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Conserved domains on  [gi|292621054|ref|XP_683890|]
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histone-lysine N-methyltransferase, H3 lysine-36 specific [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SET super family cl40432
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
1624-1765 1.61e-97

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, Enhancer-of-zeste, Trithorax (SET) domain superfamily corresponds to SET domain-containing lysine methyltransferases, which catalyze site and state-specific methylation of lysine residues in histones that are fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains has been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as N-SET and C-SET. C-SET forms an unusual and conserved knot-like structure of probable functional importance. In addition to N-SET and C-SET, an insert region (I-SET) and flanking regions of high structural variability form part of the overall structure. Some family members contain a pre-SET domain, which is found in a number of histone methyltransferases (HMTase), and a post-SET domain, which harbors a zinc-binding site.


The actual alignment was detected with superfamily member cd19210:

Pssm-ID: 394802 [Multi-domain]  Cd Length: 142  Bit Score: 309.94  E-value: 1.61e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1624 YTEVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICNFYMLTLDKDRIIDAGPKGNESRFMN 1703
Cdd:cd19210     1 YPEVEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMN 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 292621054 1704 HSCQPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYNLECLGNGKTVCKCGAPNCSGFLG 1765
Cdd:cd19210    81 HCCQPNCETQKWTVNGDTRVGLFALCDIKAGTELTFNYNLECLGNGKTVCKCGAPNCSGFLG 142
PWWP_NSD1_rpt1 cd20161
first PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and ...
283-398 5.02e-69

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: 227.36  E-value: 5.02e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054  283 SVKYSIGDVVWAKFNRRPWWPCHVTTDPQIDVHTKMKDPSRRPCRLYFVRMFGEIVDQAWVPAKATFPFEGGDQFEKLPV 362
Cdd:cd20161     1 PVKYEVGDLVWAKFSRRPWWPCRICADPLLDTHSKMKVPSRRPCRQYYVETLGELTEKAWVAAKAVVPFEGRHQFEELPV 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 292621054  363 LRRRGRQKEKDYKYTVPKRLIPSWKASVLEAEASLT 398
Cdd:cd20161    81 LRRRGKQKEKDYKHKIPQKLLSLWEASVAHAEDFLS 116
PWWP super family cl02554
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
1438-1531 1.04e-58

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.


The actual alignment was detected with superfamily member cd20164:

Pssm-ID: 470613  Cd Length: 96  Bit Score: 197.02  E-value: 1.04e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1438 HYKDILWVKVGRYRWWPAEVTQPKSVPENISRMKHEVGEFPVHFFGSKDYVWTYQARCFPYMEGDANNKEKMGKGADAVY 1517
Cdd:cd20164     1 HYKEVVWVKVGRYRWWPAEVCHPKSIPTNIQKMKHDIGEFPVLFFGSNDYLWTHQARVFPYMEGDVSSKDKMGKGVDGTY 80
                          90
                  ....*....|....
gi 292621054 1518 KKALNEAADRFREL 1531
Cdd:cd20164    81 KKALQEAAVRFEEL 94
PHD3_NSD1 cd15653
PHD finger 3 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...
1322-1375 3.49e-30

PHD finger 3 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or 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 (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the third PHD finger.


:

Pssm-ID: 277123  Cd Length: 54  Bit Score: 114.25  E-value: 3.49e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 292621054 1322 VCLSCYITNPNNPGISKGRLTRCVRCPVAYHANDYCMAAGSVPLANNSFLCPNH 1375
Cdd:cd15653     1 ICLTCHATNPSNPSASKGRLMRCVRCPVAYHANDFCLAAGSVILASNSIICPNH 54
PHD5_NSD1 cd15659
PHD finger 5 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...
1802-1844 1.17e-26

PHD finger 5 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or 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 (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fifth PHD finger.


:

Pssm-ID: 277129  Cd Length: 43  Bit Score: 103.87  E-value: 1.17e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292621054 1802 ECFYCGDGGQIVSCKKPGCPKVYHADCLNLSKRPAGRWECPWH 1844
Cdd:cd15659     1 ECFSCGDGGQLVSCKKPGCPKVYHADCLNLTKRPAGKWECPWH 43
PHD_SF super family cl22851
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
1275-1321 1.08e-25

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


The actual alignment was detected with superfamily member cd15650:

Pssm-ID: 473978  Cd Length: 47  Bit Score: 101.12  E-value: 1.08e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 292621054 1275 TCFVCKKPDKEVRRCMIPVCGKFYHMDCILKYSPTVAQNRGFRCSIH 1321
Cdd:cd15650     1 TCFVCKKSDEDVRRCMLPLCGKFYHEECVLKYPPTVMQNRGFRCSLH 47
PHD1_NSD1_2 cd15648
PHD finger 1 found in nuclear receptor-binding SET domain-containing protein NSD1 and NSD2; ...
1228-1270 3.69e-23

PHD finger 1 found in nuclear receptor-binding SET domain-containing protein NSD1 and NSD2; NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or 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). NSD2, also termed histone-lysine N-methyltransferase NSD2, or 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, by 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). Both NSD1 and NSD2 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 (Cys5HisCysHis). In addition, NSD2 harbors a high mobility group (HMG) box. The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD fingers mediate chromatin interaction and recognition of histone marks. This model corresponds to the first PHD finger.


:

Pssm-ID: 277118  Cd Length: 43  Bit Score: 93.69  E-value: 3.69e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292621054 1228 VCQVCEKTGELLLCEGQCCGAFHLQCIGLTETPKGRFICQECK 1270
Cdd:cd15648     1 VCQVCEKPGELLLCEGQCCGAFHLDCIGLSEMPSGKFICDECI 43
PHD4_NSD1 cd15656
PHD finger 4 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...
1392-1431 6.92e-21

PHD finger 4 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or 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 (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fourth PHD finger.


:

Pssm-ID: 277126  Cd Length: 40  Bit Score: 87.38  E-value: 6.92e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 292621054 1392 WCFVCSEGGSLLCCESCPAAFHRECLNIEMPQGSWFCNDC 1431
Cdd:cd15656     1 WCFVCSEGGSLLCCESCPAAFHRECLNIDMPEGSWYCNDC 40
C5HCH pfam17982
NSD Cys-His rich domain; This is an NSD-specific Cys-His rich region (C5HCH) domain. Family ...
1843-1892 4.04e-18

NSD Cys-His rich domain; This is an NSD-specific Cys-His rich region (C5HCH) domain. Family members include NSD3 (nuclear receptor SET domain-containing) proteins. This domain is located on the C-terminal of NSD1, 2 and 3 proteins. C5HCH domain lies adjacent to the fifth plant homeodomain (PHD5). The PHD5-C5HCH module of NSD3 (PHD5-C5HCHNSD3) recognizes the H3 N-terminal peptide containing unmodified K4 and trimethylated K9. Moreover, it has been reported that the PHD5-C5HCH module of NSD1 (PHD5-C5HCH) was the sole region required for tight binding of the NUP98-NSD1 fusion protein to the HoxA9 gene promoter, implicating that PHD5-C5HCH might have chromatin targeting ability.


:

Pssm-ID: 465605  Cd Length: 50  Bit Score: 79.82  E-value: 4.04e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 292621054  1843 WHQCNECGREAASYCEMCPNSYCEQHREGMLFISKLDGKLSCSEHDPCGP 1892
Cdd:pfam17982    1 WHQCSVCGSPATSFCEFCPSSFCKDHEKGALVPSALEGRLCCSEHDPESP 50
AWS super family cl39039
AWS domain; This entry represents the AWS (associated with SET domain) domain. This is a zinc ...
1584-1622 5.94e-13

AWS domain; This entry represents the AWS (associated with SET domain) domain. This is a zinc binding domain. The full AWS domain contains 8 cysteines. This entry represents the N-terminal part of the domain, with the C-terminal part interwoven with the SET domain.


The actual alignment was detected with superfamily member pfam17907:

Pssm-ID: 465559  Cd Length: 39  Bit Score: 64.75  E-value: 5.94e-13
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 292621054  1584 DENPCGIDSECINRMLLYECHSQVCPAGERCQNQSFTKR 1622
Cdd:pfam17907    1 DDPPCGCGSDCINRMLFVECTPKTCPCGESCQNQRFQRK 39
TNG2 super family cl34876
Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];
1108-1270 1.94e-03

Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];


The actual alignment was detected with superfamily member COG5034:

Pssm-ID: 227367 [Multi-domain]  Cd Length: 271  Bit Score: 42.23  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1108 RQHKTNPEESGVRDLEKqEEAGPPPSSPCAVSAQSEGElRTSSPIQPDVPSVSQIPVEGEQSSPSKPQINNEDSLISEGF 1187
Cdd:COG5034    97 RRHRKLLDDRIAKRPHE-KVAARIENCHDAVSRLERNS-YSSAARRSSGEHRSAASSQGSRHTKLKKRKNIHNLKRRSPE 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1188 AAGLNDSAFSsrdsLSGDLSGLSTNKRSVERGGGASLKENVCQVCEKTGELLLCEGQ---------CCGA------FHLQ 1252
Cdd:COG5034   175 LSSKREVSFT----LESPSVPDTATRVKEGNNGGSTKSRGVSSEDNSEGEELYCFCQqvsygqmvaCDNAnckrewFHLE 250
                         170
                  ....*....|....*...
gi 292621054 1253 CIGLTETPKGRFICQECK 1270
Cdd:COG5034   251 CVGLKEPPKGKWYCPECK 268
 
Name Accession Description Interval E-value
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
1624-1765 1.61e-97

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and similar proteins; NSD1 (EC 2.1.1.43; also termed Histone-lysine N-methyltransferase H3 lysine-36 and H4 lysine-20 specific, androgen receptor coactivator 267 kDa protein (ARA267), 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 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4. NSD1 is altered in approximately 10% of head and neck cancer patients with 55% decrease in risk of death in NSD1-mutated versus non-mutated patients; its disruption promotes favorable chemotherapeutic responses linked to hypomethylation.


Pssm-ID: 380987 [Multi-domain]  Cd Length: 142  Bit Score: 309.94  E-value: 1.61e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1624 YTEVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICNFYMLTLDKDRIIDAGPKGNESRFMN 1703
Cdd:cd19210     1 YPEVEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMN 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 292621054 1704 HSCQPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYNLECLGNGKTVCKCGAPNCSGFLG 1765
Cdd:cd19210    81 HCCQPNCETQKWTVNGDTRVGLFALCDIKAGTELTFNYNLECLGNGKTVCKCGAPNCSGFLG 142
PWWP_NSD1_rpt1 cd20161
first PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and ...
283-398 5.02e-69

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: 227.36  E-value: 5.02e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054  283 SVKYSIGDVVWAKFNRRPWWPCHVTTDPQIDVHTKMKDPSRRPCRLYFVRMFGEIVDQAWVPAKATFPFEGGDQFEKLPV 362
Cdd:cd20161     1 PVKYEVGDLVWAKFSRRPWWPCRICADPLLDTHSKMKVPSRRPCRQYYVETLGELTEKAWVAAKAVVPFEGRHQFEELPV 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 292621054  363 LRRRGRQKEKDYKYTVPKRLIPSWKASVLEAEASLT 398
Cdd:cd20161    81 LRRRGKQKEKDYKHKIPQKLLSLWEASVAHAEDFLS 116
PWWP_NSD1_rpt2 cd20164
second PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) ...
1438-1531 1.04e-58

second 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. This model corresponds to the second PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438992  Cd Length: 96  Bit Score: 197.02  E-value: 1.04e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1438 HYKDILWVKVGRYRWWPAEVTQPKSVPENISRMKHEVGEFPVHFFGSKDYVWTYQARCFPYMEGDANNKEKMGKGADAVY 1517
Cdd:cd20164     1 HYKEVVWVKVGRYRWWPAEVCHPKSIPTNIQKMKHDIGEFPVLFFGSNDYLWTHQARVFPYMEGDVSSKDKMGKGVDGTY 80
                          90
                  ....*....|....
gi 292621054 1518 KKALNEAADRFREL 1531
Cdd:cd20164    81 KKALQEAAVRFEEL 94
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
1626-1748 2.14e-44

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on outlier plant homologues


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 157.11  E-value: 2.14e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054   1626 EVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICNFYMLTLDKDRIIDAGPKGNESRFMNHS 1705
Cdd:smart00317    2 KLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAKAFYLFDIDSDLCIDARRKGNLARFINHS 81
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 292621054   1706 CQPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYNLECLGN 1748
Cdd:smart00317   82 CEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
PHD3_NSD1 cd15653
PHD finger 3 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...
1322-1375 3.49e-30

PHD finger 3 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or 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 (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the third PHD finger.


Pssm-ID: 277123  Cd Length: 54  Bit Score: 114.25  E-value: 3.49e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 292621054 1322 VCLSCYITNPNNPGISKGRLTRCVRCPVAYHANDYCMAAGSVPLANNSFLCPNH 1375
Cdd:cd15653     1 ICLTCHATNPSNPSASKGRLMRCVRCPVAYHANDFCLAAGSVILASNSIICPNH 54
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
1636-1742 4.15e-30

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 116.08  E-value: 4.15e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054  1636 GWGLRSISDIKKGAFVNEYVGE-VIDEEECRSRIKNAQDNDI---CNFYMLTLDKD--RIID--AGPKGNESRFMNHSCQ 1707
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLElrlWGPYLFTLDEDseYCIDarALYYGNWARFINHSCD 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 292621054  1708 PNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYN 1742
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
1636-1762 1.58e-29

SET domain-containing protein (function unknown) [General function prediction only];


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 115.06  E-value: 1.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1636 GWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDIcnfYMLTLDKDRIIDAGPKGNESRFMNHSCQPNCEtqkw 1715
Cdd:COG2940    17 GRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHT---YLFELDDDGVIDGALGGNPARFINHSCDPNCE---- 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 292621054 1716 TVNGDTRVGLFALEDIPKGVELTFNYNLEClGNGKTVCKCgaPNCSG 1762
Cdd:COG2940    90 ADEEDGRIFIVALRDIAAGEELTYDYGLDY-DEEEYPCRC--PNCRG 133
PHD5_NSD1 cd15659
PHD finger 5 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...
1802-1844 1.17e-26

PHD finger 5 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or 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 (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fifth PHD finger.


Pssm-ID: 277129  Cd Length: 43  Bit Score: 103.87  E-value: 1.17e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292621054 1802 ECFYCGDGGQIVSCKKPGCPKVYHADCLNLSKRPAGRWECPWH 1844
Cdd:cd15659     1 ECFSCGDGGQLVSCKKPGCPKVYHADCLNLTKRPAGKWECPWH 43
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
1441-1529 7.68e-26

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: 103.27  E-value: 7.68e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054  1441 DILWVKVGRYRWWPAEVTQPKSVPENISRMKHEVGEFPVHFFGSKDYVWTYQARCFPYMEGDANN--KEKMGKGADAVYK 1518
Cdd:pfam00855    2 DLVWAKLKGYPWWPARVVDPEELPENVLKPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEFEylKKKKKKKKKKAFK 81
                           90
                   ....*....|.
gi 292621054  1519 KALNEAADRFR 1529
Cdd:pfam00855   82 KALEEAEEALK 92
PHD2_NSD1 cd15650
PHD finger 2 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...
1275-1321 1.08e-25

PHD finger 2 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or LysineN-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 fingers are involved in protein-protein interactions. This model corresponds to the second PHD finger.


Pssm-ID: 277120  Cd Length: 47  Bit Score: 101.12  E-value: 1.08e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 292621054 1275 TCFVCKKPDKEVRRCMIPVCGKFYHMDCILKYSPTVAQNRGFRCSIH 1321
Cdd:cd15650     1 TCFVCKKSDEDVRRCMLPLCGKFYHEECVLKYPPTVMQNRGFRCSLH 47
PHD1_NSD1_2 cd15648
PHD finger 1 found in nuclear receptor-binding SET domain-containing protein NSD1 and NSD2; ...
1228-1270 3.69e-23

PHD finger 1 found in nuclear receptor-binding SET domain-containing protein NSD1 and NSD2; NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or 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). NSD2, also termed histone-lysine N-methyltransferase NSD2, or 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, by 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). Both NSD1 and NSD2 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 (Cys5HisCysHis). In addition, NSD2 harbors a high mobility group (HMG) box. The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD fingers mediate chromatin interaction and recognition of histone marks. This model corresponds to the first PHD finger.


Pssm-ID: 277118  Cd Length: 43  Bit Score: 93.69  E-value: 3.69e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292621054 1228 VCQVCEKTGELLLCEGQCCGAFHLQCIGLTETPKGRFICQECK 1270
Cdd:cd15648     1 VCQVCEKPGELLLCEGQCCGAFHLDCIGLSEMPSGKFICDECI 43
PHD4_NSD1 cd15656
PHD finger 4 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...
1392-1431 6.92e-21

PHD finger 4 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or 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 (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fourth PHD finger.


Pssm-ID: 277126  Cd Length: 40  Bit Score: 87.38  E-value: 6.92e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 292621054 1392 WCFVCSEGGSLLCCESCPAAFHRECLNIEMPQGSWFCNDC 1431
Cdd:cd15656     1 WCFVCSEGGSLLCCESCPAAFHRECLNIDMPEGSWYCNDC 40
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
1437-1499 1.01e-18

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 81.62  E-value: 1.01e-18
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 292621054   1437 PHYKDILWVKVGRYRWWPAEVTQPKSVPENISRMKHEVGEFPVHFFGSKDYVWTYQARCFPYM 1499
Cdd:smart00293    1 FKPGDLVWAKMKGFPWWPALVISPKMTPDNIMKRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
C5HCH pfam17982
NSD Cys-His rich domain; This is an NSD-specific Cys-His rich region (C5HCH) domain. Family ...
1843-1892 4.04e-18

NSD Cys-His rich domain; This is an NSD-specific Cys-His rich region (C5HCH) domain. Family members include NSD3 (nuclear receptor SET domain-containing) proteins. This domain is located on the C-terminal of NSD1, 2 and 3 proteins. C5HCH domain lies adjacent to the fifth plant homeodomain (PHD5). The PHD5-C5HCH module of NSD3 (PHD5-C5HCHNSD3) recognizes the H3 N-terminal peptide containing unmodified K4 and trimethylated K9. Moreover, it has been reported that the PHD5-C5HCH module of NSD1 (PHD5-C5HCH) was the sole region required for tight binding of the NUP98-NSD1 fusion protein to the HoxA9 gene promoter, implicating that PHD5-C5HCH might have chromatin targeting ability.


Pssm-ID: 465605  Cd Length: 50  Bit Score: 79.82  E-value: 4.04e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 292621054  1843 WHQCNECGREAASYCEMCPNSYCEQHREGMLFISKLDGKLSCSEHDPCGP 1892
Cdd:pfam17982    1 WHQCSVCGSPATSFCEFCPSSFCKDHEKGALVPSALEGRLCCSEHDPESP 50
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
289-375 1.05e-13

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: 68.61  E-value: 1.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054   289 GDVVWAKFNRRPWWPCHVTTDPQIDVHTKMKDPSRrpcRLYFVRMFGEIvDQAWVPAKATFPFEGGDQFEKLpvLRRRGR 368
Cdd:pfam00855    1 GDLVWAKLKGYPWWPARVVDPEELPENVLKPKKKD---GEYLVRFFGDS-EFAWVKPKDLKPFDEGDEFEYL--KKKKKK 74

                   ....*..
gi 292621054   369 QKEKDYK 375
Cdd:pfam00855   75 KKKKAFK 81
AWS pfam17907
AWS domain; This entry represents the AWS (associated with SET domain) domain. This is a zinc ...
1584-1622 5.94e-13

AWS domain; This entry represents the AWS (associated with SET domain) domain. This is a zinc binding domain. The full AWS domain contains 8 cysteines. This entry represents the N-terminal part of the domain, with the C-terminal part interwoven with the SET domain.


Pssm-ID: 465559  Cd Length: 39  Bit Score: 64.75  E-value: 5.94e-13
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 292621054  1584 DENPCGIDSECINRMLLYECHSQVCPAGERCQNQSFTKR 1622
Cdd:pfam17907    1 DDPPCGCGSDCINRMLFVECTPKTCPCGESCQNQRFQRK 39
AWS smart00570
associated with SET domains; subdomain of PRESET
1574-1624 5.70e-11

associated with SET domains; subdomain of PRESET


Pssm-ID: 197795  Cd Length: 50  Bit Score: 59.34  E-value: 5.70e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 292621054   1574 EIPRCNCKAT--DENPCGidSECINRMLLYEChSQVCPAGERCQNQSFTKRQY 1624
Cdd:smart00570    1 DIMTCECKPTddDETACG--SDCLNRMLFIEC-SSSCPCGSYCSNQRFQKRQY 50
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
1392-1431 4.76e-07

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 47.98  E-value: 4.76e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 292621054   1392 WCFVCSE---GGSLLCCESCPAAFHRECLNI----EMPQGSWFCNDC 1431
Cdd:smart00249    1 YCSVCGKpddGGELLQCDGCDRWYHQTCLGPplleEEPDGKWYCPKC 47
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
1392-1432 1.82e-06

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


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 46.72  E-value: 1.82e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 292621054  1392 WCFVCS---EGGSLLCCESCPAAFHRECLNI-----EMPQGSWFCNDCR 1432
Cdd:pfam00628    1 YCAVCGksdDGGELVQCDGCDDWFHLACLGPpldpaEIPSGEWLCPECK 49
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
286-350 3.38e-06

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 46.18  E-value: 3.38e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 292621054    286 YSIGDVVWAKFNRRPWWPCHVTTdpqidvHTKMKDPSRRPCR---LYFVRMFGEiVDQAWVPAKATFP 350
Cdd:smart00293    1 FKPGDLVWAKMKGFPWWPALVIS------PKMTPDNIMKRKSdenLYPVLFFGD-KDTAWIPSSKLFP 61
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
1228-1269 1.74e-04

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 41.04  E-value: 1.74e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 292621054   1228 VCQVCEK---TGELLLCEGqCCGAFHLQCIGLTET---PKGRFICQEC 1269
Cdd:smart00249    1 YCSVCGKpddGGELLQCDG-CDRWYHQTCLGPPLLeeePDGKWYCPKC 47
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
1228-1270 4.16e-04

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


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 39.78  E-value: 4.16e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 292621054  1228 VCQVCEKT---GELLLCEGqCCGAFHLQCIGLTET----PKGRFICQECK 1270
Cdd:pfam00628    1 YCAVCGKSddgGELVQCDG-CDDWFHLACLGPPLDpaeiPSGEWLCPECK 49
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
1803-1844 5.90e-04

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 39.50  E-value: 5.90e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 292621054   1803 CFYCG---DGGQIVSCKkpGCPKVYHADCLNLSKR---PAGRWECPWH 1844
Cdd:smart00249    2 CSVCGkpdDGGELLQCD--GCDRWYHQTCLGPPLLeeePDGKWYCPKC 47
TNG2 COG5034
Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];
1108-1270 1.94e-03

Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];


Pssm-ID: 227367 [Multi-domain]  Cd Length: 271  Bit Score: 42.23  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1108 RQHKTNPEESGVRDLEKqEEAGPPPSSPCAVSAQSEGElRTSSPIQPDVPSVSQIPVEGEQSSPSKPQINNEDSLISEGF 1187
Cdd:COG5034    97 RRHRKLLDDRIAKRPHE-KVAARIENCHDAVSRLERNS-YSSAARRSSGEHRSAASSQGSRHTKLKKRKNIHNLKRRSPE 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1188 AAGLNDSAFSsrdsLSGDLSGLSTNKRSVERGGGASLKENVCQVCEKTGELLLCEGQ---------CCGA------FHLQ 1252
Cdd:COG5034   175 LSSKREVSFT----LESPSVPDTATRVKEGNNGGSTKSRGVSSEDNSEGEELYCFCQqvsygqmvaCDNAnckrewFHLE 250
                         170
                  ....*....|....*...
gi 292621054 1253 CIGLTETPKGRFICQECK 1270
Cdd:COG5034   251 CVGLKEPPKGKWYCPECK 268
TNG2 COG5034
Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];
1786-1853 4.26e-03

Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];


Pssm-ID: 227367 [Multi-domain]  Cd Length: 271  Bit Score: 41.46  E-value: 4.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 292621054 1786 SGKRKSQSEVTKErEDECFYC----GDGGQIVSCKKPGCPKV-YHADCLNLSKRPAGRWECPwhqcnECGREA 1853
Cdd:COG5034   205 STKSRGVSSEDNS-EGEELYCfcqqVSYGQMVACDNANCKREwFHLECVGLKEPPKGKWYCP-----ECKKAA 271
 
Name Accession Description Interval E-value
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
1624-1765 1.61e-97

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and similar proteins; NSD1 (EC 2.1.1.43; also termed Histone-lysine N-methyltransferase H3 lysine-36 and H4 lysine-20 specific, androgen receptor coactivator 267 kDa protein (ARA267), 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 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4. NSD1 is altered in approximately 10% of head and neck cancer patients with 55% decrease in risk of death in NSD1-mutated versus non-mutated patients; its disruption promotes favorable chemotherapeutic responses linked to hypomethylation.


Pssm-ID: 380987 [Multi-domain]  Cd Length: 142  Bit Score: 309.94  E-value: 1.61e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1624 YTEVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICNFYMLTLDKDRIIDAGPKGNESRFMN 1703
Cdd:cd19210     1 YPEVEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMN 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 292621054 1704 HSCQPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYNLECLGNGKTVCKCGAPNCSGFLG 1765
Cdd:cd19210    81 HCCQPNCETQKWTVNGDTRVGLFALCDIKAGTELTFNYNLECLGNGKTVCKCGAPNCSGFLG 142
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
1624-1765 5.01e-96

SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, NSD2, NSD3 and similar proteins; The nuclear receptor-binding SET Domain (NSD) family of histone H3 lysine 36 methyltransferases is comprised of NSD1, NSD2, and NSD3, which are primarily known to be involved in chromatin integrity and gene expression through mono-, di-, or tri-methylating lysine 36 of histone H3 (H3K36), respectively. NSD1 (EC 2.1.1.43; also termed histone-lysine N-methyltransferase H3 lysine-36 and H4 lysine-20 specific, androgen receptor coactivator 267 kDa protein (ARA267), 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 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4. NSD2 (EC 2.1.1.43; also termed multiple myeloma SET domain-containing protein (MMSET), protein trithorax-5 (TRX5), or wolf-Hirschhorn syndrome candidate 1 protein (WHSC1)) acts as histone-lysine N-methyltransferase with histone H3 'Lys-27' (H3K27me) methyltransferase activity. NSD3 (EC 2.1.1.43; also termed protein whistle, WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1L1), or WHSC1-like protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-4' and 'Lys-27' of histone H3.


Pssm-ID: 380950 [Multi-domain]  Cd Length: 142  Bit Score: 305.78  E-value: 5.01e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1624 YTEVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICNFYMLTLDKDRIIDAGPKGNESRFMN 1703
Cdd:cd19173     1 YPPTEPFKTGDRGWGLRTKRDIKKGDFVIEYVGELIDEEECRRRLKKAHENNITNFYMLTLDKDRIIDAGPKGNLSRFMN 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 292621054 1704 HSCQPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYNLECLGNGKTVCKCGAPNCSGFLG 1765
Cdd:cd19173    81 HSCQPNCETQKWTVNGDTRVGLFAVRDIPAGEELTFNYNLDCLGNEKKVCRCGAPNCSGFLG 142
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
1624-1765 1.27e-88

SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins; NSD2 (EC 2.1.1.43; also termed multiple myeloma SET domain-containing protein (MMSET), protein trithorax-5 (TRX5), or wolf-Hirschhorn syndrome candidate 1 protein (WHSC1)) acts as histone-lysine N-methyltransferase with histone H3 'Lys-36' (H3K36me) methyltransferase activity. NSD2 has been shown to mediate di- and trimethylation of H3K36 and dimethylation of H4K20 in different systems, and has been characterized as a transcriptional repressor interacting with histone deacetylase HDAC1 and histone demethylase LSD1. NSD2 mediates constitutive NF-kappaB signaling for cancer cell proliferation, survival and tumor growth. It is highly overexpressed in several types of human cancers, including small-cell lung cancers, neuroblastoma, carcinomas of stomach and colon, and bladder cancers, and its overexpression tends to be associated with tumor aggressiveness. WHSC1 is frequently deleted in Wolf-Hirschhorn syndrome (WHS).


Pssm-ID: 380988 [Multi-domain]  Cd Length: 142  Bit Score: 284.58  E-value: 1.27e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1624 YTEVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICNFYMLTLDKDRIIDAGPKGNESRFMN 1703
Cdd:cd19211     1 YPETKIIKTEGKGWGLIAKRDIKKGEFVNEYVGELIDEEECMARIKHAHENDITHFYMLTIDKDRIIDAGPKGNYSRFMN 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 292621054 1704 HSCQPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYNLECLGNGKTVCKCGAPNCSGFLG 1765
Cdd:cd19211    81 HSCQPNCETQKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLGNEKTVCRCGAPNCSGFLG 142
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
1624-1765 1.64e-84

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing protein 3 (NSD3) and similar proteins; NSD3 (EC 2.1.1.43; also termed protein whistle, WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1L1), or WHSC1-like protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. NSD3 is amplified and overexpressed in multiple cancer types, including acute myeloid leukemia (AML), breast, lung, pancreatic and bladder cancers, as well as squamous cell carcinoma of the head and neck (SCCHN). NSD3 contributes to tumorigenesis by interacting with bromodomain-containing protein 4 (BRD4), the bromodomain and extraterminal (BET) protein, which is a potential therapeutic target in acute myeloid leukemia (AML). NSD3 is amplified in primary tumors and cell lines from breast carcinoma, and can promote the cell viability of small-cell lung cancer and pancreatic ductal adenocarcinoma. High NSD3 expression is implicated in poor grade and heavy smoking history in SCCHN. Thus, NSD3 may serve as a potential druggable target for selective cancer therapy.


Pssm-ID: 380989 [Multi-domain]  Cd Length: 142  Bit Score: 272.95  E-value: 1.64e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1624 YTEVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICNFYMLTLDKDRIIDAGPKGNESRFMN 1703
Cdd:cd19212     1 YPDAEIIKTERRGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRIKRAHENSVTNFYMLTVTKDRIIDAGPKGNYSRFMN 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 292621054 1704 HSCQPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYNLECLGNGKTVCKCGAPNCSGFLG 1765
Cdd:cd19212    81 HSCNPNCETQKWTVNGDVRVGLFALCDIPAGMELTFNYNLDCLGNGRTECHCGADNCSGFLG 142
PWWP_NSD1_rpt1 cd20161
first PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and ...
283-398 5.02e-69

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: 227.36  E-value: 5.02e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054  283 SVKYSIGDVVWAKFNRRPWWPCHVTTDPQIDVHTKMKDPSRRPCRLYFVRMFGEIVDQAWVPAKATFPFEGGDQFEKLPV 362
Cdd:cd20161     1 PVKYEVGDLVWAKFSRRPWWPCRICADPLLDTHSKMKVPSRRPCRQYYVETLGELTEKAWVAAKAVVPFEGRHQFEELPV 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 292621054  363 LRRRGRQKEKDYKYTVPKRLIPSWKASVLEAEASLT 398
Cdd:cd20161    81 LRRRGKQKEKDYKHKIPQKLLSLWEASVAHAEDFLS 116
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
1624-1765 3.69e-67

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and similar proteins; SETD2 (also termed HIF-1, huntingtin yeast partner B, huntingtin-interacting protein 1 (HIP-1), huntingtin-interacting protein B, lysine N-methyltransferase 3A or protein-lysine N-methyltransferase SETD2) acts as histone-lysine N-methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using demethylated 'Lys-36' (H3K36me2) as substrate. It has been shown that methylation is a posttranslational modification of dynamic microtubules and that SETD2 methylates alpha-tubulin at lysine 40, the same lysine that is marked by acetylation on microtubules. Methylation of microtubules occurs during mitosis and cytokinesis and can be ablated by SETD2 deletion, which causes mitotic spindle and cytokinesis defects, micronuclei, and polyploidy.


Pssm-ID: 380949 [Multi-domain]  Cd Length: 142  Bit Score: 223.23  E-value: 3.69e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1624 YTEVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICNFYMLTLDKDRIIDAGPKGNESRFMN 1703
Cdd:cd19172     1 YAKVEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYAREGNRHYYFMALKSDEIIDATKKGNLSRFIN 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 292621054 1704 HSCQPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYNLECLGNGKTVCKCGAPNCSGFLG 1765
Cdd:cd19172    81 HSCEPNCETQKWTVNGELRVGFFAKRDIPAGEELTFDYQFERYGKEAQKCYCGSPNCRGYIG 142
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
1626-1761 1.33e-66

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), nuclear SETD2 (NSD2), ASH1-like protein (ASH1L) and similar proteins; This family includes SET domain-containing protein 2 (SETD2), nuclear SETD2 (NSD2) and ASH1-like protein (ASH1L), which function as histone-lysine N-methyltransferases. SETD2 specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using demethylated 'Lys-36' (H3K36me2) as substrate. NSD2 shows histone H3 'Lys-27' (H3K27me) methyltransferase activity. ASH1L specifically methylates 'Lys-36' of histone H3 (H3K36me). The family also includes Arabidopsis thaliana ASH1-related protein 3 (ASHR3) and similar proteins.


Pssm-ID: 380929  Cd Length: 136  Bit Score: 221.36  E-value: 1.33e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1626 EVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICNFYMLTLDKDRIIDAGPKGNESRFMNHS 1705
Cdd:cd10531     1 KLELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERLDEYEELGKSNFYILSLSDDVVIDATRKGNLSRFINHS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 292621054 1706 CQPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYNLECLGNGKTVCKCGAPNCS 1761
Cdd:cd10531    81 CEPNCETQKWIVNGEYRIGIFALRDIPAGEELTFDYNFVNYNEAKQVCLCGAQNCR 136
PWWP_NSD1_rpt2 cd20164
second PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) ...
1438-1531 1.04e-58

second 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. This model corresponds to the second PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438992  Cd Length: 96  Bit Score: 197.02  E-value: 1.04e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1438 HYKDILWVKVGRYRWWPAEVTQPKSVPENISRMKHEVGEFPVHFFGSKDYVWTYQARCFPYMEGDANNKEKMGKGADAVY 1517
Cdd:cd20164     1 HYKEVVWVKVGRYRWWPAEVCHPKSIPTNIQKMKHDIGEFPVLFFGSNDYLWTHQARVFPYMEGDVSSKDKMGKGVDGTY 80
                          90
                  ....*....|....
gi 292621054 1518 KKALNEAADRFREL 1531
Cdd:cd20164    81 KKALQEAAVRFEEL 94
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
1626-1765 1.19e-57

SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ASH1L (EC 2.1.1.43; also termed absent small and homeotic disks protein 1 homolog, KMT2H, or lysine N-methyltransferase 2H) acts as histone-lysine N-methyltransferase that specifically methylates 'Lys-36' of histone H3 (H3K36me). It plays important roles in development; heterozygous mutation of ASH1L is associated with severe intellectual disability (ID) and multiple congenital anomaly (MCA).


Pssm-ID: 380951 [Multi-domain]  Cd Length: 141  Bit Score: 195.97  E-value: 1.19e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1626 EVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICnFYMLTLDKDRIIDAGPKGNESRFMNHS 1705
Cdd:cd19174     1 GLERFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMIEQYHNHSH-HYCLNLDSGMVIDGYRMGNEARFVNHS 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 292621054 1706 CQPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYNLECLG-NGKTVCKCGAPNCSGFLG 1765
Cdd:cd19174    80 CDPNCEMQKWSVNGVYRIGLFALKDIPAGEELTYDYNFHSFNvEKQQPCKCGSPNCRGVIG 140
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
1627-1765 1.45e-55

SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 (ASHR3) and similar proteins; This family includes Arabidopsis thaliana ASH1-related protein 3 (ASHR3, also termed protein SET DOMAIN GROUP 4 or protein stamen loss), ASH1 homolog 3 (ASHH3, also termed protein SET DOMAIN GROUP 7) and homolog 4 (ASHH4, also termed protein SET DOMAIN GROUP 24). They all function as histone-lysine N-methyltransferases (EC 2.1.1.43).


Pssm-ID: 380952 [Multi-domain]  Cd Length: 139  Bit Score: 189.94  E-value: 1.45e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1627 VEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICNFYMLTLDKDRIIDAGPKGNESRFMNHSC 1706
Cdd:cd19175     2 MKLVKTEKCGWGLVADEDINAGEFIIEYVGEVIDDKTCEERLWDMKHKGEKNFYMCEIDKDMVIDATFKGNLSRFINHSC 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 292621054 1707 QPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYNLECLGNgKTVCKCGAPNCSGFLG 1765
Cdd:cd19175    82 DPNCELQKWQVDGETRIGVFAIRDIKKGEELTYDYQFVQFGA-DQDCHCGSKNCRGKLG 139
PWWP_NSD2_rpt2 cd20165
second PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar ...
1438-1531 1.92e-45

second 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, an 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 second PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438993  Cd Length: 96  Bit Score: 159.35  E-value: 1.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1438 HYKDILWVKVGRYRWWPAEVTQPKSVPENISRMKHEVGEFPVHFFGSKDYVWTYQARCFPYMEGDANNKEKMGKGADAVY 1517
Cdd:cd20165     1 RFQDIIWVKLGNYRWWPAEVCHPKNVPPNIQKMKHEIGEFPVFFFGSKDYYWTHQARVFPYMEGDRGSKYQGGKGIGKVF 80
                          90
                  ....*....|....
gi 292621054 1518 KKALNEAADRFREL 1531
Cdd:cd20165    81 KNALQEAEARFREI 94
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
1626-1748 2.14e-44

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on outlier plant homologues


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 157.11  E-value: 2.14e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054   1626 EVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICNFYMLTLDKDRIIDAGPKGNESRFMNHS 1705
Cdd:smart00317    2 KLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAKAFYLFDIDSDLCIDARRKGNLARFINHS 81
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 292621054   1706 CQPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYNLECLGN 1748
Cdd:smart00317   82 CEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
PWWP_NSD_rpt2 cd05838
second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
1438-1531 2.94e-44

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: 155.86  E-value: 2.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1438 HYKDILWVKVGRYRWWPAEVTQPKSVPENISRMKHEVGEFPVHFFGSKDYVWTYQARCFPYMEGDANNKEKMGKGADAVY 1517
Cdd:cd05838     1 LYGDIVWVKLGNYRWWPAEILHPREVPDNIQSLPHPPGEFPVRFFGSHDYYWVHRGRVFLFEEGDKGSKEKSKKSLDKSF 80
                          90
                  ....*....|....
gi 292621054 1518 KKALNEAADRFREL 1531
Cdd:cd05838    81 KRALKEANEAFREL 94
PWWP_NSD3_rpt2 cd20166
second PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar ...
1438-1531 6.51e-42

second 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 second PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438994  Cd Length: 95  Bit Score: 148.97  E-value: 6.51e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1438 HYKDILWVKVGRYRWWPAEVTQPKSVPENISRMKHEVGEFPVHFFGSKDYVWTYQARCFPYMEGDANNKEKMGKGaDAVY 1517
Cdd:cd20166     1 HYKQIVWVKLGNYRWWPAEICNPRSVPLNIQGLKHDIGDFPVFFFGSHDYYWVHQGRVFPYVEGDKSFAEGQTSI-NKTF 79
                          90
                  ....*....|....
gi 292621054 1518 KKALNEAADRFREL 1531
Cdd:cd20166    80 KKALEEAAKRFQEL 93
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
1636-1760 1.13e-36

SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), histone-lysine N-methyltransferases (KMT2A/KMT2B/KMT2C/KMT2D) and similar proteins; This family includes SET domain-containing protein 1A (SETD1A), 1B (SETD1B), as well as histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B), 2C (KMT2C), 2D (KMT2D). These proteins are histone-lysine N-methyltransferases (EC 2.1.1.43) that specifically methylate 'Lys-4' of histone H3 (H3K4me).


Pssm-ID: 380916  Cd Length: 150  Bit Score: 136.19  E-value: 1.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1636 GWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICNFYMLTLDKDRIIDAGPKGNESRFMNHSCQPNCETQKW 1715
Cdd:cd10518    25 GWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKRYDEEGGGGTYMFRIDEDLVIDATKKGNIARFINHSCDPNCYAKII 104
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 292621054 1716 TVNGDTRVGLFALEDIPKGVELTFNYNLECLGNGKTVCKCGAPNC 1760
Cdd:cd10518   105 TVDGEKHIVIFAKRDIAPGEELTYDYKFPIEDEEKIPCLCGAPNC 149
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
1601-1764 2.38e-36

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 homologs, SUV39H1, SUV39H2 and similar proteins; This family includes SUV39H1 (also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A, KMT1A, position-effect variegation 3-9 homolog, SUV39H, or Su(var)3-9 homolog 1) and SUV39H2 (also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B, KMT1B, or Su(var)3-9 homolog 2), both act as histone-lysine N-methyltransferases that specifically trimethylate 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. They mainly function in heterochromatin regions, thereby playing central roles in the establishment of constitutive heterochromatin at pericentric and telomere regions. Also included are Schizosaccharomyces pombe H3K9 methyltransferase Clr4 (SUV39H homolog) and Neurospora crassa DIM-5, both of which also methylate 'Lys-9' of histone H3.


Pssm-ID: 380940 [Multi-domain]  Cd Length: 245  Bit Score: 138.97  E-value: 2.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1601 YECHSQvCPAGERCQNQSFTK-RQYtEVEIFRT-LSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICn 1678
Cdd:cd10542    64 YECNSR-CKCGPDCPNRVVQRgRKV-PLCIFRTsNGRGWGVKTLEDIKKGTFVMEYVGEIITSEEAERRGKIYDANGRT- 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1679 fYMLTLDKDRI-----IDAGPKGNESRFMNHSCQPNCET-QKWTVNGDT---RVGLFALEDIPKGVELTFNYNL------ 1743
Cdd:cd10542   141 -YLFDLDYNDDdceytVDAAYYGNISHFINHSCDPNLAVyAVWINHLDPrlpRIAFFAKRDIKAGEELTFDYLMtgtggs 219
                         170       180
                  ....*....|....*....|....*.
gi 292621054 1744 -ECLGNGK----TVCKCGAPNCSGFL 1764
Cdd:cd10542   220 sESTIPKPkdvrVPCLCGSKNCRKYL 245
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
1575-1764 2.68e-35

SET domain (including pre-SET and post-SET domains) found in SET domain and mariner transposase fusion protein (SETMAR) and similar proteins; SETMAR (also termed metnase) is a DNA-binding protein that is indirectly recruited to sites of DNA damage through protein-protein interactions. It has a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity. SETMAR also acts as a histone-lysine N-methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3. It specifically mediates dimethylation of H3 'Lys-36' at sites of DNA double-strand break and may recruit proteins required for efficient DSB repair through non-homologous end-joining.


Pssm-ID: 380942 [Multi-domain]  Cd Length: 254  Bit Score: 136.27  E-value: 2.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1575 IPRCNCKatdENPCGIDSE-CI---------NRMLL----------YECHSQvCPAGERCQNQSFTKRQYTEVEIFRTLS 1634
Cdd:cd10544    24 FPGCDCK---TSSCEPETCsCLrkygpnyddDGCLLdfdgkysgpvFECNSM-CKCSESCQNRVVQNGLQFKLQVFKTPK 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1635 RGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDicNFYMLTLDKDR--------IIDAGPKGNESRFMNHSC 1706
Cdd:cd10544   100 KGWGLRTLEFIPKGRFVCEYAGEVIGFEEARRRTKSQTKGD--MNYIIVLREHLssgkvletFVDPTYIGNIGRFLNHSC 177
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 292621054 1707 QPNCETQKWTVNGDT-RVGLFALEDIPKGVELTFNY-------------NLECLGNGKTVCKCGAPNCSGFL 1764
Cdd:cd10544   178 EPNLFMVPVRVDSMVpKLALFAARDIVAGEELSFDYsgefsnsvesvtlARQDESKSRKPCLCGAENCRGFL 249
SET_SETDB-like cd10538
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
1551-1742 9.99e-34

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) and 2 (SETDB2), suppressor of variegation 3-9 homologs, SUV39H1 and SUV39H2, euchromatic histone-lysine N-methyltransferase EHMT1 and EHMT2, and similar proteins; The family includes SET domain bifurcated 1 (SETDB1) and 2 (SETDB2), suppressor of variegation 3-9 homologs, SUV39H1 and SUV39H2, euchromatic histone-lysine N-methyltransferase EHMT1 and EHMT2. SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis. SUV39H1 (also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A, KMT1A, position-effect variegation 3-9 homolog, SUV39H, or Su(var)3-9 homolog 1) and SUV39H2 (also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B, KMT1B, or Su(var)3-9 homolog 2), both act as histone-lysine N-methyltransferases that specifically trimethylate 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. They mainly function in heterochromatin regions, thereby playing central roles in the establishment of constitutive heterochromatin at pericentric and telomere regions. EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, lysine N-methyltransferase 1D, or KMT1D) and EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C, KMT1C, or protein G9a), both act as histone-lysine N-methyltransferases that specifically mono- and dimethylate 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. This family also includes the pre-SET domain, which is found in a number of histone methyltransferases (HMTase), N-terminal to the SET domain. Pre-SET domain is a zinc binding motif which contains 9 conserved cysteines that coordinate three zinc ions. It is thought that this region plays a structural role in stabilizing SET domains. Most family members, except for Arabidopsis thaliana SUVH9, contain a post-SET domain which harbors a zinc-binding site.


Pssm-ID: 380936 [Multi-domain]  Cd Length: 217  Bit Score: 130.18  E-value: 9.99e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1551 PPYKHIKVNkQIGKVLIITADLSEIPRCNCK-----------ATDENPCGIDSECINRM-----LLYECHSQvCPAGERC 1614
Cdd:cd10538     1 PSFTYIKDN-IVGKNVQPFSNIIDSVGCKCKddcldskcacaAESDGIFAYTKNGLLRLnnsppPIFECNSK-CSCDDDC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1615 QNQSFTKRQYTEVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKnAQDNDiCNFYMLTLDKDR------ 1688
Cdd:cd10538    79 KNRVVQRGLQARLQVFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGK-IYDKS-GGSYLFDLDEFSdsdgdg 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 292621054 1689 ---IIDAGPKGNESRFMNHSCQPNCETQK-WTVNGDT---RVGLFALEDIPKGVELTFNYN 1742
Cdd:cd10538   157 eelCVDATFCGNVSRFINHSCDPNLFPFNvVIDHDDLrypRIALFATRDILPGEELTFDYG 217
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
1597-1764 2.84e-32

SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; This subfamily contains Neurospora crassa DIM-5 (also termed H3-K9-HMTase dim-5, or HKMT) which functions as histone-lysine N-methyltransferase that specifically trimethylates histone H3 to form H3K9me3.


Pssm-ID: 380996 [Multi-domain]  Cd Length: 274  Bit Score: 127.82  E-value: 2.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1597 RMLLYECHSQvCPAGERCQNQSFTKRQYTEVEIFRT-LSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNA---Q 1672
Cdd:cd19473    78 RLPIYECHEG-CACSDDCPNRVVERGRKVPLQIFRTsDGRGWGVRSTVDIKRGQFVDCYVGEIITPEEAQRRRDAAtiaQ 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1673 DNDIcnfYMLTLDK--------DRI------ID----AGPkgneSRFMNHSCQPNCETQkwtvngdTRVG---------- 1724
Cdd:cd19473   157 RKDV---YLFALDKfsdpdsldPRLrgdpyeIDgefmSGP----TRFINHSCDPNLRIF-------ARVGdhadkhihdl 222
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 292621054 1725 -LFALEDIPKGVELTFNY-----------NLECLGNGKTVCKCGAPNCSGFL 1764
Cdd:cd19473   223 aFFAIKDIPRGTELTFDYvdgvtgldddaGDEEKEKEMTKCLCGSPKCRGYL 274
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
1636-1741 2.54e-31

SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar proteins; The family includes EZH1 and EZH2. EZH1 (EC 2.1.1.43; also termed ENX-2, or histone-lysine N-methyltransferase EZH1) is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. EZH2 (EC 2.1.1.43; also termed lysine N-methyltransferase 6, ENX-1, or histone-lysine N-methyltransferase EZH2) is a catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Both, EZH1 and EZH2, can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively.


Pssm-ID: 380917  Cd Length: 117  Bit Score: 119.66  E-value: 2.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1636 GWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKnAQDNDICNfYMLTLDKDRIIDAGPKGNESRFMNHSCQPNCETQKW 1715
Cdd:cd10519    12 GWGLFLKEPIKKDEFIGEYTGELISQDEADRRGK-IYDKYNSS-YLFNLNDQFVVDATRKGNKIRFANHSSNPNCYAKVM 89
                          90       100
                  ....*....|....*....|....*.
gi 292621054 1716 TVNGDTRVGLFALEDIPKGVELTFNY 1741
Cdd:cd10519    90 MVNGDHRIGIFAKRDIEAGEELFFDY 115
PHD3_NSD1 cd15653
PHD finger 3 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...
1322-1375 3.49e-30

PHD finger 3 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or 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 (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the third PHD finger.


Pssm-ID: 277123  Cd Length: 54  Bit Score: 114.25  E-value: 3.49e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 292621054 1322 VCLSCYITNPNNPGISKGRLTRCVRCPVAYHANDYCMAAGSVPLANNSFLCPNH 1375
Cdd:cd15653     1 ICLTCHATNPSNPSASKGRLMRCVRCPVAYHANDFCLAAGSVILASNSIICPNH 54
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
1636-1742 4.15e-30

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 116.08  E-value: 4.15e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054  1636 GWGLRSISDIKKGAFVNEYVGE-VIDEEECRSRIKNAQDNDI---CNFYMLTLDKD--RIID--AGPKGNESRFMNHSCQ 1707
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLElrlWGPYLFTLDEDseYCIDarALYYGNWARFINHSCD 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 292621054  1708 PNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYN 1742
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
1636-1762 1.58e-29

SET domain-containing protein (function unknown) [General function prediction only];


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 115.06  E-value: 1.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1636 GWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDIcnfYMLTLDKDRIIDAGPKGNESRFMNHSCQPNCEtqkw 1715
Cdd:COG2940    17 GRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHT---YLFELDDDGVIDGALGGNPARFINHSCDPNCE---- 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 292621054 1716 TVNGDTRVGLFALEDIPKGVELTFNYNLEClGNGKTVCKCgaPNCSG 1762
Cdd:COG2940    90 ADEEDGRIFIVALRDIAAGEELTYDYGLDY-DEEEYPCRC--PNCRG 133
PWWP_NSD_rpt1 cd20144
first PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
288-394 1.99e-29

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: 113.95  E-value: 1.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054  288 IGDVVWAKFNRRPWWPCHVTTDPQIDVHTKMKDPSRRPCRLYFVRMFGEIVDQAWVPAKATFPFEGGDQFEKLPV-LRRR 366
Cdd:cd20144     1 VGDLVWAKVSGHPWWPCMVTYDPESGLYTKIKGSGGRTYRQYHVQFFGDNGERGWVSEKSLMPFEGKEKFEELVKeLKKK 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 292621054  367 GRQKEKDYKYT--VPKRLIPSWKASVLEAE 394
Cdd:cd20144    81 AKKKSKKAKLEkkVKPSRRKKWEIAVEEAE 110
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
1631-1760 2.67e-29

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), 2D (KMT2D) and similar proteins; This family includes KMT2C and KMT2D. Both, KMT2C (also termed HALR or MLL3) and KMT2D (also termed ALR or MLL2), act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me). They are subunits of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation.


Pssm-ID: 380948 [Multi-domain]  Cd Length: 153  Bit Score: 115.22  E-value: 2.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1631 RTLSRGWGLRSISDIKKGAFVNEYVGEVIDEE--ECRSRIKNAQDNDIcnfYMLTLDKDRIIDAGPKGNESRFMNHSCQP 1708
Cdd:cd19171    20 RSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEvaNRREKIYESQNRGI---YMFRIDNDWVIDATMTGGPARYINHSCNP 96
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 292621054 1709 NCETQKWTVNGDTRVGLFALEDIPKGVELTFNYNLECLGNG-KTVCKCGAPNC 1760
Cdd:cd19171    97 NCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQhKIPCLCGAPNC 149
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
1600-1764 7.16e-28

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) and similar proteins; SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes.


