NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|374107812|gb|AEY96719|]
View 

FAEL263Cp [Eremothecium gossypii FDAG1]

Protein Classification

PWWP_ScIOC4-like domain-containing protein( domain architecture ID 10146972)

PWWP_ScIOC4-like domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 9-97 8.56e-32

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: 114.32  E-value: 8.56e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374107812   9 GDRVLCKVGDFPPWPAVVVPQR-----FLSKLVYSGKRSKSYVCVAFFNDDSYYWKEPRHLTLLTDKMCTDWMKNSKSKD 83
Cdd:cd05840    1 GDLVLAKVKGYPPWPAMVLPEEllpknVLKAKKRKPKSKKTVYPVQFFPDNEYYWVSPSSLKPLTKEEIDKFLSKSKRKN 80

                         90
                 ....*....|....
gi 374107812  84 EALIGAYQQAIEYK 97
Cdd:cd05840   81 KDLIEAYEVALEPP 94
 
Name Accession Description Interval E-value
PWWP_ScIOC4-like cd05840
PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar ...
 9-97 8.56e-32

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: 114.32  E-value: 8.56e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374107812   9 GDRVLCKVGDFPPWPAVVVPQR-----FLSKLVYSGKRSKSYVCVAFFNDDSYYWKEPRHLTLLTDKMCTDWMKNSKSKD 83
Cdd:cd05840    1 GDLVLAKVKGYPPWPAMVLPEEllpknVLKAKKRKPKSKKTVYPVQFFPDNEYYWVSPSSLKPLTKEEIDKFLSKSKRKN 80

                         90
                 ....*....|....
gi 374107812  84 EALIGAYQQAIEYK 97
Cdd:cd05840   81 KDLIEAYEVALEPP 94
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 9-96 1.17e-21

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: 87.48  E-value: 1.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374107812    9 GDRVLCKVGDFPPWPAVVVPQRFLSKLVYSGKRSKSYVCVAFFNDDSYYWKEPRHLTLLTDKMCTDWMK--NSKSKDEAL 86
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVVDPEELPENVLKPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEFEYLKkkKKKKKKKAF 80

                          90
                  ....*....|
gi 374107812   87 IGAYQQAIEY 96
Cdd:pfam00855  81 KKALEEAEEA 90
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 6-68 4.15e-11

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 57.74  E-value: 4.15e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374107812     6 IRTGDRVLCKVGDFPPWPAVVVPQRFLSKLVYSGKRSKSYVCVAFFNDDSYYWKEPRHLTLLT 68
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISPKMTPDNIMKRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
 
Name Accession Description Interval E-value
PWWP_ScIOC4-like cd05840
PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar ...
 9-97 8.56e-32

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: 114.32  E-value: 8.56e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374107812   9 GDRVLCKVGDFPPWPAVVVPQR-----FLSKLVYSGKRSKSYVCVAFFNDDSYYWKEPRHLTLLTDKMCTDWMKNSKSKD 83
Cdd:cd05840    1 GDLVLAKVKGYPPWPAMVLPEEllpknVLKAKKRKPKSKKTVYPVQFFPDNEYYWVSPSSLKPLTKEEIDKFLSKSKRKN 80

                         90
                 ....*....|....
gi 374107812  84 EALIGAYQQAIEYK 97
Cdd:cd05840   81 KDLIEAYEVALEPP 94
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 9-96 1.17e-21

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: 87.48  E-value: 1.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374107812    9 GDRVLCKVGDFPPWPAVVVPQRFLSKLVYSGKRSKSYVCVAFFNDDSYYWKEPRHLTLLTDKMCTDWMK--NSKSKDEAL 86
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVVDPEELPENVLKPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEFEYLKkkKKKKKKKAF 80

                          90
                  ....*....|
gi 374107812   87 IGAYQQAIEY 96
Cdd:pfam00855  81 KKALEEAEEA 90
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
 9-96 4.75e-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: 60.97  E-value: 4.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374107812   9 GDRVLCKVGDFPPWPAVVVPQRFLSKLVYSgKRSKSYVCVAFFNDDSYYWKEPRHLTLLTDKMCTDwMKNSKSKDEALIG 88
Cdd:cd05162    1 GDLVWAKLKGYPWWPARVVDPEELPEEVGK-KKKKGGVLVQFFGDNDYAWVKSKNIKPFEEGFKKE-FKKKKKKSKKFKK 78


                 ....*...
gi 374107812  89 AYQQAIEY 96
Cdd:cd05162   79 AVEEAEEA 86
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 6-68 4.15e-11

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 57.74  E-value: 4.15e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374107812     6 IRTGDRVLCKVGDFPPWPAVVVPQRFLSKLVYSGKRSKSYVCVAFFNDDSYYWKEPRHLTLLT 68
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISPKMTPDNIMKRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
PWWP_AtATX3-like cd20143
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
 9-95 1.47e-07

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: 48.90  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374107812   9 GDRVLCKVGDFPPWPAVVV-PQRFLSKLVYSGKrsKSYVCVAFF---NDDSYYWKEPRHLTLLTDKMctDWMKNSKSKDE 84
Cdd:cd20143    3 GDLVWAKVGTHPFWPARVVePAEQAEEVRRRCV--PGSLCVYFFgpgGSRDYGWVRRSMIFPFTDDL--ARFQTQKIKNK 78

                         90
                 ....*....|.
gi 374107812  85 ALIGAYQQAIE 95
Cdd:cd20143   79 KRPQEFQEALE 89
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 9-95 4.10e-05

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: 41.44  E-value: 4.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374107812   9 GDRVLCKVGDFPPWPA-VVVPqrflSKLVYSGKRSKSYVCVAFFNDDSYYWKEPRHLTLLTDKMcTDWMKNSKSKdeali 87
Cdd:cd05836    4 GDLVWAKMKGFPPWPGkIVNP----PPDLKKPPRKKKMHCVYFFGSENYAWIEDENIKPYEEFK-EEMLKSKKSA----- 73


                 ....*...
gi 374107812  88 gAYQQAIE 95
Cdd:cd05836   74 -GFKDAVE 80
PWWP_NSD_rpt2 cd05838
second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 9-100 7.91e-05

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: 41.07  E-value: 7.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374107812   9 GDRVLCKVGDFPPWPAVVVPQRFLSKLVYSGKRSKSYVCVAFFNDDSYYWKEPRHLTLLT--DKMCTDwmKNSKSKDEAL 86
Cdd:cd05838    3 GDIVWVKLGNYRWWPAEILHPREVPDNIQSLPHPPGEFPVRFFGSHDYYWVHRGRVFLFEegDKGSKE--KSKKSLDKSF 80

                         90
                 ....*....|....
gi 374107812  87 IGAYQQAIEYKRLF 100
Cdd:cd05838   81 KRALKEANEAFREL 94
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH