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Conserved domains on  [gi|528061693|gb|EPX71257|]
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PWWP domain-containing protein [Schizosaccharomyces octosporus yFS286]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PWWP_ScIOC4-like cd05840
PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar ...
 143-233 1.51e-30

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: 114.71  E-value: 1.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528061693 143 GMRVLTKLAGFPWWPSMIITEDKMTSVAL---KSKPKRAENYHPVIFFPNKEYLWASPDALSPLSEDAISEYLEKPKPKT 219
Cdd:cd05840    1 GDLVLAKVKGYPPWPAMVLPEELLPKNVLkakKRKPKSKKTVYPVQFFPDNEYYWVSPSSLKPLTKEEIDKFLSKSKRKN 80

                         90
                 ....*....|....
gi 528061693 220 ASLIKAYKVAQATK 233
Cdd:cd05840   81 KDLIEAYEVALEPP 94
LGT super family cl00478
Prolipoprotein diacylglyceryl transferase;
10-134 1.59e-03

Prolipoprotein diacylglyceryl transferase;


The actual alignment was detected with superfamily member PRK13108:

Pssm-ID: 469786 [Multi-domain]  Cd Length: 460  Bit Score: 41.12  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528061693  10 DSVVEDKKETPNQVSEETTekpetnevedAQEKKANDSEFQQTAEvKPEEAPEQNgTSTEEKEPTTAE--EEPKENGTVE 87
Cdd:PRK13108 327 DDVAEAVKAEVAEVTDEVA----------AESVVQVADRDGESTP-AVEETSEAD-IEREQPGDLAGQapAAHQVDAEAA 394

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 528061693  88 KEEDAEIKDQeekPSEDSKTEESTEKQKSEGTPKSAVKNTTKQKGGE 134
Cdd:PRK13108 395 SAAPEEPAAL---ASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPG 438
LGT super family cl00478
Prolipoprotein diacylglyceryl transferase;
459-578 5.55e-03

Prolipoprotein diacylglyceryl transferase;


The actual alignment was detected with superfamily member PRK13108:

Pssm-ID: 469786 [Multi-domain]  Cd Length: 460  Bit Score: 39.58  E-value: 5.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528061693 459 PAEQEESIKKICHELLEDKWKPIMQAISQQKQSSGETKS---ETPEPTAEQAEETKSVEGNDAVEKKVETEESKEPSQDL 535
Cdd:PRK13108 323 PNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPaveETSEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPA 402

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 528061693 536 DEKVEnEPESNEKSESETTESKDTPMTDATPSTTE-ASAPADSE 578
Cdd:PRK13108 403 ALASE-AHDETEPEVPEKAAPIPDPAKPDELAVAGpGDDPAEPD 445
 
Name Accession Description Interval E-value
PWWP_ScIOC4-like cd05840
PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar ...
 143-233 1.51e-30

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: 114.71  E-value: 1.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528061693 143 GMRVLTKLAGFPWWPSMIITEDKMTSVAL---KSKPKRAENYHPVIFFPNKEYLWASPDALSPLSEDAISEYLEKPKPKT 219
Cdd:cd05840    1 GDLVLAKVKGYPPWPAMVLPEELLPKNVLkakKRKPKSKKTVYPVQFFPDNEYYWVSPSSLKPLTKEEIDKFLSKSKRKN 80

                         90
                 ....*....|....
gi 528061693 220 ASLIKAYKVAQATK 233
Cdd:cd05840   81 KDLIEAYEVALEPP 94
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 140-204 1.58e-20

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 85.47  E-value: 1.58e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528061693   140 YKPGMRVLTKLAGFPWWPSMIITEdKMTSVALKsKPKRAENYHPVIFFPNKEYLWASPDALSPLS 204
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISP-KMTPDNIM-KRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 143-231 1.75e-18

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: 80.55  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528061693  143 GMRVLTKLAGFPWWPSMIItEDKMTSVALKSKPKRAENYHpVIFFPNKEYLWASPDALSPLSEDAISEYLEKPKPKTA-- 220
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVV-DPEELPENVLKPKKKDGEYL-VRFFGDSEFAWVKPKDLKPFDEGDEFEYLKKKKKKKKkk 78

                          90
                  ....*....|.
gi 528061693  221 SLIKAYKVAQA 231
Cdd:pfam00855  79 AFKKALEEAEE 89
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 10-134 1.59e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 41.12  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528061693  10 DSVVEDKKETPNQVSEETTekpetnevedAQEKKANDSEFQQTAEvKPEEAPEQNgTSTEEKEPTTAE--EEPKENGTVE 87
Cdd:PRK13108 327 DDVAEAVKAEVAEVTDEVA----------AESVVQVADRDGESTP-AVEETSEAD-IEREQPGDLAGQapAAHQVDAEAA 394