Pssm-ID: 380915 [Multi-domain]  Cd Length: 288  Bit Score: 115.46  E-value: 7.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1600 LYECHSQvCPAGERCQNQSFTKRQYTEVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICNF 1679
Cdd:cd10517   105 VYECNSR-CKCDKRCYNRVVQNGLQVRLQVFKTEKKGWGIRCLDDIPKGSFVCIYAGQILTEDEANEEGLQYGDEYFAEL 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1680 -YMLTLDKDR------------IIDAGPKGNESRFMNHSCQPNCETQKWTVNG-DTR---VGLFALEDIPKGVELTFNYN 1742
Cdd:cd10517   184 dYIEVVEKLKegyesdveehcyIIDAKSEGNLGRYLNHSCSPNLFVQNVFVDThDLRfpwVAFFASRYIRAGTELTWDYN 263
                         170       180
                  ....*....|....*....|....*
gi 292621054 1743 LEcLGN--GKTV-CKCGAPNCSGFL 1764
Cdd:cd10517   264 YE-VGSvpGKVLyCYCGSSNCRGRL 287
SET_SET1 cd20072
SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...
1637-1760 1.68e-27

SET domain (including post-SET domain) found in catalytic component of the Saccharomyces cerevisiae COMPASS complex and similar proteins; The family contains mostly fungal SET domains, including SET1 found in the catalytic component of the Saccharomyces cerevisiae COMPASS (complex of proteins associated with Set1). SET1 is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me), when part of the SET1 histone methyltransferase (HMT) complex. The activity of this catalytic domain is established through forming a complex with a set of core proteins; it is extensively contacted by Cps60 (Bre2), Cps50 (Swd1), and Cps30 (Swd3).


Pssm-ID: 380998  Cd Length: 148  Bit Score: 109.82  E-value: 1.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1637 WGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICNFYMLTLDKDRIIDAGPKGNESRFMNHSCQPNCETQKWT 1716
Cdd:cd20072    25 WGLYAMENISAKDMVIEYVGEVIRQQVADEREKRYLRQGIGSSYLFRIDDDTVVDATKKGNIARFINHCCDPNCTAKIIK 104
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 292621054 1717 VNGDTRVGLFALEDIPKGVELTFNYNLECLGNgKTVCKCGAPNC 1760
Cdd:cd20072   105 VEGEKRIVIYAKRDIAAGEELTYDYKFPREED-KIPCLCGAPNC 147
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
1600-1764 2.77e-27

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 homolog 2 (SUV39H2) and similar proteins; SUV39H2 (EC 2.1.1.43; also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B (KMT1B), or Su(var)3-9 homolog 2) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. It mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions.


Pssm-ID: 380930 [Multi-domain]  Cd Length: 243  Bit Score: 112.68  E-value: 2.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1600 LYECHSQvCPAGERCQNQSFTKRQYTEVEIFRTLS-RGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICN 1678
Cdd:cd10532    60 IYECNSR-CKCGPDCPNRVVQKGTQYSLCIFRTSNgRGWGVKTLQKIKKNSFVMEYVGEVITSEEAERRGQFYDSKGITY 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1679 FYMLTLDKDRI-IDAGPKGNESRFMNHSCQPNceTQKWTV---NGDT---RVGLFALEDIPKGVELTFNYNLECLGN--- 1748
Cdd:cd10532   139 LFDLDYESDEFtVDAARYGNVSHFVNHSCDPN--LQVFNVfidNLDTrlpRIALFSTRTIKAGEELTFDYQMKGSGDlss 216
                         170       180
                  ....*....|....*....|....*..
gi 292621054 1749 -----------GKTVCKCGAPNCSGFL 1764
Cdd:cd10532   217 dsidnspakkrVRTVCKCGAVTCRGYL 243
PHD5_NSD1 cd15659
PHD finger 5 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...
1802-1844 1.17e-26

PHD finger 5 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or 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 (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fifth PHD finger.


Pssm-ID: 277129  Cd Length: 43  Bit Score: 103.87  E-value: 1.17e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292621054 1802 ECFYCGDGGQIVSCKKPGCPKVYHADCLNLSKRPAGRWECPWH 1844
Cdd:cd15659     1 ECFSCGDGGQLVSCKKPGCPKVYHADCLNLTKRPAGKWECPWH 43
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
1599-1742 1.39e-26

SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar proteins; Arabidopsis thaliana SUVH protein (also termed suppressor of variegation 3-9 homolog protein) is a histone-lysine N-methyltransferase that methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression. Some family members contain a post-SET domain which binds a Zn2+ ion. Most family members, except for Arabidopsis thaliana SUVH9, contain a post-SET domain which harbors a zinc-binding site.


Pssm-ID: 380943 [Multi-domain]  Cd Length: 232  Bit Score: 110.19  E-value: 1.39e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1599 LLYECHSQvCPAGERCQNQSFTKRQYTEVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNaqDN---D 1675
Cdd:cd10545    61 AIYECGPL-CKCPPSCYNRVTQKGLRYRLEVFKTAERGWGVRSWDSIPAGSFICEYVGELLDTSEADTRSGN--DDylfD 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1676 ICNFYMLTLDKDR-----------------------IIDAGPKGNESRFMNHSCQPNCETQKWTV-NGDTR---VGLFAL 1728
Cdd:cd10545   138 IDNRQTNRGWDGGqrldvgmsdgerssaedeessefTIDAGSFGNVARFINHSCSPNLFVQCVLYdHNDLRlprVMLFAA 217
                         170
                  ....*....|....
gi 292621054 1729 EDIPKGVELTFNYN 1742
Cdd:cd10545   218 DNIPPLQELTYDYG 231
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
1441-1529 7.68e-26

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: 103.27  E-value: 7.68e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054  1441 DILWVKVGRYRWWPAEVTQPKSVPENISRMKHEVGEFPVHFFGSKDYVWTYQARCFPYMEGDANN--KEKMGKGADAVYK 1518
Cdd:pfam00855    2 DLVWAKLKGYPWWPARVVDPEELPENVLKPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEFEylKKKKKKKKKKAFK 81
                           90
                   ....*....|.
gi 292621054  1519 KALNEAADRFR 1529
Cdd:pfam00855   82 KALEEAEEALK 92
PHD2_NSD1 cd15650
PHD finger 2 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...
1275-1321 1.08e-25

PHD finger 2 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or LysineN-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 fingers are involved in protein-protein interactions. This model corresponds to the second PHD finger.


Pssm-ID: 277120  Cd Length: 47  Bit Score: 101.12  E-value: 1.08e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 292621054 1275 TCFVCKKPDKEVRRCMIPVCGKFYHMDCILKYSPTVAQNRGFRCSIH 1321
Cdd:cd15650     1 TCFVCKKSDEDVRRCMLPLCGKFYHEECVLKYPPTVMQNRGFRCSLH 47
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
1636-1760 1.19e-25

SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and similar proteins; This family includes SET domain-containing protein 1A (SETD1A) and SET domain-containing protein 1B (SETD1B). These proteins are histone-lysine N-methyltransferases that specifically methylate 'Lys-4' of histone H3 (H3K4me) when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated.


Pssm-ID: 380946  Cd Length: 148  Bit Score: 104.73  E-value: 1.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1636 GWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICNFYMLTLDKDRIIDAGPKGNESRFMNHSCQPNCETQKW 1715
Cdd:cd19169    24 DWGLFALEPIAADEMVIEYVGQVIRQSVADEREKRYEAIGIGSSYLFRVDDDTIIDATKCGNLARFINHSCNPNCYAKII 103
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 292621054 1716 TVNGDTRVGLFALEDIPKGVELTFNYNLEcLGNGKTVCKCGAPNC 1760
Cdd:cd19169   104 TVESQKKIVIYSKRPIAVNEEITYDYKFP-IEDEKIPCLCGAPQC 147
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
1627-1764 1.25e-25

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B) and similar proteins; This family includes KMT2A and KMT2B. Both KMT2A (also termed ALL-1 or CXXC7 or MLL or MLL1 or TRX1 or HRX) and KMT2B (also termed MLL4 or TRX2) act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me).


Pssm-ID: 380947 [Multi-domain]  Cd Length: 152  Bit Score: 104.78  E-value: 1.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1627 VEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDI-CnfYMLTLDKDRIIDAGPKGNESRFMNHS 1705
Cdd:cd19170    16 VGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGIgC--YMFRIDDDEVVDATMHGNAARFINHS 93
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 292621054 1706 CQPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYNLEcLGNGKTVCKCGAPNCSGFL 1764
Cdd:cd19170    94 CEPNCYSRVVNIDGKKHIVIFALRRILRGEELTYDYKFP-IEDVKIPCTCGSKKCRKYL 151
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
1576-1760 4.08e-25

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase EHMT1, EHMT2 and similar proteins; This family includes EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, lysine N-methyltransferase 1D, or KMT1D) and EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C, KMT1C, or protein G9a), both act as histone-lysine N-methyltransferases that specifically mono- and dimethylate 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin.


Pssm-ID: 380941 [Multi-domain]  Cd Length: 231  Bit Score: 105.88  E-value: 4.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1576 PRCNCKATDENpCGIDSEC--------INRMLLYEChSQVCPAGERCQNQSFTKRQYTEVEIFRTLSRGWGLRSISDIKK 1647
Cdd:cd10543    36 DNCVCGRLSVR-CWYDKEGrllpdfnkLDPPLIFEC-NRACSCWRNCRNRVVQNGIRYRLQLFRTRGMGWGVRALQDIPK 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1648 GAFVNEYVGEVIDEEECRSRiknaQDNDicnfYMLTLD-KDR---IIDAGPKGNESRFMNHSCQPNCETQKWTVNGDT-- 1721
Cdd:cd10543   114 GTFVCEYIGELISDSEADSR----EDDS----YLFDLDnKDGetyCIDARRYGNISRFINHLCEPNLIPVRVFVEHQDlr 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 292621054 1722 --RVGLFALEDIPKGVELTFNYnleclGN------GKTV-CKCGAPNC 1760
Cdd:cd10543   186 fpRIAFFASRDIKAGEELGFDY-----GEkfwrikGKYFtCRCGSPKC 228
SET_SUV39H_Clr4-like cd20073
SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...
1571-1764 4.22e-25

SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 methyltransferase Clr4, and similar proteins; This subfamily contains fission yeast Schizosaccharomyces pombe H3K9 methyltransferase Clr4 (also known as Suv39h), the sole homolog of the mammalian SUV39H1 and SUV39H2 enzymes, that has a critical role in preventing aberrant heterochromatin formation. It is known to di- and tri-methylate Lys-9 of histone H3, a central heterochromatic histone modification, with its specificity profile most similar to that of the human SUV39H2 homolog.


Pssm-ID: 380999 [Multi-domain]  Cd Length: 259  Bit Score: 106.89  E-value: 4.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1571 DLSEIPRCNC-KATDENPCGIDSE----CINRMLLYECHSQvCPAGERCQNQSFTKRQYTEVEIFRTLSRGWGLRSISDI 1645
Cdd:cd20073    35 DLNNPGSCQClEDSNEKSFAYDEYgrvrANTGSIIYECNEN-CDCGINCPNRVVQRGRKLPLEIFKTKHKGWGLRCPRFI 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1646 KKGAFVNEYVGEVIDEEECRSRIKNAQDNDICNFYMLTLDKDRI-----IDAGPKGNESRFMNHSCQPNCETQKWTVNGD 1720
Cdd:cd20073   114 KAGTFIGVYLGEVITQSEAEIRGKKYDNVGVTYLFDLDLFEDQVdeyytVDAQYCGDVTRFINHSCDPNLAIYSVLRDKS 193
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 292621054 1721 TR----VGLFALEDIPKGVELTFNYN-------LECLGNGKTV----------CKCGAPNCSGFL 1764
Cdd:cd20073   194 DSkiydLAFFAIKDIPALEELTFDYSgrnnfdqLGFIGNRSNSkyinlknkrpCYCGSANCRGWL 258
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
1636-1742 1.82e-23

SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and similar proteins; LegAS4 is a type IV secretion system effector of Legionella pneumophila. It contains a SET domain that is involved in the modification of Lys4 of histone H3 (H3K4) in the nucleolus of the host cell, thereby enhancing heterochromatic rDNA transcription. It also contains an ankyrin repeat domain of unknown function at its C-terminal region.


Pssm-ID: 380920 [Multi-domain]  Cd Length: 122  Bit Score: 97.41  E-value: 1.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1636 GWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDicnfYMLTLDKD-RIIDAGPKGNESRFMNHSCQPNCETQK 1714
Cdd:cd10522    14 GLGLFAAETIAKGEFVGEYTGEVLDRWEEDRDSVYHYDPL----YPFDLNGDiLVIDAGKKGNLTRFINHSDQPNLELIV 89
                          90       100
                  ....*....|....*....|....*...
gi 292621054 1715 WTVNGDTRVGLFALEDIPKGVELTFNYN 1742
Cdd:cd10522    90 RTLKGEQHIGFVAIRDIKPGEELFISYG 117
PHD1_NSD1_2 cd15648
PHD finger 1 found in nuclear receptor-binding SET domain-containing protein NSD1 and NSD2; ...
1228-1270 3.69e-23

PHD finger 1 found in nuclear receptor-binding SET domain-containing protein NSD1 and NSD2; NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or 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). NSD2, also termed histone-lysine N-methyltransferase NSD2, or 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, by 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). Both NSD1 and NSD2 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 (Cys5HisCysHis). In addition, NSD2 harbors a high mobility group (HMG) box. The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD fingers mediate chromatin interaction and recognition of histone marks. This model corresponds to the first PHD finger.


Pssm-ID: 277118  Cd Length: 43  Bit Score: 93.69  E-value: 3.69e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292621054 1228 VCQVCEKTGELLLCEGQCCGAFHLQCIGLTETPKGRFICQECK 1270
Cdd:cd15648     1 VCQVCEKPGELLLCEGQCCGAFHLDCIGLSEMPSGKFICDECI 43
PWWP_NSD3_rpt1 cd20163
first PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar proteins; ...
286-397 5.94e-23

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: 96.16  E-value: 5.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054  286 YSIGDVVWAKFNRRPWWPCHVTTDPQIDVHTKMkdpSRRPCRLYFVRMFGEIVDQAWVPAKATFPFEGGDQFEKL--PVL 363
Cdd:cd20163     1 FQVGDLVWSKVGTYPWWPCMVSSDPQLEVHTKI---NTRGAREYHVQFFSSQPERAWVHEKRVREYKGHKQYEELlaEAT 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 292621054  364 RRRGRQKEK-DYKYTVPKRLIPSWKASVLEAEASL 397
Cdd:cd20163    78 KQASNHSEKqKIRKPRPQRERAQWDIGIAHAEKAL 112
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
1636-1741 6.94e-23

SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43), also termed lysine N-methyltransferase 6, or ENX-1, or histone-lysine N-methyltransferase EZH2, is a catalytic subunit of the polycomb repressive complex 2 (PRC2)/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. It can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. PRC2 is involved in several cancers; EZH2 is overexpressed in breast, liver and prostate cancer, while point mutations in EZH2 alter the substrate preference and product specificity of PRC2 in Non-Hodgkin lymphomas (NHLs). Thus, PRC2 is a popular target for cancer therapeutics.


Pssm-ID: 380995  Cd Length: 120  Bit Score: 95.75  E-value: 6.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1636 GWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKnAQDNDICNFyMLTLDKDRIIDAGPKGNESRFMNHSCQPNCETQKW 1715
Cdd:cd19218    15 GWGIFIKDPVQKNEFISEYCGEIISQDEADRRGK-VYDKYMCSF-LFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVM 92
                          90       100
                  ....*....|....*....|....*.
gi 292621054 1716 TVNGDTRVGLFALEDIPKGVELTFNY 1741
Cdd:cd19218    93 MVNGDHRIGIFAKRAIQTGEELFFDY 118
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
1600-1764 3.83e-22

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 homolog 1 (SUV39H1) and similar proteins; SUV39H1 (EC 2.1.1.43; also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A (KMT1A), position-effect variegation 3-9 homolog (SUV39H), or Su(var)3-9 homolog 1) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. It mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions.


Pssm-ID: 380923 [Multi-domain]  Cd Length: 255  Bit Score: 98.04  E-value: 3.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1600 LYECHSQvCPAGERCQNQSFTKRQYTEVEIFRTLS-RGWGLRSISDIKKGAFVNEYVGEVI--DEEECRSRIKNAQDNDi 1676
Cdd:cd10525    62 IYECNSR-CRCGPDCPNRVVQKGIQYDLCIFRTDNgRGWGVRTLEKIRKNSFVMEYVGEIItsEEAERRGQIYDRQGAT- 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1677 cnfYMLTLD--KD-RIIDAGPKGNESRFMNHSCQPNceTQKWTVNGDT------RVGLFALEDIPKGVELTFNYNLEC-- 1745
Cdd:cd10525   140 ---YLFDLDyvEDvYTVDAAYYGNISHFVNHSCDPN--LQVYNVFIDNlderlpRIALFATRTIRAGEELTFDYNMQVdp 214
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 292621054 1746 -----------LGNG----------KTVCKCGAPNCSGFL 1764
Cdd:cd10525   215 vdaestkmdsnFGLAglpgspkkrvRIECKCGVRSCRKYL 254
PWWP_NSD2_rpt1 cd20162
first PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins; ...
286-397 8.67e-22

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: 93.05  E-value: 8.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054  286 YSIGDVVWAKFNRRPWWPCHVTTDPQIDVHTKMKDpSRRPCRLYFVRMFGEIVDQAWVPAKATFPFEGGDQFEKL--PVL 363
Cdd:cd20162     1 YNVGDLVWSKVSGYPWWPCMVSADPLLHSHTKLKG-QKKSARQYHVQFFGDAPERAWIFEKSLVPFEGEGQFEQLcqESA 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 292621054  364 RRRGRQKEKD-YKYTVPKRLIPSWKASVLEAEASL 397
Cdd:cd20162    80 KQAPTKAEKIkLLKPISGKLRAQWDMGIVQAEEAA 114
PHD5_NSD cd15568
PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
1802-1844 1.45e-21

PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family 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 to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant 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 (Cys5HisCysHis). This model corresponds to the fifth PHD finger.


Pssm-ID: 277043 [Multi-domain]  Cd Length: 43  Bit Score: 89.31  E-value: 1.45e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292621054 1802 ECFYCGDGGQIVSCKKPGCPKVYHADCLNLSKRPAGRWECPWH 1844
Cdd:cd15568     1 ECFRCGDGGDLVLCDFKGCPKVYHLSCLGLEKPPGGKWICPWH 43
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
1599-1760 1.95e-21

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase 1 (EHMT1) and similar proteins; EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, or lysine N-methyltransferase 1D (KMT1D)) acts as a histone-lysine N-methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin.


Pssm-ID: 380933 [Multi-domain]  Cd Length: 231  Bit Score: 95.38  E-value: 1.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1599 LLYEChSQVCPAGERCQNQSFTKRQYTEVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAqdndicn 1678
Cdd:cd10535    66 LIFEC-NHACSCWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDS------- 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1679 fYMLTLD-KDR---IIDAGPKGNESRFMNHSCQPN-CETQKWTVNGD---TRVGLFALEDIPKGVELTFNYNLECLG-NG 1749
Cdd:cd10535   138 -YLFDLDnKDGevyCIDARFYGNVSRFINHHCEPNlVPVRVFMAHQDlrfPRIAFFSTRLIEAGEQLGFDYGERFWDiKG 216
                         170
                  ....*....|..
gi 292621054 1750 KTV-CKCGAPNC 1760
Cdd:cd10535   217 KLFsCRCGSPKC 228
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
1627-1764 4.03e-21

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) and similar proteins; KMT2A (EC2.1.1.43; also termed lysine N-methyltransferase 2A, ALL-1, CXXC-type zinc finger protein 7 (CXXC7), myeloid/lymphoid or mixed-lineage leukemia (MLL), myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), trithorax-like protein (TRX1), or zinc finger protein HRX) acts as a histone methyltransferase that plays an essential role in early development and hematopoiesis. It is a catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac).


Pssm-ID: 380983 [Multi-domain]  Cd Length: 154  Bit Score: 92.01  E-value: 4.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1627 VEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDIcNFYMLTLDKDRIIDAGPKGNESRFMNHSC 1706
Cdd:cd19206    16 VGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKYYDSKGI-GCYMFRIDDSEVVDATMHGNAARFINHSC 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1707 QPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYN--LECLGNgKTVCKCGAPNCSGFL 1764
Cdd:cd19206    95 EPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKfpIEDASN-KLPCNCGAKKCRKFL 153
PHD4_NSD1 cd15656
PHD finger 4 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...
1392-1431 6.92e-21

PHD finger 4 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or 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 (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fourth PHD finger.


Pssm-ID: 277126  Cd Length: 40  Bit Score: 87.38  E-value: 6.92e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 292621054 1392 WCFVCSEGGSLLCCESCPAAFHRECLNIEMPQGSWFCNDC 1431
Cdd:cd15656     1 WCFVCSEGGSLLCCESCPAAFHRECLNIDMPEGSWYCNDC 40
PHD4_NSD2 cd15657
PHD finger 4 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed ...
1392-1432 5.89e-20

PHD finger 4 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed histone-lysine N-methyltransferase NSD2, or 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, by 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 fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD fingers mediate chromatin interaction and recognition of histone marks. This model corresponds to the fourth PHD finger.


Pssm-ID: 277127  Cd Length: 41  Bit Score: 84.67  E-value: 5.89e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 292621054 1392 WCFVCSEGGSLLCCESCPAAFHRECLNIEMPQGSWFCNDCR 1432
Cdd:cd15657     1 WCFVCSKGGSLLCCESCPAAFHPDCLNIEMPDGSWFCNDCR 41
SET_EZH-like cd19168
SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb ...
1630-1741 6.03e-20

SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb repressive complex 2 (PRC2), and similar proteins; The family includes EZH1 and EZH2. EZH1 (EC 2.1.1.43; also termed ENX-2, or histone-lysine N-methyltransferase EZH1) is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. EZH2 (EC 2.1.1.43; also termed lysine N-methyltransferase 6, ENX-1, or histone-lysine N-methyltransferase EZH2) is a catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Both EZH1 and EZH2 can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. PRC2 is involved in several cancers; EZH2 is overexpressed in breast, liver and prostate cancer, while point mutations in EZH2 alter the substrate preference and product specificity of PRC2 in Non-Hodgkin lymphomas (NHLs). Thus, PRC2 is a popular target for cancer therapeutics.


Pssm-ID: 380945  Cd Length: 124  Bit Score: 87.63  E-value: 6.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1630 FRTLSRGWGLRSISDIKKGAFVNEYVGEVI--DEEECRSRIknaqDNDICNFYMLTLDKDRIIDAGPKGNESRFMNHSCQ 1707
Cdd:cd19168     7 KSQLECGLGLFAAEDIKEGEFVIEYTGELIshDEGVRREHR----RGDVSYLYLFEEQEGIWVDAAIYGNLSRYINHATD 82
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 292621054 1708 P----NCETQKWTVNGDTRVGLFALEDIPKGVELTFNY 1741
Cdd:cd19168    83 KvktgNCMPKIMYVNHEWRIKFTAIKDIKIGEELFFNY 120
PHD4_NSD3 cd15658
PHD finger 4 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...
1392-1431 6.37e-20

PHD finger 4 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed histone-lysine N-methyltransferase NSD3, or protein whistle, or 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 fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fourth PHD finger.


Pssm-ID: 277128  Cd Length: 40  Bit Score: 84.58  E-value: 6.37e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 292621054 1392 WCFVCSEGGSLLCCESCPAAFHRECLNIEMPQGSWFCNDC 1431
Cdd:cd15658     1 FCFVCARGGRLLCCESCPASFHPECLSIEMPEGCWNCNEC 40
PHD4_NSD cd15567
PHD finger 4 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
1392-1431 1.42e-19

PHD finger 4 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family 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 to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant 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 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 (Cys5HisCysHis). This model corresponds to the fourth PHD finger.


Pssm-ID: 277042 [Multi-domain]  Cd Length: 41  Bit Score: 83.45  E-value: 1.42e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 292621054 1392 WCFVCSEGGSLLCCESCPAAFHRECLNIE-MPQGSWFCNDC 1431
Cdd:cd15567     1 WCFICSEGGSLICCESCPASFHPECLGLEpPPEGKFYCEDC 41
PHD3_NSD2 cd15654
PHD finger 3 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed ...
1323-1375 1.46e-19

PHD finger 3 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed histone-lysine N-methyltransferase NSD2, or 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, by 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 fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD fingers mediate chromatin interaction and recognition of histone marks. This model corresponds to the third PHD finger.


Pssm-ID: 277124  Cd Length: 54  Bit Score: 83.74  E-value: 1.46e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 292621054 1323 CLSCYITNPNNPGISKGRLTRCVRCPVAYHANDYCMAAGSVPLANNSFLCPNH 1375
Cdd:cd15654     2 CVSCHASNPSNPRATKGKMMRCVRCPVAYHGGDLCIAAGCAVLTSNSIICTNH 54
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
1621-1764 4.50e-19

SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and similar proteins; SETD1B (EC2.1.1.43), also termed lysine N-methyltransferase 2G, is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me) when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. Loss of SETD1B occurs in up to half the gastric and colorectal cancers, most commonly via SETD1B mutations, while de novo variants in SETD1B are associated with intellectual disability, epilepsy and autism.


Pssm-ID: 380982 [Multi-domain]  Cd Length: 153  Bit Score: 85.88  E-value: 4.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1621 KRQYTEVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICNFYMLTLDKDRIIDAGPKGNESR 1700
Cdd:cd19205    10 KFRKKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGIGSSYMFRVDHDTIIDATKCGNFAR 89
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 292621054 1701 FMNHSCQPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYNLEcLGNGKTVCKCGAPNCSGFL 1764
Cdd:cd19205    90 FINHSCNPNCYAKVITVESQKKIVIYSKQHINVNEEITYDYKFP-IEDVKIPCLCGSENCRGTL 152
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
1636-1741 4.89e-19

SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43), also termed ENX-2, or histone-lysine N-methyltransferase EZH1, is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. It can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively.


Pssm-ID: 380994  Cd Length: 136  Bit Score: 85.50  E-value: 4.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1636 GWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKnAQDNDICNFyMLTLDKDRIIDAGPKGNESRFMNHSCQPNCETQKW 1715
Cdd:cd19217    17 GWGTFIKESVQKNEFISEYCGELISQDEADRRGK-VYDKYMSSF-LFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVV 94
                          90       100
                  ....*....|....*....|....*.
gi 292621054 1716 TVNGDTRVGLFALEDIPKGVELTFNY 1741
Cdd:cd19217    95 MVNGDHRIGIFAKRAIQQGEELFFDY 120
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
1599-1760 5.52e-19

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase 2 (EHMT2) and similar proteins; EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C (KMT1C), or protein G9a) acts as a histone-lysine N-methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin.


