSKKTVYPVQFFPDN-EYYWVSPSSLK 62
PWWP_MBD5 cd20141
PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is ...
318-412 8.73e-03

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: 36.14  E-value: 8.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1884086654 318 PGSIIWAKQYGYPWWPGMIESDPDLGEyflftshldSLPSKYHVTFFGeTVSRAWIPVNMLKNFQE-LSLELSVMKKRRN 396
Cdd:cd20141     3 VGDLVWGQIRGFPSWPGKLVSENDVGK---------TNEGKVWVSWFG-DHSFGQVEPDKLKTLSEgLEAHHRARKRTRK 72
                          90
                  ....*....|....*..
gi 1884086654 397 dcSQKLGVALMMA-QEA 412
Cdd:cd20141    73 --GRKLNNHLEAAiQEA 87
PWWP_NSD_rpt2 cd05838
second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
319-365 9.01e-03

second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein family consists of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising in suppressing cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play nonredundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (C5HCH). This model corresponds to the second PWWP domain. The family also includes Drosophila melanogaster maternal-effect sterile 4 (dMes4) that may act as a histone-lysine N-methyltransferase required for wing morphogenesis. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438963 [Multi-domain]  Cd Length: 96  Bit Score: 36.06  E-value: 9.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1884086654 319 GSIIWAKQYGYPWWPGMIesdpdlgeyfLFTSHL-DSLPSKYH------VTFFG 365
Cdd:cd05838     3 GDIVWVKLGNYRWWPAEI----------LHPREVpDNIQSLPHppgefpVRFFG 46
 
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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