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 528061693  88 KEEDAEIKDQeekPSEDSKTEESTEKQKSEGTPKSAVKNTTKQKGGE 134
Cdd:PRK13108 395 SAAPEEPAAL---ASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPG 438
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 459-578 5.55e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 39.58  E-value: 5.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528061693 459 PAEQEESIKKICHELLEDKWKPIMQAISQQKQSSGETKS---ETPEPTAEQAEETKSVEGNDAVEKKVETEESKEPSQDL 535
Cdd:PRK13108 323 PNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPaveETSEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPA 402

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 528061693 536 DEKVEnEPESNEKSESETTESKDTPMTDATPSTTE-ASAPADSE 578
Cdd:PRK13108 403 ALASE-AHDETEPEVPEKAAPIPDPAKPDELAVAGpGDDPAEPD 445
 
Name Accession Description Interval E-value
PWWP_ScIOC4-like cd05840
PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar ...
 143-233 1.51e-30

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: 114.71  E-value: 1.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528061693 143 GMRVLTKLAGFPWWPSMIITEDKMTSVAL---KSKPKRAENYHPVIFFPNKEYLWASPDALSPLSEDAISEYLEKPKPKT 219
Cdd:cd05840    1 GDLVLAKVKGYPPWPAMVLPEELLPKNVLkakKRKPKSKKTVYPVQFFPDNEYYWVSPSSLKPLTKEEIDKFLSKSKRKN 80

                         90
                 ....*....|....
gi 528061693 220 ASLIKAYKVAQATK 233
Cdd:cd05840   81 KDLIEAYEVALEPP 94
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 140-204 1.58e-20

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 85.47  E-value: 1.58e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528061693   140 YKPGMRVLTKLAGFPWWPSMIITEdKMTSVALKsKPKRAENYHPVIFFPNKEYLWASPDALSPLS 204
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISP-KMTPDNIM-KRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 143-231 1.75e-18

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: 80.55  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528061693  143 GMRVLTKLAGFPWWPSMIItEDKMTSVALKSKPKRAENYHpVIFFPNKEYLWASPDALSPLSEDAISEYLEKPKPKTA-- 220
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVV-DPEELPENVLKPKKKDGEYL-VRFFGDSEFAWVKPKDLKPFDEGDEFEYLKKKKKKKKkk 78

                          90
                  ....*....|.
gi 528061693  221 SLIKAYKVAQA 231
Cdd:pfam00855  79 AFKKALEEAEE 89
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
 143-231 2.31e-12

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: 62.90  E-value: 2.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528061693 143 GMRVLTKLAGFPWWPSMIITEDkmtSVALKSKPKRAENYHPVIFFPNKEYLWASPDALSPLSEDAIsEYLEKPKPKTASL 222
Cdd:cd05162    1 GDLVWAKLKGYPWWPARVVDPE---ELPEEVGKKKKKGGVLVQFFGDNDYAWVKSKNIKPFEEGFK-KEFKKKKKKSKKF 76


                 ....*....
gi 528061693 223 IKAYKVAQA 231
Cdd:cd05162   77 KKAVEEAEE 85
PWWP_BRPF cd05839
PWWP domain found in the bromodomain and PHD finger-containing (BRPF) protein family; The BRPF ...
 140-229 8.89e-06

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: 44.95  E-value: 8.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528061693 140 YKPGMRVLTKLAGFPWWPSMIITEDKMTS--------VALKSKPKRAENYHPVIFFPNKE-YLWASPDALSPLSEDA--- 207
Cdd:cd05839    1 LEPGDLVWAKCRGYPWYPAEIVDPKDPKEgngvpipvPPDRVLKKSNEKLYLVLFFDAKRtWGWLPRNKLRPLGVDEeld 80

                         90       100
                 ....*....|....*....|...
gi 528061693 208 ISEYLEKPKPK-TASLIKAYKVA 229
Cdd:cd05839   81 KLKLSEAKKSKrRKEVRKAYERA 103
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 140-218 2.78e-04

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: 39.90  E-value: 2.78e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528061693 140 YKPGMRVLTKLAGFPWWPSMIITEDKmtsvALKsKPKRAENYHPVIFFPNKEYLWASPDALSPLSEDAiSEYLEKPKPK 218
Cdd:cd05836    1 FKIGDLVWAKMKGFPPWPGKIVNPPP----DLK-KPPRKKKMHCVYFFGSENYAWIEDENIKPYEEFK-EEMLKSKKSA 73
PWWP_HRP cd05834
PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The ...
 140-218 3.31e-04