Pssm-ID: 380931 [Multi-domain]  Cd Length: 239  Bit Score: 88.54  E-value: 5.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1599 LLYEChSQVCPAGERCQNQSFTKRQYTEVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRiknaQDNDicn 1678
Cdd:cd10533    66 LIFEC-NQACSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR----EDDS--- 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1679 fYMLTLD-KD---RIIDAGPKGNESRFMNHSCQPN-CETQKWTVNGD---TRVGLFALEDIPKGVELTFNY--NLECLGN 1748
Cdd:cd10533   138 -YLFDLDnKDgevYCIDARYYGNISRFINHLCDPNiIPVRVFMLHQDlrfPRIAFFSSRDIRTGEELGFDYgdRFWDIKS 216
                         170
                  ....*....|..
gi 292621054 1749 GKTVCKCGAPNC 1760
Cdd:cd10533   217 KYFTCQCGSEKC 228
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
1437-1499 1.01e-18

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 81.62  E-value: 1.01e-18
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 292621054   1437 PHYKDILWVKVGRYRWWPAEVTQPKSVPENISRMKHEVGEFPVHFFGSKDYVWTYQARCFPYM 1499
Cdd:smart00293    1 FKPGDLVWAKMKGFPWWPALVISPKMTPDNIMKRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
1600-1764 2.60e-18

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), SET domain bifurcated 2 (SETDB2), and similar proteins; SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis.


Pssm-ID: 380939 [Multi-domain]  Cd Length: 236  Bit Score: 86.44  E-value: 2.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1600 LYEChSQVCPAGER-CQNQSFTKRQYTEVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECrsrikNAQDNDICN 1678
Cdd:cd10541    67 VYEC-NKLCKCDPNmCQNRLVQHGLQVRLQLFKTQNKGWGIRCLDDIAKGTFVCIYAGKILTDDFA-----DKEGLEMGD 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1679 FYMLTLDKDR----IIDAGPKGNESRFMNHSCQPNCETQKWTVNGDTR----VGLFALEDIPKGVELTFNYNLEC--LGN 1748
Cdd:cd10541   141 EYFANLDHIEescyIIDAKLEGNLGRYLNHSCSPNLFVQNVFVDTHDLrfpwVAFFASKRIKAGTELTWDYNYEVgsVEG 220
                         170
                  ....*....|....*.
gi 292621054 1749 GKTVCKCGAPNCSGFL 1764
Cdd:cd10541   221 KELLCCCGSNECRGRL 236
C5HCH pfam17982
NSD Cys-His rich domain; This is an NSD-specific Cys-His rich region (C5HCH) domain. Family ...
1843-1892 4.04e-18

NSD Cys-His rich domain; This is an NSD-specific Cys-His rich region (C5HCH) domain. Family members include NSD3 (nuclear receptor SET domain-containing) proteins. This domain is located on the C-terminal of NSD1, 2 and 3 proteins. C5HCH domain lies adjacent to the fifth plant homeodomain (PHD5). The PHD5-C5HCH module of NSD3 (PHD5-C5HCHNSD3) recognizes the H3 N-terminal peptide containing unmodified K4 and trimethylated K9. Moreover, it has been reported that the PHD5-C5HCH module of NSD1 (PHD5-C5HCH) was the sole region required for tight binding of the NUP98-NSD1 fusion protein to the HoxA9 gene promoter, implicating that PHD5-C5HCH might have chromatin targeting ability.


Pssm-ID: 465605  Cd Length: 50  Bit Score: 79.82  E-value: 4.04e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 292621054  1843 WHQCNECGREAASYCEMCPNSYCEQHREGMLFISKLDGKLSCSEHDPCGP 1892
Cdd:pfam17982    1 WHQCSVCGSPATSFCEFCPSSFCKDHEKGALVPSALEGRLCCSEHDPESP 50
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
1627-1764 5.87e-18

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) and similar proteins; KMT2D (EC2.1.1.43; also termed lysine N-methyltransferase 2D, ALL1-related protein (ALR), or myeloid/lymphoid or mixed-lineage leukemia protein 2 (MLL2)), acts as histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me). It is a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription. KMT2D is a subunit of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation.


Pssm-ID: 380986 [Multi-domain]  Cd Length: 155  Bit Score: 82.82  E-value: 5.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1627 VEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEEC--RSRIKNAQDNDIcnfYMLTLDKDRIIDAGPKGNESRFMNH 1704
Cdd:cd19209    18 VYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVAnrREKIYEEQNRGI---YMFRINNEHVIDATLTGGPARYINH 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 292621054 1705 SCQPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYNLECLGNGKTV-CKCGAPNCSGFL 1764
Cdd:cd19209    95 SCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIpCHCGAWNCRKWM 155
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
1637-1764 9.20e-18

SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and similar proteins; SETD1A (EC2.1.1.43), also termed lysine N-methyltransferase 2F, or Set1/Ash2 histone methyltransferase complex subunit SET1, is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me), when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. Human SET domain containing protein 1A (hSETD1A) expression occurs at a high rate in hepatocellular carcinoma patients and controls tumor metastasis in breast cancer by activating MMP expression.


Pssm-ID: 380981 [Multi-domain]  Cd Length: 153  Bit Score: 82.38  E-value: 9.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1637 WGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDICNFYMLTLDKDRIIDAGPKGNESRFMNHSCQPNCETQKWT 1716
Cdd:cd19204    26 WGLFAMEPIAADEMVIEYVGQNIRQVVADMREKRYVQEGIGSSYLFRVDHDTIIDATKCGNLARFINHCCTPNCYAKVIT 105
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 292621054 1717 VNGDTRVGLFALEDIPKGVELTFNYNLEcLGNGKTVCKCGAPNCSGFL 1764
Cdd:cd19204   106 IESQKKIVIYSKQPIGVNEEITYDYKFP-IEDNKIPCLCGTENCRGTL 152
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
1625-1764 1.62e-17

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) and similar proteins; KMT2C (EC2.1.1.43; also termed lysine N-methyltransferase 2C, homologous to ALR protein (HALR) myeloid/lymphoid, or mixed-lineage leukemia protein 3 (MLL3)), acts as a histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me) and may be involved in leukemogenesis and developmental disorder. KMT2C is a catalytic subunit of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation. Overexpression of KMT2C is associated with estrogen receptor-positive breast cancer; KMT2C mediates the estrogen dependence of breast cancer through regulation of estrogen receptor alpha (ERalpha) enhancer function. KMT2C is frequently mutated in certain populations with diffuse-type gastric adenocarcinomas (DGA); its loss promotes epithelial-to-mesenchymal transition (EMT) and is associated with worse overall survival.


Pssm-ID: 380985 [Multi-domain]  Cd Length: 154  Bit Score: 81.60  E-value: 1.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1625 TEVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEEC--RSRIKNAQDNDIcnfYMLTLDKDRIIDAGPKGNESRFM 1702
Cdd:cd19208    15 SNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVAnrKEKLYESQNRGV---YMFRIDNDHVIDATLTGGPARYI 91
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 292621054 1703 NHSCQPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYNLECLGNG-KTVCKCGAPNCSGFL 1764
Cdd:cd19208    92 NHSCAPNCVAEVVTFEKGHKIIISSSRRIQKGEELCYDYKFDFEDDQhKIPCHCGAVNCRKWM 154
PHD5_NSD3 cd15661
PHD finger 5 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...
1803-1844 1.89e-17

PHD finger 5 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed histone-lysine N-methyltransferase NSD3, or protein whistle, or 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 fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fifth PHD finger.


Pssm-ID: 277131  Cd Length: 43  Bit Score: 77.70  E-value: 1.89e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 292621054 1803 CFYCGDGGQIVSCKKPGCPKVYHADCLNLSKRPAGRWECPWH 1844
Cdd:cd15661     2 CFQCGDGGELVMCDKKDCPKAYHLLCLNLTQPPYGKWECPWH 43
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
1627-1764 4.93e-17

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) and similar proteins; KMT2B (EC2.1.1.43; also termed lysine N-methyltransferase 2B, myeloid/lymphoid or mixed-lineage leukemia protein 4 (MLL2/MLL4), trithorax homolog 2 (TRX2), or WW domain-binding protein 7 (WBP-7)), acts as a histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me). It is required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that precedes resumption of meiosis, oocyte survival and normal zygotic genome activation.


Pssm-ID: 380984 [Multi-domain]  Cd Length: 154  Bit Score: 80.07  E-value: 4.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1627 VEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVIDEEECRSRIKNAQDNDIcNFYMLTLDKDRIIDAGPKGNESRFMNHSC 1706
Cdd:cd19207    16 VGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDSKGI-GCYMFRIDDFDVVDATMHGNAARFINHSC 94
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 292621054 1707 QPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYNLECL-GNGKTVCKCGAPNCSGFL 1764
Cdd:cd19207    95 EPNCYSRVIHVEGQKHIVIFALRKIYRGEELTYDYKFPIEdASNKLPCNCGAKRCRRFL 153
PHD5_NSD2 cd15660
PHD finger 5 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed ...
1802-1844 4.97e-17

PHD finger 5 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed histone-lysine N-methyltransferase NSD2, or 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, by 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 fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD fingers mediate chromatin interaction and recognition of histone marks. This model corresponds to the fifth PHD finger.


Pssm-ID: 277130  Cd Length: 43  Bit Score: 76.51  E-value: 4.97e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292621054 1802 ECFYCGDGGQIVSCKKPGCPKVYHADCLNLSKRPAGRWECPWH 1844
Cdd:cd15660     1 ECFRCGDGGQLVLCDRKSCTKAYHLSCLGLTKRPFGKWECPWH 43
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
1600-1764 1.15e-16

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) and similar proteins; SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis.


Pssm-ID: 380921 [Multi-domain]  Cd Length: 266  Bit Score: 82.19  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1600 LYECHSQVCPAGERCQNQSFTKRQYTEVEIFRTLSRGWGLRSISDIKKGAFVNEYVGEVI------DEEECRSRIKNAQD 1673
Cdd:cd10523    83 LYECNVSCKCNRMLCQNRVVQHGLQVRLQVFKTEKKGWGVRCLDDIDKGTFVCIYAGRVLsrarspTEPLPPKLELPSEN 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1674 NDICNFYMLTLDKDR-------IIDAGPKGNESRFMNHSCQPNCETQKWTVNGDTR----VGLFALEDIPKGVELTFNYN 1742
Cdd:cd10523   163 EVEVVTSWLILSKKRklrenvcFLDASKEGNVGRFLNHSCCPNLFVQNVFVDTHDKnfpwVAFFTNRVVKAGTELTWDYS 242
                         170       180
                  ....*....|....*....|....
gi 292621054 1743 LE--CLGNGKTVCKCGAPNCSGFL 1764
Cdd:cd10523   243 YDagTSPEQEIPCLCGVNKCQKKI 266
PHD1_NSD cd15564
PHD finger 1 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
1228-1270 1.39e-16

PHD finger 1 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family 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 to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they non-redundant 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 (Cys5HisCysHis). This model corresponds to the first PHD finger.


Pssm-ID: 277039  Cd Length: 43  Bit Score: 75.06  E-value: 1.39e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292621054 1228 VCQVCEKTGELLLCEGQCCGAFHLQCIGLTETPKGRFICQECK 1270
Cdd:cd15564     1 VCQICEKPGKLLTCEGPCCGHFHLDCLGLSEQPDEPFKCDECT 43
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
1638-1742 2.30e-16

SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar proteins; SETD5 is a probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. KMT2E (also termed inactive lysine N-methyltransferase 2E or myeloid/lymphoid or mixed-lineage leukemia protein 5 (MLL5)) associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription. The family also includes Saccharomyces cerevisiae SET domain-containing proteins, SET3 and SET4, and Schizosaccharomyces pombe SET3. Most of these family members contain a post-SET domain which harbors a zinc-binding site.


Pssm-ID: 380927  Cd Length: 127  Bit Score: 77.31  E-value: 2.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1638 GLRSISDIKKGAFVNEYVGEVIDEEECRSRikNAQDNDICNF---YMLTLDKDRIIDAGPKGNESRFMNHSCQPNCETQK 1714
Cdd:cd10529    18 GLVATEDISPGEPILEYKGEVSLRSEFKED--NGFFKRPSPFvffYDGFEGLPLCVDARKYGNEARFIRRSCRPNAELRH 95
                          90       100       110
                  ....*....|....*....|....*....|.
gi 292621054 1715 WTVNGDT-RVGLFALEDIPKGVELT--FNYN 1742
Cdd:cd10529    96 VVVSNGElRLFIFALKDIRKGTEITipFDYD 126
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
1626-1742 3.95e-16

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, Enhancer-of-zeste, Trithorax (SET) domain superfamily corresponds to SET domain-containing lysine methyltransferases, which catalyze site and state-specific methylation of lysine residues in histones that are fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains has been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as N-SET and C-SET. C-SET forms an unusual and conserved knot-like structure of probable functional importance. In addition to N-SET and C-SET, an insert region (I-SET) and flanking regions of high structural variability form part of the overall structure. Some family members contain a pre-SET domain, which is found in a number of histone methyltransferases (HMTase), and a post-SET domain, which harbors a zinc-binding site.


Pssm-ID: 380914 [Multi-domain]  Cd Length: 72  Bit Score: 74.59  E-value: 3.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1626 EVEIFRTLSRGWGLRSISDIKKGafvnEYVGEvideeecrsriknaqdndicnfymltldkdriidagpkgneSRFMNHS 1705
Cdd:cd08161     1 EIRPSTIPGAGFGLFATRDIPKG----EVIGL-----------------------------------------ARFINHS 35
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 292621054 1706 CQPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYN 1742
Cdd:cd08161    36 CEPNCEFEEVYVGGKPRVFIVALRDIKAGEELTVDYG 72
SET_SETD8 cd10528
SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...
1636-1741 1.47e-15

SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2.1.1.43; also termed N-lysine methyltransferase KMT5A, H4-K20-HMTase KMT5A, lysine N-methyltransferase 5A, lysine-specific methylase 5A, PR/SET domain-containing protein 07, PR-Set7 or PR/SET07) is a nucleosomal histone-lysine N-methyltransferase that specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). It plays a central role in the silencing of euchromatic genes.


Pssm-ID: 380926 [Multi-domain]  Cd Length: 141  Bit Score: 75.31  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1636 GWGLRSISDIKKGAFVNEYVGEVIDEEECRSR-IKNAQDNDI-CnfYML---TLDKDRIIDA-GPKGNESRFMNHSCQ-P 1708
Cdd:cd10528    28 GRGVIATRPFEKGDFVVEYHGDLITITEAKKReALYAKDPSTgC--YMYyfqYKGKTYCVDAtKESGRLGRLINHSKKkP 105
                          90       100       110
                  ....*....|....*....|....*....|...
gi 292621054 1709 NCETQKWTVNGDTRVGLFALEDIPKGVELTFNY 1741
Cdd:cd10528   106 NLKTKLLVIDGVPHLILVAKRDIKPGEELLYDY 138
PHD1_NSD3 cd15649
PHD finger 1 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...
1228-1270 2.69e-15

PHD finger 1 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed histone-lysine N-methyltransferase NSD3, or protein whistle, or 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 fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the first PHD finger.


Pssm-ID: 277119  Cd Length: 44  Bit Score: 71.34  E-value: 2.69e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 292621054 1228 VCQVCEKTGE-LLLCEGQCCGAFHLQCIGLTETPKGRFICQECK 1270
Cdd:cd15649     1 VCQVCESFGEsLVTCEGECCGLFHLECLGLTSLPDEKFICQECK 44
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
289-375 1.05e-13

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: 68.61  E-value: 1.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054   289 GDVVWAKFNRRPWWPCHVTTDPQIDVHTKMKDPSRrpcRLYFVRMFGEIvDQAWVPAKATFPFEGGDQFEKLpvLRRRGR 368
Cdd:pfam00855    1 GDLVWAKLKGYPWWPARVVDPEELPENVLKPKKKD---GEYLVRFFGDS-EFAWVKPKDLKPFDEGDEFEYL--KKKKKK 74

                   ....*..
gi 292621054   369 QKEKDYK 375
Cdd:pfam00855   75 KKKKAFK 81
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
1441-1524 1.06e-13

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: 68.29  E-value: 1.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1441 DILWVKVGRYRWWPAEVTQPKSVPENIsRMKHEVGEFPVHFFGSKDYVWTYQARCFPYmEGDANNKEKMGKGADAVYKKA 1520
Cdd:cd05162     2 DLVWAKLKGYPWWPARVVDPEELPEEV-GKKKKKGGVLVQFFGDNDYAWVKSKNIKPF-EEGFKKEFKKKKKKSKKFKKA 79

                  ....
gi 292621054 1521 LNEA 1524
Cdd:cd05162    80 VEEA 83
PHD2_NSD2 cd15651
PHD finger 2 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed ...
1275-1321 1.72e-13

PHD finger 2 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed histone-lysine N-methyltransferase NSD2, or 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, by 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 fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD fingers mediate chromatin interaction and recognition of histone marks. This model corresponds to the second PHD finger.


Pssm-ID: 277121  Cd Length: 47  Bit Score: 66.40  E-value: 1.72e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 292621054 1275 TCFVCKKPDKEVRRCMIPVCGKFYHMDCILKYSPTVAQNRGFRCSIH 1321
Cdd:cd15651     1 SCFVCKESKGDVKRCVVLHCGKFYHEACVRKYPLTVFENRGFRCPLH 47
AWS pfam17907
AWS domain; This entry represents the AWS (associated with SET domain) domain. This is a zinc ...
1584-1622 5.94e-13

AWS domain; This entry represents the AWS (associated with SET domain) domain. This is a zinc binding domain. The full AWS domain contains 8 cysteines. This entry represents the N-terminal part of the domain, with the C-terminal part interwoven with the SET domain.


Pssm-ID: 465559  Cd Length: 39  Bit Score: 64.75  E-value: 5.94e-13
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 292621054  1584 DENPCGIDSECINRMLLYECHSQVCPAGERCQNQSFTKR 1622
Cdd:pfam17907    1 DDPPCGCGSDCINRMLFVECTPKTCPCGESCQNQRFQRK 39
PWWP_AtATX3-like cd20143
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
1441-1526 1.44e-12

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: 65.47  E-value: 1.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1441 DILWVKVGRYRWWPAEVTQPKSVPENiSRMKHEVGEFPVHFFG---SKDYVWTYQARCFPYMEGDA--NNKEKMGKGADA 1515
Cdd:cd20143     4 DLVWAKVGTHPFWPARVVEPAEQAEE-VRRRCVPGSLCVYFFGpggSRDYGWVRRSMIFPFTDDLArfQTQKIKNKKRPQ 82
                          90
                  ....*....|.
gi 292621054 1516 VYKKALNEAAD 1526
Cdd:cd20143    83 EFQEALEEAKL 93
PWWP_ZCWPW1 cd20145
PWWP domain found in zinc finger CW-type PWWP domain protein 1 (ZCWPW1) and similar proteins; ...
285-397 1.51e-12

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: 66.03  E-value: 1.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054  285 KYSIGDVVWAKFNRRPWWPCHVTTDPQIDVHTKMKDPSRRPCRlYFVRMFGEIVDQAWVPAKATFPfeggdqFEKLPVLR 364
Cdd:cd20145     5 KYTPGSLVWAKMPGYPWWPAMVEDDPDTEEFFWLDEESDIPTK-YHVTFFDKPVSRAWVRASSIKP------FTDNSNEP 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 292621054  365 RRGRQKEKDYKytvpKRLipswKASVLEAEASL 397
Cdd:cd20145    78 NLTKKKGKKYK----KRL----NEAVEMAREAL 102
PHD3_NSD cd15566
PHD finger 3 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
1322-1375 1.16e-11

PHD finger 3 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family 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 to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant 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 (Cys5HisCysHis). This model corresponds to the third PHD finger.


Pssm-ID: 277041  Cd Length: 48  Bit Score: 61.29  E-value: 1.16e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 292621054 1322 VCLSCYITNPNnpgiSKGRLTRCVRCPVAYHANdyCMAAGSVPLANNSFLCPNH 1375
Cdd:cd15566     1 TCATCEASGDG----SSGKLVRCIRCPRAYHAG--CIPAGSKLLNKKLIICPKH 48
PHD2_CHD_II cd15532
PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...
1393-1431 1.60e-11

PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD proteins includes chromodomain-helicase-DNA-binding protein CHD3, CHD4, and CHD5, which are nuclear and ubiquitously expressed chromatin remodelling ATPases generally associated with histone deacetylases (HDACs). They are involved in DNA Double Strand Break (DSB) signaling, DSB repair and/or p53-dependent pathways such as apoptosis and senescence, as well as in the maintenance of genomic stability, and/or cancer prevention. They function as subunits of the Nucleosome Remodelling and Deacetylase (NuRD) complex, which is generally associated with gene repression, heterochromatin formation, and overall chromatin compaction. In contrast to the class I CHD enzymes (CHD1 and CHD2), class II CHD proteins lack identifiable DNA-binding domains, but possess a C-terminal coiled-coil region. Moreover, in addition to the tandem chromodomains and a helicase domain, they all harbor tandem plant homeodomain (PHD) zinc fingers involved in the recognition of methylated histone tails. This model corresponds to the second PHD finger.


Pssm-ID: 277007 [Multi-domain]  Cd Length: 43  Bit Score: 60.76  E-value: 1.60e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 292621054 1393 CFVCSEGGSLLCCESCPAAFHRECLN---IEMPQGSWFCNDC 1431
Cdd:cd15532     2 CRVCKDGGELLCCDGCPSSYHLHCLNpplAEIPDGDWFCPRC 43
PHD1_AIRE cd15539
PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune ...
1393-1431 4.47e-11

PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune polyendocrinopathy candidiasis ectodermal dystrophy (APECED) protein, functions as a regulator of gene transcription in the thymus. It is essential for prevention of autoimmunity. AIRE plays a critical role in the induction of central tolerance. It promotes self-tolerance through tissue-specific antigen (TSA) expression. It also acts as an active regulator of chondrocyte differentiation. AIRE contains a homogeneously-staining region (HSR) or caspase-recruitment domain (CARD), a nuclear localization signal (NLS), a SAND (for Sp100, AIRE, nuclear phosphoprotein 41/75 or NucP41/75, and deformed epidermal auto regulatory factor 1 or Deaf1) domain, two plant homeodomain (PHD) fingers, and four LXXLL (where L stands for leucine) motifs. This model corresponds to the first PHD finger that recognizes the unmethylated tail of histone H3 and targets AIRE-dependent genes.


Pssm-ID: 277014 [Multi-domain]  Cd Length: 43  Bit Score: 59.39  E-value: 4.47e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 292621054 1393 CFVCSEGGSLLCCESCPAAFHRECLNI---EMPQGSWFCNDC 1431
Cdd:cd15539     2 CAVCGDGGELLCCDGCPRAFHLACLVPpltLIPSGTWRCSSC 43
AWS smart00570
associated with SET domains; subdomain of PRESET
1574-1624 5.70e-11

associated with SET domains; subdomain of PRESET


Pssm-ID: 197795  Cd Length: 50  Bit Score: 59.34  E-value: 5.70e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 292621054   1574 EIPRCNCKAT--DENPCGidSECINRMLLYEChSQVCPAGERCQNQSFTKRQY 1624
Cdd:smart00570    1 DIMTCECKPTddDETACG--SDCLNRMLFIEC-SSSCPCGSYCSNQRFQKRQY 50
PHD2_NSD3 cd15652
PHD finger 2 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...
1275-1321 1.79e-10

PHD finger 2 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed histone-lysine N-methyltransferase NSD3, or protein whistle, or 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 fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the second PHD finger.


Pssm-ID: 277122  Cd Length: 47  Bit Score: 57.96  E-value: 1.79e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 292621054 1275 TCFVCKKPDKEVRRCMIPVCGKFYHMDCILKYSPTVAQNRGFRCSIH 1321
Cdd:cd15652     1 PCFSCKVPGKDVKRCSVNACGRFYHEACVRKYTTSAFESKGFRCPQH 47
PHD2_NSD cd15565
PHD finger 2 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
1275-1321 1.91e-10

PHD finger 2 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family 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 to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant 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 (Cys5HisCysHis). This model corresponds to the second PHD finger.


Pssm-ID: 277040  Cd Length: 51  Bit Score: 57.82  E-value: 1.91e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 292621054 1275 TCFVCKKP---DKEVRRCMIPVCGKFYHMDCILKYSPT-VAQNRGFRCSIH 1321
Cdd:cd15565     1 SCFVCKKLgsvGGEVFKCSVASCGKFYHEECLKKWPLTtISDSKKFRCPLH 51
PWWP_MSH6 cd05837
PWWP domain found in DNA mismatch repair protein MSH6 and similar proteins; MSH6, also called ...
286-397 2.83e-10

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: 59.22  E-value: 2.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054  286 YSIGDVVWAKFNRRPWWPCHVTTDPQIDVHTKMKDPSRrpcrlYFVRMFGEIVDQAWVPAKATFPFEGGDQFEklpvLRR 365
Cdd:cd05837     1 FSPGDLVWAKLEGYPWWPSLVCNHPTTGFHKKFGKKGE-----VHVQFFDDPPSRAWVKAKNVKPFTGSDDKE----FQK 71
                          90       100       110
                  ....*....|....*....|....*....|..
gi 292621054  366 RGRQKEKDykytvpkrliPSWKASVLEAEASL 397
Cdd:cd05837    72 GGMFFSKD----------PKWKKAVKEADKAL 93
PHD1_PHF12 cd15533
PHD finger 1 found in PHD finger protein 12 (PHF12); PHF12, also termed PHD factor 1 (Pf1), is ...
1393-1431 3.86e-10

PHD finger 1 found in PHD finger protein 12 (PHF12); PHF12, also termed PHD factor 1 (Pf1), is a plant homeodomain (PHD) zinc finger-containing protein that bridges the transducin-like enhancer of split (TLE) corepressor to the mSin3A-histone deacetylase (HDAC)-complex, and further represses transcription at targeted genes. PHF12 also interacts with MRG15 (mortality factor-related genes on chromosome 15), a member of the mortality factor (MORF) family of proteins implicated in regulating cellular senescence. PHF12 contains two plant-homeodomain (PHD) zinc fingers followed by a polybasic region. The PHD fingers function downstream of phosphoinositide signaling triggered by the interaction between polybasic regions and phosphoinositides. This model corresponds to the first PHD finger.


Pssm-ID: 277008 [Multi-domain]  Cd Length: 45  Bit Score: 56.98  E-value: 3.86e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 292621054 1393 CFVCSEGGSLLCCESCPAAFHRECLN-----IEMPQGSWFCNDC 1431
Cdd:cd15533     2 CDSCGEGGDLLCCDRCPASFHLQCCNppldeEDLPPGEWLCHRC 45
PHD3_NSD3 cd15655
PHD finger 3 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...
1337-1375 1.03e-09

PHD finger 3 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed histone-lysine N-methyltransferase NSD3, or protein whistle, or 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 fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the third PHD finger.