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: 39.46  E-value: 3.31e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528061693 140 YKPGMRVLTKLAGFPWWPSMIiteDKMTSVALKSKPKraenyHPVIFFPNKEYLWASPDALSPLSEDAisEYLEKPKPK 218
Cdd:cd05834    1 FKPGDLVFAKVKGYPPWPARI---DEIPEGAKIPKNK-----YPVFFYGTHETAFLKPKDLFPYEENK--EKYGKPRKR 69
PWWP_AtATX1-like cd20142
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
 142-216 8.25e-04

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: 38.87  E-value: 8.25e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528061693 142 PGMRVLTKLAGFPWWPSMIITEDKMTSVALKSKPKRAENYHPVIFFPNKEYLWASPDALSPLSEDAISEYLEKPK 216
Cdd:cd20142    2 PGDVVWAKVKGYPMWPALVIDEEHAERCGLEANRPGKKGTVPVQFFGTYEVARLNPKKVVGFSKGLDLKYHSKCK 76
PWWP_HULK cd20147
PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family ...
 146-220 1.46e-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: 38.24  E-value: 1.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528061693 146 VLTKLAGFPWWPSMIitedkmtSVALKSKPKRAENYHPVIFFPNKEYLWASPDALSPLSEDAISEYLEKPKPKTA 220
Cdd:cd20147    4 VLAKVKGFPAWPAQV-------SEPEDWGSAPDPKKVFVHFFGTQQIGFCNPGELSEFTEEIKQSLLARTLKKKK 71
PWWP_HDGFL2 cd20149
PWWP domain found in Hepatoma-derived growth factor-related protein 2 (HDGFL2); HDGFL2, also ...
 140-202 1.55e-03

PWWP domain found in Hepatoma-derived growth factor-related protein 2 (HDGFL2); 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. It contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438977 [Multi-domain]  Cd Length: 84  Bit Score: 37.96  E-value: 1.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528061693 140 YKPGMRVLTKLAGFPWWPSMIiteDKMTSVALKSKPkraeNYHPVIFFPNKEYLWASPDALSP 202
Cdd:cd20149    1 FKPGDLVFAKMKGYPHWPARI---DDIADGAVKPPP----NKYPIFFFGTHETAFLGPKDLFP 56
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 10-134 1.59e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 41.12  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528061693  10 DSVVEDKKETPNQVSEETTekpetnevedAQEKKANDSEFQQTAEvKPEEAPEQNgTSTEEKEPTTAE--EEPKENGTVE 87
Cdd:PRK13108 327 DDVAEAVKAEVAEVTDEVA----------AESVVQVADRDGESTP-AVEETSEAD-IEREQPGDLAGQapAAHQVDAEAA 394

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 528061693  88 KEEDAEIKDQeekPSEDSKTEESTEKQKSEGTPKSAVKNTTKQKGGE 134
Cdd:PRK13108 395 SAAPEEPAAL---ASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPG 438
PWWP_NSD2_rpt1 cd20162
first PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins; ...
 140-221 3.72e-03

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: 37.97  E-value: 3.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528061693 140 YKPGMRVLTKLAGFPWWPSMIITEDKMTS-VALKSKPKRAENYHPVIFFPNKEYLWASPDALSPLSEDAISEYLEKPKPK 218
Cdd:cd20162    1 YNVGDLVWSKVSGYPWWPCMVSADPLLHShTKLKGQKKSARQYHVQFFGDAPERAWIFEKSLVPFEGEGQFEQLCQESAK 80


                 ...
gi 528061693 219 TAS 221
Cdd:cd20162   81 QAP 83
PWWP_NSD_rpt1 cd20144
first PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 148-234 3.86e-03

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: 37.29  E-value: 3.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528061693 148 TKLAGFPWWPSMiITED-------KMtsvalKSKPKRAEN-YHpVIFF-PNKEYLWASPDALSP-LSEDAISEYLEKPKP 217
Cdd:cd20144    7 AKVSGHPWWPCM-VTYDpesglytKI-----KGSGGRTYRqYH-VQFFgDNGERGWVSEKSLMPfEGKEKFEELVKELKK 79

                         90
                 ....*....|....*..
gi 528061693 218 KTASLIKAYKVAQATKS 234
Cdd:cd20144   80 KAKKKSKKAKLEKKVKP 96
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 4-123 4.21e-03