Pssm-ID: 277125  Cd Length: 53  Bit Score: 56.05  E-value: 1.03e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 292621054 1337 SKGRLTRCVRCPVAYHANDYCMAAGSVPLANNSFLCPNH 1375
Cdd:cd15655    15 SKGRMMRCLRCPVAYHTGDGCVAAGSVLVTPHIIICSNH 53
PHD5_NSD cd15568
PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
1392-1428 3.13e-09

PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family 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 to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant 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 (Cys5HisCysHis). This model corresponds to the fifth PHD finger.


Pssm-ID: 277043 [Multi-domain]  Cd Length: 43  Bit Score: 54.26  E-value: 3.13e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 292621054 1392 WCFVCSEGGSLLCC--ESCPAAFHRECLNIEMPQ-GSWFC 1428
Cdd:cd15568     1 ECFRCGDGGDLVLCdfKGCPKVYHLSCLGLEKPPgGKWIC 40
PHD1_Rco1 cd15535
PHD finger 1 found in Saccharomyces cerevisiae transcriptional regulatory protein Rco1 and ...
1393-1431 5.29e-09

PHD finger 1 found in Saccharomyces cerevisiae transcriptional regulatory protein Rco1 and similar proteins; Rco1 is a component of the Rpd3S histone deacetylase complex that plays an important role at actively transcribed genes. Rco1 contains two plant homeodomain (PHD) fingers, which are required for the methylation of histone H3 lysine 36 (H3K36) nucleosome recognition by Rpd3S. This model corresponds to the first PHD finger.


Pssm-ID: 277010 [Multi-domain]  Cd Length: 45  Bit Score: 53.58  E-value: 5.29e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 292621054 1393 CFVCSEGGSLLCCESCPAAFHRECLNI-----EMPQGSWFCNDC 1431
Cdd:cd15535     2 CSACGGYGSFLCCDGCPRSFHFSCLDPpleedNLPDDEWFCNEC 45
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
1625-1741 9.32e-09

SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET domain-containing protein 3 (SETD3) and similar proteins; Schizosaccharomyces pombe SETD3 functions as a transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. It is required for both, gene activation and repression.


Pssm-ID: 380960  Cd Length: 173  Bit Score: 56.64  E-value: 9.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1625 TEVEIFRTLSRGW-GLRSISDIKKGAFVNEYVGEVideeecrSRIKNAQDNDICNFYMLTLDKDRI---------IDAGP 1694
Cdd:cd19183     1 TEISSIGLANASRfGLFADRPIPAGDPIQELLGEI-------GLQSEYIADPENQYQILGAPKPHVffhpqsplyIDTRR 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 292621054 1695 KGNESRFMNHSCQPNCE--TQKWTVNGDTRVGLFALEDIPKGVELTFNY 1741
Cdd:cd19183    74 SGSVARFIRRSCRPNAElvTVASDSGSVLKFVLYASRDISPGEEITIGW 122
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
289-395 1.68e-08

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: 53.66  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054  289 GDVVWAKFNRRPWWPCHVTTDPQIDVHTKMKDPSRRpcrlYFVRMFGEiVDQAWVPAKATFPFEggdqfeklpvlrrrgr 368
Cdd:cd05162     1 GDLVWAKLKGYPWWPARVVDPEELPEEVGKKKKKGG----VLVQFFGD-NDYAWVKSKNIKPFE---------------- 59
                          90       100
                  ....*....|....*....|....*..
gi 292621054  369 qKEKDYKYTVPKRLIPSWKASVLEAEA 395
Cdd:cd05162    60 -EGFKKEFKKKKKKSKKFKKAVEEAEE 85
PWWP_NSD_rpt1 cd20144
first PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
1441-1561 2.37e-08

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: 53.86  E-value: 2.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1441 DILWVKVGRYRWWPAEVTQ---------PKSVPENISRMKHevgefpVHFFGSKDYV-WTYQARCFPYmEGdannKEKmg 1510
Cdd:cd20144     3 DLVWAKVSGHPWWPCMVTYdpesglytkIKGSGGRTYRQYH------VQFFGDNGERgWVSEKSLMPF-EG----KEK-- 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 292621054 1511 kgadavykkalneaadrFRELLKEkemrQLQEDRKNDKKPPPYKHIKVNKQ 1561
Cdd:cd20144    70 -----------------FEELVKE----LKKKAKKKSKKAKLEKKVKPSRR 99
PHD_TIF1gamma cd15624
PHD finger found in transcriptional intermediary factor 1 gamma (TIF1gamma); TIF1gamma, also ...
1392-1432 4.97e-08

PHD finger found in transcriptional intermediary factor 1 gamma (TIF1gamma); TIF1gamma, also termed tripartite motif-containing 33 (trim33), or ectodermin, or RFG7, or PTC7, is an E3-ubiquitin ligase that functions as a regulator of transforming growth factor beta (TGFbeta) signaling; it inhibits the Smad4-mediated TGFbeta response by interaction with Smad2/3 or ubiquitylation of Smad4. Moreover, TIF1gamma is an important regulator of transcription during hematopoiesis, as well as a key factor of tumorigenesis. Like other TIF1 family members, TIF1gamma also contains an intrinsic transcriptional silencing function. It can control erythroid cell fate by regulating transcription elongation. It can bind to the anaphase-promoting complex/cyclosome (APC/C) and promotes mitosis. TIF1gamma contains an N-terminal RBCC (RING finger, B-box zinc-fingers, coiled-coil), a plant homeodomain (PHD) finger, followed by a bromodomain in the C-terminal region.


Pssm-ID: 277094  Cd Length: 46  Bit Score: 50.82  E-value: 4.97e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 292621054 1392 WCFVCSEGGSLLCCESCPAAFHREC---LNIEMPQGSWFCNDCR 1432
Cdd:cd15624     1 WCAVCQNGGDLLCCEKCPKVFHLTChvpTLLSFPSGDWICTFCR 44
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
1701-1741 5.19e-08

SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing protein, and similar proteins; The family includes SET and MYND domain-containing proteins, SMYD1-SYMD5. SMYD1 (EC 2.1.1.43; also termed BOP) is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD2 (also termed HSKM-B, or lysine N-methyltransferase 3C (KMT3C)) functions as a histone methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. It specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex. SMYD4 functions as a potential tumor suppressor that plays a critical role in breast carcinogenesis at least partly through inhibiting the expression of PDGFR-alpha. SMYD5 (also termed protein NN8-4AG, or retinoic acid-induced protein 15) functions as histone lysine methyltransferase that mediates H4K20me3 at heterochromatin regions.


Pssm-ID: 380997 [Multi-domain]  Cd Length: 122  Bit Score: 53.15  E-value: 5.19e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 292621054 1701 FMNHSCQPNCEtqkWTVNGDTRVGLFALEDIPKGVELTFNY 1741
Cdd:cd20071    58 LLNHSCDPNAV---VVFDGNGTLRVRALRDIKAGEELTISY 95
PHD1_BPTF cd15559
PHD finger 1 found in bromodomain and PHD finger-containing transcription factor (BPTF); BPTF, ...
1393-1431 9.54e-08

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


Pssm-ID: 277034 [Multi-domain]  Cd Length: 43  Bit Score: 50.11  E-value: 9.54e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 292621054 1393 CFVCSEGGSLLCCESCPAAFHRECLN---IEMPQGSWFCNDC 1431
Cdd:cd15559     2 CRVCHKLGDLLCCETCSAVYHLECVDpplEEVPEEDWQCEVC 43
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
1441-1526 1.54e-07

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: 50.68  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1441 DILWVKVGRYRWWPAEVTQPksvPENISRMKHEVGEFPVHFFGSKDYVWTYQARCFPYMEgdanNKEKMGKGA-DAVYKK 1519
Cdd:cd05836     5 DLVWAKMKGFPPWPGKIVNP---PPDLKKPPRKKKMHCVYFFGSENYAWIEDENIKPYEE----FKEEMLKSKkSAGFKD 77

                  ....*..
gi 292621054 1520 ALNEAAD 1526
Cdd:cd05836    78 AVEAIEE 84
SET_ATXR5_6-like cd10539
SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The ...
1644-1742 1.56e-07

SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The family includes Arabidopsis thaliana ATXR5 and ATXR6. Both ATXR5 (also termed protein SET DOMAIN GROUP 15, or TRX-related protein 5) and ATXR6 (also termed protein SET DOMAIN GROUP 34, or TRX-related protein 6) function as histone methyltransferase that specifically monomethylates 'Lys-37' of histone H3 (H3K27me1). They are required for chromatin structure and gene silencing.


Pssm-ID: 380937  Cd Length: 138  Bit Score: 52.41  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1644 DIKKGAFVNEYVGEVideEECRSRIKNAQDNdicnfyMLTL------DKDRIIDAGPKGNESRFM----NHSCQ----PN 1709
Cdd:cd10539    23 FIKDLTIIAEYTGDV---DYIRNREFDDNDS------IMTLllagdpSKSLVICPDKRGNIARFIsginNHTKDgkkkQN 93
                          90       100       110
                  ....*....|....*....|....*....|...
gi 292621054 1710 CETQKWTVNGDTRVGLFALEDIPKGVELTFNYN 1742
Cdd:cd10539    94 CKCVRYSINGEARVLLVATRDIAKGERLYYDYN 126
PHD_TIF1alpha cd15622
PHD finger found in transcription intermediary factor 1-alpha (TIF1-alpha); TIF1-alpha, also ...
1392-1431 2.80e-07

PHD finger found in transcription intermediary factor 1-alpha (TIF1-alpha); TIF1-alpha, also termed tripartite motif-containing protein 24 (TRIM24), or E3 ubiquitin-protein ligase TRIM24, or RING finger protein 82, belongs to the TRIM/RBCC protein family. It interacts specifically and in a ligand-dependent manner with the ligand binding domain (LBD) of several nuclear receptors (NRs), including retinoid X (RXR), retinoic acid (RAR), vitamin D3 (VDR), estrogen (ER), and progesterone (PR) receptors. It also associates with heterochromatin-associated factors HP1alpha, MOD1 (HP1beta) and MOD2 (HP1gamma), as well as vertebrate Kruppel-type (C2H2) zinc finger proteins that contain transcriptional silencing domain KRAB. TIF1-alpha is a ligand-dependent co-repressor of retinoic acid receptor (RAR) that interacts with multiple nuclear receptors in vitro via an LXXLL motif, and further acts as a gatekeeper of liver carcinogenesis. It also functions as an E3-ubiquitin ligase targeting p53 and is broadly associated with chromatin silencing. Moreover, it is a chromatin regulator that recognizes specific, combinatorial histone modifications through its C-terminal plant homeodomain (PHD)-Bromodomain (Bromo) region. In addition, it interacts with chromatin and estrogen receptor to activate estrogen-dependent genes associated with cellular proliferation and tumor development. TIF1-alpha contains an N-terminal RBCC (RING finger, B-box zinc-fingers, coiled-coil), a plant homeodomain (PHD) finger, followed by a bromodomain in the C-terminal region.


Pssm-ID: 277092  Cd Length: 43  Bit Score: 48.91  E-value: 2.80e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292621054 1392 WCFVCSEGGSLLCCESCPAAFHREC---LNIEMPQGSWFCNDC 1431
Cdd:cd15622     1 WCAVCQNGGELLCCEKCPKVFHLSChvpTLMNFPSGEWICTFC 43
PHD5_NSD cd15568
PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
1228-1267 3.84e-07

PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family 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 to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant 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 (Cys5HisCysHis). This model corresponds to the fifth PHD finger.


Pssm-ID: 277043 [Multi-domain]  Cd Length: 43  Bit Score: 48.09  E-value: 3.84e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 292621054 1228 VCQVCEKTGELLLCEGQCCG-AFHLQCIGLTETPKGRFICQ 1267
Cdd:cd15568     1 ECFRCGDGGDLVLCDFKGCPkVYHLSCLGLEKPPGGKWICP 41
PHD1_CHD_II cd15531
PHD finger 1 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...
1392-1431 4.31e-07

PHD finger 1 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD proteins includes chromodomain-helicase-DNA-binding protein CHD3, CHD4, and CHD5, which are nuclear and ubiquitously expressed chromatin remodelling ATPases generally associated with histone deacetylases (HDACs). They are involved in DNA Double Strand Break (DSB) signaling, DSB repair and/or p53-dependent pathways such as apoptosis and senescence, as well as in the maintenance of genomic stability, and/or cancer prevention. They function as subunits of the Nucleosome Remodelling and Deacetylase (NuRD) complex, which is generally associated with gene repression, heterochromatin formation, and overall chromatin compaction. In contrast to the class I CHD enzymes (CHD1 and CHD2), class II CHD proteins lack identifiable DNA-binding domains, but possess a C-terminal coiled-coil region. Moreover, in addition to the tandem chromodomains and a helicase domain, they all harbor tandem plant homeodomain (PHD) zinc fingers involved in the recognition of methylated histone tails. This model corresponds to the first PHD finger.


Pssm-ID: 277006 [Multi-domain]  Cd Length: 43  Bit Score: 47.98  E-value: 4.31e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292621054 1392 WCFVCSEGGSLLCCESCPAAFHRECLNIEM---PQGSWFCNDC 1431
Cdd:cd15531     1 YCEVCQQGGEIILCDTCPRAYHLVCLDPELekaPEGKWSCPHC 43
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
1392-1431 4.76e-07

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 47.98  E-value: 4.76e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 292621054   1392 WCFVCSE---GGSLLCCESCPAAFHRECLNI----EMPQGSWFCNDC 1431
Cdd:smart00249    1 YCSVCGKpddGGELLQCDGCDRWYHQTCLGPplleEEPDGKWYCPKC 47
PHD4_NSD cd15567
PHD finger 4 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
1229-1269 5.06e-07

PHD finger 4 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family 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 to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant 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 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 (Cys5HisCysHis). This model corresponds to the fourth PHD finger.


Pssm-ID: 277042 [Multi-domain]  Cd Length: 41  Bit Score: 48.01  E-value: 5.06e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 292621054 1229 CQVCEKTGELLLCEGqCCGAFHLQCIGLTETPKGRFICQEC 1269
Cdd:cd15567     2 CFICSEGGSLICCES-CPASFHPECLGLEPPPEGKFYCEDC 41
PHD_TIF1_like cd15541
PHD finger found in the transcriptional intermediary factor 1 (TIF1) family and similar ...
1392-1431 5.85e-07

PHD finger found in the transcriptional intermediary factor 1 (TIF1) family and similar proteins; The TIF1 family of transcriptional cofactors includes TIF1alpha (TRIM24), TIF1beta (TRIM28), TIF1gamma (TRIM33), and TIF1delta (TRIM66), which are characterized by an N-terminal RING-finger B-box coiled-coil (RBCC/TRIM) motif and plant homeodomain (PHD) finger followed by a bromodomain in the C-terminal region. TIF1 proteins couple chromatin modifications to transcriptional regulation, signaling, and tumor suppression. They exert a deacetylase-dependent silencing effect when tethered to a promoter region. TIF1alpha, TIF1beta, and TIF1delta can homodimerize and contain a PXVXL motif necessary and sufficient for heterochromatin protein 1(HP1) binding. TIF1alpha and TIF1beta bind nuclear receptors and Kruppel-associated boxes (KRAB) specifically and respectively. In contrast, TIF1delta appears to lack nuclear receptor- and KRAB-binding activity. Moreover, TIF1delta is specifically involved in heterochromatin-mediated gene silencing during postmeiotic phases of spermatogenesis. TIF1gamma is structurally closely related to TIF1alpha and TIF1beta, but has very little functional features in common with them. It does not interact with the KRAB silencing domain of KOX1 or the heterochromatinic proteins HP1alpha, beta, and gamma. It cannot bind to nuclear receptors (NRs). This family also includes Sp100/Sp140 family proteins, the nuclear body SP100 and SP140. Sp110 is a leukocyte-specific component of the nuclear body. It may function as a nuclear hormone receptor transcriptional coactivator that may play a role in inducing differentiation of myeloid cells. It is also involved in resisting intracellular pathogens and functions as an important drug target for preventing intracellular pathogen diseases, such as tuberculosis, hepatic veno-occlusive disease, and intracellular cancers. SP140 is an interferon inducible nuclear leukocyte-specific protein involved in primary biliary cirrhosis and a risk factor in chronic lymphocytic leukemia. It is also implicated in innate immune response to human immunodeficiency virus type 1 (HIV-1) by binding to the virus viral infectivity factor (Vif) protein. Both Sp110 and Sp140 contain a SAND domain, a plant homeodomain (PHD) finger, and a bromodomain (BRD).


Pssm-ID: 277016 [Multi-domain]  Cd Length: 43  Bit Score: 47.72  E-value: 5.85e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 292621054 1392 WCFVCSEGGSLLCCESCPAAFHREClNI----EMPQGSWFCNDC 1431
Cdd:cd15541     1 WCAVCQNGGELLCCDKCPRVFHLDC-HIppipEFPSGEWSCSLC 43
PWWP_NSD_rpt2 cd05838
second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
289-395 9.79e-07

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: 48.78  E-value: 9.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054  289 GDVVWAKFNRRPWWPCHVtTDPQiDVHTKMKDPSRRPCRlYFVRMFGEiVDQAWVPAKATFPFEGGDqfeklpvlrrrgr 368
Cdd:cd05838     3 GDIVWVKLGNYRWWPAEI-LHPR-EVPDNIQSLPHPPGE-FPVRFFGS-HDYYWVHRGRVFLFEEGD------------- 65
                          90       100
                  ....*....|....*....|....*..
gi 292621054  369 qkeKDYKYTVPKRLIPSWKASVLEAEA 395
Cdd:cd05838    66 ---KGSKEKSKKSLDKSFKRALKEANE 89
PHD_TIF1delta cd15625
PHD finger found in transcriptional intermediary factor 1 delta (TIF1delta); TIF1delta, also ...
1389-1432 1.07e-06

PHD finger found in transcriptional intermediary factor 1 delta (TIF1delta); TIF1delta, also termed tripartite motif-containing protein 66 (TRIM66), is a novel heterochromatin protein 1 (HP1)-interacting member of the transcriptional intermediary factor1 (TIF1) family expressed by elongating spermatids. Like other TIF1 proteins, TIF1delta displays a potent trichostatin A (TSA)-sensitive repression function; TSA is a specific inhibitor of histone deacetylases. Moreover, TIF1delta plays an important role in heterochromatin-mediated gene silencing during postmeiotic phases of spermatogenesis. It functions as a negative regulator of postmeiotic genes acting through HP1 isotype gamma (HP1gamma) complex formation and centromere association. TIF1delta contains an N-terminal RBCC (RING finger, B-box zinc-fingers, coiled-coil), a plant homeodomain (PHD) finger, followed by a bromodomain in the C-terminal region.


Pssm-ID: 277095 [Multi-domain]  Cd Length: 49  Bit Score: 47.26  E-value: 1.07e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 292621054 1389 NVSWCFVCSEGGSLLCCESCPAAFHREC---LNIEMPQGSWFCNDCR 1432
Cdd:cd15625     1 NEDFCAVCLNGGELLCCDRCPKVFHLSChvpALLSFPVGEWVCTLCR 47
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
1639-1760 1.17e-06

SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and similar proteins; SETD5 is a probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. SETD5 loss-of-function mutations are a likely cause of a familial syndromic intellectual disability with variable phenotypic expression.


Pssm-ID: 380958  Cd Length: 150  Bit Score: 50.01  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1639 LRSISDIKKGAFVNEYVGEVIDEEECRSrikNA----QDNDICNFYMLTLDKDRIIDAGPKGNESRFMNHSCQPNCETQK 1714
Cdd:cd19181    21 LRAARDLALDTLIIEYRGKVMLRQQFEV---NGhffkRPYPFVLFYSKFNGVEMCVDARTFGNDARFIRRSCTPNAEVRH 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 292621054 1715 WTVNGDTRVGLFALEDIPKGVELTFNYNLE---ClgNGKTVCKC--GAPNC 1760
Cdd:cd19181    98 MIADGMIHLCIYAVAAIAKDAEVTIAFDYEysnC--NYKVDCAChkGNRNC 146
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
1634-1746 1.21e-06

SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of variegation 4-20 (Suv4-20) and similar proteins; Suv4-20 (also termed Su(var)4-20) is a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-20' of histone H4. It acts as a dominant suppressor of position-effect variegation. The family also includes Suv4-20 homologs, lysine N-methyltransferase 5B (KMT5B) and lysine N-methyltransferase 5C (KMT5C). Both KMT5B (also termed lysine-specific methyltransferase 5B, or suppressor of variegation 4-20 homolog 1, or Su(var)4-20 homolog 1, or Suv4-20h1) and KMT5C (also termed lysine-specific methyltransferase 5C, or suppressor of variegation 4-20 homolog 2, or Su(var)4-20 homolog 2, or Suv4-20h2) are histone methyltransferases that specifically trimethylate 'Lys-20' of histone H4 (H4K20me3). They play central roles in the establishment of constitutive heterochromatin in pericentric heterochromatin regions.


Pssm-ID: 380922 [Multi-domain]  Cd Length: 141  Bit Score: 49.97  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1634 SRGWGLRSISDIKKGAFVNEYVGEVI-DEEECRSRIKNAQdNDICNFYMLTLDKDRIIDaGPkgneSRFMNHSCQPNCet 1712
Cdd:cd10524    17 HYGAKIIATKPIKKGEKIHELCGCIAeLSEEEEALLRPGG-NDFSVMYSSRKKCSQLWL-GP----AAFINHDCRPNC-- 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 292621054 1713 qKWTVNGDTRVGLFALEDIPKGVELTFNY--------NLECL 1746
Cdd:cd10524    89 -KFVPTGKSTACVKVLRDIEPGEEITVYYgdnyfgenNEECE 129
PHD4_NSD cd15567
PHD finger 4 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
1803-1841 1.39e-06

PHD finger 4 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family 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 to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant 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 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 (Cys5HisCysHis). This model corresponds to the fourth PHD finger.


Pssm-ID: 277042 [Multi-domain]  Cd Length: 41  Bit Score: 46.47  E-value: 1.39e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 292621054 1803 CFYCGDGGQIVSCKkpGCPKVYHADCLNLSKRPAGRWEC 1841
Cdd:cd15567     2 CFICSEGGSLICCE--SCPASFHPECLGLEPPPEGKFYC 38
PHD2_CHD_II cd15532
PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...
1803-1842 1.82e-06

PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD proteins includes chromodomain-helicase-DNA-binding protein CHD3, CHD4, and CHD5, which are nuclear and ubiquitously expressed chromatin remodelling ATPases generally associated with histone deacetylases (HDACs). They are involved in DNA Double Strand Break (DSB) signaling, DSB repair and/or p53-dependent pathways such as apoptosis and senescence, as well as in the maintenance of genomic stability, and/or cancer prevention. They function as subunits of the Nucleosome Remodelling and Deacetylase (NuRD) complex, which is generally associated with gene repression, heterochromatin formation, and overall chromatin compaction. In contrast to the class I CHD enzymes (CHD1 and CHD2), class II CHD proteins lack identifiable DNA-binding domains, but possess a C-terminal coiled-coil region. Moreover, in addition to the tandem chromodomains and a helicase domain, they all harbor tandem plant homeodomain (PHD) zinc fingers involved in the recognition of methylated histone tails. This model corresponds to the second PHD finger.


Pssm-ID: 277007 [Multi-domain]  Cd Length: 43  Bit Score: 46.50  E-value: 1.82e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 292621054 1803 CFYCGDGGQIVSCKkpGCPKVYHADCLN--LSKRPAGRWECP 1842
Cdd:cd15532     2 CRVCKDGGELLCCD--GCPSSYHLHCLNppLAEIPDGDWFCP 41
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
1392-1432 1.82e-06

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


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 46.72  E-value: 1.82e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 292621054  1392 WCFVCS---EGGSLLCCESCPAAFHRECLNI-----EMPQGSWFCNDCR 1432
Cdd:pfam00628    1 YCAVCGksdDGGELVQCDGCDDWFHLACLGPpldpaEIPSGEWLCPECK 49
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
286-350 3.38e-06

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 46.18  E-value: 3.38e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 292621054    286 YSIGDVVWAKFNRRPWWPCHVTTdpqidvHTKMKDPSRRPCR---LYFVRMFGEiVDQAWVPAKATFP 350
Cdd:smart00293    1 FKPGDLVWAKMKGFPWWPALVIS------PKMTPDNIMKRKSdenLYPVLFFGD-KDTAWIPSSKLFP 61
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
1627-1742 5.52e-06

SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces pombe Set7 is a novel histone-lysine N-methyltransferase. The family also includes a viral histone H3 lysine 27 methyltransferase from Paramecium bursaria Chlorella virus 1 (PBCV-1).


Pssm-ID: 380938  Cd Length: 112  Bit Score: 47.25  E-value: 5.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1627 VEIFRTLSRGWGLRSISDIKKGafvneyvgEVIdEEECRSRIKNAQDNDICnfymLTLDKDRIIDAG------PKGNESR 1700
Cdd:cd10540     2 LEVKPSTLKGRGVFATRPIKKG--------EVI-EEAPVIVLPKEEYQHLC----KTVLDHYVFSWGdgclalALGYGSM 68
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 292621054 1701 FmNHSCQPNCEtqKWTVNGDTRVGLFALEDIPKGVELTFNYN 1742
Cdd:cd10540    69 F-NHSYTPNAE--YEIDFENQTIVFYALRDIEAGEELTINYG 107
PHD1_Lid2p_like cd15519
PHD finger 1 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar ...
1393-1431 6.92e-06

PHD finger 1 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar proteins; Lid2p is a trimethyl H3K4 (H3K4me3) demethylase responsible for H3K4 hypomethylation in heterochromatin. It interacts with the histone lysine-9 methyltransferase, Clr4, through the Dos1/Clr8-Rik1 complex, and mediates H3K9 methylation and small RNA production. It also acts cooperatively with the histone modification enzymes Set1 and Lsd1 and plays an essential role in cross-talk between H3K4 and H3K9 methylation in euchromatin. Lid2p contains a JmjC domain, three PHD fingers and a JmjN domain. This model corresponds to the first PHD finger.


Pssm-ID: 276994 [Multi-domain]  Cd Length: 46  Bit Score: 44.76  E-value: 6.92e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 292621054 1393 CFVCS---EGGSLLCCESCPAAFHRECLN---IEMPQGSWFCNDC 1431
Cdd:cd15519     2 CEVCGlddNEGEVLLCDGCDAEYHTSCLDpplGEIPPGTWFCPSC 46
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
1690-1744 7.67e-06

SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar proteins; KMT2E (also termed inactive lysine N-methyltransferase 2E, myeloid/lymphoid or mixed-lineage leukemia protein 5 (MLL5)) plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. It associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription. Lack of key residues in the SET domain as well as the presence of an unusually large loop in the SET-I subdomain preclude the interaction of MLL5 SET with its cofactor and substrate thus making MLL5 devoid of any in vitro methyltransferase activity on full-length histones and histone H3 peptide.