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 40.15  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528061693    4 ESLEEN--DSVVEDKKETPNQVSEETTEKPETNEVEDAQEkkaNDSEFQQTAEVKPEEAPEQNGTSTEEKEPTTAEEEPK 81
Cdd:PTZ00341 1001 ENIEENveENVEENIEENVEEYDEENVEEVEENVEEYDEE---NVEEIEENAEENVEENIEENIEEYDEENVEEIEENIE 1077

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 528061693   82 ENGTVEKEEDAEIKDQEEKPSEDSKTEESTEKQKSEGTPKSA 123
Cdd:PTZ00341 1078 ENIEENVEENVEENVEEIEENVEENVEENAEENAEENAEENA 1119
PWWP_HDGF cd20148
PWWP domain found in Hepatoma-derived growth factor (HDGF); HDGF, also called high mobility ...
 140-205 4.76e-03

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: 36.54  E-value: 4.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528061693 140 YKPGMRVLTKLAGFPWWPSMIiteDKMTSVALKSkpkrAENYHPVIFFPNKEYLWASPDALSPLSE 205
Cdd:cd20148    1 YKCGDLVFAKMKGYPHWPARI---DEMPEAAVKS----TANKYQVFFFGTHETAFLGPKDLFPYEE 59
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 53-179 5.50e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 39.67  E-value: 5.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528061693  53 AEVKPEEAPEQNGTSTEEKEPTTAEEEPKENGTVEKEEDAEIKDQ-----EEKPSED---SKTEESTEKQKSEGTPKSAv 124
Cdd:PTZ00449 516 ASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKpgpakEHKPSKIptlSKKPEFPKDPKHPKDPEEP- 594

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528061693 125 KNTTKQKGGEKPTTDYKPGMRVLTKLAGFPWWPSMIITEDKMTSVALKSKPKRAE 179
Cdd:PTZ00449 595 KKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSPERPE 649
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 459-578 5.55e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 39.58  E-value: 5.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528061693 459 PAEQEESIKKICHELLEDKWKPIMQAISQQKQSSGETKS---ETPEPTAEQAEETKSVEGNDAVEKKVETEESKEPSQDL 535
Cdd:PRK13108 323 PNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPaveETSEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPA 402

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 528061693 536 DEKVEnEPESNEKSESETTESKDTPMTDATPSTTE-ASAPADSE 578
Cdd:PRK13108 403 ALASE-AHDETEPEVPEKAAPIPDPAKPDELAVAGpGDDPAEPD 445
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 496-590 5.79e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 39.58  E-value: 5.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528061693 496 KSETPEPTAEQAEETKSVEGNDAVEKKVETEESKEP------SQDLDEKVENEPESNEKSESET-TESKDTPMTD---AT 565
Cdd:PRK13108 334 KAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEAdiereqPGDLAGQAPAAHQVDAEAASAApEEPAALASEAhdeTE 413

                         90       100
                 ....*....|....*....|....*.
gi 528061693 566 PSTTEASAP-ADSEKPTEEQKEEPSA 590
Cdd:PRK13108 414 PEVPEKAAPiPDPAKPDELAVAGPGD 439
PWWP_ZCWPW1 cd20145
PWWP domain found in zinc finger CW-type PWWP domain protein 1 (ZCWPW1) and similar proteins; ...
 138-236 5.83e-03

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: 36.76  E-value: 5.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528061693 138 TDYKPGMRVLTKLAGFPWWPSMI----ITEDKMTSVALKSKPKRaenYHpVIFFpNKE--YLWASPDALSPLSEDaiSEY 211
Cdd:cd20145    4 TKYTPGSLVWAKMPGYPWWPAMVeddpDTEEFFWLDEESDIPTK---YH-VTFF-DKPvsRAWVRASSIKPFTDN--SNE 76

                         90       100
                 ....*....|....*....|....*..
gi 528061693 212 LEKPKPKTASLIKAYKVA--QATKSLE 236
Cdd:cd20145   77 PNLTKKKGKKYKKRLNEAveMAREALK 103
PWWP_PSIP cd20151
PWWP domain found in PC4 and SFRS1-interacting protein (PSIP); PSIP, also called ...
 140-206 7.25e-03

PWWP domain found in PC4 and SFRS1-interacting protein (PSIP); 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. It contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438979 [Multi-domain]  Cd Length: 88  Bit Score: 36.12  E-value: 7.25e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528061693 140 YKPGMRVLTKLAGFPWWPSMIiteDKMTSVALKSkpkrAENYHPVIFFPNKEYLWASPDALSPLSED 206
Cdd:cd20151    1 FKPGDLIFAKMKGYPHWPARV---DEVPDGAVKP----PTNKLPIFFFGTHETAFLGPKDIFPYSEN 60
 
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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