Pssm-ID: 380959  Cd Length: 129  Bit Score: 47.19  E-value: 7.67e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 292621054 1690 IDAGPKGNESRFMNHSCQPNCETQKWTVNGDTRVGLFALEDIPKGVELTFNYNLE 1744
Cdd:cd19182    73 VDARTFGNEARFIRRSCTPNAEVRHVIEDGTIHLYIYSIRSIPKGTEITIAFDFD 127
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
1393-1431 1.21e-05

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


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 44.23  E-value: 1.21e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 292621054 1393 CFVCSEGG----SLLCCESCPAAFHRECLNIE----MPQGSWFCNDC 1431
Cdd:cd15489     2 CIVCGKGGdlggELLQCDGCGKWFHADCLGPPlssfVPNGKWICPVC 48
PHD_PRKCBP1 cd15538
PHD finger found in protein kinase C-binding protein 1 (PRKCBP1); PRKCBP1, also termed ...
1393-1431 1.29e-05

PHD finger found in protein kinase C-binding protein 1 (PRKCBP1); PRKCBP1, also termed cutaneous T-cell lymphoma-associated antigen se14-3 (CTCL-associated antigen se14-3), or 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; the 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.


Pssm-ID: 277013  Cd Length: 41  Bit Score: 43.85  E-value: 1.29e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 292621054 1393 CFVCSEGGSLLCCESCPAAFHRECLNI-EMPQGSWFCNDC 1431
Cdd:cd15538     2 CWRCHKEGQVLCCSLCPRVYHKKCLKLtSEPDEDWVCPEC 41
PHD1_NSD1_2 cd15648
PHD finger 1 found in nuclear receptor-binding SET domain-containing protein NSD1 and NSD2; ...
1393-1432 1.45e-05

PHD finger 1 found in nuclear receptor-binding SET domain-containing protein NSD1 and NSD2; NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or 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). NSD2, also termed histone-lysine N-methyltransferase NSD2, or 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, by 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). Both NSD1 and NSD2 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 (Cys5HisCysHis). In addition, NSD2 harbors a high mobility group (HMG) box. The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD fingers mediate chromatin interaction and recognition of histone marks. This model corresponds to the first PHD finger.


Pssm-ID: 277118  Cd Length: 43  Bit Score: 44.00  E-value: 1.45e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 292621054 1393 CFVCSEGGSLLCCE-SCPAAFHRECLNI-EMPQGSWFCNDCR 1432
Cdd:cd15648     2 CQVCEKPGELLLCEgQCCGAFHLDCIGLsEMPSGKFICDECI 43
PHD1_AIRE cd15539
PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune ...
1229-1269 2.18e-05

PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune polyendocrinopathy candidiasis ectodermal dystrophy (APECED) protein, functions as a regulator of gene transcription in the thymus. It is essential for prevention of autoimmunity. AIRE plays a critical role in the induction of central tolerance. It promotes self-tolerance through tissue-specific antigen (TSA) expression. It also acts as an active regulator of chondrocyte differentiation. AIRE contains a homogeneously-staining region (HSR) or caspase-recruitment domain (CARD), a nuclear localization signal (NLS), a SAND (for Sp100, AIRE, nuclear phosphoprotein 41/75 or NucP41/75, and deformed epidermal auto regulatory factor 1 or Deaf1) domain, two plant homeodomain (PHD) fingers, and four LXXLL (where L stands for leucine) motifs. This model corresponds to the first PHD finger that recognizes the unmethylated tail of histone H3 and targets AIRE-dependent genes.


Pssm-ID: 277014 [Multi-domain]  Cd Length: 43  Bit Score: 43.21  E-value: 2.18e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292621054 1229 CQVCEKTGELLLCEGqCCGAFHLQCIG--LTETPKGRFICQEC 1269
Cdd:cd15539     2 CAVCGDGGELLCCDG-CPRAFHLACLVppLTLIPSGTWRCSSC 43
PWWP_AtATX3-like cd20143
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
289-374 3.61e-05

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: 44.67  E-value: 3.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054  289 GDVVWAKFNRRPWWPCHVtTDPqidvhTKMKDPSRRPCR--LYFVRMFGEIVDQ--AWVPAKATFPFeggdqFEKLPVLR 364
Cdd:cd20143     3 GDLVWAKVGTHPFWPARV-VEP-----AEQAEEVRRRCVpgSLCVYFFGPGGSRdyGWVRRSMIFPF-----TDDLARFQ 71
                          90
                  ....*....|...
gi 292621054  365 RR---GRQKEKDY 374
Cdd:cd20143    72 TQkikNKKRPQEF 84
PHD1_AIRE cd15539
PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune ...
1802-1849 3.92e-05

PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune polyendocrinopathy candidiasis ectodermal dystrophy (APECED) protein, functions as a regulator of gene transcription in the thymus. It is essential for prevention of autoimmunity. AIRE plays a critical role in the induction of central tolerance. It promotes self-tolerance through tissue-specific antigen (TSA) expression. It also acts as an active regulator of chondrocyte differentiation. AIRE contains a homogeneously-staining region (HSR) or caspase-recruitment domain (CARD), a nuclear localization signal (NLS), a SAND (for Sp100, AIRE, nuclear phosphoprotein 41/75 or NucP41/75, and deformed epidermal auto regulatory factor 1 or Deaf1) domain, two plant homeodomain (PHD) fingers, and four LXXLL (where L stands for leucine) motifs. This model corresponds to the first PHD finger that recognizes the unmethylated tail of histone H3 and targets AIRE-dependent genes.


Pssm-ID: 277014 [Multi-domain]  Cd Length: 43  Bit Score: 42.44  E-value: 3.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 292621054 1802 ECFYCGDGGQIVSCKkpGCPKVYHADCLN--LSKRPAGRWecpwhQCNEC 1849
Cdd:cd15539     1 ECAVCGDGGELLCCD--GCPRAFHLACLVppLTLIPSGTW-----RCSSC 43
PWWP_ZCWPW2 cd20146
PWWP domain found in zinc finger CW-type PWWP domain protein 2 (ZCWPW2) and similar proteins; ...
285-378 4.91e-05

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: 44.59  E-value: 4.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054  285 KYSIGDVVWAKFNRRPWWPCHVTTDPQIDVHTKmKDPSRRPcRLYFVRMFGEIVDQAWVPAKATFPFEGGdqFEKLPVLR 364
Cdd:cd20146     8 QLPLGSLVWAKMTGYPRWPAILTPDPICGEYVD-YDEDGEV-EKYHVEFLGKPHSHAWISAKSVEPYNSN--TKTPKCKT 83
                          90
                  ....*....|....
gi 292621054  365 RRGRQKEKDYKYTV 378
Cdd:cd20146    84 KKSKKRKKSYESAL 97
PHD5_NSD3 cd15661
PHD finger 5 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...
1392-1428 7.52e-05

PHD finger 5 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed histone-lysine N-methyltransferase NSD3, or protein whistle, or 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 fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fifth PHD finger.


Pssm-ID: 277131  Cd Length: 43  Bit Score: 41.88  E-value: 7.52e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 292621054 1392 WCFVCSEGGSLLCCES--CPAAFHRECLNIEMPQ-GSWFC 1428
Cdd:cd15661     1 YCFQCGDGGELVMCDKkdCPKAYHLLCLNLTQPPyGKWEC 40
PWWP_DNMT3 cd05835
PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family ...
288-393 7.87e-05

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: 43.02  E-value: 7.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054  288 IGDVVWAKFNRRPWWPCHVttdpqidVHTKMKdpSRRPCRlyfvrmfgeiVDQAWVpakatFPFegGD-QFEKLPVLRRR 366
Cdd:cd05835     2 IGDLVWAKLKGSPWWPGIV-------VSHKDC--GQKPPA----------EGSVWV-----FWF--GDhKVSEVPLDKIL 55
                          90       100
                  ....*....|....*....|....*..
gi 292621054  367 GRQKEKDYKYTvPKRLIPSWKASVLEA 393
Cdd:cd05835    56 PFAEFFNKFYI-SKNSSKLYKKAVYEA 81
PHD_Yng1p_like cd15587
PHD finger found in yeast orthologs of ING tumor suppressor family; The yeast orthologs of the ...
1236-1270 8.48e-05

PHD finger found in yeast orthologs of ING tumor suppressor family; The yeast orthologs of the plant homeodomain (PHD) finger-containing ING tumor suppressor family consists of chromatin modification-related protein YNG1 (Yng1p), YNG2 (Yng2p), and transcriptional regulatory protein PHO23 (Pho23p). Yng1p, also termed ING1 homolog 1, is one of the components of the NuA3 histone acetyltransferase (HAT) complex. Its PHD finger binding to H3 Trimethylated at K4 (H3K4me3) promotes NuA3 H3 HAT activity at K14 of H3 on chromatin. Yng2p, also termed ESA1-associated factor 4, or ING1 homolog 2, is a subunit of the NuA4 HAT complex. It plays a critical role in intra-S-phase DNA damage response. Pho23p is part of the Rpd3/Sin3 histone deacetylase (HDAC) complex. It is required for the normal function of Rpd3 in the silencing of rDNA, telomeric, and mating-type loci. Yng1p and Pho23p inhibit p53-dependent transcription. In contrast, Yng2p has the opposite effect. All family members contain an N-terminal ING histone-binding domain and a C-terminal PHD finger.


Pssm-ID: 277062 [Multi-domain]  Cd Length: 47  Bit Score: 41.63  E-value: 8.48e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 292621054 1236 GELLLCEGQCCGA--FHLQCIGLTETPKGRFICQECK 1270
Cdd:cd15587    10 GEMVACDNPDCKIewFHFECVGLTETPKGKWYCSDCK 46
PHD_RSF1 cd15543
PHD finger found in Remodeling and spacing factor 1 (Rsf-1); Rsf-1, also termed HBV ...
1393-1431 8.63e-05

PHD finger found in Remodeling and spacing factor 1 (Rsf-1); Rsf-1, also termed HBV pX-associated protein 8, or Hepatitis B virus X-associated protein alpha (HBxAPalpha), or p325 subunit of RSF chromatin-remodeling complex, is a novel nuclear protein with histone chaperon function. It is a subunit of an ISWI chromatin remodeling complex, remodeling and spacing factor (RSF), and plays a role in mediating ATPase-dependent chromatin remodeling and conferring tumor aggressiveness in common carcinomas. As an ataxia-telangiectasia mutated (ATM)-dependent chromatin remodeler, Rsf-1 facilitates DNA damage checkpoints and homologous recombination repair. It regulates the mitotic spindle checkpoint and chromosome instability through the association with serine/threonine kinase BubR1 (BubR1) and Hepatitis B virus (HBV) X protein (HBx) in the chromatin fraction during mitosis. It also interacts with cyclin E1 and promotes tumor development. Rsf-1 contains a plant homeodomain (PHD) finger.


Pssm-ID: 277018 [Multi-domain]  Cd Length: 46  Bit Score: 41.87  E-value: 8.63e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 292621054 1393 CFVCSEGGSLLCCESCPAAFHRECLN---IEMPQGSWFCNDC 1431
Cdd:cd15543     5 CGLSDHPEWILLCDRCDAGYHTACLRpplMIIPDGNWFCPPC 46
PHD_PHF21A cd15523
PHD finger found in PHD finger protein 21A (PHF21A); PHF21A (also termed BHC80a or BRAF35-HDAC ...
1393-1431 8.69e-05

PHD finger found in PHD finger protein 21A (PHF21A); PHF21A (also termed BHC80a or BRAF35-HDAC complex protein BHC80) along with HDAC1/2, CtBP1, CoREST, and BRAF35, is associated with LSD1, a lysine (K)-specific histone demethylase. It inhibits LSD1-mediated histone demethylation in vitro. PHF21A is predominantly present in the central nervous system and spermatogenic cells and is one of the six components of BRAF-HDAC complex (BHC) involved in REST-dependent transcriptional repression of neuron-specific genes in non-neuronal cells. It acts as a scaffold protein in BHC in neuronal as well as non-neuronal cells and also plays a role in spermatogenesis. PHF21A contains a C-terminal plant homeodomain (PHD) finger that is responsible for the binding directly to each of five other components of BHC, and of organizing BHC mediating transcriptional repression.


Pssm-ID: 276998 [Multi-domain]  Cd Length: 43  Bit Score: 41.61  E-value: 8.69e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 292621054 1393 CFVCSEGGSLLCCESCPAAFHRECLN---IEMPQGSWFCNDC 1431
Cdd:cd15523     2 CSVCRKSGELLMCDTCSLVYHLDCLDpplKTIPKGMWICPKC 43
PHD2_KAT6A_6B cd15527
PHD finger 2 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ, ...
1393-1431 1.21e-04

PHD finger 2 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ, also termed histone acetyltransferase KAT6A, YBF2/SAS3, SAS2 and TIP60 protein 3 (MYST-3), or runt-related transcription factor-binding protein 2, or zinc finger protein 220, is a MYST-type histone acetyltransferase (HAT) that functions as a coactivator for acute myeloid leukemia 1 protein (AML1)- and p53-dependent transcription. It possesses intrinsic HAT activity to acetylate both itself and lysine (K) residues on histone H2B, histone H3 (K14) and histone H4 (K5, K8, K12 and K16) in vitro and H3K9 in vivo. MOZ-related factor (MORF), also termed MOZ2, or histone acetyltransferase KAT6B, or MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4 (MYST4), is a ubiquitously expressed transcriptional regulator with intrinsic HAT activity. It can interact with the Runt-domain transcription factor Runx2 and form a tetrameric complex with BRPFs, ING5, and EAF6. Both MOZ and MORF are catalytic subunits of HAT complexes that are required for normal developmental programs, such as hematopoiesis, neurogenesis, and skeletogenesis, and are also implicated in human leukemias. MOZ is also the catalytic subunit of a tetrameric inhibitor of growth 5 (ING5) complex, which specifically acetylates nucleosomal histone H3K14. Moreover, MOZ and MORF are involved in regulating transcriptional activation mediated by Runx2 (or Cbfa1), a Runt-domain transcription factor known to play important roles in T cell lymphomagenesis and bone development, and its homologs. MOZ contains a linker histone 1 and histone 5 domains and two plant homeodomain (PHD) fingers. In contrast, MORF contains an N-terminal region containing two PHD fingers, a putative HAT domain, an acidic region, and a C-terminal Ser/Met-rich domain. The family corresponds to the first PHD finger.


Pssm-ID: 277002  Cd Length: 46  Bit Score: 41.21  E-value: 1.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 292621054 1393 CFVCSEGG---SLLCCESCPAAFHRECLN---IEMPQGSWFCNDC 1431
Cdd:cd15527     2 CSVCQDSGnadNLLFCDACDKGFHMECHDpplTRMPKGKWVCQIC 46
PHD_PHF21A cd15523
PHD finger found in PHD finger protein 21A (PHF21A); PHF21A (also termed BHC80a or BRAF35-HDAC ...
1228-1269 1.54e-04

PHD finger found in PHD finger protein 21A (PHF21A); PHF21A (also termed BHC80a or BRAF35-HDAC complex protein BHC80) along with HDAC1/2, CtBP1, CoREST, and BRAF35, is associated with LSD1, a lysine (K)-specific histone demethylase. It inhibits LSD1-mediated histone demethylation in vitro. PHF21A is predominantly present in the central nervous system and spermatogenic cells and is one of the six components of BRAF-HDAC complex (BHC) involved in REST-dependent transcriptional repression of neuron-specific genes in non-neuronal cells. It acts as a scaffold protein in BHC in neuronal as well as non-neuronal cells and also plays a role in spermatogenesis. PHF21A contains a C-terminal plant homeodomain (PHD) finger that is responsible for the binding directly to each of five other components of BHC, and of organizing BHC mediating transcriptional repression.


Pssm-ID: 276998 [Multi-domain]  Cd Length: 43  Bit Score: 40.84  E-value: 1.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 292621054 1228 VCQVCEKTGELLLCEgQCCGAFHLQCIG--LTETPKGRFICQEC 1269
Cdd:cd15523     1 FCSVCRKSGELLMCD-TCSLVYHLDCLDppLKTIPKGMWICPKC 43
PWWP_AtATX1-like cd20142
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
1441-1537 1.70e-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: 42.34  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1441 DILWVKVGRYRWWPA-----EVTQPKSVPENISRMKHEVgefPVHFFGSKDYvwtyqARcfpymegdANNK--EKMGKGA 1513
Cdd:cd20142     4 DVVWAKVKGYPMWPAlvideEHAERCGLEANRPGKKGTV---PVQFFGTYEV-----AR--------LNPKkvVGFSKGL 67
                          90       100
                  ....*....|....*....|....
gi 292621054 1514 DAVYKKALneAADRFRELLKEKEM 1537
Cdd:cd20142    68 DLKYHSKC--KAPVFRQALEEAER 89
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
1228-1269 1.74e-04

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 41.04  E-value: 1.74e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 292621054   1228 VCQVCEK---TGELLLCEGqCCGAFHLQCIGLTET---PKGRFICQEC 1269
Cdd:smart00249    1 YCSVCGKpddGGELLQCDG-CDRWYHQTCLGPPLLeeePDGKWYCPKC 47
PHD1_CHD_II cd15531
PHD finger 1 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...
1803-1842 2.11e-04

PHD finger 1 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD proteins includes chromodomain-helicase-DNA-binding protein CHD3, CHD4, and CHD5, which are nuclear and ubiquitously expressed chromatin remodelling ATPases generally associated with histone deacetylases (HDACs). They are involved in DNA Double Strand Break (DSB) signaling, DSB repair and/or p53-dependent pathways such as apoptosis and senescence, as well as in the maintenance of genomic stability, and/or cancer prevention. They function as subunits of the Nucleosome Remodelling and Deacetylase (NuRD) complex, which is generally associated with gene repression, heterochromatin formation, and overall chromatin compaction. In contrast to the class I CHD enzymes (CHD1 and CHD2), class II CHD proteins lack identifiable DNA-binding domains, but possess a C-terminal coiled-coil region. Moreover, in addition to the tandem chromodomains and a helicase domain, they all harbor tandem plant homeodomain (PHD) zinc fingers involved in the recognition of methylated histone tails. This model corresponds to the first PHD finger.


Pssm-ID: 277006 [Multi-domain]  Cd Length: 43  Bit Score: 40.66  E-value: 2.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 292621054 1803 CFYCGDGGQIVSCKKpgCPKVYHADCLN--LSKRPAGRWECP 1842
Cdd:cd15531     2 CEVCQQGGEIILCDT--CPRAYHLVCLDpeLEKAPEGKWSCP 41
PHD_PHF21B cd15524
PHD finger found in PHD finger protein 21B (PHF21B); PHF21B is a plant homeodomain (PHD) ...
1392-1431 2.36e-04

PHD finger found in PHD finger protein 21B (PHF21B); PHF21B is a plant homeodomain (PHD) finger-containing protein whose biological function remains unclear. It shows high sequence similarity with PHF21A, which is associated with LSD1, a lysine (K)-specific histone demethylase and inhibits LSD1-mediated histone demethylation in vitro. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins.


Pssm-ID: 276999 [Multi-domain]  Cd Length: 43  Bit Score: 40.26  E-value: 2.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292621054 1392 WCFVCSEGGSLLCCESCPAAFHRECLNIEM---PQGSWFCNDC 1431
Cdd:cd15524     1 HCAACKRGGNLQPCGTCPRAYHLDCLDPPLktaPKGVWVCPKC 43
PHD5_NSD1 cd15659
PHD finger 5 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...
1393-1428 2.37e-04

PHD finger 5 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or 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 (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fifth PHD finger.


Pssm-ID: 277129  Cd Length: 43  Bit Score: 40.31  E-value: 2.37e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 292621054 1393 CFVCSEGGSLLCCES--CPAAFHRECLNI-EMPQGSWFC 1428
Cdd:cd15659     2 CFSCGDGGQLVSCKKpgCPKVYHADCLNLtKRPAGKWEC 40
PWWP_PWWP2A cd20152
PWWP domain found in PWWP domain-containing protein 2A (PWWP2A); PWWP2A is a H2A.Z-specific ...
1441-1534 2.52e-04

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: 42.69  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1441 DILWVKVGRYRWWPAEV-TQPKSVPENISRMKHEVgefPVHFFGSKDYVWTYQARCFPYMEgdaNNKEKMGKGADAVYKK 1519
Cdd:cd20152    24 DIVWAKIYGFPWWPARIlAITVSRKDNGLLVRQEA---RISWFGSPTTSFLALSQLAPFLE---NFQSRFNKKRKGLYRK 97
                          90
                  ....*....|....*
gi 292621054 1520 ALNEAADRFRELLKE 1534
Cdd:cd20152    98 AITEAAKAAKQLTPE 112
PWWP_HRP cd05834
PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The ...
1441-1524 2.58e-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: 41.38  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1441 DILWVKVGRYRWWPAEVTqpkSVPENISRMKhevGEFPVHFFGSKDyVWTYQARC-FPYMEgdanNKEKMGKGADavyKK 1519
Cdd:cd05834     5 DLVFAKVKGYPPWPARID---EIPEGAKIPK---NKYPVFFYGTHE-TAFLKPKDlFPYEE----NKEKYGKPRK---RK 70

                  ....*
gi 292621054 1520 ALNEA 1524
Cdd:cd05834    71 GFNEG 75
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
1701-1741 3.76e-04

SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing protein 4 (SMYD4) and similar proteins; SMYD4 functions as a potential tumor suppressor that plays a critical role in breast carcinogenesis at least partly through inhibiting the expression of PDGFR-alpha. In zebrafish, SMYD4 is ubiquitously expressed in early embryos and becomes enriched in the developing heart; mutants show a strong defect in cardiomyocyte proliferation, which lead to a severe cardiac malformation.


Pssm-ID: 380934 [Multi-domain]  Cd Length: 218  Bit Score: 44.21  E-value: 3.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 292621054 1701 FMNHSCQPNCETqkwTVNGDTrVGLFALEDIPKGVELTFNY 1741
Cdd:cd10536   153 LLNHSCDPNTIR---SFYGNT-IVVRATRPIKKGEEITICY 189
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
1228-1270 4.16e-04

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


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 39.78  E-value: 4.16e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 292621054  1228 VCQVCEKT---GELLLCEGqCCGAFHLQCIGLTET----PKGRFICQECK 1270
Cdd:pfam00628    1 YCAVCGKSddgGELVQCDG-CDDWFHLACLGPPLDpaeiPSGEWLCPECK 49
PHD1_CHD_II cd15531
PHD finger 1 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...
1229-1269 4.74e-04

PHD finger 1 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD proteins includes chromodomain-helicase-DNA-binding protein CHD3, CHD4, and CHD5, which are nuclear and ubiquitously expressed chromatin remodelling ATPases generally associated with histone deacetylases (HDACs). They are involved in DNA Double Strand Break (DSB) signaling, DSB repair and/or p53-dependent pathways such as apoptosis and senescence, as well as in the maintenance of genomic stability, and/or cancer prevention. They function as subunits of the Nucleosome Remodelling and Deacetylase (NuRD) complex, which is generally associated with gene repression, heterochromatin formation, and overall chromatin compaction. In contrast to the class I CHD enzymes (CHD1 and CHD2), class II CHD proteins lack identifiable DNA-binding domains, but possess a C-terminal coiled-coil region. Moreover, in addition to the tandem chromodomains and a helicase domain, they all harbor tandem plant homeodomain (PHD) zinc fingers involved in the recognition of methylated histone tails. This model corresponds to the first PHD finger.


Pssm-ID: 277006 [Multi-domain]  Cd Length: 43  Bit Score: 39.51  E-value: 4.74e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292621054 1229 CQVCEKTGELLLCEgQCCGAFHLQCIG--LTETPKGRFICQEC 1269
Cdd:cd15531     2 CEVCQQGGEIILCD-TCPRAYHLVCLDpeLEKAPEGKWSCPHC 43
PWWP_PWWP2 cd20140
PWWP domain found in the PWWP domain-containing protein 2 (PWWP2) family; The PWWP2 family ...
289-308 5.01e-04

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: 41.09  E-value: 5.01e-04
                          10        20
                  ....*....|....*....|
gi 292621054  289 GDVVWAKFNRRPWWPCHVTT 308
Cdd:cd20140     7 GDIVWGKIHGFPWWPGRILS 26
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
1228-1269 5.24e-04

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


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 39.61  E-value: 5.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 292621054 1228 VCQVCEKTG----ELLLCEGqCCGAFHLQCIGLTET---PKGRFICQEC 1269
Cdd:cd15489     1 SCIVCGKGGdlggELLQCDG-CGKWFHADCLGPPLSsfvPNGKWICPVC 48
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
1803-1844 5.90e-04

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 39.50  E-value: 5.90e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 292621054   1803 CFYCG---DGGQIVSCKkpGCPKVYHADCLNLSKR---PAGRWECPWH 1844
Cdd:smart00249    2 CSVCGkpdDGGELLQCD--GCDRWYHQTCLGPPLLeeePDGKWYCPKC 47
PWWP_AtATX1-like cd20142
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
289-354 8.22e-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: 40.41  E-value: 8.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 292621054  289 GDVVWAKFNRRPWWPCHVTTDPQIdVHTKMKDPSRRPCRLYFVRMFGEiVDQAWVPAKATFPFEGG 354
Cdd:cd20142     3 GDVVWAKVKGYPMWPALVIDEEHA-ERCGLEANRPGKKGTVPVQFFGT-YEVARLNPKKVVGFSKG 66
PHD4_NSD3 cd15658
PHD finger 4 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...
1803-1849 9.19e-04

PHD finger 4 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed histone-lysine N-methyltransferase NSD3, or protein whistle, or 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 fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fourth PHD finger.


Pssm-ID: 277128  Cd Length: 40  Bit Score: 38.74  E-value: 9.19e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 292621054 1803 CFYCGDGGQIVSCKkpGCPKVYHADCLNLsKRPAGRWecpwhQCNEC 1849
Cdd:cd15658     2 CFVCARGGRLLCCE--SCPASFHPECLSI-EMPEGCW-----NCNEC 40
PHD5_NSD2 cd15660
PHD finger 5 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed ...
1229-1266 9.27e-04

PHD finger 5 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed histone-lysine N-methyltransferase NSD2, or 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, by 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 fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD fingers mediate chromatin interaction and recognition of histone marks. This model corresponds to the fifth PHD finger.


Pssm-ID: 277130  Cd Length: 43  Bit Score: 38.76  E-value: 9.27e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 292621054 1229 CQVCEKTGELLLCEGQ-CCGAFHLQCIGLTETPKGRFIC 1266
Cdd:cd15660     2 CFRCGDGGQLVLCDRKsCTKAYHLSCLGLTKRPFGKWEC 40
PWWP_PSIP cd20151
PWWP domain found in PC4 and SFRS1-interacting protein (PSIP); PSIP, also called ...
1441-1523 9.51e-04

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: 39.97  E-value: 9.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1441 DILWVKVGRYRWWPAEVTQpksVPEniSRMKHEVGEFPVHFFGSKDYVWTYQARCFPYMEgdanNKEKMGKGADavyKKA 1520
Cdd:cd20151     5 DLIFAKMKGYPHWPARVDE---VPD--GAVKPPTNKLPIFFFGTHETAFLGPKDIFPYSE----NKEKYGKPNK---RKG 72

                  ...
gi 292621054 1521 LNE 1523
Cdd:cd20151    73 FNE 75
PHD_ING3 cd15585
PHD finger found in inhibitor of growth protein 3 (ING3) and similar proteins; ING3, also ...
1236-1269 1.04e-03

PHD finger found in inhibitor of growth protein 3 (ING3) and similar proteins; ING3, also termed p47ING3, is one member of the inhibitor of growth (ING) family of type II tumor suppressors. It is ubiquitously expressed and has been implicated in transcription modulation, cell cycle control, and the induction of apoptosis. It is an important subunit of human NuA4 histone acetyltransferase complex, which regulates the acetylation of histones H2A and H4. Moreover, ING3 promotes ultraviolet (UV)-induced apoptosis through the Fas/caspase-8-dependent pathway in melanoma cells. It physically interacts with subunits of E3 ligase Skp1-Cullin-F-boxprotein complex (SCF complex) and is degraded by the SCF (F-box protein S-phase kinase-associated protein 2, Skp2)-mediated ubiquitin-proteasome system. It also acts as a suppression factor during tumorigenesis and progression of hepatocellular carcinoma (HCC). ING3 contains an N-terminal ING domain and a C-terminal plant homeodomain (PHD) finger.


Pssm-ID: 277060 [Multi-domain]  Cd Length: 45  Bit Score: 38.59  E-value: 1.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 292621054 1236 GELLLCEGQCCGA--FHLQCIGLTETPKGRFICQEC 1269
Cdd:cd15585    10 GEMVGCDNDDCPIewFHYGCVGLTEAPKGKWYCPQC 45
PHD_ING cd15505
PHD finger found in the inhibitor of growth (ING) protein family; The ING family includes a ...
1236-1269 1.15e-03

PHD finger found in the inhibitor of growth (ING) protein family; The ING family includes a group of tumor suppressors, ING1-5, which act as readers and writers of the histone epigenetic code, affecting DNA damage response, chromatin remodeling, cellular senescence, differentiation, cell cycle regulation and apoptosis. They may have a general role in mediating the cellular response to genotoxic stress through binding to and regulating the activities of histone acetyltransferase (HAT) and histone deacetylase (HDAC) chromatin remodeling complexes. All ING proteins contain an N-terminal ING domain and a C-terminal plant homeodomain (PHD) finger.


Pssm-ID: 276980 [Multi-domain]  Cd Length: 45  Bit Score: 38.43  E-value: 1.15e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 292621054 1236 GELLLCEGQCC--GAFHLQCIGLTETPKGRFICQEC 1269
Cdd:cd15505    10 GEMVACDNPNCpiEWFHFECVGLTAKPKGKWYCPEC 45
PHD2_PHF10 cd15529
PHD finger 2 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed ...
1228-1269 1.20e-03

PHD finger 2 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed BRG1-associated factor 45a (BAF45a), or XAP135, is a ubiquitously expressed transcriptional regulator that is required for maintaining the undifferentiated status of neuroblasts. It contains a SAY (supporter of activation of yellow) domain and two adjacent plant homeodomain (PHD) fingers. This model corresponds to the second PHD finger.


Pssm-ID: 277004  Cd Length: 44  Bit Score: 38.44  E-value: 1.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 292621054 1228 VCQVCEKTG---ELLLCEgQCCGAFHLQCIGLTETPKGRFICQEC 1269
Cdd:cd15529     1 TCTKCGDPHdedKMMFCD-QCDRGYHTFCVGLRSIPDGRWICPLC 44
PHD_PRKCBP1 cd15538
PHD finger found in protein kinase C-binding protein 1 (PRKCBP1); PRKCBP1, also termed ...
1229-1269 1.21e-03

PHD finger found in protein kinase C-binding protein 1 (PRKCBP1); PRKCBP1, also termed cutaneous T-cell lymphoma-associated antigen se14-3 (CTCL-associated antigen se14-3), or 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; the 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.


Pssm-ID: 277013  Cd Length: 41  Bit Score: 38.46  E-value: 1.21e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 292621054 1229 CQVCEKTGELLLCEgQCCGAFHLQCIGLTETPKGRFICQEC 1269
Cdd:cd15538     2 CWRCHKEGQVLCCS-LCPRVYHKKCLKLTSEPDEDWVCPEC 41
PHD_BAZ2A_like cd15545
PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A) and 2B ...
1393-1431 1.24e-03

PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A) and 2B (BAZ2B); BAZ2A, also termed transcription termination factor I-interacting protein 5 (TTF-I-interacting protein 5, or Tip5), or WALp3, is an epigenetic regulator. It has been implicated in epigenetic rRNA gene silencing, as the large subunit of the SNF2h-containing chromatin-remodeling complex NoRC that induces nucleosome sliding in an ATP- and histone H4 tail-dependent fashion. BAZ2A has also been shown to be broadly overexpressed in prostate cancer, to regulate numerous protein-coding genes and to cooperate with EZH2 (enhancer of zeste homolog 2) to maintain epigenetic silencing at genes repressed in prostate cancer metastasis. Its overexpression is tightly associated with a prostate cancer subtype displaying CpG island methylator phenotype (CIMP) in tumors and with prostate cancer recurrence in patients. BAZ2B, also termed WALp4, is a bromodomain-containing protein whose biological role is still elusive. It shows high sequence similarly with BAZ2A. Both BAZ2A and BAZ2B contain a TAM (TIP5/ARBP/MBD) domain, a DDT domain, four AT-hooks, BAZ 1 and BAZ 2 motifs, a WAKZ (WSTF/Acf1/KIAA0314/ZK783.4) motif, a plant homeodomain (PHD) finger, and a bromodomain. BAZ2B also harbors an extra Apolipophorin-III like domain in its N-terminal region.


Pssm-ID: 277020 [Multi-domain]  Cd Length: 46  Bit Score: 38.45  E-value: 1.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 292621054 1393 CFVCSEG---GSLLCCESCPAAFHRECLNIEM---PQGSWFCNDC 1431
Cdd:cd15545     2 CQICRSGdneDQLLLCDGCDRGYHTYCFKPKMtnvPEGDWFCPEC 46
PWWP_NSD3_rpt1 cd20163
first PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar proteins; ...
1438-1498 1.40e-03

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: 40.69  E-value: 1.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 292621054 1438 HYKDILWVKVGRYRWWPAEVTQPKSVPENISRMKHEVGEFPVHFFGSK-DYVWTYQARCFPY 1498
Cdd:cd20163     2 QVGDLVWSKVGTYPWWPCMVSSDPQLEVHTKINTRGAREYHVQFFSSQpERAWVHEKRVREY 63
PHD2_CHD_II cd15532
PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...
1228-1269 1.55e-03

PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD proteins includes chromodomain-helicase-DNA-binding protein CHD3, CHD4, and CHD5, which are nuclear and ubiquitously expressed chromatin remodelling ATPases generally associated with histone deacetylases (HDACs). They are involved in DNA Double Strand Break (DSB) signaling, DSB repair and/or p53-dependent pathways such as apoptosis and senescence, as well as in the maintenance of genomic stability, and/or cancer prevention. They function as subunits of the Nucleosome Remodelling and Deacetylase (NuRD) complex, which is generally associated with gene repression, heterochromatin formation, and overall chromatin compaction. In contrast to the class I CHD enzymes (CHD1 and CHD2), class II CHD proteins lack identifiable DNA-binding domains, but possess a C-terminal coiled-coil region. Moreover, in addition to the tandem chromodomains and a helicase domain, they all harbor tandem plant homeodomain (PHD) zinc fingers involved in the recognition of methylated histone tails. This model corresponds to the second PHD finger.


Pssm-ID: 277007 [Multi-domain]  Cd Length: 43  Bit Score: 38.03  E-value: 1.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 292621054 1228 VCQVCEKTGELLLCEGqCCGAFHLQCIG--LTETPKGRFICQEC 1269
Cdd:cd15532     1 FCRVCKDGGELLCCDG-CPSSYHLHCLNppLAEIPDGDWFCPRC 43
PHD_ING3 cd15585
PHD finger found in inhibitor of growth protein 3 (ING3) and similar proteins; ING3, also ...
1810-1846 1.66e-03

PHD finger found in inhibitor of growth protein 3 (ING3) and similar proteins; ING3, also termed p47ING3, is one member of the inhibitor of growth (ING) family of type II tumor suppressors. It is ubiquitously expressed and has been implicated in transcription modulation, cell cycle control, and the induction of apoptosis. It is an important subunit of human NuA4 histone acetyltransferase complex, which regulates the acetylation of histones H2A and H4. Moreover, ING3 promotes ultraviolet (UV)-induced apoptosis through the Fas/caspase-8-dependent pathway in melanoma cells. It physically interacts with subunits of E3 ligase Skp1-Cullin-F-boxprotein complex (SCF complex) and is degraded by the SCF (F-box protein S-phase kinase-associated protein 2, Skp2)-mediated ubiquitin-proteasome system. It also acts as a suppression factor during tumorigenesis and progression of hepatocellular carcinoma (HCC). ING3 contains an N-terminal ING domain and a C-terminal plant homeodomain (PHD) finger.


Pssm-ID: 277060 [Multi-domain]  Cd Length: 45  Bit Score: 38.20  E-value: 1.66e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 292621054 1810 GQIVSCKKPGCP-KVYHADCLNLSKRPAGRWECPwhQC 1846
Cdd:cd15585    10 GEMVGCDNDDCPiEWFHYGCVGLTEAPKGKWYCP--QC 45
PHD4_NSD3 cd15658
PHD finger 4 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...
1229-1269 1.81e-03

PHD finger 4 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed histone-lysine N-methyltransferase NSD3, or protein whistle, or 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 fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fourth PHD finger.


Pssm-ID: 277128  Cd Length: 40  Bit Score: 37.97  E-value: 1.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 292621054 1229 CQVCEKTGELLLCEGqCCGAFHLQCIGLtETPKGRFICQEC 1269
Cdd:cd15658     2 CFVCARGGRLLCCES-CPASFHPECLSI-EMPEGCWNCNEC 40
PHD_PRKCBP1 cd15538
PHD finger found in protein kinase C-binding protein 1 (PRKCBP1); PRKCBP1, also termed ...
1803-1842 1.82e-03

PHD finger found in protein kinase C-binding protein 1 (PRKCBP1); PRKCBP1, also termed cutaneous T-cell lymphoma-associated antigen se14-3 (CTCL-associated antigen se14-3), or 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; the 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.


Pssm-ID: 277013  Cd Length: 41  Bit Score: 37.69  E-value: 1.82e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 292621054 1803 CFYCGDGGQIVSCKKpgCPKVYHADCLNLSKRPAGRWECP 1842
Cdd:cd15538     2 CWRCHKEGQVLCCSL--CPRVYHKKCLKLTSEPDEDWVCP 39
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
286-359 1.86e-03

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: 39.12  E-value: 1.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 292621054  286 YSIGDVVWAKFNRRPWWPCHVtTDPQIDVhtkMKDPSRRPCrlYFVRMFGEiVDQAWVPAKATFPFEGG-DQFEK 359
Cdd:cd05836     1 FKIGDLVWAKMKGFPPWPGKI-VNPPPDL---KKPPRKKKM--HCVYFFGS-ENYAWIEDENIKPYEEFkEEMLK 68
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
1275-1321 1.89e-03

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


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 38.07  E-value: 1.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 292621054 1275 TCFVCKKPDKEVRRCMI-PVCGKFYHMDCILKYSPTVAQNRGFRCSIH 1321
Cdd:cd15489     1 SCIVCGKGGDLGGELLQcDGCGKWFHADCLGPPLSSFVPNGKWICPVC 48
PHD_TIF1_like cd15541
PHD finger found in the transcriptional intermediary factor 1 (TIF1) family and similar ...
1802-1841 1.92e-03

PHD finger found in the transcriptional intermediary factor 1 (TIF1) family and similar proteins; The TIF1 family of transcriptional cofactors includes TIF1alpha (TRIM24), TIF1beta (TRIM28), TIF1gamma (TRIM33), and TIF1delta (TRIM66), which are characterized by an N-terminal RING-finger B-box coiled-coil (RBCC/TRIM) motif and plant homeodomain (PHD) finger followed by a bromodomain in the C-terminal region. TIF1 proteins couple chromatin modifications to transcriptional regulation, signaling, and tumor suppression. They exert a deacetylase-dependent silencing effect when tethered to a promoter region. TIF1alpha, TIF1beta, and TIF1delta can homodimerize and contain a PXVXL motif necessary and sufficient for heterochromatin protein 1(HP1) binding. TIF1alpha and TIF1beta bind nuclear receptors and Kruppel-associated boxes (KRAB) specifically and respectively. In contrast, TIF1delta appears to lack nuclear receptor- and KRAB-binding activity. Moreover, TIF1delta is specifically involved in heterochromatin-mediated gene silencing during postmeiotic phases of spermatogenesis. TIF1gamma is structurally closely related to TIF1alpha and TIF1beta, but has very little functional features in common with them. It does not interact with the KRAB silencing domain of KOX1 or the heterochromatinic proteins HP1alpha, beta, and gamma. It cannot bind to nuclear receptors (NRs). This family also includes Sp100/Sp140 family proteins, the nuclear body SP100 and SP140. Sp110 is a leukocyte-specific component of the nuclear body. It may function as a nuclear hormone receptor transcriptional coactivator that may play a role in inducing differentiation of myeloid cells. It is also involved in resisting intracellular pathogens and functions as an important drug target for preventing intracellular pathogen diseases, such as tuberculosis, hepatic veno-occlusive disease, and intracellular cancers. SP140 is an interferon inducible nuclear leukocyte-specific protein involved in primary biliary cirrhosis and a risk factor in chronic lymphocytic leukemia. It is also implicated in innate immune response to human immunodeficiency virus type 1 (HIV-1) by binding to the virus viral infectivity factor (Vif) protein. Both Sp110 and Sp140 contain a SAND domain, a plant homeodomain (PHD) finger, and a bromodomain (BRD).


Pssm-ID: 277016 [Multi-domain]  Cd Length: 43  Bit Score: 37.71  E-value: 1.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 292621054 1802 ECFYCGDGGQIVSCKKpgCPKVYHADCL--NLSKRPAGRWEC 1841
Cdd:cd15541     1 WCAVCQNGGELLCCDK--CPRVFHLDCHipPIPEFPSGEWSC 40
TNG2 COG5034
Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];
1108-1270 1.94e-03

Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];


Pssm-ID: 227367 [Multi-domain]  Cd Length: 271  Bit Score: 42.23  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1108 RQHKTNPEESGVRDLEKqEEAGPPPSSPCAVSAQSEGElRTSSPIQPDVPSVSQIPVEGEQSSPSKPQINNEDSLISEGF 1187
Cdd:COG5034    97 RRHRKLLDDRIAKRPHE-KVAARIENCHDAVSRLERNS-YSSAARRSSGEHRSAASSQGSRHTKLKKRKNIHNLKRRSPE 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1188 AAGLNDSAFSsrdsLSGDLSGLSTNKRSVERGGGASLKENVCQVCEKTGELLLCEGQ---------CCGA------FHLQ 1252
Cdd:COG5034   175 LSSKREVSFT----LESPSVPDTATRVKEGNNGGSTKSRGVSSEDNSEGEELYCFCQqvsygqmvaCDNAnckrewFHLE 250
                         170
                  ....*....|....*...
gi 292621054 1253 CIGLTETPKGRFICQECK 1270
Cdd:COG5034   251 CVGLKEPPKGKWYCPECK 268
PHD1_PHF12 cd15533
PHD finger 1 found in PHD finger protein 12 (PHF12); PHF12, also termed PHD factor 1 (Pf1), is ...
1228-1269 1.98e-03

PHD finger 1 found in PHD finger protein 12 (PHF12); PHF12, also termed PHD factor 1 (Pf1), is a plant homeodomain (PHD) zinc finger-containing protein that bridges the transducin-like enhancer of split (TLE) corepressor to the mSin3A-histone deacetylase (HDAC)-complex, and further represses transcription at targeted genes. PHF12 also interacts with MRG15 (mortality factor-related genes on chromosome 15), a member of the mortality factor (MORF) family of proteins implicated in regulating cellular senescence. PHF12 contains two plant-homeodomain (PHD) zinc fingers followed by a polybasic region. The PHD fingers function downstream of phosphoinositide signaling triggered by the interaction between polybasic regions and phosphoinositides. This model corresponds to the first PHD finger.


Pssm-ID: 277008 [Multi-domain]  Cd Length: 45  Bit Score: 37.72  E-value: 1.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 292621054 1228 VCQVCEKTGELLLCEgQCCGAFHLQC----IGLTETPKGRFICQEC 1269
Cdd:cd15533     1 YCDSCGEGGDLLCCD-RCPASFHLQCcnppLDEEDLPPGEWLCHRC 45
PHD_BAZ1A cd15627
PHD finger found in bromodomain adjacent to zinc finger domain protein 1A (BAZ1A); BAZ1A, also ...
1393-1431 2.00e-03

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


Pssm-ID: 277097 [Multi-domain]  Cd Length: 46  Bit Score: 37.76  E-value: 2.00e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 292621054 1393 CFVCSEGG---SLLCCESCPAAFHRECLNIEM---PQGSWFCNDC 1431
Cdd:cd15627     2 CRICRRKGdaeKMLLCDGCDRGHHMYCLRPPLkkvPEGDWFCPDC 46
PHD_BS69 cd15537
PHD finger found in protein BS69; Protein BS69, also termed zinc finger MYND domain-containing ...
1392-1431 2.22e-03

PHD finger found in protein BS69; Protein BS69, also termed 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.


Pssm-ID: 277012  Cd Length: 43  Bit Score: 37.71  E-value: 2.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292621054 1392 WCFVCSEGGSLLCCESCPAAFHRECLNIEMPQGS---WFCNDC 1431
Cdd:cd15537     1 YCFECHAPGEVLPCSGCFRVYHSDCLSEDFRPDStshWTCPVC 43
PHD5_NSD3 cd15661
PHD finger 5 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...
1229-1266 2.36e-03

PHD finger 5 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed histone-lysine N-methyltransferase NSD3, or protein whistle, or 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 fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fifth PHD finger.


Pssm-ID: 277131  Cd Length: 43  Bit Score: 37.64  E-value: 2.36e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 292621054 1229 CQVCEKTGELLLCEGQ-CCGAFHLQCIGLTETPKGRFIC 1266
Cdd:cd15661     2 CFQCGDGGELVMCDKKdCPKAYHLLCLNLTQPPYGKWEC 40
PHD_ING4_5 cd15586
PHD finger found in inhibitor of growth protein 4 (ING4) and 5 (ING5); ING4, also termed ...
1236-1269 2.45e-03

PHD finger found in inhibitor of growth protein 4 (ING4) and 5 (ING5); ING4, also termed p29ING4, and ING5, also termed p28ING5, belong to the inhibitor of growth (ING) family of type II tumor suppressors. ING4 acts as an E3 ubiquitin ligase to induce ubiquitination of the p65 subunit of NF-kappaB and inhibit the transactivation of NF-kappaB target genes. It also induces apoptosis through a p53 dependent pathway, including increasing p53 acetylation, inhibiting Mdm2-mediated degradation of p53 and enhancing the expression of p53 responsive genes both at the transcriptional and post-translational levels. Moreover, ING4 can inhibit the translation of proto-oncogene MYC by interacting with AUF1. It also regulates other transcription factors, such as hypoxia-inducible factor (HIF). ING5 is a Tip60 cofactor that acetylates p53 at K120 and subsequently activates the expression of p53-dependent apoptotic genes in response to DNA damage. Aberrant ING5 expression may contribute to pathogenesis, growth, and invasion of gastric carcinomas and colorectal cancer. ING5 can physically interact with p300 and p53 in vivo, and its overexpression induces apoptosis in colorectal cancer cells. It also associates with cyclin A1 (INCA1) and functions as a growth suppressor with suppressed expression in Acute Myeloid Leukemia (AML). Moreover, ING5 translocation from the nucleus to the cytoplasm might be a critical event for carcinogenesis and tumor progression in human head and neck squamous cell carcinoma. Both ING4 and ING5 contain an N-terminal ING histone-binding domain and a C-terminal plant homeodomain (PHD) finger. They associate with histone acetyltransferase (HAT) complexes containing MOZ (monocytic leukemia zinc finger protein)/MORF (MOZ-related factor) and HBO1, and further direct the MOZ/MORF and HBO1 complexes to chromatin.


Pssm-ID: 277061 [Multi-domain]  Cd Length: 45  Bit Score: 37.55  E-value: 2.45e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 292621054 1236 GELLLCEGQCCGA--FHLQCIGLTETPKGRFICQEC 1269
Cdd:cd15586    10 GEMIGCDNPDCPIewFHFACVGLTTKPKGKWFCPRC 45
PHD_BAZ1A_like cd15544
PHD finger found in bromodomain adjacent to zinc finger domain protein BAZ1A and BAZ1B; BAZ1A, ...
1393-1431 2.89e-03

PHD finger found in bromodomain adjacent to zinc finger domain protein BAZ1A and BAZ1B; BAZ1A, also termed ATP-dependent chromatin-remodeling protein, or ATP-utilizing chromatin assembly and remodeling factor 1 (ACF1), or CHRAC subunit ACF1, or Williams syndrome transcription factor-related chromatin-remodeling factor 180 (WCRF180), or WALp1, is a subunit of the conserved imitation switch (ISWI)-family ATP-dependent chromatin assembly and remodeling factor (ACF)/chromatin accessibility complex (CHRAC) chromatin remodeling complex, which is required for DNA replication through heterochromatin. It alters the remodeling properties of the ATPase motor protein sucrose nonfermenting-2 homolog (SNF2H). Moreover, BAZ1A and its complexes play important roles in DNA double-strand break (DSB) repair. It is essential for averting improper gene expression during spermatogenesis. It also regulates transcriptional repression of vitamin D3 receptor-regulated genes. BAZ1B, also termed Tyrosine-protein kinase BAZ1B, or Williams syndrome transcription factor (WSTF), or Williams-Beuren syndrome chromosomal region 10 protein, Williams-Beuren syndrome chromosomal region 9 protein, or WALp2, is a multifunctional protein implicated in several nuclear processes, including replication, transcription, and the DNA damage response. BAZ1B/WSTF, together with the imitation switch (ISWI) ATPase, forms a WSTF-ISWI chromatin remodeling complex (WICH), which transiently associates with the human inactive X chromosome (Xi) during late S-phase prior to BRCA1 and gamma-H2AX. Moreover, BAZ1B/WSTF, SNF2h, and nuclear myosin 1 (NM1) forms the chromatin remodeling complex B-WICH that is involved in regulating rDNA transcription. Both BAZ1A and BAZ1B contain a WAC motif, a DDT domain, BAZ 1 and BAZ 2 motifs, a WAKZ (WSTF/Acf1/KIAA0314/ZK783.4) motif, a plant homeodomain (PHD) finger, and a bromodomain.


Pssm-ID: 277019  Cd Length: 46  Bit Score: 37.39  E-value: 2.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 292621054 1393 CFVC---SEGGSLLCCESCPAAFHRECLN---IEMPQGSWFCNDC 1431
Cdd:cd15544     2 CKVCrkkGDPDNMILCDGCDKAFHLYCLRpalREVPSGDWFCPAC 46
PHD_Phf1p_Phf2p_like cd15502
PHD finger found in Schizosaccharomyces pombe SWM histone demethylase complex subunits Phf1 ...
1393-1431 2.91e-03

PHD finger found in Schizosaccharomyces pombe SWM histone demethylase complex subunits Phf1 (Phf1p) and Phf2 (Phf2p); Phf1p and Phf2p are components of the SWM histone demethylase complex that specifically demethylates histone H3 at lysine 9 (H3K9me2), a specific tag for epigenetic transcriptional activation. They function as corepressors and play roles in regulating heterochromatin propagation and euchromatic transcription. Both Phf1p and Phf2p contain a plant homeodomain (PHD) finger.


Pssm-ID: 276977  Cd Length: 52  Bit Score: 37.80  E-value: 2.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 292621054 1393 CFVCSEGGS-----LLCCESCPAAFHRECLN-------IEMPQGSWFCNDC 1431
Cdd:cd15502     2 CIVCQRGHSpksnrIVFCDGCNTPYHQLCHDpsiddevVEDPDAEWFCKKC 52
PHD4_NSD2 cd15657
PHD finger 4 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed ...
1803-1841 3.12e-03

PHD finger 4 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed histone-lysine N-methyltransferase NSD2, or 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, by 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 fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD fingers mediate chromatin interaction and recognition of histone marks. This model corresponds to the fourth PHD finger.


Pssm-ID: 277127  Cd Length: 41  Bit Score: 37.29  E-value: 3.12e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 292621054 1803 CFYCGDGGQIVSCKKpgCPKVYHADCLNLSkRPAGRWEC 1841
Cdd:cd15657     2 CFVCSKGGSLLCCES--CPAAFHPDCLNIE-MPDGSWFC 37
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
1803-1844 3.37e-03

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


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 37.30  E-value: 3.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 292621054 1803 CFYCGDGGQ----IVSCKKpgCPKVYHADCLNL---SKRPAGRWECPWH 1844
Cdd:cd15489     2 CIVCGKGGDlggeLLQCDG--CGKWFHADCLGPplsSFVPNGKWICPVC 48
PWWP_PRKCBP1 cd20160
PWWP domain found in protein kinase C-binding protein 1 (PRKCBP1) and similar proteins; ...
1435-1535 3.48e-03

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: 38.70  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1435 KKPHYkdILWVKVGRYRWWPAEVtqpksvpenisrMKHEVGEFPVHFFGSKDYVWTYQARCFPYMEGDANNKEKMGKGad 1514
Cdd:cd20160     4 RKPHL--LVWAKLKGFPFWPAKA------------LRVNNGQVDVRFFGAHDRAWVPVKDCYLYSKEPPTSVKKKKSG-- 67
                          90       100
                  ....*....|....*....|.
gi 292621054 1515 avYKKALNEaADRFRELLKEK 1535
Cdd:cd20160    68 --LDEAMEE-LEIHIEKLREK 85
PHD5_NSD2 cd15660
PHD finger 5 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed ...
1393-1428 3.87e-03

PHD finger 5 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed histone-lysine N-methyltransferase NSD2, or 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, by 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 fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD fingers mediate chromatin interaction and recognition of histone marks. This model corresponds to the fifth PHD finger.


Pssm-ID: 277130  Cd Length: 43  Bit Score: 36.84  E-value: 3.87e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 292621054 1393 CFVCSEGGSLLCCE--SCPAAFHRECLNI-EMPQGSWFC 1428
Cdd:cd15660     2 CFRCGDGGQLVLCDrkSCTKAYHLSCLGLtKRPFGKWEC 40
TNG2 COG5034
Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];
1786-1853 4.26e-03

Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];


Pssm-ID: 227367 [Multi-domain]  Cd Length: 271  Bit Score: 41.46  E-value: 4.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 292621054 1786 SGKRKSQSEVTKErEDECFYC----GDGGQIVSCKKPGCPKV-YHADCLNLSKRPAGRWECPwhqcnECGREA 1853
Cdd:COG5034   205 STKSRGVSSEDNS-EGEELYCfcqqVSYGQMVACDNANCKREwFHLECVGLKEPPKGKWYCP-----ECKKAA 271
PHD_BAZ1A_like cd15544
PHD finger found in bromodomain adjacent to zinc finger domain protein BAZ1A and BAZ1B; BAZ1A, ...
1229-1269 4.60e-03

PHD finger found in bromodomain adjacent to zinc finger domain protein BAZ1A and BAZ1B; BAZ1A, also termed ATP-dependent chromatin-remodeling protein, or ATP-utilizing chromatin assembly and remodeling factor 1 (ACF1), or CHRAC subunit ACF1, or Williams syndrome transcription factor-related chromatin-remodeling factor 180 (WCRF180), or WALp1, is a subunit of the conserved imitation switch (ISWI)-family ATP-dependent chromatin assembly and remodeling factor (ACF)/chromatin accessibility complex (CHRAC) chromatin remodeling complex, which is required for DNA replication through heterochromatin. It alters the remodeling properties of the ATPase motor protein sucrose nonfermenting-2 homolog (SNF2H). Moreover, BAZ1A and its complexes play important roles in DNA double-strand break (DSB) repair. It is essential for averting improper gene expression during spermatogenesis. It also regulates transcriptional repression of vitamin D3 receptor-regulated genes. BAZ1B, also termed Tyrosine-protein kinase BAZ1B, or Williams syndrome transcription factor (WSTF), or Williams-Beuren syndrome chromosomal region 10 protein, Williams-Beuren syndrome chromosomal region 9 protein, or WALp2, is a multifunctional protein implicated in several nuclear processes, including replication, transcription, and the DNA damage response. BAZ1B/WSTF, together with the imitation switch (ISWI) ATPase, forms a WSTF-ISWI chromatin remodeling complex (WICH), which transiently associates with the human inactive X chromosome (Xi) during late S-phase prior to BRCA1 and gamma-H2AX. Moreover, BAZ1B/WSTF, SNF2h, and nuclear myosin 1 (NM1) forms the chromatin remodeling complex B-WICH that is involved in regulating rDNA transcription. Both BAZ1A and BAZ1B contain a WAC motif, a DDT domain, BAZ 1 and BAZ 2 motifs, a WAKZ (WSTF/Acf1/KIAA0314/ZK783.4) motif, a plant homeodomain (PHD) finger, and a bromodomain.


Pssm-ID: 277019  Cd Length: 46  Bit Score: 37.01  E-value: 4.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 292621054 1229 CQVCEKTGE---LLLCEGqCCGAFHLQCI--GLTETPKGRFICQEC 1269
Cdd:cd15544     2 CKVCRKKGDpdnMILCDG-CDKAFHLYCLrpALREVPSGDWFCPAC 46
PHD1_BPTF cd15559
PHD finger 1 found in bromodomain and PHD finger-containing transcription factor (BPTF); BPTF, ...
1229-1269 4.80e-03

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


Pssm-ID: 277034 [Multi-domain]  Cd Length: 43  Bit Score: 36.62  E-value: 4.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292621054 1229 CQVCEKTGELLLCEgQCCGAFHLQCIG--LTETPKGRFICQEC 1269
Cdd:cd15559     2 CRVCHKLGDLLCCE-TCSAVYHLECVDppLEEVPEEDWQCEVC 43
PHD2_KAT6A_6B cd15527
PHD finger 2 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ, ...
1229-1269 5.09e-03

PHD finger 2 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ, also termed histone acetyltransferase KAT6A, YBF2/SAS3, SAS2 and TIP60 protein 3 (MYST-3), or runt-related transcription factor-binding protein 2, or zinc finger protein 220, is a MYST-type histone acetyltransferase (HAT) that functions as a coactivator for acute myeloid leukemia 1 protein (AML1)- and p53-dependent transcription. It possesses intrinsic HAT activity to acetylate both itself and lysine (K) residues on histone H2B, histone H3 (K14) and histone H4 (K5, K8, K12 and K16) in vitro and H3K9 in vivo. MOZ-related factor (MORF), also termed MOZ2, or histone acetyltransferase KAT6B, or MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4 (MYST4), is a ubiquitously expressed transcriptional regulator with intrinsic HAT activity. It can interact with the Runt-domain transcription factor Runx2 and form a tetrameric complex with BRPFs, ING5, and EAF6. Both MOZ and MORF are catalytic subunits of HAT complexes that are required for normal developmental programs, such as hematopoiesis, neurogenesis, and skeletogenesis, and are also implicated in human leukemias. MOZ is also the catalytic subunit of a tetrameric inhibitor of growth 5 (ING5) complex, which specifically acetylates nucleosomal histone H3K14. Moreover, MOZ and MORF are involved in regulating transcriptional activation mediated by Runx2 (or Cbfa1), a Runt-domain transcription factor known to play important roles in T cell lymphomagenesis and bone development, and its homologs. MOZ contains a linker histone 1 and histone 5 domains and two plant homeodomain (PHD) fingers. In contrast, MORF contains an N-terminal region containing two PHD fingers, a putative HAT domain, an acidic region, and a C-terminal Ser/Met-rich domain. The family corresponds to the first PHD finger.


Pssm-ID: 277002  Cd Length: 46  Bit Score: 36.59  E-value: 5.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 292621054 1229 CQVCEKTGE---LLLCEGqCCGAFHLQCIG--LTETPKGRFICQEC 1269
Cdd:cd15527     2 CSVCQDSGNadnLLFCDA-CDKGFHMECHDppLTRMPKGKWVCQIC 46
PWWP_PWWP2B cd20153
PWWP domain found in PWWP domain-containing protein 2B (PWWP2B); PWWP2B is a paralog of PWWP2A, ...
1434-1534 5.28e-03

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


Pssm-ID: 438981  Cd Length: 116  Bit Score: 38.78  E-value: 5.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292621054 1434 GKKPHYKDILWVKVGRYRWWPAEVTqpksvpeNISRMKHEVG-----EFPVHFFGSKDYVWTYQARCFPYMEgdaNNKEK 1508
Cdd:cd20153    11 GRTVSVGDIVWGKIHGFPWWPARVL-------SISLSQKEDGepswqEAKVSWFGSPTTSLLSVSKLSPFSE---FFKLR 80
                          90       100
                  ....*....|....*....|....*.
gi 292621054 1509 MGKGADAVYKKALNEAADRFRELLKE 1534
Cdd:cd20153    81 FNRKKKGMYRKAITEAAKAAEHLTPE 106
PHD1_Lid2p_like cd15519
PHD finger 1 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar ...
1803-1842 5.29e-03

PHD finger 1 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar proteins; Lid2p is a trimethyl H3K4 (H3K4me3) demethylase responsible for H3K4 hypomethylation in heterochromatin. It interacts with the histone lysine-9 methyltransferase, Clr4, through the Dos1/Clr8-Rik1 complex, and mediates H3K9 methylation and small RNA production. It also acts cooperatively with the histone modification enzymes Set1 and Lsd1 and plays an essential role in cross-talk between H3K4 and H3K9 methylation in euchromatin. Lid2p contains a JmjC domain, three PHD fingers and a JmjN domain. This model corresponds to the first PHD finger.


Pssm-ID: 276994 [Multi-domain]  Cd Length: 46  Bit Score: 36.67  E-value: 5.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 292621054 1803 CFYCG---DGGQIVSCKkpGCPKVYHADCLN--LSKRPAGRWECP 1842
Cdd:cd15519     2 CEVCGlddNEGEVLLCD--GCDAEYHTSCLDppLGEIPPGTWFCP 44
PHD_PHF21A cd15523
PHD finger found in PHD finger protein 21A (PHF21A); PHF21A (also termed BHC80a or BRAF35-HDAC ...
1803-1842 5.81e-03

PHD finger found in PHD finger protein 21A (PHF21A); PHF21A (also termed BHC80a or BRAF35-HDAC complex protein BHC80) along with HDAC1/2, CtBP1, CoREST, and BRAF35, is associated with LSD1, a lysine (K)-specific histone demethylase. It inhibits LSD1-mediated histone demethylation in vitro. PHF21A is predominantly present in the central nervous system and spermatogenic cells and is one of the six components of BRAF-HDAC complex (BHC) involved in REST-dependent transcriptional repression of neuron-specific genes in non-neuronal cells. It acts as a scaffold protein in BHC in neuronal as well as non-neuronal cells and also plays a role in spermatogenesis. PHF21A contains a C-terminal plant homeodomain (PHD) finger that is responsible for the binding directly to each of five other components of BHC, and of organizing BHC mediating transcriptional repression.


Pssm-ID: 276998 [Multi-domain]  Cd Length: 43  Bit Score: 36.60  E-value: 5.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 292621054 1803 CFYCGDGGQIVSCKKpgCPKVYHADCLN--LSKRPAGRWECP 1842
Cdd:cd15523     2 CSVCRKSGELLMCDT--CSLVYHLDCLDppLKTIPKGMWICP 41
PWWP_HRP cd05834
PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The ...
286-352 6.30e-03

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


Pssm-ID: 438959 [Multi-domain]  Cd Length: 82  Bit Score: 37.53  E-value: 6.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 292621054  286 YSIGDVVWAKFNRRPWWPCHVTTDPQIDVHTKMKdpsrrpcrlYFVRMFG--EIvdqAWVPAKATFPFE 352
Cdd:cd05834     1 FKPGDLVFAKVKGYPPWPARIDEIPEGAKIPKNK---------YPVFFYGthET---AFLKPKDLFPYE 57
PHD_BS69 cd15537
PHD finger found in protein BS69; Protein BS69, also termed zinc finger MYND domain-containing ...
1803-1843 6.51e-03

PHD finger found in protein BS69; Protein BS69, also termed 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.


Pssm-ID: 277012  Cd Length: 43  Bit Score: 36.17  E-value: 6.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292621054 1803 CFYCGDGGQIVSCKkpGCPKVYHADCLNLSKRP--AGRWECPW 1843
Cdd:cd15537     2 CFECHAPGEVLPCS--GCFRVYHSDCLSEDFRPdsTSHWTCPV 42
PHD_TIF1alpha cd15622
PHD finger found in transcription intermediary factor 1-alpha (TIF1-alpha); TIF1-alpha, also ...
1229-1269 6.57e-03

PHD finger found in transcription intermediary factor 1-alpha (TIF1-alpha); TIF1-alpha, also termed tripartite motif-containing protein 24 (TRIM24), or E3 ubiquitin-protein ligase TRIM24, or RING finger protein 82, belongs to the TRIM/RBCC protein family. It interacts specifically and in a ligand-dependent manner with the ligand binding domain (LBD) of several nuclear receptors (NRs), including retinoid X (RXR), retinoic acid (RAR), vitamin D3 (VDR), estrogen (ER), and progesterone (PR) receptors. It also associates with heterochromatin-associated factors HP1alpha, MOD1 (HP1beta) and MOD2 (HP1gamma), as well as vertebrate Kruppel-type (C2H2) zinc finger proteins that contain transcriptional silencing domain KRAB. TIF1-alpha is a ligand-dependent co-repressor of retinoic acid receptor (RAR) that interacts with multiple nuclear receptors in vitro via an LXXLL motif, and further acts as a gatekeeper of liver carcinogenesis. It also functions as an E3-ubiquitin ligase targeting p53 and is broadly associated with chromatin silencing. Moreover, it is a chromatin regulator that recognizes specific, combinatorial histone modifications through its C-terminal plant homeodomain (PHD)-Bromodomain (Bromo) region. In addition, it interacts with chromatin and estrogen receptor to activate estrogen-dependent genes associated with cellular proliferation and tumor development. TIF1-alpha contains an N-terminal RBCC (RING finger, B-box zinc-fingers, coiled-coil), a plant homeodomain (PHD) finger, followed by a bromodomain in the C-terminal region.


Pssm-ID: 277092  Cd Length: 43  Bit Score: 36.58  E-value: 6.57e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 292621054 1229 CQVCEKTGELLLCEgQCCGAFHLQC--IGLTETPKGRFICQEC 1269
Cdd:cd15622     2 CAVCQNGGELLCCE-KCPKVFHLSChvPTLMNFPSGEWICTFC 43
PHD_ING5 cd15685
PHD finger found in inhibitor of growth protein 5 (ING5); ING5, also termed p28ING5, is one ...
1810-1842 7.26e-03

PHD finger found in inhibitor of growth protein 5 (ING5); ING5, also termed p28ING5, is one member of the inhibitor of growth (ING) family of type II tumor suppressors. It acts as a Tip60 cofactor that acetylates p53 at K120 and subsequently activates the expression of p53-dependent apoptotic genes in response to DNA damage. Aberrant ING5 expression may contribute to pathogenesis, growth, and invasion of gastric carcinomas and colorectal cancer. ING5 can physically interact with p300 and p53 in vivo, and its overexpression induces apoptosis in colorectal cancer cells. It also associates with cyclin A1 (INCA1) and functions as a growth suppressor with suppressed expression in Acute Myeloid Leukemia (AML). Moreover, ING5 translocation from the nucleus to the cytoplasm might be a critical event for carcinogenesis and tumor progression in human head and neck squamous cell carcinoma. In addition, ING5 associates with histone acetyltransferase (HAT) complexes containing MOZ (monocytic leukemia zinc finger protein)/MORF (MOZ-related factor) and HBO1, and further directs the MOZ/MORF and HBO1 complexes to chromatin. ING5 contains an N-terminal ING histone-binding domain and a C-terminal plant homeodomain (PHD) finger.


Pssm-ID: 277155 [Multi-domain]  Cd Length: 49  Bit Score: 36.57  E-value: 7.26e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 292621054 1810 GQIVSCKKPGCP-KVYHADCLNLSKRPAGRWECP 1842
Cdd:cd15685    11 GEMIGCDNPDCPiEWFHFACVDLTTKPKGKWFCP 44
PHD2_PHF12_Rco1 cd15534
PHD finger 2 found in PHD finger protein 12 (PHF12), yeast Rco1, and similar proteins; PHF12, ...
1803-1844 7.91e-03

PHD finger 2 found in PHD finger protein 12 (PHF12), yeast Rco1, and similar proteins; PHF12, also termed PHD factor 1 (Pf1), is a plant homeodomain (PHD) zinc finger-containing protein that bridges the transducin-like enhancer of split (TLE) corepressor to the mSin3A-histone deacetylase (HDAC)-complex, and further represses transcription at targeted genes. PHF12 also interacts with MRG15 (mortality factor-related genes on chromosome 15), a member of the mortality factor (MORF) family of proteins implicated in regulating cellular senescence. PHF12 contains two plant homeodomain (PHD) zinc fingers followed by a polybasic region. The PHD fingers function downstream of phosphoinositide signaling triggered by the interaction between polybasic regions and phosphoinositides. This subfamily also includes yeast transcriptional regulatory protein Rco1 and similar proteins. Rco1 is a component of the Rpd3S histone deacetylase complex that plays an important role at actively transcribed genes. Rco1 contains two PHD fingers, which are required for the methylation of histone H3 lysine 36 (H3K36) nucleosome recognition by Rpd3S. This model corresponds to the second PHD finger.


Pssm-ID: 277009  Cd Length: 47  Bit Score: 36.17  E-value: 7.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 292621054 1803 CFYC---GDGGQIVSCKKpgCPKVYHADCLN--LSKRPA-GRWECPWH 1844
Cdd:cd15534     2 CFKCnrsCRVAPLIQCDY--CPLLFHLDCLDppLTHPPAtGRWMCPNH 47
ADDz_Dnmt3 cd11725
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 (Dnmt3); Dnmt3 is a de ...
1803-1831 8.46e-03

ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 (Dnmt3); Dnmt3 is a de novo DNA methyltransferase family that includes two active enzymes Dnmt3a and -3b and one regulatory factor Dnmt3l. The ADDz domain of Dnmt3 is located in the C-terminal region of Dnmt3, which is an active catalytic domain in Dnmt3a and -b, but lacks some residues for enzymatic activity in Dnmt3l. DNA methylation is an important epigenetic mechanism involved in diverse biological processes such as embryonic development, gene expression, and genomic imprinting. The ADDz_Dnmt3 domain is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif.


Pssm-ID: 277251 [Multi-domain]  Cd Length: 108  Bit Score: 38.14  E-value: 8.46e-03
                          10        20
                  ....*....|....*....|....*....
gi 292621054 1803 CFYCGDGGQIVSCKKPGCPKVYHADCLNL 1831
Cdd:cd11725    50 CTICGGGGEVVLCDNPDCTRVYCTECLDL 78
PHD1_NSD cd15564
PHD finger 1 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
1393-1432 8.64e-03

PHD finger 1 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family 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 to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they non-redundant 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 (Cys5HisCysHis). This model corresponds to the first PHD finger.


Pssm-ID: 277039  Cd Length: 43  Bit Score: 36.16  E-value: 8.64e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 292621054 1393 CFVCSEGGSLLCCE-SCPAAFHRECLNI-EMPQGSWFCNDCR 1432
Cdd:cd15564     2 CQICEKPGKLLTCEgPCCGHFHLDCLGLsEQPDEPFKCDECT 43
PHD_ING4_5 cd15586
PHD finger found in inhibitor of growth protein 4 (ING4) and 5 (ING5); ING4, also termed ...
1810-1842 8.74e-03

PHD finger found in inhibitor of growth protein 4 (ING4) and 5 (ING5); ING4, also termed p29ING4, and ING5, also termed p28ING5, belong to the inhibitor of growth (ING) family of type II tumor suppressors. ING4 acts as an E3 ubiquitin ligase to induce ubiquitination of the p65 subunit of NF-kappaB and inhibit the transactivation of NF-kappaB target genes. It also induces apoptosis through a p53 dependent pathway, including increasing p53 acetylation, inhibiting Mdm2-mediated degradation of p53 and enhancing the expression of p53 responsive genes both at the transcriptional and post-translational levels. Moreover, ING4 can inhibit the translation of proto-oncogene MYC by interacting with AUF1. It also regulates other transcription factors, such as hypoxia-inducible factor (HIF). ING5 is a Tip60 cofactor that acetylates p53 at K120 and subsequently activates the expression of p53-dependent apoptotic genes in response to DNA damage. Aberrant ING5 expression may contribute to pathogenesis, growth, and invasion of gastric carcinomas and colorectal cancer. ING5 can physically interact with p300 and p53 in vivo, and its overexpression induces apoptosis in colorectal cancer cells. It also associates with cyclin A1 (INCA1) and functions as a growth suppressor with suppressed expression in Acute Myeloid Leukemia (AML). Moreover, ING5 translocation from the nucleus to the cytoplasm might be a critical event for carcinogenesis and tumor progression in human head and neck squamous cell carcinoma. Both ING4 and ING5 contain an N-terminal ING histone-binding domain and a C-terminal plant homeodomain (PHD) finger. They associate with histone acetyltransferase (HAT) complexes containing MOZ (monocytic leukemia zinc finger protein)/MORF (MOZ-related factor) and HBO1, and further direct the MOZ/MORF and HBO1 complexes to chromatin.


Pssm-ID: 277061 [Multi-domain]  Cd Length: 45  Bit Score: 36.01  E-value: 8.74e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 292621054 1810 GQIVSCKKPGCP-KVYHADCLNLSKRPAGRWECP 1842
Cdd:cd15586    10 GEMIGCDNPDCPiEWFHFACVGLTTKPKGKWFCP 43
PWWP_MUM1-like cd06080
PWWP domain found in mutated melanoma-associated antigen 1 (MUM-1) and similar proteins; MUM-1, ...
286-307 9.00e-03

PWWP domain found in mutated melanoma-associated antigen 1 (MUM-1) and similar proteins; MUM-1, also called PWWP domain-containing DNA repair factor 3A (PWWP3A), or protein expandere (EXPAND1), is a melanoma-associated antigen (MAA) that belongs to the mutated or aberrantly expressed type of MAAs, along with antigens such as CDK4, beta-catenin, gp100-in4, p15, and N-acetylglucosaminyltransferase V. It is highly expressed in several types of human cancers and involved in the DNA damage response pathway by contributing to the maintenance of chromatin architecture. MUM-1 is recruited to the vicinity of DNA breaks by TP53BP1 and plays an accessory role to facilitate damage-induced chromatin changes and promoting chromatin relaxation. It is required for efficient DNA repair and cell survival following DNA damage. This subfamily also includes mutated melanoma-associated antigen 1-like protein 1 (MUM1L1), also called MUM1-like protein 1, or PWWP domain-containing DNA repair factor 3B (PWWP3B). Its biological function remains unclear. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438967  Cd Length: 90  Bit Score: 37.23  E-value: 9.00e-03
                          10        20
                  ....*....|....*....|..
gi 292621054  286 YSIGDVVWAKFNRRPWWPCHVT 307
Cdd:cd06080     1 FSKGDIVWAKYRKYPYWPAVVK 22
PHD1_PHF12 cd15533
PHD finger 1 found in PHD finger protein 12 (PHF12); PHF12, also termed PHD factor 1 (Pf1), is ...
1803-1846 9.11e-03

PHD finger 1 found in PHD finger protein 12 (PHF12); PHF12, also termed PHD factor 1 (Pf1), is a plant homeodomain (PHD) zinc finger-containing protein that bridges the transducin-like enhancer of split (TLE) corepressor to the mSin3A-histone deacetylase (HDAC)-complex, and further represses transcription at targeted genes. PHF12 also interacts with MRG15 (mortality factor-related genes on chromosome 15), a member of the mortality factor (MORF) family of proteins implicated in regulating cellular senescence. PHF12 contains two plant-homeodomain (PHD) zinc fingers followed by a polybasic region. The PHD fingers function downstream of phosphoinositide signaling triggered by the interaction between polybasic regions and phosphoinositides. This model corresponds to the first PHD finger.


Pssm-ID: 277008 [Multi-domain]  Cd Length: 45  Bit Score: 36.18  E-value: 9.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 292621054 1803 CFYCGDGGQIVSCKKpgCPKVYHADCLN----LSKRPAGRWECpwHQC 1846
Cdd:cd15533     2 CDSCGEGGDLLCCDR--CPASFHLQCCNppldEEDLPPGEWLC--HRC 45
PHD_ING1 cd15682
PHD finger found in inhibitor of growth protein 1 (ING1); ING1 is an epigenetic regulator and ...
1236-1270 9.94e-03

PHD finger found in inhibitor of growth protein 1 (ING1); ING1 is an epigenetic regulator and a type II tumor suppressor that impacts cell growth, aging, apoptosis, and DNA repair, by affecting chromatin conformation and gene expression. It acts as a reader of the active chromatin mark, the trimethylation of histone H3 lysine 4 (H3K4me3). It binds and directs Growth arrest and DNA damage inducible protein 45 a (Gadd45a) to target sites, thus linking the histone code with DNA demethylation. It interacts with the proliferating cell nuclear antigen (PCNA) via the PCNA-interacting protein (PIP) domain in a UV-inducible manner. It also interacts with a PCNA-interacting protein, p15 (PAF). Moreover, ING1 associates with members of the 14-3-3 family, which is necessary for the cytoplasmic relocalization. Endogenous ING1 protein specifically interacts with the pro-apoptotic BCL2 family member BAX and colocalizes with BAX in a UV-inducible manner. It stabilizes the p53 tumor suppressor by inhibiting polyubiquitination of multi-monoubiquitinated forms via interaction with and colocalization of the herpesvirus-associated ubiquitin-specific protease (HAUSP)-deubiquitinase with p53. It is also involved in trichostatin A-induced apoptosis and caspase 3 signaling in p53-deficient glioblastoma cells. In addition, tyrosine kinase Src can bind phosphorylate ING1 and further regulates its activity. ING1 contains an N-terminal ING domain and a C-terminal plant homeodomain (PHD) finger.


Pssm-ID: 277152 [Multi-domain]  Cd Length: 49  Bit Score: 36.14  E-value: 9.94e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 292621054 1236 GELLLCEGQCCGA--FHLQCIGLTETPKGRFICQECK 1270
Cdd:cd15682    11 GEMIGCDNDECPIewFHFSCVGLNHKPKGKWYCPKCR 47
PHD_BRPF_JADE_like cd15492
PHD finger found in BRPF proteins, Jade proteins, protein AF-10, AF-17, and similar proteins; ...
1393-1431 9.96e-03

PHD finger found in BRPF proteins, Jade proteins, protein AF-10, AF-17, and similar proteins; The family includes BRPF proteins, Jade proteins, protein AF-10 and AF-17. BRPF proteins 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 canonical Cys4HisCys3 plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. PHD and ePHD fingers both bind to lysine 4 of histone H3 (K4H3), bromodomains interact with acetylated lysines on N-terminal tails of histones and other proteins, and PWWP domains show histone-binding and chromatin association properties. Jade proteins are required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and EAF6, to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. AF-10, also termed ALL1 (acute lymphoblastic leukemia)-fused gene from chromosome 10 protein, is a transcription factor that has been implicated in the development of leukemia following chromosomal rearrangements between the AF10 gene and one of at least two other genes, MLL and CALM. AF-17, also termed ALL1-fused gene from chromosome 17 protein, is a putative transcription factor that may play a role in multiple signaling pathways. All Jade proteins, AF-10, and AF-17 contain a canonical PHD finger followed by a non-canonical ePHD finger. This model corresponds to the canonical PHD finger.


Pssm-ID: 276967 [Multi-domain]  Cd Length: 46  Bit Score: 36.06  E-value: 9.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 292621054 1393 CFVCSEGGS-----LLCCESCPAAFHRECLNIE-MPQGSWFCNDC 1431
Cdd:cd15492     2 CDVCLDGESeddneIVFCDGCNVAVHQSCYGIPlIPEGDWFCRKC 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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